메뉴 건너뛰기




Volumn 76, Issue 2, 2012, Pages 115-158

Biology of the heat shock response and protein chaperones: Budding yeast (Saccharomyces cerevisiae) as a model system

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CALNEXIN; CELL CYCLE PROTEIN 37; CHAPERONE; CHAPERONIN; CYCLINE; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 26; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; MESSENGER RNA; PROTEASOME; PROTEIN DISULFIDE ISOMERASE; SACCHAROMYCES CEREVISIAE PROTEIN; SMALL HEAT SHOCK PROTEIN; SUPEROXIDE DISMUTASE; TRANSCRIPTOME;

EID: 84862550502     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.05018-11     Document Type: Review
Times cited : (432)

References (532)
  • 1
  • 2
    • 0033959642 scopus 로고    scopus 로고
    • The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
    • Abbas-Terki T, Donze O, Picard D. 2000. The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest. FEBS Lett. 467:111-116.
    • (2000) FEBS Lett. , vol.467 , pp. 111-116
    • Abbas-Terki, T.1    Donze, O.2    Picard, D.3
  • 3
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis
    • Aguilaniu H, Gustafsson L, Rigoulet M, Nystrom T. 2003. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 299:1751-1753.
    • (2003) Science , vol.299 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nystrom, T.4
  • 4
    • 0037442768 scopus 로고    scopus 로고
    • Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress
    • Ahn SG, Thiele DJ. 2003. Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress. Genes Dev. 17:516-528.
    • (2003) Genes Dev. , vol.17 , pp. 516-528
    • Ahn, S.G.1    Thiele, D.J.2
  • 5
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • Akerfelt M, Morimoto RI, Sistonen L. 2010. Heat shock factors: integrators of cell stress, development and lifespan. Nat. Rev. Mol. Cell Biol. 11:545-555.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 6
    • 0032710810 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae RanGTP-binding protein Msn5p is involved in different signal transduction pathways
    • Alepuz PM, Matheos D, Cunningham KW, Estruch F. 1999. The Saccharomyces cerevisiae RanGTP-binding protein Msn5p is involved in different signal transduction pathways. Genetics 153:1219-1231.
    • (1999) Genetics , vol.153 , pp. 1219-1231
    • Alepuz, P.M.1    Matheos, D.2    Cunningham, K.W.3    Estruch, F.4
  • 7
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali MM, et al. 2006. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440:1013-1017.
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1
  • 8
    • 77951229568 scopus 로고    scopus 로고
    • The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110
    • Andreasson C, Rampelt H, Fiaux J, Druffel-Augustin S, Bukau B. 2010. The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J. Biol. Chem. 285:12445-12453.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12445-12453
    • Andreasson, C.1    Rampelt, H.2    Fiaux, J.3    Druffel-Augustin, S.4    Bukau, B.5
  • 9
    • 33744948235 scopus 로고    scopus 로고
    • Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p
    • Andrew AJ, Dutkiewicz R, Knieszner H, Craig EA, Marszalek J. 2006. Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p. J. Biol. Chem. 281:14580-14587.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14580-14587
    • Andrew, A.J.1    Dutkiewicz, R.2    Knieszner, H.3    Craig, E.A.4    Marszalek, J.5
  • 11
    • 55249120532 scopus 로고    scopus 로고
    • Protein quality control: On IPODs and other JUNQ
    • Bagola K, Sommer T. 2008. Protein quality control: on IPODs and other JUNQ. Curr. Biol. 18:R1019-R1021.
    • (2008) Curr. Biol. , vol.18
    • Bagola, K.1    Sommer, T.2
  • 12
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: Hsp70 as a potential autoregulatory factor
    • Baler R, Welch WJ, Voellmy R. 1992. Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. J. Cell Biol. 117:1151-1159.
    • (1992) J. Cell Biol. , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 13
    • 0347481390 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone complex regulates maltose induction and stability of the Saccharomyces MAL gene transcription activator Mal63p
    • Bali M, Zhang B, Morano KA, Michels CA. 2003. The Hsp90 molecular chaperone complex regulates maltose induction and stability of the Saccharomyces MAL gene transcription activator Mal63p. J. Biol. Chem. 278:47441-47448.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47441-47448
    • Bali, M.1    Zhang, B.2    Morano, K.A.3    Michels, C.A.4
  • 14
    • 0025310194 scopus 로고
    • Thermotolerance is independent of induction of the full spectrum of heat shock proteins and of cell cycle blockage in the yeast Saccharomyces cerevisiae
    • Barnes CA, Johnston GC, Singer RA. 1990. Thermotolerance is independent of induction of the full spectrum of heat shock proteins and of cell cycle blockage in the yeast Saccharomyces cerevisiae. J. Bacteriol. 172:4352-4358.
    • (1990) J. Bacteriol. , vol.172 , pp. 4352-4358
    • Barnes, C.A.1    Johnston, G.C.2    Singer, R.A.3
  • 15
    • 79251562819 scopus 로고    scopus 로고
    • Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast
    • Batista-Nascimento L, Neef DW, Liu PC, Rodrigues-Pousada C, Thiele DJ. 2011. Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast. PLoS One 6:e15976.
    • (2011) PLoS One , vol.6
    • Batista-Nascimento, L.1    Neef, D.W.2    Liu, P.C.3    Rodrigues-Pousada, C.4    Thiele, D.J.5
  • 16
    • 0034731487 scopus 로고    scopus 로고
    • Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae
    • Baumann F, Milisav I, Neupert W, Herrmann JM. 2000. Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae. FEBS Lett. 487:307-312.
    • (2000) FEBS Lett. , vol.487 , pp. 307-312
    • Baumann, F.1    Milisav, I.2    Neupert, W.3    Herrmann, J.M.4
  • 17
    • 0029802682 scopus 로고    scopus 로고
    • SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum
    • Baxter BK, James P, Evans T, Craig EA. 1996. SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum. Mol. Cell. Biol. 16:6444-6456.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6444-6456
    • Baxter, B.K.1    James, P.2    Evans, T.3    Craig, E.A.4
  • 18
    • 0033540030 scopus 로고    scopus 로고
    • The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors
    • Beck T, Hall MN. 1999. The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors. Nature 402:689-692.
    • (1999) Nature , vol.402 , pp. 689-692
    • Beck, T.1    Hall, M.N.2
  • 19
    • 0029954823 scopus 로고    scopus 로고
    • Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo
    • Becker J, Walter W, Yan W, Craig EA. 1996. Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo. Mol. Cell. Biol. 16:4378-4386.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4378-4386
    • Becker, J.1    Walter, W.2    Yan, W.3    Craig, E.A.4
  • 20
    • 79956277243 scopus 로고    scopus 로고
    • Expression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast
    • Bell SL, Chiang AN, Brodsky JL. 2011. Expression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast. PLoS One 6:e20047.
    • (2011) PLoS One , vol.6
    • Bell, S.L.1    Chiang, A.N.2    Brodsky, J.L.3
  • 21
    • 0035968318 scopus 로고    scopus 로고
    • Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals
    • Benaroudj N, Lee DH, Goldberg AL. 2001. Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals. J. Biol. Chem. 276:24261-24267.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24261-24267
    • Benaroudj, N.1    Lee, D.H.2    Goldberg, A.L.3
  • 23
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales S, Papa FR, Walter P. 2006. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 22:487-508.
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 24
    • 55449104987 scopus 로고    scopus 로고
    • Stress-activated genomic expression changes serve a preparative role for impending stress in yeast
    • Berry DB, Gasch AP. 2008. Stress-activated genomic expression changes serve a preparative role for impending stress in yeast. Mol. Biol. Cell 19:4580-4587.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4580-4587
    • Berry, D.B.1    Gasch, A.P.2
  • 25
    • 0025971921 scopus 로고
    • A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast
    • Blumberg H, Silver PA. 1991. A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast. Nature 349:627-630.
    • (1991) Nature , vol.349 , pp. 627-630
    • Blumberg, H.1    Silver, P.A.2
  • 26
    • 0032553527 scopus 로고    scopus 로고
    • Interaction of Kar2p and Sls1p is required for efficient cotranslational translocation of secreted proteins in the yeast Yarrowia lipolytica
    • Boisrame A, Kabani M, Beckerich JM, Hartmann E, Gaillardin C. 1998. Interaction of Kar2p and Sls1p is required for efficient cotranslational translocation of secreted proteins in the yeast Yarrowia lipolytica. J. Biol. Chem. 273:30903-30908.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30903-30908
    • Boisrame, A.1    Kabani, M.2    Beckerich, J.M.3    Hartmann, E.4    Gaillardin, C.5
  • 27
    • 0040667180 scopus 로고    scopus 로고
    • Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane
    • Bomer U, et al. 1997. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane. EMBO J. 16:2205-2216.
    • (1997) EMBO J. , vol.16 , pp. 2205-2216
    • Bomer, U.1
  • 28
    • 0028047311 scopus 로고
    • Interactions between DNA-bound trimers of the yeast heat shock factor
    • Bonner JJ, Ballou C, Fackenthal DL. 1994. Interactions between DNA-bound trimers of the yeast heat shock factor. Mol. Cell. Biol. 14:501-508.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 501-508
    • Bonner, J.J.1    Ballou, C.2    Fackenthal, D.L.3
  • 29
    • 0034071558 scopus 로고    scopus 로고
    • Complex regulation of the yeast heat shock transcription factor
    • Bonner JJ, et al. 2000. Complex regulation of the yeast heat shock transcription factor. Mol. Biol. Cell 11:1739-1751.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1739-1751
    • Bonner, J.J.1
  • 30
    • 0026526179 scopus 로고
    • Temperature-dependent regulation of a heterologous transcription activation domain fused to yeast heat shock transcription factor
    • Bonner JJ, Heyward S, Fackenthal DL. 1992. Temperature-dependent regulation of a heterologous transcription activation domain fused to yeast heat shock transcription factor. Mol. Cell. Biol. 12:1021-1030.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1021-1030
    • Bonner, J.J.1    Heyward, S.2    Fackenthal, D.L.3
  • 31
    • 0025351346 scopus 로고
    • Transcriptional regulation of SSA3, an HSP70 gene from Saccharomyces cerevisiae
    • Boorstein WR, Craig EA. 1990. Transcriptional regulation of SSA3, an HSP70 gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 10:3262-3267.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3262-3267
    • Boorstein, W.R.1    Craig, E.A.2
  • 32
    • 0024421221 scopus 로고
    • Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich KA, Farrelly FW, Finkelstein DB, Taulien J, Lindquist S. 1989. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9:3919-3930.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 33
    • 77950599685 scopus 로고    scopus 로고
    • Ssz1 restores endoplasmic reticulum-associated protein degradation in cells expressing defective Cdc48-Ufd1-Npl4 complex by upregulating Cdc48
    • Bosis E, et al. 2009. Ssz1 restores endoplasmic reticulum-associated protein degradation in cells expressing defective Cdc48-Ufd1-Npl4 complex by upregulating Cdc48. Genetics 184:695-706.
    • (2009) Genetics , vol.184 , pp. 695-706
    • Bosis, E.1
  • 34
    • 13244296811 scopus 로고    scopus 로고
    • Identification of genes and proteins induced during the lag and early exponential phase of lager brewing yeasts
    • Brejning J, Arneborg N, Jespersen L. 2005. Identification of genes and proteins induced during the lag and early exponential phase of lager brewing yeasts. J. Appl. Microbiol. 98:261-271.
    • (2005) J. Appl. Microbiol. , vol.98 , pp. 261-271
    • Brejning, J.1    Arneborg, N.2    Jespersen, L.3
  • 35
    • 0020585357 scopus 로고
    • Isolation and transcriptional characterization of three genes which function at start, the controlling event of the Saccharomyces cerevisiae cell division cycle: CDC36, CDC37, and CDC39
    • Breter HJ, Ferguson J, Peterson TA, Reed SI. 1983. Isolation and transcriptional characterization of three genes which function at start, the controlling event of the Saccharomyces cerevisiae cell division cycle: CDC36, CDC37, and CDC39. Mol. Cell. Biol. 3:881-891.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 881-891
    • Breter, H.J.1    Ferguson, J.2    Peterson, T.A.3    Reed, S.I.4
  • 36
    • 0032963615 scopus 로고    scopus 로고
    • Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiae
    • Brizzio V, et al. 1999. Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiae. Mol. Biol. Cell 10:609-626.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 609-626
    • Brizzio, V.1
  • 37
    • 0028822223 scopus 로고
    • BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum
    • Brodsky JL, Goeckeler J, Schekman R. 1995. BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 92:9643-9646.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9643-9646
    • Brodsky, J.L.1    Goeckeler, J.2    Schekman, R.3
  • 38
    • 0027759380 scopus 로고
    • A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky JL, Schekman R. 1993. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J. Cell Biol. 123:1355-1363.
    • (1993) J. Cell Biol. , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 39
    • 77954994781 scopus 로고    scopus 로고
    • The relevance of heat shock regulation in fungal pathogens of humans
    • Brown AJ, Leach MD, Nicholls S. 2010. The relevance of heat shock regulation in fungal pathogens of humans. Virulence 1:330-332.
    • (2010) Virulence , vol.1 , pp. 330-332
    • Brown, A.J.1    Leach, M.D.2    Nicholls, S.3
  • 40
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • Buchan JR, Parker R. 2009. Eukaryotic stress granules: the ins and outs of translation. Mol. Cell 36:932-941.
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 41
    • 77949461455 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones
    • Buck TM, Kolb AR, Boyd CR, Kleyman TR, Brodsky JL. 2010. The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones. Mol. Biol. Cell 21:1047-1058.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1047-1058
    • Buck, T.M.1    Kolb, A.R.2    Boyd, C.R.3    Kleyman, T.R.4    Brodsky, J.L.5
  • 42
    • 13944259772 scopus 로고    scopus 로고
    • Role of trehalose and heat in the structure of the C-terminal activation domain of the heat shock transcription factor
    • Bulman AL, Nelson HC. 2005. Role of trehalose and heat in the structure of the C-terminal activation domain of the heat shock transcription factor. Proteins 58:826-835.
    • (2005) Proteins , vol.58 , pp. 826-835
    • Bulman, A.L.1    Nelson, H.C.2
  • 44
    • 0024151629 scopus 로고
    • Fungal cell wall synthesis: The construction of a biological structure
    • Cabib E, Bowers B, Sburlati A, Silverman SJ. 1988. Fungal cell wall synthesis: the construction of a biological structure. Microbiol. Sci. 5:370-375.
    • (1988) Microbiol. Sci. , vol.5 , pp. 370-375
    • Cabib, E.1    Bowers, B.2    Sburlati, A.3    Silverman, S.J.4
  • 45
    • 0024597893 scopus 로고
    • Chitin synthase 1, an auxiliary enzyme for chitin synthesis in Saccharomyces cerevisiae
    • Cabib E, Sburlati A, Bowers B, Silverman SJ. 1989. Chitin synthase 1, an auxiliary enzyme for chitin synthesis in Saccharomyces cerevisiae. J. Cell Biol. 108:1665-1672.
    • (1989) J. Cell Biol. , vol.108 , pp. 1665-1672
    • Cabib, E.1    Sburlati, A.2    Bowers, B.3    Silverman, S.J.4
  • 46
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • Cai H, Wang CC, Tsou CL. 1994. Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J. Biol. Chem. 269:24550-24552.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24550-24552
    • Cai, H.1    Wang, C.C.2    Tsou, C.L.3
  • 47
    • 0026661615 scopus 로고
    • Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase
    • Cairns BR, Ramer SW, Kornberg RD. 1992. Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase. Genes Dev. 6:1305-1318.
    • (1992) Genes Dev. , vol.6 , pp. 1305-1318
    • Cairns, B.R.1    Ramer, S.W.2    Kornberg, R.D.3
  • 48
    • 0041669463 scopus 로고    scopus 로고
    • The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20
    • Camasses A, Bogdanova A, Shevchenko A, Zachariae W. 2003. The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20. Mol. Cell 12:87-100.
    • (2003) Mol. Cell , vol.12 , pp. 87-100
    • Camasses, A.1    Bogdanova, A.2    Shevchenko, A.3    Zachariae, W.4
  • 49
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • Campuzano V, et al. 1996. Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion. Science 271:1423-1427.
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1
  • 50
    • 0025745326 scopus 로고
    • Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein
    • Caplan AJ, Douglas MG. 1991. Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J. Cell Biol. 114:609-621.
    • (1991) J. Cell Biol. , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 51
    • 0026686468 scopus 로고
    • Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae
    • Caplan AJ, Tsai J, Casey PJ, Douglas MG. 1992. Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae. J. Biol. Chem. 267:18890-18895.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18890-18895
    • Caplan, A.J.1    Tsai, J.2    Casey, P.J.3    Douglas, M.G.4
  • 52
    • 77957829719 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase Slt2 regulates nuclear retention of non-heat shock mRNAs during heat shock-induced stress
    • Carmody SR, Tran EJ, Apponi LH, Corbett AH, Wente SR. 2010. The mitogen-activated protein kinase Slt2 regulates nuclear retention of non-heat shock mRNAs during heat shock-induced stress. Mol. Cell. Biol. 30:5168-5179.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5168-5179
    • Carmody, S.R.1    Tran, E.J.2    Apponi, L.H.3    Corbett, A.H.4    Wente, S.R.5
  • 53
    • 0035239206 scopus 로고    scopus 로고
    • Structural comparison of prokaryotic and eukaryotic chaperonins
    • Carrascosa JL, Llorca O, Valpuesta JM. 2001. Structural comparison of prokaryotic and eukaryotic chaperonins. Micron 32:43-50.
    • (2001) Micron , vol.32 , pp. 43-50
    • Carrascosa, J.L.1    Llorca, O.2    Valpuesta, J.M.3
  • 54
    • 0029913811 scopus 로고    scopus 로고
    • Membrane lipid perturbation modifies the set point of the temperature of heat shock response in yeast
    • Carratu L, et al. 1996. Membrane lipid perturbation modifies the set point of the temperature of heat shock response in yeast. Proc. Natl. Acad. Sci. U. S. A. 93:3870-3875.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3870-3875
    • Carratu, L.1
  • 55
    • 0023403484 scopus 로고
    • Heat shock 70 gene is differentially expressed in Histoplasma capsulatum strains with different levels of thermotolerance and pathogenicity
    • Caruso M, Sacco M, Medoff G, Maresca B. 1987. Heat shock 70 gene is differentially expressed in Histoplasma capsulatum strains with different levels of thermotolerance and pathogenicity. Mol. Microbiol. 1:151-158.
    • (1987) Mol. Microbiol. , vol.1 , pp. 151-158
    • Caruso, M.1    Sacco, M.2    Medoff, G.3    Maresca, B.4
  • 56
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    • Cashikar AG, Duennwald M, Lindquist SL. 2005. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J. Biol. Chem. 280:23869-23875.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 57
    • 0036238432 scopus 로고    scopus 로고
    • Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein
    • Cashikar AG, et al. 2002. Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol. Cell 9:751-760.
    • (2002) Mol. Cell , vol.9 , pp. 751-760
    • Cashikar, A.G.1
  • 58
    • 0035149551 scopus 로고    scopus 로고
    • Remodeling of yeast genome expression in response to environmental changes
    • Causton HC, et al. 2001. Remodeling of yeast genome expression in response to environmental changes. Mol. Biol. Cell 12:323-337.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 323-337
    • Causton, H.C.1
  • 59
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the Hsp90 cochaperone Sti1 (p60)
    • Chang HC, Nathan DF, Lindquist S. 1997. In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol. Cell. Biol. 17:318-325.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 60
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham ME, Caplan AJ. 1998. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3:28-36.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 61
    • 84859462516 scopus 로고    scopus 로고
    • Cross-talks of sensory transcription networks in response to various environmental stresses
    • Chen T, Li F, Chen BS. 2009. Cross-talks of sensory transcription networks in response to various environmental stresses. Interdiscip. Sci. 1:46-54.
    • (2009) Interdiscip. Sci. , vol.1 , pp. 46-54
    • Chen, T.1    Li, F.2    Chen, B.S.3
  • 62
    • 0027491654 scopus 로고
    • Identification of the C-terminal activator domain in yeast heat shock factor: Independent control of transient and sustained transcriptional activity
    • Chen Y, Barlev NA, Westergaard O, Jakobsen BK. 1993. Identification of the C-terminal activator domain in yeast heat shock factor: independent control of transient and sustained transcriptional activity. EMBO J. 12:5007-5018.
    • (1993) EMBO J. , vol.12 , pp. 5007-5018
    • Chen, Y.1    Barlev, N.A.2    Westergaard, O.3    Jakobsen, B.K.4
  • 63
    • 0024972083 scopus 로고
    • Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
    • Cheng MY, et al. 1989. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337:620-625.
    • (1989) Nature , vol.337 , pp. 620-625
    • Cheng, M.Y.1
  • 64
    • 0030039788 scopus 로고    scopus 로고
    • Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy
    • Cho HS, et al. 1996. Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. Protein Sci. 5:262-269.
    • (1996) Protein Sci. , vol.5 , pp. 262-269
    • Cho, H.S.1
  • 65
    • 0034625349 scopus 로고    scopus 로고
    • Sphingolipids signal heat stress-induced ubiquitin-dependent proteolysis
    • Chung N, Jenkins G, Hannun YA, Heitman J, Obeid LM. 2000. Sphingolipids signal heat stress-induced ubiquitin-dependent proteolysis. J. Biol. Chem. 275:17229-17232.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17229-17232
    • Chung, N.1    Jenkins, G.2    Hannun, Y.A.3    Heitman, J.4    Obeid, L.M.5
  • 66
    • 0035870560 scopus 로고    scopus 로고
    • The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity
    • Cicero MP, et al. 2001. The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity. Nucleic Acids Res. 29:1715-1723.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1715-1723
    • Cicero, M.P.1
  • 68
    • 33846909430 scopus 로고    scopus 로고
    • The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor
    • Conlin LK, Nelson HC. 2007. The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor. Mol. Cell. Biol. 27:1505-1515.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1505-1515
    • Conlin, L.K.1    Nelson, H.C.2
  • 69
    • 36348993862 scopus 로고    scopus 로고
    • Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex
    • Conz C, et al. 2007. Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex. J. Biol. Chem. 282:33977-33984.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33977-33984
    • Conz, C.1
  • 70
    • 0030930513 scopus 로고    scopus 로고
    • The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae
    • Corsi AK, Schekman R. 1997. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J. Cell Biol. 137:1483-1493.
    • (1997) J. Cell Biol. , vol.137 , pp. 1483-1493
    • Corsi, A.K.1    Schekman, R.2
  • 71
    • 77956632480 scopus 로고    scopus 로고
    • Sphingolipids mediate formation of mRNA processing bodies during the heatstress response of Saccharomyces cerevisiae
    • Cowart LA, Gandy JL, Tholanikunnel B, Hannun YA. 2010. Sphingolipids mediate formation of mRNA processing bodies during the heatstress response of Saccharomyces cerevisiae. Biochem. J. 431:31-38.
    • (2010) Biochem. J. , vol.431 , pp. 31-38
    • Cowart, L.A.1    Gandy, J.L.2    Tholanikunnel, B.3    Hannun, Y.A.4
  • 72
    • 0043031395 scopus 로고    scopus 로고
    • Roles for sphingolipid biosynthesis in mediation of specific programs of the heat stress response determined through gene expression profiling
    • Cowart LA, et al. 2003. Roles for sphingolipid biosynthesis in mediation of specific programs of the heat stress response determined through gene expression profiling. J. Biol. Chem. 278:30328-30338.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30328-30338
    • Cowart, L.A.1
  • 74
    • 25844530060 scopus 로고    scopus 로고
    • Hsp90 potentiates the rapid evolution of new traits: Drug resistance in diverse fungi
    • Cowen LE, Lindquist S. 2005. Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science 309:2185-2189.
    • (2005) Science , vol.309 , pp. 2185-2189
    • Cowen, L.E.1    Lindquist, S.2
  • 75
    • 62449104891 scopus 로고    scopus 로고
    • Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease
    • Cowen LE, et al. 2009. Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc. Natl. Acad. Sci. U. S. A. 106:2818-2823.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2818-2823
    • Cowen, L.E.1
  • 76
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox JS, Walter P. 1996. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87:391-404.
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 77
    • 0002237472 scopus 로고
    • Cytosolic hsp70s of Saccharomyces cerevisiae: Roles in protein synthesis, protein translocation, proteolysis, and regulation
    • Morimoto RI, Tissieres A, Georgopolous C (ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Craig EA, Baxter BK, Becker J, Halladay J, Ziegelhoffer T. 1994. Cytosolic hsp70s of Saccharomyces cerevisiae: roles in protein synthesis, protein translocation, proteolysis, and regulation, p 31-52. In Morimoto RI, Tissieres A, Georgopolous C (ed), The biology of heat shock proteins and molecular chaperones, vol 26. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , vol.26 , pp. 31-52
    • Craig, E.A.1    Baxter, B.K.2    Becker, J.3    Halladay, J.4    Ziegelhoffer, T.5
  • 78
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig EA, Gambill BD, Nelson RJ. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402-414.
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 79
  • 80
    • 0022352154 scopus 로고
    • Mutations in cognate genes of Saccharomyces cerevisiae hsp70 result in reduced growth rates at low temperatures
    • Craig EA, Jacobsen K. 1985. Mutations in cognate genes of Saccharomyces cerevisiae hsp70 result in reduced growth rates at low temperatures. Mol. Cell. Biol. 5:3517-3524.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3517-3524
    • Craig, E.A.1    Jacobsen, K.2
  • 81
    • 0021685896 scopus 로고
    • Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth
    • Craig EA, Jacobsen K. 1984. Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth. Cell 38:841-849.
    • (1984) Cell , vol.38 , pp. 841-849
    • Craig, E.A.1    Jacobsen, K.2
  • 82
    • 0023182502 scopus 로고
    • SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth
    • Craig EA, Kramer J, Kosic-Smithers J. 1987. SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth. Proc. Natl. Acad. Sci. U. S. A. 84:4156-4160.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 4156-4160
    • Craig, E.A.1    Kramer, J.2    Kosic-Smithers, J.3
  • 83
    • 0024309756 scopus 로고
    • SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein
    • Craig EA, et al. 1989. SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein. Mol. Cell. Biol. 9:3000-3008.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3000-3008
    • Craig, E.A.1
  • 84
    • 0029969899 scopus 로고    scopus 로고
    • A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors
    • Craven RA, Egerton M, Stirling CJ. 1996. A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors. EMBO J. 15:2640-2650.
    • (1996) EMBO J. , vol.15 , pp. 2640-2650
    • Craven, R.A.1    Egerton, M.2    Stirling, C.J.3
  • 85
    • 0024293409 scopus 로고
    • CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast. I. Overall organization of the protein sequence displays several novel structural domains
    • Creusot F, Verdiere J, Gaisne M, Slonimski PP. 1988. CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast. I. Overall organization of the protein sequence displays several novel structural domains. J. Mol. Biol. 204:263-276.
    • (1988) J. Mol. Biol. , vol.204 , pp. 263-276
    • Creusot, F.1    Verdiere, J.2    Gaisne, M.3    Slonimski, P.P.4
  • 86
    • 84934441777 scopus 로고    scopus 로고
    • Trehalose as a "chemical chaperone": Fact and fantasy
    • Crowe JH. 2007. Trehalose as a "chemical chaperone": fact and fantasy. Adv. Exp. Med. Biol. 594:143-158.
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 143-158
    • Crowe, J.H.1
  • 87
    • 0242355632 scopus 로고    scopus 로고
    • Calcineurin signaling in Saccharomyces cerevisiae: How yeast go crazy in response to stress
    • Cyert MS. 2003. Calcineurin signaling in Saccharomyces cerevisiae: how yeast go crazy in response to stress. Biochem. Biophys. Res. Commun. 311:1143-1150.
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 1143-1150
    • Cyert, M.S.1
  • 88
    • 44649095580 scopus 로고    scopus 로고
    • Swapping nucleotides, tuning Hsp70
    • Cyr DM. 2008. Swapping nucleotides, tuning Hsp70. Cell 133:945-947.
    • (2008) Cell , vol.133 , pp. 945-947
    • Cyr, D.M.1
  • 89
    • 33846147991 scopus 로고    scopus 로고
    • The yeast PH domain proteins Slm1 and Slm2 are targets of sphingolipid signaling during the response to heat stress
    • Daquinag A, Fadri M, Jung SY, Qin J, Kunz J. 2007. The yeast PH domain proteins Slm1 and Slm2 are targets of sphingolipid signaling during the response to heat stress. Mol. Cell. Biol. 27:633-650.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 633-650
    • Daquinag, A.1    Fadri, M.2    Jung, S.Y.3    Qin, J.4    Kunz, J.5
  • 91
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • Decker CJ, Teixeira D, Parker R. 2007. Edc3p and a glutamine/asparagine- rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J. Cell Biol. 179:437-449.
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 92
    • 0027472047 scopus 로고
    • Evolution of the alphacrystallin/small heat-shock protein family
    • de Jong WW, Leunissen JA, Voorter CE. 1993. Evolution of the alphacrystallin/small heat-shock protein family. Mol. Biol. Evol. 10:103-126.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 93
    • 70450245119 scopus 로고    scopus 로고
    • Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo
    • de Keyzer J, Steel GJ, Hale SJ, Humphries D, Stirling CJ. 2009. Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo. J. Biol. Chem. 284:31564-31571.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31564-31571
    • De Keyzer, J.1    Steel, G.J.2    Hale, S.J.3    Humphries, D.4    Stirling, C.J.5
  • 94
    • 0034597012 scopus 로고    scopus 로고
    • H2O2 sensing through oxidation of the Yap1 transcription factor
    • Delaunay A, Isnard AD, Toledano MB. 2000. H2O2 sensing through oxidation of the Yap1 transcription factor. EMBO J. 19:5157-5166.
    • (2000) EMBO J. , vol.19 , pp. 5157-5166
    • Delaunay, A.1    Isnard, A.D.2    Toledano, M.B.3
  • 95
    • 0037110454 scopus 로고    scopus 로고
    • A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation
    • Delaunay A, Pflieger D, Barrault MB, Vinh J, Toledano MB. 2002. A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation. Cell 111:471-481.
    • (2002) Cell , vol.111 , pp. 471-481
    • Delaunay, A.1    Pflieger, D.2    Barrault, M.B.3    Vinh, J.4    Toledano, M.B.5
  • 96
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi JL, Iyer VR, Brown PO. 1997. Exploring the metabolic and genetic control of gene expression on a genomic scale. Science 278:680-686.
    • (1997) Science , vol.278 , pp. 680-686
    • DeRisi, J.L.1    Iyer, V.R.2    Brown, P.O.3
  • 97
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332:800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 98
    • 0028047402 scopus 로고
    • The role of trehalose synthesis for the acquisition of thermotolerance in yeast. I. Genetic evidence that trehalose is a thermoprotectant
    • De Virgilio C, Hottiger T, Dominguez J, Boller T, Wiemken A. 1994. The role of trehalose synthesis for the acquisition of thermotolerance in yeast. I. Genetic evidence that trehalose is a thermoprotectant. Eur. J. Biochem. 219:179-186.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 179-186
    • De Virgilio, C.1    Hottiger, T.2    Dominguez, J.3    Boller, T.4    Wiemken, A.5
  • 99
    • 28644434811 scopus 로고    scopus 로고
    • A dual role for PP1 in shaping the Msn2-dependent transcriptional response to glucose starvation
    • De Wever V, Reiter W, Ballarini A, Ammerer G, Brocard C. 2005. A dual role for PP1 in shaping the Msn2-dependent transcriptional response to glucose starvation. EMBO J. 24:4115-4123.
    • (2005) EMBO J. , vol.24 , pp. 4115-4123
    • De Wever, V.1    Reiter, W.2    Ballarini, A.3    Ammerer, G.4    Brocard, C.5
  • 100
    • 0037071871 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae
    • Dickson RC, Lester RL. 2002. Sphingolipid functions in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1583:13-25.
    • (2002) Biochim. Biophys. Acta , vol.1583 , pp. 13-25
    • Dickson, R.C.1    Lester, R.L.2
  • 101
    • 14444283860 scopus 로고    scopus 로고
    • Sphingolipids are potential heat stress signals in Saccharomyces
    • Dickson RC, et al. 1997. Sphingolipids are potential heat stress signals in Saccharomyces. J. Biol. Chem. 272:30196-30200.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30196-30200
    • Dickson, R.C.1
  • 102
    • 0036161746 scopus 로고    scopus 로고
    • Paracoccidioides brasiliensis 87-kilodalton antigen, a heat shock protein useful in diagnosis: Characterization, purification, and detection in biopsy material via immunohistochemistry
    • Diez S, Gomez BL, Restrepo A, Hay RJ, Hamilton AJ. 2002. Paracoccidioides brasiliensis 87-kilodalton antigen, a heat shock protein useful in diagnosis: characterization, purification, and detection in biopsy material via immunohistochemistry. J. Clin. Microbiol. 40:359-365.
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 359-365
    • Diez, S.1    Gomez, B.L.2    Restrepo, A.3    Hay, R.J.4    Hamilton, A.J.5
  • 103
    • 79959385317 scopus 로고    scopus 로고
    • Insights into prion biology: Integrating a protein misfolding pathway with its cellular environment
    • DiSalvo S, Serio TR. 2011. Insights into prion biology: integrating a protein misfolding pathway with its cellular environment. Prion 5:76-83.
    • (2011) Prion , vol.5 , pp. 76-83
    • DiSalvo, S.1    Serio, T.R.2
  • 104
    • 4644360186 scopus 로고    scopus 로고
    • The Reg1-interacting proteins, Bmh1, Bmh2, Ssb1, and Ssb2, have roles in maintaining glucose repression in Saccharomyces cerevisiae
    • Dombek KM, Kacherovsky N, Young ET. 2004. The Reg1-interacting proteins, Bmh1, Bmh2, Ssb1, and Ssb2, have roles in maintaining glucose repression in Saccharomyces cerevisiae. J. Biol. Chem. 279:39165-39174.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39165-39174
    • Dombek, K.M.1    Kacherovsky, N.2    Young, E.T.3
  • 105
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: Protein disaggregating machines
    • Doyle SM, Wickner S. 2009. Hsp104 and ClpB: protein disaggregating machines. Trends Biochem. Sci. 34:40-48.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 106
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU. 2006. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 25:2519-2528.
    • (2006) EMBO J. , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 107
    • 33751517708 scopus 로고    scopus 로고
    • Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p
    • Dragovic Z, Shomura Y, Tzvetkov N, Hartl FU, Bracher A. 2006. Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p. Biol. Chem. 387:1593-1600.
    • (2006) Biol. Chem. , vol.387 , pp. 1593-1600
    • Dragovic, Z.1    Shomura, Y.2    Tzvetkov, N.3    Hartl, F.U.4    Bracher, A.5
  • 108
    • 0031576350 scopus 로고    scopus 로고
    • The GCN4 leucine zipper can functionally substitute for the heat shock transcription factor's trimerization domain
    • Drees BL, Grotkopp EK, Nelson HC. 1997. The GCN4 leucine zipper can functionally substitute for the heat shock transcription factor's trimerization domain. J. Mol. Biol. 273:61-74.
    • (1997) J. Mol. Biol. , vol.273 , pp. 61-74
    • Drees, B.L.1    Grotkopp, E.K.2    Nelson, H.C.3
  • 109
    • 0345133332 scopus 로고    scopus 로고
    • J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix
    • D'Silva PD, Schilke B, Walter W, Andrew A, Craig EA. 2003. J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix. Proc. Natl. Acad. Sci. U. S. A. 100:13839-13844.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13839-13844
    • D'Silva, P.D.1    Schilke, B.2    Walter, W.3    Andrew, A.4    Craig, E.A.5
  • 110
    • 24644486039 scopus 로고    scopus 로고
    • Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane
    • D'Silva PR, Schilke B, Walter W, Craig EA. 2005. Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane. Proc. Natl. Acad. Sci. U. S. A. 102:12419-12424.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 12419-12424
    • D'Silva, P.R.1    Schilke, B.2    Walter, W.3    Craig, E.A.4
  • 111
    • 0032531727 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10
    • Dubaquie Y, Looser R, Funfschilling U, Jeno P, Rospert S. 1998. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. EMBO J. 17:5868-5876.
    • (1998) EMBO J. , vol.17 , pp. 5868-5876
    • Dubaquie, Y.1    Looser, R.2    Funfschilling, U.3    Jeno, P.4    Rospert, S.5
  • 112
  • 113
    • 0032563195 scopus 로고    scopus 로고
    • Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response
    • Duina AA, Kalton HM, Gaber RF. 1998. Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J. Biol. Chem. 273:18974-18978.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18974-18978
    • Duina, A.A.1    Kalton, H.M.2    Gaber, R.F.3
  • 114
    • 0042531776 scopus 로고    scopus 로고
    • Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart
    • Dutkiewicz R, et al. 2003. Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart. J. Biol. Chem. 278:29719-29727.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29719-29727
    • Dutkiewicz, R.1
  • 115
    • 0037385220 scopus 로고    scopus 로고
    • A yeast homologue of Hsp70, Ssa1p, regulates turnover of the MFA2 transcript through its AU-rich 3′ untranslated region
    • Duttagupta R, Vasudevan S, Wilusz CJ, Peltz SW. 2003. A yeast homologue of Hsp70, Ssa1p, regulates turnover of the MFA2 transcript through its AU-rich 3′ untranslated region. Mol. Cell. Biol. 23:2623-2632.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2623-2632
    • Duttagupta, R.1    Vasudevan, S.2    Wilusz, C.J.3    Peltz, S.W.4
  • 116
    • 0033625965 scopus 로고    scopus 로고
    • The hsp110 and Grp170 stress proteins: Newly recognized relatives of the Hsp70s
    • Easton DP, Kaneko Y, Subjeck JR. 2000. The hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones 5:276-290.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 276-290
    • Easton, D.P.1    Kaneko, Y.2    Subjeck, J.R.3
  • 117
    • 79960452274 scopus 로고    scopus 로고
    • Global functional map of the p23 molecular chaperone reveals an extensive cellular network
    • Echtenkamp FJ, et al. 2011. Global functional map of the p23 molecular chaperone reveals an extensive cellular network. Mol. Cell 43:229-241.
    • (2011) Mol. Cell , vol.43 , pp. 229-241
    • Echtenkamp, F.J.1
  • 118
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A. 1999. Setting the standards: quality control in the secretory pathway. Science 286:1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 119
    • 0029861940 scopus 로고    scopus 로고
    • Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiae
    • Elliott B, Haltiwanger RS, Futcher B. 1996. Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiae. Genetics 144:923-933.
    • (1996) Genetics , vol.144 , pp. 923-933
    • Elliott, B.1    Haltiwanger, R.S.2    Futcher, B.3
  • 120
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis J. 1987. Proteins as molecular chaperones. Nature 328:378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 121
    • 34948846000 scopus 로고    scopus 로고
    • Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
    • Erjavec N, Larsson L, Grantham J, Nystrom T. 2007. Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev. 21:2410-2421.
    • (2007) Genes Dev. , vol.21 , pp. 2410-2421
    • Erjavec, N.1    Larsson, L.2    Grantham, J.3    Nystrom, T.4
  • 122
    • 0028913144 scopus 로고
    • Cloning of a DNA fragment encoding part of a 70-kDa heat shock protein of Candida albicans
    • Eroles P, Sentandreu M, Elorza MV, Sentandreu R. 1995. Cloning of a DNA fragment encoding part of a 70-kDa heat shock protein of Candida albicans. FEMS Microbiol. Lett. 128:95-100.
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 95-100
    • Eroles, P.1    Sentandreu, M.2    Elorza, M.V.3    Sentandreu, R.4
  • 123
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger JP, Berger JM. 2006. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35:93-114.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 124
    • 0033813390 scopus 로고    scopus 로고
    • Stress-controlled transcription factors, stress-induced genes and stress tolerance in budding yeast
    • Estruch F. 2000. Stress-controlled transcription factors, stress-induced genes and stress tolerance in budding yeast. FEMS Microbiol. Rev. 24:469-486.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 469-486
    • Estruch, F.1
  • 125
    • 0025875662 scopus 로고
    • The yeast putative transcriptional repressor RGM1 is a proline-rich zinc finger protein
    • Estruch F. 1991. The yeast putative transcriptional repressor RGM1 is a proline-rich zinc finger protein. Nucleic Acids Res. 19:4873-4877.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4873-4877
    • Estruch, F.1
  • 126
    • 0027253092 scopus 로고
    • Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae
    • Estruch F, Carlson M. 1993. Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae. Mol. Cell. Biol. 13:3872-3881.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3872-3881
    • Estruch, F.1    Carlson, M.2
  • 127
    • 0031832233 scopus 로고    scopus 로고
    • SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins
    • Fang Y, Fliss AE, Rao J, Caplan AJ. 1998. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol. Cell. Biol. 18:3727-3734.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3727-3734
    • Fang, Y.1    Fliss, A.E.2    Rao, J.3    Caplan, A.J.4
  • 128
    • 0025831094 scopus 로고
    • Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae
    • Farquhar R, et al. 1991. Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108:81-89.
    • (1991) Gene , vol.108 , pp. 81-89
    • Farquhar, R.1
  • 129
    • 0026690820 scopus 로고
    • Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation
    • Feldheim D, Rothblatt J, Schekman R. 1992. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol. Cell. Biol. 12:3288-3296.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3288-3296
    • Feldheim, D.1    Rothblatt, J.2    Schekman, R.3
  • 130
    • 17444389196 scopus 로고    scopus 로고
    • Protein kinase A regulates constitutive expression of small heat-shock genes in an Msn2/4p-independent and Hsf1p-dependent manner in Saccharomyces cerevisiae
    • Ferguson SB, et al. 2005. Protein kinase A regulates constitutive expression of small heat-shock genes in an Msn2/4p-independent and Hsf1p-dependent manner in Saccharomyces cerevisiae. Genetics 169:1203-1214.
    • (2005) Genetics , vol.169 , pp. 1203-1214
    • Ferguson, S.B.1
  • 131
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty KM, DeLuca-Flaherty C, McKay DB. 1990. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346:623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 132
    • 0028352287 scopus 로고
    • Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains. Implications for DNA binding by trimeric proteins
    • Flick KE, Gonzalez L, Jr, Harrison CJ, Nelson HC. 1994. Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains. Implications for DNA binding by trimeric proteins. J. Biol. Chem. 269:12475-12481.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12475-12481
    • Flick, K.E.1    Gonzalez Jr., L.2    Harrison, C.J.3    Nelson, H.C.4
  • 133
    • 34249041590 scopus 로고    scopus 로고
    • Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions
    • Flom G, Behal RH, Rosen L, Cole DG, Johnson JL. 2007. Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions. Biochem. J. 404:159-167.
    • (2007) Biochem. J. , vol.404 , pp. 159-167
    • Flom, G.1    Behal, R.H.2    Rosen, L.3    Cole, D.G.4    Johnson, J.L.5
  • 134
    • 59449095866 scopus 로고    scopus 로고
    • Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins
    • Flom GA, Lemieszek M, Fortunato EA, Johnson JL. 2008. Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins. Mol. Biol. Cell 19:5249-5258.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5249-5258
    • Flom, G.A.1    Lemieszek, M.2    Fortunato, E.A.3    Johnson, J.L.4
  • 135
    • 43249105354 scopus 로고    scopus 로고
    • p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
    • Forafonov F, et al. 2008. p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity. Mol. Cell. Biol. 28:3446-3456.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3446-3456
    • Forafonov, F.1
  • 136
    • 45249100468 scopus 로고    scopus 로고
    • The spindle position checkpoint: How to deal with spindle misalignment during asymmetric cell division in budding yeast
    • Fraschini R, Venturetti M, Chiroli E, Piatti S. 2008. The spindle position checkpoint: how to deal with spindle misalignment during asymmetric cell division in budding yeast. Biochem. Soc. Trans. 36:416-420.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 416-420
    • Fraschini, R.1    Venturetti, M.2    Chiroli, E.3    Piatti, S.4
  • 137
    • 10744229056 scopus 로고    scopus 로고
    • Pam16 has an essential role in the mitochondrial protein import motor
    • Frazier AE, et al. 2004. Pam16 has an essential role in the mitochondrial protein import motor. Nat. Struct. Mol. Biol. 11:226-233.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 226-233
    • Frazier, A.E.1
  • 138
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman RB, Hirst TR, Tuite MF. 1994. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19:331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 139
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman BC, Myers MP, Schumacher R, Morimoto RI. 1995. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14:2281-2292.
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 140
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70:603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 141
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman J, et al. 1992. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits.EMBO J. 11:4767-4778.
    • (1992) EMBO J. , vol.11 , pp. 4767-4778
    • Frydman, J.1
  • 142
    • 0034597551 scopus 로고    scopus 로고
    • The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast
    • Gall WE, et al. 2000. The auxilin-like phosphoprotein Swa2p is required for clathrin function in yeast. Curr. Biol. 10:1349-1358.
    • (2000) Curr. Biol. , vol.10 , pp. 1349-1358
    • Gall, W.E.1
  • 143
    • 0027490849 scopus 로고
    • A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins
    • Gambill BD, et al. 1993. A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins. J. Cell Biol. 123:109-117.
    • (1993) J. Cell Biol. , vol.123 , pp. 109-117
    • Gambill, B.D.1
  • 144
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • Gardner BM, Walter P. 2011. Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333:1891-1894.
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 145
    • 0033828333 scopus 로고    scopus 로고
    • Hyperphosphorylation of Msn2p and Msn4p in response to heat shock and the diauxic shift is inhibited by cAMP in Saccharomyces cerevisiae
    • Garreau H, et al. 2000. Hyperphosphorylation of Msn2p and Msn4p in response to heat shock and the diauxic shift is inhibited by cAMP in Saccharomyces cerevisiae. Microbiology 146(Pt 9):2113-2120.
    • (2000) Microbiology , vol.146 , Issue.PART 9 , pp. 2113-2120
    • Garreau, H.1
  • 146
    • 0025851170 scopus 로고
    • The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle
    • Garrett S, Menold MM, Broach JR. 1991. The Saccharomyces cerevisiae YAK1 gene encodes a protein kinase that is induced by arrest early in the cell cycle. Mol. Cell. Biol. 11:4045-4052.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4045-4052
    • Garrett, S.1    Menold, M.M.2    Broach, J.R.3
  • 147
    • 0033637153 scopus 로고    scopus 로고
    • Genomic expression programs in the response of yeast cells to environmental changes
    • Gasch AP, et al. 2000. Genomic expression programs in the response of yeast cells to environmental changes. Mol. Biol. Cell 11:4241-4257.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4241-4257
    • Gasch, A.P.1
  • 148
    • 0036728274 scopus 로고    scopus 로고
    • The genomics of yeast responses to environmental stress and starvation
    • Gasch AP, Werner-Washburne M. 2002. The genomics of yeast responses to environmental stress and starvation. Funct. Integr. Genomics 2:181-192.
    • (2002) Funct. Integr. Genomics , vol.2 , pp. 181-192
    • Gasch, A.P.1    Werner-Washburne, M.2
  • 149
    • 0035957355 scopus 로고    scopus 로고
    • RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin
    • Gautschi M, et al. 2001. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. Proc. Natl. Acad. Sci. U. S. A. 98:3762-3767.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3762-3767
    • Gautschi, M.1
  • 150
    • 0037008763 scopus 로고    scopus 로고
    • A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase
    • Germaniuk A, Liberek K, Marszalek J. 2002. A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J. Biol. Chem. 277:27801-27808.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27801-27808
    • Germaniuk, A.1    Liberek, K.2    Marszalek, J.3
  • 151
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething MJ, McCammon K, Sambrook J. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell 46:939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.J.1    McCammon, K.2    Sambrook, J.3
  • 152
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami S, et al. 2003. Global analysis of protein expression in yeast. Nature 425:737-741.
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 153
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever G, et al. 2002. Functional profiling of the Saccharomyces cerevisiae genome. Nature 418:387-391.
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1
  • 154
    • 0033611127 scopus 로고    scopus 로고
    • Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase
    • Gillece P, Luz JM, Lennarz WJ, de La Cruz FJ, Romisch K. 1999. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J. Cell Biol. 147:1443-1456.
    • (1999) J. Cell Biol. , vol.147 , pp. 1443-1456
    • Gillece, P.1    Luz, J.M.2    Lennarz, W.J.3    De La Cruz, F.J.4    Romisch, K.5
  • 155
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • Glick BS. 1995. Can Hsp70 proteins act as force-generating motors? Cell 80:11-14.
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 156
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S. 1998. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 157
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: Implications to protein folding pathways in the cell
    • Gong Y, et al. 2009. An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol. Syst. Biol. 5:275.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 275
    • Gong, Y.1
  • 158
    • 0032518996 scopus 로고    scopus 로고
    • 2 zinc finger protein Msn2p is regulated by stress and protein kinase A activity
    • 2 zinc finger protein Msn2p is regulated by stress and protein kinase A activity. Genes Dev. 12:586-597.
    • (1998) Genes Dev. , vol.12 , pp. 586-597
    • Gorner, W.1
  • 159
    • 0037080980 scopus 로고    scopus 로고
    • Acute glucose starvation activates the nuclear localization signal of a stress-specific yeast transcription factor
    • Gorner W, et al. 2002. Acute glucose starvation activates the nuclear localization signal of a stress-specific yeast transcription factor. EMBO J. 21:135-144.
    • (2002) EMBO J. , vol.21 , pp. 135-144
    • Gorner, W.1
  • 160
    • 3142633123 scopus 로고    scopus 로고
    • Being at the right place at the right time: The role of nuclear transport in dynamic transcriptional regulation in yeast
    • Gorner W, Schuller C, Ruis H. 1999. Being at the right place at the right time: the role of nuclear transport in dynamic transcriptional regulation in yeast. Biol. Chem. 380:147-150.
    • (1999) Biol. Chem. , vol.380 , pp. 147-150
    • Gorner, W.1    Schuller, C.2    Ruis, H.3
  • 162
    • 0031859045 scopus 로고    scopus 로고
    • Transcriptional and translational regulation of major heat shock proteins and patterns of trehalose mobilization during hyperthermic recovery in repressed and derepressed Saccharomyces cerevisiae
    • Gross C, Watson K. 1998. Transcriptional and translational regulation of major heat shock proteins and patterns of trehalose mobilization during hyperthermic recovery in repressed and derepressed Saccharomyces cerevisiae. Can. J. Microbiol. 44:341-350.
    • (1998) Can. J. Microbiol. , vol.44 , pp. 341-350
    • Gross, C.1    Watson, K.2
  • 163
    • 68949172267 scopus 로고    scopus 로고
    • Robust heat shock induces eIF2alpha-phosphorylation- independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae
    • Grousl T, et al. 2009. Robust heat shock induces eIF2alpha- phosphorylation- independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae. J. Cell Sci. 122:2078-2088.
    • (2009) J. Cell Sci. , vol.122 , pp. 2078-2088
    • Grousl, T.1
  • 164
    • 0025865002 scopus 로고
    • Pheromone response elements are necessary and sufficient for basal and pheromone-induced transcription of the FUS1 gene of Saccharomyces cerevisiae
    • Hagen DC, McCaffrey G, Sprague GF, Jr. 1991. Pheromone response elements are necessary and sufficient for basal and pheromone-induced transcription of the FUS1 gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 11:2952-2961.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2952-2961
    • Hagen, D.C.1    McCaffrey, G.2    Sprague Jr., G.F.3
  • 165
    • 2942598422 scopus 로고    scopus 로고
    • Genome-wide analysis of the biology of stress responses through heat shock transcription factor
    • Hahn JS, Hu Z, Thiele DJ, Iyer VR. 2004. Genome-wide analysis of the biology of stress responses through heat shock transcription factor. Mol. Cell. Biol. 24:5249-5256.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5249-5256
    • Hahn, J.S.1    Hu, Z.2    Thiele, D.J.3    Iyer, V.R.4
  • 166
    • 1242294502 scopus 로고    scopus 로고
    • Activation of the Saccharomyces cerevisiae heat shock transcription factor under glucose starvation conditions by Snf1 protein kinase
    • Hahn JS, Thiele DJ. 2004. Activation of the Saccharomyces cerevisiae heat shock transcription factor under glucose starvation conditions by Snf1 protein kinase. J. Biol. Chem. 279:5169-5176.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5169-5176
    • Hahn, J.S.1    Thiele, D.J.2
  • 167
    • 69249130057 scopus 로고    scopus 로고
    • The charged linker region is an important regulator of Hsp90 function
    • Hainzl O, Lapina MC, Buchner J, Richter K. 2009. The charged linker region is an important regulator of Hsp90 function. J. Biol. Chem. 284:22559-22567.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22559-22567
    • Hainzl, O.1    Lapina, M.C.2    Buchner, J.3    Richter, K.4
  • 168
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman BD, Hendershot LM, Johnson AE. 1998. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92:747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 169
    • 0035053046 scopus 로고    scopus 로고
    • Increasing Saccharomyces cerevisiae stress resistance, through the over-activation of the heat shock response resulting from defects in the Hsp90 chaperone, does not extend replicative life span but can be associated with slower chronological ageing of nondividing cells
    • Harris N, MacLean M, Hatzianthis K, Panaretou B, Piper PW. 2001. Increasing Saccharomyces cerevisiae stress resistance, through the over-activation of the heat shock response resulting from defects in the Hsp90 chaperone, does not extend replicative life span but can be associated with slower chronological ageing of nondividing cells. Mol. Genet. Genomics 265:258-263.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 258-263
    • Harris, N.1    MacLean, M.2    Hatzianthis, K.3    Panaretou, B.4    Piper, P.W.5
  • 170
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276:431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 171
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 172
    • 1942518714 scopus 로고    scopus 로고
    • Phosphorylation of the yeast heat shock transcription factor is implicated in gene-specific activation dependent on the architecture of the heat shock element
    • Hashikawa N, Sakurai H. 2004. Phosphorylation of the yeast heat shock transcription factor is implicated in gene-specific activation dependent on the architecture of the heat shock element. Mol. Cell. Biol. 24:3648-3659.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3648-3659
    • Hashikawa, N.1    Sakurai, H.2
  • 173
    • 34249845676 scopus 로고    scopus 로고
    • Different mechanisms are involved in the transcriptional activation by yeast heat shock transcription factor through two different types of heat shock elements
    • Hashikawa N, Yamamoto N, Sakurai H. 2007. Different mechanisms are involved in the transcriptional activation by yeast heat shock transcription factor through two different types of heat shock elements. J. Biol. Chem. 282:10333-10340.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10333-10340
    • Hashikawa, N.1    Yamamoto, N.2    Sakurai, H.3
  • 174
    • 33646013288 scopus 로고    scopus 로고
    • Recombinant expression and in vitro refolding of the yeast small heat shock protein Hsp42
    • Haslbeck M. 2006. Recombinant expression and in vitro refolding of the yeast small heat shock protein Hsp42. Int. J. Biol. Macromol. 38:107-114.
    • (2006) Int. J. Biol. Macromol. , vol.38 , pp. 107-114
    • Haslbeck, M.1
  • 175
    • 1442289304 scopus 로고    scopus 로고
    • Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae
    • Haslbeck M, et al. 2004. Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J. 23:638-649.
    • (2004) EMBO J. , vol.23 , pp. 638-649
    • Haslbeck, M.1
  • 176
    • 4644313922 scopus 로고    scopus 로고
    • A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization
    • Haslbeck M, et al. 2004. A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization. J. Mol. Biol. 343:445-455.
    • (2004) J. Mol. Biol. , vol.343 , pp. 445-455
    • Haslbeck, M.1
  • 177
    • 21244497886 scopus 로고    scopus 로고
    • Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104
    • Haslbeck M, Miess A, Stromer T, Walter S, Buchner J. 2005. Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J. Biol. Chem. 280:23861-23868.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23861-23868
    • Haslbeck, M.1    Miess, A.2    Stromer, T.3    Walter, S.4    Buchner, J.5
  • 178
    • 0033485868 scopus 로고    scopus 로고
    • Hsp26: A temperature-regulated chaperone
    • Haslbeck M, et al. 1999. Hsp26: a temperature-regulated chaperone. EMBO J. 18:6744-6751.
    • (1999) EMBO J. , vol.18 , pp. 6744-6751
    • Haslbeck, M.1
  • 179
    • 75349113019 scopus 로고    scopus 로고
    • Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation
    • Haslberger T, Bukau B, Mogk A. 2010. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem. Cell Biol. 88:63-75.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 63-75
    • Haslberger, T.1    Bukau, B.2    Mogk, A.3
  • 180
    • 33947633366 scopus 로고    scopus 로고
    • Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)
    • Hawle P, et al. 2007. Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p). Eukaryot. Cell 6:521-532.
    • (2007) Eukaryot. Cell , vol.6 , pp. 521-532
    • Hawle, P.1
  • 181
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck JW, Cheung SK, Hampton RY. 2010. Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl. Acad. Sci. U. S. A. 107:1106-1111.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 182
    • 61949349758 scopus 로고    scopus 로고
    • Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
    • Hessling M, Richter K, Buchner J. 2009. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat. Struct. Mol. Biol. 16:287-293.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 287-293
    • Hessling, M.1    Richter, K.2    Buchner, J.3
  • 183
    • 0034717895 scopus 로고    scopus 로고
    • Transport of fatty acids and metabolites across the peroxisomal membrane
    • Hettema EH, Tabak HF. 2000. Transport of fatty acids and metabolites across the peroxisomal membrane. Biochim. Biophys. Acta 1486:18-27.
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 18-27
    • Hettema, E.H.1    Tabak, H.F.2
  • 184
    • 0031896846 scopus 로고    scopus 로고
    • Directionality of polypeptide transfer in the mitochondrial pathway of chaperonemediated protein folding
    • Heyrovska N, Frydman J, Hohfeld J, Hartl FU. 1998. Directionality of polypeptide transfer in the mitochondrial pathway of chaperonemediated protein folding. Biol. Chem. 379:301-309.
    • (1998) Biol. Chem. , vol.379 , pp. 301-309
    • Heyrovska, N.1    Frydman, J.2    Hohfeld, J.3    Hartl, F.U.4
  • 185
    • 33749433916 scopus 로고    scopus 로고
    • Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators
    • Hieronymus H, et al. 2006. Gene expression signature-based chemical genomic prediction identifies a novel class of HSP90 pathway modulators. Cancer Cell 10:321-330.
    • (2006) Cancer Cell , vol.10 , pp. 321-330
    • Hieronymus, H.1
  • 186
    • 0031951035 scopus 로고    scopus 로고
    • The integral membrane protein Snl1p is genetically linked to yeast nuclear pore complex function
    • Ho AK, Raczniak GA, Ives EB, Wente SR. 1998. The integral membrane protein Snl1p is genetically linked to yeast nuclear pore complex function. Mol. Biol. Cell 9:355-373.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 355-373
    • Ho, A.K.1    Raczniak, G.A.2    Ives, E.B.3    Wente, S.R.4
  • 187
    • 0028234368 scopus 로고
    • Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria
    • Hohfeld J, Hartl FU. 1994. Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. J. Cell Biol. 126:305-315.
    • (1994) J. Cell Biol. , vol.126 , pp. 305-315
    • Hohfeld, J.1    Hartl, F.U.2
  • 188
    • 0028321786 scopus 로고
    • A short element required for turning off heat shock transcription factor: Evidence that phosphorylation enhances deactivation
    • Hoj A, Jakobsen BK. 1994. A short element required for turning off heat shock transcription factor: evidence that phosphorylation enhances deactivation. EMBO J. 13:2617-2624.
    • (1994) EMBO J. , vol.13 , pp. 2617-2624
    • Hoj, A.1    Jakobsen, B.K.2
  • 189
    • 17444422796 scopus 로고    scopus 로고
    • The heme activator protein HapI represses transcription by a heme-independent mechanism in Saccharomyces cerevisiae
    • Hon T, Lee HC, Hu Z, Iyer VR, Zhang L. 2005. The heme activator protein HapI represses transcription by a heme-independent mechanism in Saccharomyces cerevisiae. Genetics 169:1343-1352.
    • (2005) Genetics , vol.169 , pp. 1343-1352
    • Hon, T.1    Lee, H.C.2    Hu, Z.3    Iyer, V.R.4    Zhang, L.5
  • 190
    • 0030933229 scopus 로고    scopus 로고
    • Sequential action of two hsp70 complexes during protein import into mitochondria
    • Horst M, et al. 1997. Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J. 16:1842-1849.
    • (1997) EMBO J. , vol.16 , pp. 1842-1849
    • Horst, M.1
  • 191
    • 0035958083 scopus 로고    scopus 로고
    • The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes
    • Horton LE, James P, Craig EA, Hensold JO. 2001. The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. J. Biol. Chem. 276:14426-14433.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14426-14433
    • Horton, L.E.1    James, P.2    Craig, E.A.3    Hensold, J.O.4
  • 192
    • 0028054926 scopus 로고
    • The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro
    • Hottiger T, De Virgilio C, Hall MN, Boller T, Wiemken A. 1994. The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro. Eur. J. Biochem. 219:187-193.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 187-193
    • Hottiger, T.1    De Virgilio, C.2    Hall, M.N.3    Boller, T.4    Wiemken, A.5
  • 193
    • 0028501231 scopus 로고
    • Mutational analysis of the DNA-binding domain of yeast heat shock transcription factor
    • Hubl ST, Owens JC, Nelson HC. 1994. Mutational analysis of the DNA-binding domain of yeast heat shock transcription factor. Nat. Struct. Biol. 1:615-620.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 615-620
    • Hubl, S.T.1    Owens, J.C.2    Nelson, H.C.3
  • 194
    • 0037007008 scopus 로고    scopus 로고
    • The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain
    • Hundley H, et al. 2002. The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain. Proc. Natl. Acad. Sci. U. S. A. 99:4203-4208.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4203-4208
    • Hundley, H.1
  • 195
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
    • Ihara Y, Cohen-Doyle MF, Saito Y, Williams DB. 1999. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol. Cell 4:331-341.
    • (1999) Mol. Cell , vol.4 , pp. 331-341
    • Ihara, Y.1    Cohen-Doyle, M.F.2    Saito, Y.3    Williams, D.B.4
  • 196
    • 0034458959 scopus 로고    scopus 로고
    • Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin
    • Imai J, Yahara I. 2000. Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin. Mol. Cell. Biol. 20:9262-9270.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9262-9270
    • Imai, J.1    Yahara, I.2
  • 197
    • 20444480988 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae heat shock transcription factor regulates cell wall remodeling in response to heat shock
    • Imazu H, Sakurai H. 2005. Saccharomyces cerevisiae heat shock transcription factor regulates cell wall remodeling in response to heat shock. Eukaryot. Cell 4:1050-1056.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1050-1056
    • Imazu, H.1    Sakurai, H.2
  • 198
    • 4143089556 scopus 로고    scopus 로고
    • Gle2p is essential to induce adaptation of the export of bulk poly(A)+ mRNA to heat shock in Saccharomyces cerevisiae
    • Izawa S, Takemura R, Inoue Y. 2004. Gle2p is essential to induce adaptation of the export of bulk poly(A)+ mRNA to heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 279:35469-35478.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35469-35478
    • Izawa, S.1    Takemura, R.2    Inoue, Y.3
  • 199
    • 0031884897 scopus 로고    scopus 로고
    • Genetic tailoring of N-linked oligosaccharides: The role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo
    • Jakob CA, Burda P, te Heesen S, Aebi M, Roth J. 1998. Genetic tailoring of N-linked oligosaccharides: the role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo. Glycobiology 8:155-164.
    • (1998) Glycobiology , vol.8 , pp. 155-164
    • Jakob, C.A.1    Burda, P.2    Te Heesen, S.3    Aebi, M.4    Roth, J.5
  • 200
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K, Buchner J. 1993. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268:1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 201
    • 0025965063 scopus 로고
    • A conserved heptapeptide restrains the activity of the yeast heat shock transcription factor
    • Jakobsen BK, Pelham HR. 1991. A conserved heptapeptide restrains the activity of the yeast heat shock transcription factor. EMBO J. 10:369-375.
    • (1991) EMBO J. , vol.10 , pp. 369-375
    • Jakobsen, B.K.1    Pelham, H.R.2
  • 202
    • 0031016469 scopus 로고    scopus 로고
    • Functional specificity among Hsp70 molecular chaperones
    • James P, Pfund C, Craig EA. 1997. Functional specificity among Hsp70 molecular chaperones. Science 275:387-389.
    • (1997) Science , vol.275 , pp. 387-389
    • James, P.1    Pfund, C.2    Craig, E.A.3
  • 203
    • 0035896640 scopus 로고    scopus 로고
    • Role for de novo sphingoid base biosynthesis in the heat-induced transient cell cycle arrest of Saccharomyces cerevisiae
    • Jenkins GM, Hannun YA. 2001. Role for de novo sphingoid base biosynthesis in the heat-induced transient cell cycle arrest of Saccharomyces cerevisiae. J. Biol. Chem. 276:8574-8581.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8574-8581
    • Jenkins, G.M.1    Hannun, Y.A.2
  • 204
    • 0031452645 scopus 로고    scopus 로고
    • Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae
    • Jenkins GM, et al. 1997. Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae. J. Biol. Chem. 272:32566-32572.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32566-32572
    • Jenkins, G.M.1
  • 205
    • 33646361833 scopus 로고    scopus 로고
    • The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons
    • Jermy AJ, Willer M, Davis E, Wilkinson BM, Stirling CJ. 2006. The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons. J. Biol. Chem. 281:7899-7906.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7899-7906
    • Jermy, A.J.1    Willer, M.2    Davis, E.3    Wilkinson, B.M.4    Stirling, C.J.5
  • 206
    • 35649024724 scopus 로고    scopus 로고
    • Structural basis of J cochaperone binding and regulation of Hsp70
    • Jiang J, et al. 2007. Structural basis of J cochaperone binding and regulation of Hsp70. Mol. Cell 28:422-433.
    • (2007) Mol. Cell , vol.28 , pp. 422-433
    • Jiang, J.1
  • 208
    • 84857048585 scopus 로고    scopus 로고
    • Evolution and function of diverse Hsp90 homologs and cochaperone proteins
    • Johnson JL. 2012. Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochim. Biophys. Acta 1823:607-613.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 607-613
    • Johnson, J.L.1
  • 209
    • 0035911158 scopus 로고    scopus 로고
    • An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
    • Johnson JL, Craig EA. 2001. An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J. Cell Biol. 152:851-856.
    • (2001) J. Cell Biol. , vol.152 , pp. 851-856
    • Johnson, J.L.1    Craig, E.A.2
  • 210
    • 0034005058 scopus 로고    scopus 로고
    • A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast
    • Johnson JL, Craig EA. 2000. A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast. Mol. Cell. Biol. 20:3027-3036.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3027-3036
    • Johnson, J.L.1    Craig, E.A.2
  • 211
    • 33846181647 scopus 로고    scopus 로고
    • Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1
    • Johnson JL, Halas A, Flom G. 2007. Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol. Cell. Biol. 27:768-776.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 768-776
    • Johnson, J.L.1    Halas, A.2    Flom, G.3
  • 212
    • 0032043449 scopus 로고    scopus 로고
    • Iron-sulfur proteins: New roles for old clusters
    • Johnson MK. 1998. Iron-sulfur proteins: new roles for old clusters. Curr. Opin. Chem. Biol. 2:173-181.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 173-181
    • Johnson, M.K.1
  • 213
    • 77954217233 scopus 로고    scopus 로고
    • The Hsp70 chaperone Ssa1 is essential for catabolite induced degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase
    • Juretschke J, Menssen R, Sickmann A, Wolf DH. 2010. The Hsp70 chaperone Ssa1 is essential for catabolite induced degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase. Biochem. Biophys. Res. Commun. 397:447-452.
    • (2010) Biochem. Biophys. Res. Commun. , vol.397 , pp. 447-452
    • Juretschke, J.1    Menssen, R.2    Sickmann, A.3    Wolf, D.H.4
  • 214
    • 0036275663 scopus 로고    scopus 로고
    • Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
    • Kabani M, Beckerich JM, Brodsky JL. 2002. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol. Cell. Biol. 22:4677-4689.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4677-4689
    • Kabani, M.1    Beckerich, J.M.2    Brodsky, J.L.3
  • 215
    • 0033811675 scopus 로고    scopus 로고
    • Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum
    • Kabani M, Beckerich JM, Gaillardin C. 2000. Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Mol. Cell. Biol. 20:6923-6934.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6923-6934
    • Kabani, M.1    Beckerich, J.M.2    Gaillardin, C.3
  • 216
    • 0037032470 scopus 로고    scopus 로고
    • HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor
    • Kabani M, McLellan C, Raynes DA, Guerriero V, Brodsky JL. 2002. HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett. 531:339-342.
    • (2002) FEBS Lett. , vol.531 , pp. 339-342
    • Kabani, M.1    McLellan, C.2    Raynes, D.A.3    Guerriero, V.4    Brodsky, J.L.5
  • 217
    • 55349110828 scopus 로고    scopus 로고
    • Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae
    • Kabir MA, Sherman F. 2008. Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae. FEMS Yeast Res. 8:1236-1244.
    • (2008) FEMS Yeast Res. , vol.8 , pp. 1236-1244
    • Kabir, M.A.1    Sherman, F.2
  • 218
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D, Kopito R, Frydman J. 2008. Misfolded proteins partition between two distinct quality control compartments. Nature 454:1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 219
    • 0030901433 scopus 로고    scopus 로고
    • A 77-kilodalton protein of Cryptococcus neoformans, a member of the heat shock protein 70 family, is a major antigen detected in the sera of mice with pulmonary cryptococcosis
    • Kakeya H, et al. 1997. A 77-kilodalton protein of Cryptococcus neoformans, a member of the heat shock protein 70 family, is a major antigen detected in the sera of mice with pulmonary cryptococcosis. Infect. Immun. 65:1653-1658.
    • (1997) Infect. Immun. , vol.65 , pp. 1653-1658
    • Kakeya, H.1
  • 220
    • 11944273348 scopus 로고
    • The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response
    • Kamada Y, Jung US, Piotrowski J, Levin DE. 1995. The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response. Genes Dev. 9:1559-1571.
    • (1995) Genes Dev. , vol.9 , pp. 1559-1571
    • Kamada, Y.1    Jung, U.S.2    Piotrowski, J.3    Levin, D.E.4
  • 221
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga HH, Craig EA. 2010. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11:579-592.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 222
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang PJ, et al. 1990. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348:137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1
  • 224
    • 0035907297 scopus 로고    scopus 로고
    • J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins
    • Kim R, Saxena S, Gordon DM, Pain D, Dancis A. 2001. J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins. J. Biol. Chem. 276:17524-17532.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17524-17532
    • Kim, R.1    Saxena, S.2    Gordon, D.M.3    Pain, D.4    Dancis, A.5
  • 225
    • 0032573163 scopus 로고    scopus 로고
    • Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
    • Kim S, Schilke B, Craig EA, Horwich AL. 1998. Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc. Natl. Acad. Sci. U. S. A. 95:12860-12865.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12860-12865
    • Kim, S.1    Schilke, B.2    Craig, E.A.3    Horwich, A.L.4
  • 226
    • 13744258264 scopus 로고    scopus 로고
    • Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone Ssb or Zuo1 to cations, including aminoglycosides
    • Kim SY, Craig EA. 2005. Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone Ssb or Zuo1 to cations, including aminoglycosides. Eukaryot. Cell 4:82-89.
    • (2005) Eukaryot. Cell , vol.4 , pp. 82-89
    • Kim, S.Y.1    Craig, E.A.2
  • 227
    • 0038308388 scopus 로고    scopus 로고
    • Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins
    • Kimata Y, et al. 2003. Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol. Biol. Cell 14:2559-2569.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2559-2569
    • Kimata, Y.1
  • 228
    • 2942718758 scopus 로고    scopus 로고
    • Functional differences between human and yeast protein disulfide isomerase family proteins
    • Kimura T, et al. 2004. Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem. Biophys. Res. Commun. 320:359-365.
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 359-365
    • Kimura, T.1
  • 229
    • 24744471839 scopus 로고    scopus 로고
    • Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities
    • Kimura T, et al. 2005. Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities. J. Biol. Chem. 280:31438-31441.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31438-31441
    • Kimura, T.1
  • 230
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • Knight SA, Sepuri NB, Pain D, Dancis A. 1998. Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J. Biol. Chem. 273:18389-18393.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 231
    • 0025151966 scopus 로고
    • Evidence for a heat shock transcription factor-independent mechanism for heat shock induction of transcription in Saccharomyces cerevisiae
    • Kobayashi N, McEntee K. 1990. Evidence for a heat shock transcription factor-independent mechanism for heat shock induction of transcription in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 87:6550-6554.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 6550-6554
    • Kobayashi, N.1    McEntee, K.2
  • 232
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno K, Normington K, Sambrook J, Gething MJ, Mori K. 1993. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell. Biol. 13:877-890.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething, M.J.4    Mori, K.5
  • 233
    • 1442335996 scopus 로고    scopus 로고
    • The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase
    • Kozany C, Mokranjac D, Sichting M, Neupert W, Hell K. 2004. The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase. Nat. Struct. Mol. Biol. 11:234-241.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 234-241
    • Kozany, C.1    Mokranjac, D.2    Sichting, M.3    Neupert, W.4    Hell, K.5
  • 234
    • 2942519292 scopus 로고    scopus 로고
    • Functional dissection of Escherichia coli trigger factor: Unraveling the function of individual domains
    • Kramer G, et al. 2004. Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains. J. Bacteriol. 186:3777-3784.
    • (2004) J. Bacteriol. , vol.186 , pp. 3777-3784
    • Kramer, G.1
  • 235
    • 0035951385 scopus 로고    scopus 로고
    • Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
    • Krzewska J, Langer T, Liberek K. 2001. Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett. 489:92-96.
    • (2001) FEBS Lett. , vol.489 , pp. 92-96
    • Krzewska, J.1    Langer, T.2    Liberek, K.3
  • 236
    • 0028153098 scopus 로고
    • Isolation and characterization of cDNA and genomic promoter region for a heat shock protein 30 from Aspergillus nidulans
    • Kusakabe T, Koga K, Sugimoto Y. 1994. Isolation and characterization of cDNA and genomic promoter region for a heat shock protein 30 from Aspergillus nidulans. Biochim. Biophys. Acta 1219:555-558.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 555-558
    • Kusakabe, T.1    Koga, K.2    Sugimoto, Y.3
  • 237
    • 77958121046 scopus 로고    scopus 로고
    • PKC signaling regulates drug resistance of the fungal pathogen Candida albicans via circuitry comprised of Mkc1, calcineurin, and Hsp90
    • LaFayette SL, et al. 2010. PKC signaling regulates drug resistance of the fungal pathogen Candida albicans via circuitry comprised of Mkc1, calcineurin, and Hsp90. PLoS Pathog. 6:e1001069.
    • (2010) PLoS Pathog. , vol.6
    • LaFayette, S.L.1
  • 238
    • 0028356858 scopus 로고
    • A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation
    • Laloraya S, Gambill BD, Craig EA. 1994. A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation. Proc. Natl. Acad. Sci. U. S. A. 91:6481-6485.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 6481-6485
    • Laloraya, S.1    Gambill, B.D.2    Craig, E.A.3
  • 239
    • 3042595446 scopus 로고    scopus 로고
    • A novel mode of chaperone action: Heme activation of HapI by enhanced association of Hsp90 with the repressed Hsp70-HapI complex
    • Lan C, Lee HC, Tang S, Zhang L. 2004. A novel mode of chaperone action: heme activation of HapI by enhanced association of Hsp90 with the repressed Hsp70-HapI complex. J. Biol. Chem. 279:27607-27612.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27607-27612
    • Lan, C.1    Lee, H.C.2    Tang, S.3    Zhang, L.4
  • 240
    • 0029093517 scopus 로고
    • Molecular cloning and expression of a 70-kilodalton heat shock protein of Candida albicans
    • La Valle R, et al. 1995. Molecular cloning and expression of a 70-kilodalton heat shock protein of Candida albicans. Infect. Immun. 63:4039-4045.
    • (1995) Infect. Immun. , vol.63 , pp. 4039-4045
    • La Valle, R.1
  • 241
    • 0031891726 scopus 로고    scopus 로고
    • Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway
    • Lawson B, Brewer JW, Hendershot LM. 1998. Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway. J. Cell. Physiol. 174:170-178.
    • (1998) J. Cell. Physiol. , vol.174 , pp. 170-178
    • Lawson, B.1    Brewer, J.W.2    Hendershot, L.M.3
  • 242
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae
    • Lee DH, Goldberg AL. 1996. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae. J. Biol. Chem. 271:27280-27284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 243
    • 54249109491 scopus 로고    scopus 로고
    • Yeast Yak1 kinase, a bridge between PKA and stress-responsive transcription factors, Hsf1 and Msn2/Msn4
    • Lee P, Cho BR, Joo HS, Hahn JS. 2008. Yeast Yak1 kinase, a bridge between PKA and stress-responsive transcription factors, Hsf1 and Msn2/Msn4. Mol. Microbiol. 70:882-895.
    • (2008) Mol. Microbiol. , vol.70 , pp. 882-895
    • Lee, P.1    Cho, B.R.2    Joo, H.S.3    Hahn, J.S.4
  • 244
    • 78751699051 scopus 로고    scopus 로고
    • Regulation of yeast Yak1 kinase by PKA and autophosphorylation-dependent 14-3-3 binding
    • Lee P, Paik SM, Shin CS, Huh WK, Hahn JS. 2011. Regulation of yeast Yak1 kinase by PKA and autophosphorylation-dependent 14-3-3 binding. Mol. Microbiol. 79:633-646.
    • (2011) Mol. Microbiol. , vol.79 , pp. 633-646
    • Lee, P.1    Paik, S.M.2    Shin, C.S.3    Huh, W.K.4    Hahn, J.S.5
  • 245
    • 0037164751 scopus 로고    scopus 로고
    • The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability
    • Lee P, et al. 2002. The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. J. Cell Biol. 159:1051-1059.
    • (2002) J. Cell Biol. , vol.159 , pp. 1051-1059
    • Lee, P.1
  • 246
    • 0034108630 scopus 로고    scopus 로고
    • The yeast heat shock transcription factor changes conformation in response to superoxide and temperature
    • Lee S, et al. 2000. The yeast heat shock transcription factor changes conformation in response to superoxide and temperature. Mol. Biol. Cell 11:1753-1764.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1753-1764
    • Lee, S.1
  • 247
    • 77952353727 scopus 로고    scopus 로고
    • CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
    • Lee S, Sielaff B, Lee J, Tsai FT. 2010. CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc. Natl. Acad. Sci. U. S. A. 107:8135-8140.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 8135-8140
    • Lee, S.1    Sielaff, B.2    Lee, J.3    Tsai, F.T.4
  • 248
    • 19944399062 scopus 로고    scopus 로고
    • The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation - Via a newly identified Glc7/Bud14 type I protein phosphatase module - and TFIID promoter distribution
    • Lenssen E, et al. 2005. The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation - via a newly identified Glc7/Bud14 type I protein phosphatase module - and TFIID promoter distribution. Mol. Cell. Biol. 25:488-498.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 488-498
    • Lenssen, E.1
  • 249
    • 0027445711 scopus 로고
    • HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases
    • Leonhardt SA, Fearson K, Danese PN, Mason TL. 1993. HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol. Cell. Biol. 13:6304-6313.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6304-6313
    • Leonhardt, S.A.1    Fearson, K.2    Danese, P.N.3    Mason, T.L.4
  • 250
    • 20544432791 scopus 로고    scopus 로고
    • Cell wall integrity signaling in Saccharomyces cerevisiae
    • Levin DE. 2005. Cell wall integrity signaling in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 69:262-291.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 262-291
    • Levin, D.E.1
  • 251
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • Levine RL. 2002. Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic. Biol. Med. 32:790-796.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 790-796
    • Levine, R.L.1
  • 252
    • 0029126927 scopus 로고
    • Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators
    • Levy EJ, McCarty J, Bukau B, Chirico WJ. 1995. Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators. FEBS Lett. 368:435-440.
    • (1995) FEBS Lett. , vol.368 , pp. 435-440
    • Levy, E.J.1    McCarty, J.2    Bukau, B.3    Chirico, W.J.4
  • 253
    • 78650983812 scopus 로고    scopus 로고
    • Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle
    • Li J, Richter K, Buchner J. 2011. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat. Struct. Mol. Biol. 18:61-66.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 61-66
    • Li, J.1    Richter, K.2    Buchner, J.3
  • 254
    • 0042208078 scopus 로고    scopus 로고
    • Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5
    • Li XS, Reddy MS, Baev D, Edgerton M. 2003. Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. J. Biol. Chem. 278:28553-28561.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28553-28561
    • Li, X.S.1    Reddy, M.S.2    Baev, D.3    Edgerton, M.4
  • 255
    • 33747331132 scopus 로고    scopus 로고
    • Candida albicans cell wall Ssa proteins bind and facilitate import of salivary histatin 5 required for toxicity
    • Li XS, Sun JN, Okamoto-Shibayama K, Edgerton M. 2006. Candida albicans cell wall Ssa proteins bind and facilitate import of salivary histatin 5 required for toxicity. J. Biol. Chem. 281:22453-22463.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22453-22463
    • Li, X.S.1    Sun, J.N.2    Okamoto-Shibayama, K.3    Edgerton, M.4
  • 256
    • 4444315535 scopus 로고    scopus 로고
    • The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18
    • Li Y, et al. 2004. The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18. J. Biol. Chem. 279:38047-38054.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38047-38054
    • Li, Y.1
  • 257
    • 0019325433 scopus 로고
    • Varying patterns of protein synthesis in Drosophila during heat shock: Implications for regulation
    • Lindquist S. 1980. Varying patterns of protein synthesis in Drosophila during heat shock: implications for regulation. Dev. Biol. 77:463-479.
    • (1980) Dev. Biol. , vol.77 , pp. 463-479
    • Lindquist, S.1
  • 258
    • 0029950703 scopus 로고    scopus 로고
    • Heat-shock protein 104 expression is sufficient for thermotolerance in yeast
    • Lindquist S, Kim G. 1996. Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc. Natl. Acad. Sci. U. S. A. 93:5301-5306.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5301-5306
    • Lindquist, S.1    Kim, G.2
  • 259
    • 0032936785 scopus 로고    scopus 로고
    • A new use for the 'wing' of the 'winged'helix-turn-helix motif in the HSF-DNA cocrystal
    • Littlefield O, Nelson HC. 1999. A new use for the 'wing' of the 'winged'helix-turn-helix motif in the HSF-DNA cocrystal. Nat. Struct. Mol. Biol. 6:464-470.
    • (1999) Nat. Struct. Mol. Biol. , vol.6 , pp. 464-470
    • Littlefield, O.1    Nelson, H.C.2
  • 260
    • 81855218130 scopus 로고    scopus 로고
    • Segregation of protein aggregates involves actin and the polarity machinery
    • Liu B, et al. 2011. Segregation of protein aggregates involves actin and the polarity machinery. Cell 147:959-961.
    • (2011) Cell , vol.147 , pp. 959-961
    • Liu, B.1
  • 261
    • 0035794158 scopus 로고    scopus 로고
    • Mitochondrial Hsp70 Ssc1: Role in protein folding
    • Liu Q, Krzewska J, Liberek K, Craig EA. 2001. Mitochondrial Hsp70 Ssc1: role in protein folding. J. Biol. Chem. 276:6112-6118.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6112-6118
    • Liu, Q.1    Krzewska, J.2    Liberek, K.3    Craig, E.A.4
  • 262
    • 0029664413 scopus 로고    scopus 로고
    • Oxidative stress induced heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription
    • Liu XD, Thiele DJ. 1996. Oxidative stress induced heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription. Genes Dev. 10:592-603.
    • (1996) Genes Dev. , vol.10 , pp. 592-603
    • Liu, X.D.1    Thiele, D.J.2
  • 263
    • 0033578875 scopus 로고    scopus 로고
    • The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone
    • Liu XD, Morano KA, Thiele DJ. 1999. The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. J. Biol. Chem. 274:26654-26660.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26654-26660
    • Liu, X.D.1    Morano, K.A.2    Thiele, D.J.3
  • 264
    • 84862556771 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 265
    • 33845656956 scopus 로고    scopus 로고
    • Mitochondrial retrograde signaling
    • Liu Z, Butow RA. 2006. Mitochondrial retrograde signaling. Annu. Rev. Genet. 40:159-185.
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 159-185
    • Liu, Z.1    Butow, R.A.2
  • 266
    • 0032962417 scopus 로고    scopus 로고
    • SSB, encoding a ribosome-associated chaperone, is coordinately regulated with ribosomal protein genes
    • Lopez N, Halladay J, Walter W, Craig EA. 1999. SSB, encoding a ribosome-associated chaperone, is coordinately regulated with ribosomal protein genes. J. Bacteriol. 181:3136-3143.
    • (1999) J. Bacteriol. , vol.181 , pp. 3136-3143
    • Lopez, N.1    Halladay, J.2    Walter, W.3    Craig, E.A.4
  • 267
    • 0030035771 scopus 로고    scopus 로고
    • Evidence for presence in the cell wall of Candida albicans of a protein related to the hsp70 family
    • Lopez-Ribot JL, Alloush HM, Masten BJ, Chaffin WL. 1996. Evidence for presence in the cell wall of Candida albicans of a protein related to the hsp70 family. Infect. Immun. 64:3333-3340.
    • (1996) Infect. Immun. , vol.64 , pp. 3333-3340
    • Lopez-Ribot, J.L.1    Alloush, H.M.2    Masten, B.J.3    Chaffin, W.L.4
  • 268
    • 0031795189 scopus 로고    scopus 로고
    • Hsp90 is required for pheromone signaling in yeast
    • Louvion JF, Abbas-Terki T, Picard D. 1998. Hsp90 is required for pheromone signaling in yeast. Mol. Biol. Cell 9:3071-3083.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3071-3083
    • Louvion, J.F.1    Abbas-Terki, T.2    Picard, D.3
  • 269
    • 57649187079 scopus 로고    scopus 로고
    • Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding
    • Lum R, Niggemann M, Glover JR. 2008. Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J. Biol. Chem. 283:30139-30150.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30139-30150
    • Lum, R.1    Niggemann, M.2    Glover, J.R.3
  • 270
    • 15444360108 scopus 로고    scopus 로고
    • Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae
    • Lussier M, et al. 1997. Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae. Genetics 147:435-450.
    • (1997) Genetics , vol.147 , pp. 435-450
    • Lussier, M.1
  • 271
    • 0035970292 scopus 로고    scopus 로고
    • The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
    • Lutz T, Westermann B, Neupert W, Herrmann JM. 2001. The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J. Mol. Biol. 307:815-825.
    • (2001) J. Mol. Biol. , vol.307 , pp. 815-825
    • Lutz, T.1    Westermann, B.2    Neupert, W.3    Herrmann, J.M.4
  • 272
    • 0025972887 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase
    • Lyles MM, Gilbert HF. 1991. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase. Biochemistry 30:619-625.
    • (1991) Biochemistry , vol.30 , pp. 619-625
    • Lyles, M.M.1    Gilbert, H.F.2
  • 273
    • 0028809495 scopus 로고
    • Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae
    • Lyman SK, Schekman R. 1995. Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae. J. Cell Biol. 131:1163-1171.
    • (1995) J. Cell Biol. , vol.131 , pp. 1163-1171
    • Lyman, S.K.1    Schekman, R.2
  • 274
    • 39649122369 scopus 로고    scopus 로고
    • The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly
    • Mackay RG, Helsen CW, Tkach JM, Glover JR. 2008. The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly. Biochemistry 47:1918-1927.
    • (2008) Biochemistry , vol.47 , pp. 1918-1927
    • Mackay, R.G.1    Helsen, C.W.2    Tkach, J.M.3    Glover, J.R.4
  • 275
    • 79953222615 scopus 로고    scopus 로고
    • The Yak1 protein kinase lies at the center of a regulatory cascade affecting adhesive growth and stress resistance in Saccharomyces cerevisiae
    • Malcher M, Schladebeck S, Mosch HU. 2011. The Yak1 protein kinase lies at the center of a regulatory cascade affecting adhesive growth and stress resistance in Saccharomyces cerevisiae. Genetics 187:717-730.
    • (2011) Genetics , vol.187 , pp. 717-730
    • Malcher, M.1    Schladebeck, S.2    Mosch, H.U.3
  • 276
    • 77951754467 scopus 로고    scopus 로고
    • Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system
    • Mandal AK, et al. 2010. Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol. Biol. Cell 21:1439-1448.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1439-1448
    • Mandal, A.K.1
  • 277
    • 33846588436 scopus 로고    scopus 로고
    • Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote post-translational maturation
    • Mandal AK, et al. 2007. Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote post-translational maturation. J. Cell Biol. 176:319-328.
    • (2007) J. Cell Biol. , vol.176 , pp. 319-328
    • Mandal, A.K.1
  • 278
    • 0031009877 scopus 로고    scopus 로고
    • Molecular cloning of a Candida albicans gene (SSB1) coding for a protein related to the Hsp70 family
    • Maneu V, Cervera AM, Martinez JP, Gozalbo D. 1997. Molecular cloning of a Candida albicans gene (SSB1) coding for a protein related to the Hsp70 family. Yeast 13:677-681.
    • (1997) Yeast , vol.13 , pp. 677-681
    • Maneu, V.1    Cervera, A.M.2    Martinez, J.P.3    Gozalbo, D.4
  • 279
    • 0033694951 scopus 로고    scopus 로고
    • Complementation of Saccharomyces cerevisiae mutations in genes involved in translation and protein folding (EFB1 and SSB1) with Candida albicans cloned genes
    • Maneu V, Roig P, Gozalbo D. 2000. Complementation of Saccharomyces cerevisiae mutations in genes involved in translation and protein folding (EFB1 and SSB1) with Candida albicans cloned genes. Res. Microbiol. 151:739-746.
    • (2000) Res. Microbiol. , vol.151 , pp. 739-746
    • Maneu, V.1    Roig, P.2    Gozalbo, D.3
  • 280
    • 0027433380 scopus 로고
    • Activity of the yeast MAP kinase homologue Slt2 is critically required for cell integrity at 37°C
    • Martin H, Arroyo J, Sanchez M, Molina M, Nombela C. 1993. Activity of the yeast MAP kinase homologue Slt2 is critically required for cell integrity at 37°C. Mol. Gen. Genet. 241:177-184.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 177-184
    • Martin, H.1    Arroyo, J.2    Sanchez, M.3    Molina, M.4    Nombela, C.5
  • 281
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Δpsi drives the movement of presequences
    • Martin J, Mahlke K, Pfanner N. 1991. Role of an energized inner membrane in mitochondrial protein import. Δpsi drives the movement of presequences. J. Biol. Chem. 266:18051-18057.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 282
    • 0029879360 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress response element (STRE)
    • Martinez-Pastor MT, et al. 1996. The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress response element (STRE). EMBO J. 15:2227-2235.
    • (1996) EMBO J. , vol.15 , pp. 2227-2235
    • Martinez-Pastor, M.T.1
  • 283
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack KES, Misselwitz B, Plath K, Rapoport TA. 1999. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97:553-564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.S.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 284
    • 27644455770 scopus 로고    scopus 로고
    • The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae
    • Matsumoto R, Akama K, Rakwal R, Iwahashi H. 2005. The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae. BMC Genomics 6:141.
    • (2005) BMC Genomics , vol.6 , pp. 141
    • Matsumoto, R.1    Akama, K.2    Rakwal, R.3    Iwahashi, H.4
  • 285
    • 0037144584 scopus 로고    scopus 로고
    • Convergence of the target of rapamycin and the Snf1 protein kinase pathways in the regulation of the subcellular localization of Msn2, a transcriptional activator of STRE (stress response element)-regulated genes
    • Mayordomo I, Estruch F, Sanz P. 2002. Convergence of the target of rapamycin and the Snf1 protein kinase pathways in the regulation of the subcellular localization of Msn2, a transcriptional activator of STRE (stress response element)-regulated genes. J. Biol. Chem. 277:35650-35656.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35650-35656
    • Mayordomo, I.1    Estruch, F.2    Sanz, P.3
  • 286
    • 0033785942 scopus 로고    scopus 로고
    • Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum
    • McClellan AJ, Brodsky JL. 2000. Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum. Genetics 156:501-512.
    • (2000) Genetics , vol.156 , pp. 501-512
    • McClellan, A.J.1    Brodsky, J.L.2
  • 287
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • McClellan AJ, et al. 2007. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 131:121-135.
    • (2007) Cell , vol.131 , pp. 121-135
    • McClellan, A.J.1
  • 288
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • McCracken AA, Brodsky JL. 1996. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132:291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 289
    • 33644851220 scopus 로고    scopus 로고
    • Sphingoid base is required for translation initiation during heat stress in Saccharomyces cerevisiae
    • Meier KD, Deloche O, Kajiwara K, Funato K, Riezman H. 2006. Sphingoid base is required for translation initiation during heat stress in Saccharomyces cerevisiae. Mol. Biol. Cell 17:1164-1175.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1164-1175
    • Meier, K.D.1    Deloche, O.2    Kajiwara, K.3    Funato, K.4    Riezman, H.5
  • 290
    • 0037404423 scopus 로고    scopus 로고
    • The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
    • Melville MW, McClellan AJ, Meyer AS, Darveau A, Frydman J. 2003. The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex. Mol. Cell. Biol. 23:3141-3151.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3141-3151
    • Melville, M.W.1    McClellan, A.J.2    Meyer, A.S.3    Darveau, A.4    Frydman, J.5
  • 292
    • 10744221887 scopus 로고    scopus 로고
    • Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
    • Meyer P, et al. 2004. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 23:1402-1410.
    • (2004) EMBO J. , vol.23 , pp. 1402-1410
    • Meyer, P.1
  • 293
    • 0031556950 scopus 로고    scopus 로고
    • Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
    • Miao B, Davis JE, Craig EA. 1997. Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae. J. Mol. Biol. 265:541-552.
    • (1997) J. Mol. Biol. , vol.265 , pp. 541-552
    • Miao, B.1    Davis, J.E.2    Craig, E.A.3
  • 294
    • 0025997535 scopus 로고
    • The intron-containing hsp82 gene of the dimorphic pathogenic fungus Histoplasma capsulatum is properly spliced in severe heat shock conditions
    • Minchiotti G, Gargano S, Maresca B. 1991. The intron-containing hsp82 gene of the dimorphic pathogenic fungus Histoplasma capsulatum is properly spliced in severe heat shock conditions. Mol. Cell. Biol. 11:5624-5630.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5624-5630
    • Minchiotti, G.1    Gargano, S.2    Maresca, B.3
  • 295
    • 0026582040 scopus 로고
    • Molecular cloning and expression of hsp82 gene of the dimorphic pathogenic fungus Histoplasma capsulatum
    • Minchiotti G, Gargano S, Maresca B. 1992. Molecular cloning and expression of hsp82 gene of the dimorphic pathogenic fungus Histoplasma capsulatum. Biochim. Biophys. Acta 1131:103-107.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 103-107
    • Minchiotti, G.1    Gargano, S.2    Maresca, B.3
  • 296
    • 58149464713 scopus 로고    scopus 로고
    • Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae
    • Mir SS, Fiedler D, Cashikar AG. 2009. Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae. Mol. Cell. Biol. 29:187-200.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 187-200
    • Mir, S.S.1    Fiedler, D.2    Cashikar, A.G.3
  • 297
    • 0025244292 scopus 로고
    • Purification and characterization of yeast protein disulfide isomerase
    • Mizunaga T, Katakura Y, Miura T, Maruyama Y. 1990. Purification and characterization of yeast protein disulfide isomerase. J. Biochem. 108:846-851.
    • (1990) J. Biochem. , vol.108 , pp. 846-851
    • Mizunaga, T.1    Katakura, Y.2    Miura, T.3    Maruyama, Y.4
  • 298
    • 0029583429 scopus 로고
    • The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function
    • Moczko M, Schonfisch B, Voos W, Pfanner N, Rassow J. 1995. The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J. Mol. Biol. 254:538-543.
    • (1995) J. Mol. Biol. , vol.254 , pp. 538-543
    • Moczko, M.1    Schonfisch, B.2    Voos, W.3    Pfanner, N.4    Rassow, J.5
  • 299
    • 33749360278 scopus 로고    scopus 로고
    • Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor
    • Mokranjac D, Bourenkov G, Hell K, Neupert W, Groll M. 2006. Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor. EMBO J. 25:4675-4685.
    • (2006) EMBO J. , vol.25 , pp. 4675-4685
    • Mokranjac, D.1    Bourenkov, G.2    Hell, K.3    Neupert, W.4    Groll, M.5
  • 300
    • 0141865519 scopus 로고    scopus 로고
    • Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria
    • Mokranjac D, Sichting M, Neupert W, Hell K. 2003. Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria. EMBO J. 22:4945-4956.
    • (2003) EMBO J. , vol.22 , pp. 4945-4956
    • Mokranjac, D.1    Sichting, M.2    Neupert, W.3    Hell, K.4
  • 301
    • 24744446437 scopus 로고    scopus 로고
    • The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2
    • Mokranjac D, et al. 2005. The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2. J. Biol. Chem. 280:31608-31614.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31608-31614
    • Mokranjac, D.1
  • 302
    • 84857044092 scopus 로고    scopus 로고
    • Post-translational modifications of Hsp90 and their contributions to chaperone regulation
    • Mollapour M, Neckers L. 2012. Post-translational modifications of Hsp90 and their contributions to chaperone regulation. Biochim. Biophys. Acta 1823:648-655.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 648-655
    • Mollapour, M.1    Neckers, L.2
  • 303
    • 0032931842 scopus 로고    scopus 로고
    • A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress
    • Morano KA, Santoro N, Kock KA, Thiele DJ. 1999. A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress. Mol. Cell. Biol. 19:402-411.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 402-411
    • Morano, K.A.1    Santoro, N.2    Kock, K.A.3    Thiele, D.J.4
  • 304
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori K, et al. 1992. A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J. 11:2583-2593.
    • (1992) EMBO J. , vol.11 , pp. 2583-2593
    • Mori, K.1
  • 305
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto RI. 2008. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22:1427-1438.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 306
    • 0025039721 scopus 로고
    • A subunit of yeast site-specific endonuclease SceI is a mitochondrial version of the 70-kDa heat shock protein
    • Morishima N, Nakagawa K, Yamamoto E, Shibata T. 1990. A subunit of yeast site-specific endonuclease SceI is a mitochondrial version of the 70-kDa heat shock protein. J. Biol. Chem. 265:15189-15197.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15189-15197
    • Morishima, N.1    Nakagawa, K.2    Yamamoto, E.3    Shibata, T.4
  • 307
    • 0036510606 scopus 로고    scopus 로고
    • Mitochondrial protein import: Molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44
    • Moro F, Okamoto K, Donzeau M, Neupert W, Brunner M. 2002. Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44. J. Biol. Chem. 277:6874-6880.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6874-6880
    • Moro, F.1    Okamoto, K.2    Donzeau, M.3    Neupert, W.4    Brunner, M.5
  • 308
    • 1242292279 scopus 로고    scopus 로고
    • LEA (late embryonic abundant)-like protein Hsp 12 (heat-shock protein 12) is present in the cell wall and enhances the barotolerance of the yeast Saccharomyces cerevisiae
    • Motshwene P, Karreman R, Kgari G, Brandt W, Lindsey G. 2004. LEA (late embryonic abundant)-like protein Hsp 12 (heat-shock protein 12) is present in the cell wall and enhances the barotolerance of the yeast Saccharomyces cerevisiae. Biochem. J. 377:769-774.
    • (2004) Biochem. J. , vol.377 , pp. 769-774
    • Motshwene, P.1    Karreman, R.2    Kgari, G.3    Brandt, W.4    Lindsey, G.5
  • 309
    • 0027445375 scopus 로고
    • Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family
    • Mukai H, et al. 1993. Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family. Gene 132:57-66.
    • (1993) Gene , vol.132 , pp. 57-66
    • Mukai, H.1
  • 310
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan DF, Vos MH, Lindquist S. 1997. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc. Natl. Acad. Sci. U. S. A. 94:12949-12956.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 311
    • 70350159136 scopus 로고    scopus 로고
    • Enhancer of decapping proteins 1 and 2 are important for translation during heat stress in Saccharomyces cerevisiae
    • Neef DW, Thiele DJ. 2009. Enhancer of decapping proteins 1 and 2 are important for translation during heat stress in Saccharomyces cerevisiae. Mol. Microbiol. 73:1032-1042.
    • (2009) Mol. Microbiol. , vol.73 , pp. 1032-1042
    • Neef, D.W.1    Thiele, D.J.2
  • 312
    • 75749136948 scopus 로고    scopus 로고
    • Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease
    • Neef DW, Turski ML, Thiele DJ. 2010. Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol. 8:e1000291.
    • (2010) PLoS Biol. , vol.8
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 313
    • 0026645052 scopus 로고
    • Isolation and characterization of extragenic suppressors of mutations in the SSA hsp70 genes of Saccharomyces cerevisiae
    • Nelson RJ, Heschl MF, Craig EA. 1992. Isolation and characterization of extragenic suppressors of mutations in the SSA hsp70 genes of Saccharomyces cerevisiae. Genetics 131:277-285.
    • (1992) Genetics , vol.131 , pp. 277-285
    • Nelson, R.J.1    Heschl, M.F.2    Craig, E.A.3
  • 314
    • 0026649409 scopus 로고
    • The translation machinery and 70 kd heat shock protein cooperate in protein synthesis
    • Nelson RJ, Ziegelhoffer T, Nicolet C, Werner-Washburne M, Craig EA. 1992. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71:97-105.
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 315
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. 1997. Protein import into mitochondria. Annu. Rev. Biochem. 66:863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 316
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO. 1999. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19:1325-1333.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1325-1333
    • Newnam, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 317
    • 0034632033 scopus 로고    scopus 로고
    • The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control
    • Ng DT, Spear ED, Walter P. 2000. The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J. Cell Biol. 150:77-88.
    • (2000) J. Cell Biol. , vol.150 , pp. 77-88
    • Ng, D.T.1    Spear, E.D.2    Walter, P.3
  • 318
    • 70449568487 scopus 로고    scopus 로고
    • Role of the heat shock transcription factor, Hsf1, in a major fungal pathogen that is obligately associated with warm-blooded animals
    • Nicholls S, Leach MD, Priest CL, Brown AJ. 2009. Role of the heat shock transcription factor, Hsf1, in a major fungal pathogen that is obligately associated with warm-blooded animals. Mol. Microbiol. 74:844-861.
    • (2009) Mol. Microbiol. , vol.74 , pp. 844-861
    • Nicholls, S.1    Leach, M.D.2    Priest, C.L.3    Brown, A.J.4
  • 319
    • 78751627330 scopus 로고    scopus 로고
    • Activation of the heat shock transcription factor Hsf1 is essential for the full virulence of the fungal pathogen Candida albicans
    • Nicholls S, et al. 2011. Activation of the heat shock transcription factor Hsf1 is essential for the full virulence of the fungal pathogen Candida albicans. Fungal Genet. Biol. 48:297-305.
    • (2011) Fungal Genet. Biol. , vol.48 , pp. 297-305
    • Nicholls, S.1
  • 320
    • 0025122831 scopus 로고
    • The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions
    • Nieto-Sotelo J, Wiederrecht G, Okuda A, Parker CS. 1990. The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions. Cell 62:807-817.
    • (1990) Cell , vol.62 , pp. 807-817
    • Nieto-Sotelo, J.1    Wiederrecht, G.2    Okuda, A.3    Parker, C.S.4
  • 321
    • 77954196466 scopus 로고    scopus 로고
    • Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins
    • Nillegoda NB, et al. 2010. Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol. Biol. Cell 21:2102-2116.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2102-2116
    • Nillegoda, N.B.1
  • 322
    • 0030949349 scopus 로고    scopus 로고
    • The yeast Jem1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion
    • Nishikawa S, Endo T. 1997. The yeast Jem1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion. J. Biol. Chem. 272:12889-12892.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12889-12892
    • Nishikawa, S.1    Endo, T.2
  • 323
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • Nishikawa SI, Fewell SW, Kato Y, Brodsky JL, Endo T. 2001. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J. Cell Biol. 153:1061-1070.
    • (2001) J. Cell Biol. , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 324
    • 0035972295 scopus 로고    scopus 로고
    • Functional differences in yeast protein disulfide isomerases
    • Norgaard P, et al. 2001. Functional differences in yeast protein disulfide isomerases. J. Cell Biol. 152:553-562.
    • (2001) J. Cell Biol. , vol.152 , pp. 553-562
    • Norgaard, P.1
  • 325
    • 0024395160 scopus 로고
    • S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington K, Kohno K, Kozutsumi Y, Gething MJ, Sambrook J. 1989. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57:1223-1236.
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.5
  • 326
    • 0030590848 scopus 로고    scopus 로고
    • The heat shock factor and mitochondrial Hsp70 are necessary for survival of heat shock in Saccharomyces cerevisiae
    • Nwaka S, Mechler B, von Ahsen O, Holzer H. 1996. The heat shock factor and mitochondrial Hsp70 are necessary for survival of heat shock in Saccharomyces cerevisiae. FEBS Lett. 399:259-263.
    • (1996) FEBS Lett. , vol.399 , pp. 259-263
    • Nwaka, S.1    Mechler, B.2    Von Ahsen, O.3    Holzer, H.4
  • 327
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann J, Horwich AL, Neupert W, Hartl FU. 1989. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341:125-130.
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.U.4
  • 328
    • 84055211709 scopus 로고    scopus 로고
    • Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor
    • Pais JE, Schilke B, Craig EA. 2011. Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor. Mol. Biol. Cell 22:4740-4749.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4740-4749
    • Pais, J.E.1    Schilke, B.2    Craig, E.A.3
  • 329
    • 0036931438 scopus 로고    scopus 로고
    • Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone Aha1
    • Panaretou B, et al. 2002. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone Aha1. Mol. Cell 10:1307-1318.
    • (2002) Mol. Cell , vol.10 , pp. 1307-1318
    • Panaretou, B.1
  • 330
    • 79956328648 scopus 로고    scopus 로고
    • Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae
    • Pareek G, Samaddar M, D'Silva P. 2011. Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae. J. Biol. Chem. 286:19001-19013.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19001-19013
    • Pareek, G.1    Samaddar, M.2    D'Silva, P.3
  • 331
    • 0021068221 scopus 로고
    • Saccharomyces cerevisiae: Heat and gluculase sensitivities of starved cells
    • Paris S, Pringle JR. 1983. Saccharomyces cerevisiae: heat and gluculase sensitivities of starved cells. Ann. Microbiol. 134B:379-385.
    • (1983) Ann. Microbiol. 134B , pp. 379-385
    • Paris, S.1    Pringle, J.R.2
  • 332
    • 33846107847 scopus 로고    scopus 로고
    • The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system
    • Park SH, et al. 2007. The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. Mol. Biol. Cell 18:153-165.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 153-165
    • Park, S.H.1
  • 333
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R, Sheth U. 2007. P bodies and the control of mRNA translation and degradation. Mol. Cell 25:635-646.
    • (2007) Mol. Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 334
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus
    • Parlati F, Dominguez M, Bergeron JJM, Thomas DY. 1995. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J. Biol. Chem. 270:244-253.
    • (1995) J. Biol. Chem. , vol.270 , pp. 244-253
    • Parlati, F.1    Dominguez, M.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 335
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, Kowal AS, Singer MA, Lindquist S. 1994. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 336
    • 33947408308 scopus 로고    scopus 로고
    • The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state
    • Pattaramanon N, Sangha N, Gafni A. 2007. The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state. Biochemistry 46:3405-3415.
    • (2007) Biochemistry , vol.46 , pp. 3405-3415
    • Pattaramanon, N.1    Sangha, N.2    Gafni, A.3
  • 337
    • 77953021149 scopus 로고    scopus 로고
    • The ribosome-bound Hsp70 homolog Ssb of Saccharomyces cerevisiae
    • Peisker K, Chiabudini M, Rospert S. 2010. The ribosome-bound Hsp70 homolog Ssb of Saccharomyces cerevisiae. Biochim. Biophys. Acta 1803:662-672.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 662-672
    • Peisker, K.1    Chiabudini, M.2    Rospert, S.3
  • 338
    • 0024850646 scopus 로고
    • Stable binding of Drosophila heat shock factor to head-to-head and tail-to-tail repeats of a conserved 5 bp recognition unit
    • Perisic O, Xiao H, Lis JT. 1989. Stable binding of Drosophila heat shock factor to head-to-head and tail-to-tail repeats of a conserved 5 bp recognition unit. Cell 59:797-806.
    • (1989) Cell , vol.59 , pp. 797-806
    • Perisic, O.1    Xiao, H.2    Lis, J.T.3
  • 339
    • 0026621935 scopus 로고
    • Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil
    • Peteranderl R, Nelson HC. 1992. Trimerization of the heat shock transcription factor by a triple-stranded alpha-helical coiled-coil. Biochemistry 31:12272-12276.
    • (1992) Biochemistry , vol.31 , pp. 12272-12276
    • Peteranderl, R.1    Nelson, H.C.2
  • 340
    • 0033596861 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of the trimerization domain from the heat shock transcription factor
    • Peteranderl R, et al. 1999. Biochemical and biophysical characterization of the trimerization domain from the heat shock transcription factor. Biochemistry 38:3559-3569.
    • (1999) Biochemistry , vol.38 , pp. 3559-3569
    • Peteranderl, R.1
  • 341
    • 0023649577 scopus 로고
    • Yeast HAP1 activator competes with the factor RC2 for binding to the upstream activation site UAS1 of the CYC1 gene
    • Pfeifer K, Arcangioli B, Guarente L. 1987. Yeast HAP1 activator competes with the factor RC2 for binding to the upstream activation site UAS1 of the CYC1 gene. Cell 49:9-18.
    • (1987) Cell , vol.49 , pp. 9-18
    • Pfeifer, K.1    Arcangioli, B.2    Guarente, L.3
  • 342
    • 0035658334 scopus 로고    scopus 로고
    • Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s
    • Pfund C, Huang P, Lopez-Hoyo N, Craig EA. 2001. Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s. Mol. Biol. Cell 12:3773-3782.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3773-3782
    • Pfund, C.1    Huang, P.2    Lopez-Hoyo, N.3    Craig, E.A.4
  • 343
    • 0032528301 scopus 로고    scopus 로고
    • The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex
    • Pfund C, et al. 1998. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.EMBO J. 17:3981-3989.
    • (1998) EMBO J. , vol.17 , pp. 3981-3989
    • Pfund, C.1
  • 344
    • 0030935908 scopus 로고    scopus 로고
    • Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H(+)-ATPase
    • Piper PW, Ortiz-Calderon C, Holyoak C, Coote P, Cole M. 1997. Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H(+)-ATPase. Cell Stress Chaperones 2:12-24.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 12-24
    • Piper, P.W.1    Ortiz-Calderon, C.2    Holyoak, C.3    Coote, P.4    Cole, M.5
  • 345
    • 0028151517 scopus 로고
    • Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold
    • Piper PW, et al. 1994. Induction of major heat-shock proteins of Saccharomyces cerevisiae, including plasma membrane Hsp30, by ethanol levels above a critical threshold. Microbiology 140(Pt 11):3031-3038.
    • (1994) Microbiology , vol.140 , Issue.PART 11 , pp. 3031-3038
    • Piper, P.W.1
  • 346
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper RK, Bohmler S, Bordallo J, Sommer T, Wolf DH. 1997. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388:891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 347
    • 0023147386 scopus 로고
    • Effect of cell cycle position on thermotolerance in Saccharomyces cerevisiae
    • Plesset J, Ludwig JR, Cox BS, McLaughlin CS. 1987. Effect of cell cycle position on thermotolerance in Saccharomyces cerevisiae. J. Bacteriol. 169:779-784.
    • (1987) J. Bacteriol. , vol.169 , pp. 779-784
    • Plesset, J.1    Ludwig, J.R.2    Cox, B.S.3    McLaughlin, C.S.4
  • 348
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • Polier S, Dragovic Z, Hartl FU, Bracher A. 2008. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133:1068-1079.
    • (2008) Cell , vol.133 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 349
    • 11844258269 scopus 로고    scopus 로고
    • A role for the non-phosphorylated form of yeast Snf1: Tolerance to toxic cations and activation of potassium transport
    • Portillo F, Mulet JM, Serrano R. 2005. A role for the non-phosphorylated form of yeast Snf1: tolerance to toxic cations and activation of potassium transport. FEBS Lett. 579:512-516.
    • (2005) FEBS Lett. , vol.579 , pp. 512-516
    • Portillo, F.1    Mulet, J.M.2    Serrano, R.3
  • 350
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, et al. 1997. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90:65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1
  • 351
    • 0028242359 scopus 로고
    • The role of the thiol/disulfide centers and peptide binding site in the chaperone and antichaperone activities of protein disulfide isomerase
    • Puig A, Lyles MM, Noiva R, Gilbert HF. 1994. The role of the thiol/disulfide centers and peptide binding site in the chaperone and antichaperone activities of protein disulfide isomerase. J. Biol. Chem. 269:19128-19135.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19128-19135
    • Puig, A.1    Lyles, M.M.2    Noiva, R.3    Gilbert, H.F.4
  • 352
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran SK, Haroun RI, Clos J, Wisniewski J, Wu C. 1993. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259:230-234.
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 353
    • 0028025643 scopus 로고
    • Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo
    • Rabindran SK, Wisniewski J, Li L, Li GC, Wu C. 1994. Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo. Mol. Cell. Biol. 14:6552-6560.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6552-6560
    • Rabindran, S.K.1    Wisniewski, J.2    Li, L.3    Li, G.C.4    Wu, C.5
  • 354
    • 0033048143 scopus 로고    scopus 로고
    • Heat-induced cell cycle arrest of Saccharomyces cerevisiae: Involvement of the RAD6/UBC2 and WSC2 genes in its reversal
    • Raboy B, Marom A, Dor Y, Kulka RG. 1999. Heat-induced cell cycle arrest of Saccharomyces cerevisiae: involvement of the RAD6/UBC2 and WSC2 genes in its reversal. Mol. Microbiol. 32:729-739.
    • (1999) Mol. Microbiol. , vol.32 , pp. 729-739
    • Raboy, B.1    Marom, A.2    Dor, Y.3    Kulka, R.G.4
  • 355
    • 4744374703 scopus 로고    scopus 로고
    • The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae
    • Rakwalska M, Rospert S. 2004. The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae. Mol. Cell. Biol. 24:9186-9197.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9186-9197
    • Rakwalska, M.1    Rospert, S.2
  • 356
    • 52049091534 scopus 로고    scopus 로고
    • Hsp90/Hsp70 chaperone machine regulation of the Saccharomyces MAL-activator as determined in vivo using noninducible and constitutive mutant alleles
    • Ran F, Bali M, Michels CA. 2008. Hsp90/Hsp70 chaperone machine regulation of the Saccharomyces MAL-activator as determined in vivo using noninducible and constitutive mutant alleles. Genetics 179:331-343.
    • (2008) Genetics , vol.179 , pp. 331-343
    • Ran, F.1    Bali, M.2    Michels, C.A.3
  • 357
    • 0035937187 scopus 로고    scopus 로고
    • Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor
    • Rao J, et al. 2001. Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. J. Biol. Chem. 276:5814-5820.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5814-5820
    • Rao, J.1
  • 358
    • 0028046847 scopus 로고
    • Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
    • Rassow J, et al. 1994. Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127:1547-1556.
    • (1994) J. Cell Biol. , vol.127 , pp. 1547-1556
    • Rassow, J.1
  • 359
    • 22144451849 scopus 로고    scopus 로고
    • Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
    • Rauch T, et al. 2005. Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli. Mol. Microbiol. 57:357-365.
    • (2005) Mol. Microbiol. , vol.57 , pp. 357-365
    • Rauch, T.1
  • 360
    • 29344449706 scopus 로고    scopus 로고
    • Human and yeast Hsp110 chaperones exhibit functional differences
    • Raviol H, Bukau B, Mayer MP. 2006. Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett. 580:168-174.
    • (2006) FEBS Lett. , vol.580 , pp. 168-174
    • Raviol, H.1    Bukau, B.2    Mayer, M.P.3
  • 361
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B. 2006. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25:2510-2518.
    • (2006) EMBO J. , vol.25 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 362
    • 0024972079 scopus 로고
    • Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor
    • Reading DS, Hallberg RL, Myers AM. 1989. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337:655-659.
    • (1989) Nature , vol.337 , pp. 655-659
    • Reading, D.S.1    Hallberg, R.L.2    Myers, A.M.3
  • 363
    • 0035793088 scopus 로고    scopus 로고
    • Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins
    • Requena JR, Chao CC, Levine RL, Stadtman ER. 2001. Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proc. Natl. Acad. Sci. U. S. A. 98:69-74.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 69-74
    • Requena, J.R.1    Chao, C.C.2    Levine, R.L.3    Stadtman, E.R.4
  • 364
    • 0033992274 scopus 로고    scopus 로고
    • Characterization of a cDNA clone, encoding a 70 kDa heat shock protein from the dermatophyte pathogen Trichophyton rubrum
    • Rezaie S, et al. 2000. Characterization of a cDNA clone, encoding a 70 kDa heat shock protein from the dermatophyte pathogen Trichophyton rubrum. Gene 241:27-33.
    • (2000) Gene , vol.241 , pp. 27-33
    • Rezaie, S.1
  • 365
    • 0030868257 scopus 로고    scopus 로고
    • Trehalose synthesis is important for the acquisition of thermotolerance in Schizosaccharomyces pombe
    • Ribeiro MJ, Reinders A, Boller T, Wiemken A, De Virgilio C. 1997. Trehalose synthesis is important for the acquisition of thermotolerance in Schizosaccharomyces pombe. Mol. Microbiol. 25:571-581.
    • (1997) Mol. Microbiol. , vol.25 , pp. 571-581
    • Ribeiro, M.J.1    Reinders, A.2    Boller, T.3    Wiemken, A.4    De Virgilio, C.5
  • 366
    • 0037518202 scopus 로고    scopus 로고
    • Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle
    • Richter K, Muschler P, Hainzl O, Reinstein J, Buchner J. 2003. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle. J. Biol. Chem. 278:10328-10333.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10328-10333
    • Richter, K.1    Muschler, P.2    Hainzl, O.3    Reinstein, J.4    Buchner, J.5
  • 367
    • 80053455899 scopus 로고    scopus 로고
    • Hsp90 governs dispersion and drug resistance of fungal biofilms
    • Robbins N, et al. 2011. Hsp90 governs dispersion and drug resistance of fungal biofilms. PLoS Pathog. 7:e1002257.
    • (2011) PLoS Pathog. , vol.7
    • Robbins, N.1
  • 368
    • 0742269688 scopus 로고    scopus 로고
    • The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)
    • Roe SM, et al. 2004. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 116:87-98.
    • (2004) Cell , vol.116 , pp. 87-98
    • Roe, S.M.1
  • 369
    • 2442694192 scopus 로고    scopus 로고
    • The nuclear pore complex and the DEAD box protein Rat8p/Dbp5p have nonessential features which appear to facilitate mRNA export following heat shock
    • Rollenhagen C, Hodge CA, Cole CN. 2004. The nuclear pore complex and the
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4869-4879
    • Rollenhagen, C.1    Hodge, C.A.2    Cole, C.N.3
  • 370
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose MD, Misra LM, Vogel JP. 1989. KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57:1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 371
    • 0030063416 scopus 로고    scopus 로고
    • Hsp60-independent protein folding in the matrix of yeast mitochondria
    • Rospert S, et al. 1996. Hsp60-independent protein folding in the matrix of yeast mitochondria. EMBO J. 15:764-774.
    • (1996) EMBO J. , vol.15 , pp. 764-774
    • Rospert, S.1
  • 372
    • 1842457138 scopus 로고    scopus 로고
    • The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix
    • Rottgers K, Zufall N, Guiard B, Voos W. 2002. The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J. Biol. Chem. 277:45829-45837.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45829-45837
    • Rottgers, K.1    Zufall, N.2    Guiard, B.3    Voos, W.4
  • 373
    • 0027509063 scopus 로고
    • Heat shock-mediated cell cycle blockage and G1 cyclin expression in the yeast Saccharomyces cerevisiae
    • Rowley A, Johnston GC, Butler B, Werner-Washburne M, Singer RA. 1993. Heat shock-mediated cell cycle blockage and G1 cyclin expression in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1034-1041.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1034-1041
    • Rowley, A.1    Johnston, G.C.2    Butler, B.3    Werner-Washburne, M.4    Singer, R.A.5
  • 374
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley N, et al. 1994. Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77:249-259.
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1
  • 375
    • 0029737693 scopus 로고    scopus 로고
    • Regulation ofmRNAexport in response to stress in Saccharomyces cerevisiae
    • Saavedra C, Tung KS, Amberg DC, Hopper AK, Cole CN. 1996. Regulation ofmRNAexport in response to stress in Saccharomyces cerevisiae. Genes Dev. 10:1608-1620.
    • (1996) Genes Dev. , vol.10 , pp. 1608-1620
    • Saavedra, C.1    Tung, K.S.2    Amberg, D.C.3    Hopper, A.K.4    Cole, C.N.5
  • 376
    • 9844219734 scopus 로고    scopus 로고
    • Yeast heat-shock mRNAs are exported through a distinct pathway defined by Rip1p
    • Saavedra CA, Hammell CM, Heath CV, Cole CN. 1997. Yeast heat-shock mRNAs are exported through a distinct pathway defined by Rip1p. Genes Dev. 11:2845-2856.
    • (1997) Genes Dev. , vol.11 , pp. 2845-2856
    • Saavedra, C.A.1    Hammell, C.M.2    Heath, C.V.3    Cole, C.N.4
  • 377
    • 80052232255 scopus 로고    scopus 로고
    • Fine-tuning of the Msn2/4-mediated yeast stress responses as revealed by systematic deletion of Msn2/4 partners
    • Sadeh A, Movshovich N, Volokh M, Gheber L, Aharoni A. 2011. Fine-tuning of the Msn2/4-mediated yeast stress responses as revealed by systematic deletion of Msn2/4 partners. Mol. Biol. Cell 22:3127-3138.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3127-3138
    • Sadeh, A.1    Movshovich, N.2    Volokh, M.3    Gheber, L.4    Aharoni, A.5
  • 378
    • 0024787847 scopus 로고
    • A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein
    • Sadler I, et al. 1989. A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein. J. Cell Biol. 109:2665-2675.
    • (1989) J. Cell Biol. , vol.109 , pp. 2665-2675
    • Sadler, I.1
  • 379
    • 46149116088 scopus 로고    scopus 로고
    • Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities
    • Sadlish H, et al. 2008. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS One 3:e1763.
    • (2008) PLoS One , vol.3
    • Sadlish, H.1
  • 380
    • 34249853249 scopus 로고    scopus 로고
    • Network of general and specialty J protein chaperones of the yeast cytosol
    • Sahi C, Craig EA. 2007. Network of general and specialty J protein chaperones of the yeast cytosol. Proc. Natl. Acad. Sci. U. S. A. 104:7163-7168.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7163-7168
    • Sahi, C.1    Craig, E.A.2
  • 381
    • 34250309182 scopus 로고    scopus 로고
    • Interaction between heat shock transcription factors (HSFs) and divergent binding sequences: Binding specificities of yeast HSFs and human HSF1
    • Sakurai H, Takemori Y. 2007. Interaction between heat shock transcription factors (HSFs) and divergent binding sequences: binding specificities of yeast HSFs and human HSF1. J. Biol. Chem. 282:13334-13341.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13334-13341
    • Sakurai, H.1    Takemori, Y.2
  • 382
    • 0033967755 scopus 로고    scopus 로고
    • The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress
    • Sales K, Brandt W, Rumbak E, Lindsey G. 2000. The LEA-like protein HSP 12 in Saccharomyces cerevisiae has a plasma membrane location and protects membranes against desiccation and ethanol-induced stress. Biochim. Biophys. Acta 1463:267-278.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 267-278
    • Sales, K.1    Brandt, W.2    Rumbak, E.3    Lindsey, G.4
  • 383
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez Y, Lindquist SL. 1990. HSP104 required for induced thermotolerance. Science 248:1112-1115.
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 384
    • 0026523626 scopus 로고
    • Hsp104 is required for tolerance to many forms of stress
    • Sanchez Y, Taulien J, Borkovich KA, Lindquist S. 1992. Hsp104 is required for tolerance to many forms of stress. EMBO J. 11:2357-2364.
    • (1992) EMBO J. , vol.11 , pp. 2357-2364
    • Sanchez, Y.1    Taulien, J.2    Borkovich, K.A.3    Lindquist, S.4
  • 385
    • 0026589260 scopus 로고
    • Sec61p and BiP directly facilitate polypeptide translocation into the ER
    • Sanders SL, Whitfield KM, Vogel JP, Rose MD, Schekman RW. 1992. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69:353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.L.1    Whitfield, K.M.2    Vogel, J.P.3    Rose, M.D.4    Schekman, R.W.5
  • 386
    • 0031771494 scopus 로고    scopus 로고
    • Heat shock element architecture is an important determinant in the temperature and transactivation domain requirements for heat shock transcription factor
    • Santoro N, Johansson N, Thiele DJ. 1998. Heat shock element architecture is an important determinant in the temperature and transactivation domain requirements for heat shock transcription factor. Mol. Cell. Biol. 18:6340-6352.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6340-6352
    • Santoro, N.1    Johansson, N.2    Thiele, D.J.3
  • 387
    • 0031008564 scopus 로고    scopus 로고
    • The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates
    • Saris N, Holkeri H, Craven RA, Stirling CJ, Makarow M. 1997. The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. J. Cell Biol. 137:813-824.
    • (1997) J. Cell Biol. , vol.137 , pp. 813-824
    • Saris, N.1    Holkeri, H.2    Craven, R.A.3    Stirling, C.J.4    Makarow, M.5
  • 388
    • 0342748522 scopus 로고    scopus 로고
    • Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole
    • Satyanarayana C, Schroder-Kohne S, Craig EA, Schu PV, Horst M. 2000. Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole. FEBS Lett. 470:232-238.
    • (2000) FEBS Lett. , vol.470 , pp. 232-238
    • Satyanarayana, C.1    Schroder-Kohne, S.2    Craig, E.A.3    Schu, P.V.4    Horst, M.5
  • 389
    • 0025673942 scopus 로고
    • A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein
    • Scherer PE, Krieg UC, Hwang ST, Vestweber D, Schatz G. 1990. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein. EMBO J. 9:4315-4322.
    • (1990) EMBO J. , vol.9 , pp. 4315-4322
    • Scherer, P.E.1    Krieg, U.C.2    Hwang, S.T.3    Vestweber, D.4    Schatz, G.5
  • 390
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C, et al. 2000. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101:199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1
  • 391
    • 0029757416 scopus 로고    scopus 로고
    • The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA
    • Schilke B, et al. 1996. The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA. J. Cell Biol. 134:603-613.
    • (1996) J. Cell Biol. , vol.134 , pp. 603-613
    • Schilke, B.1
  • 392
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • Schilke B, Voisine C, Beinert H, Craig E. 1999. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 96:10206-10211.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 394
    • 0029021905 scopus 로고
    • A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s
    • Schlenstedt G, Harris S, Risse B, Lill R, Silver PA. 1995. A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J. Cell Biol. 129:979-988.
    • (1995) J. Cell Biol. , vol.129 , pp. 979-988
    • Schlenstedt, G.1    Harris, S.2    Risse, B.3    Lill, R.4    Silver, P.A.5
  • 395
    • 0035850757 scopus 로고    scopus 로고
    • The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1
    • Schmidt S, Strub A, Rottgers K, Zufall N, Voos W. 2001. The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1. J. Mol. Biol. 313:13-26.
    • (2001) J. Mol. Biol. , vol.313 , pp. 13-26
    • Schmidt, S.1    Strub, A.2    Rottgers, K.3    Zufall, N.4    Voos, W.5
  • 396
    • 0030003064 scopus 로고    scopus 로고
    • Msn2p, a zinc finger DNA-binding protein, is the transcriptional activator of the multistress response in Saccharomyces cerevisiae
    • Schmitt AP, McEntee K. 1996. Msn2p, a zinc finger DNA-binding protein, is the transcriptional activator of the multistress response in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 93:5777-5782.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5777-5782
    • Schmitt, A.P.1    McEntee, K.2
  • 397
    • 0029045002 scopus 로고
    • Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70
    • Schmitt M, Neupert W, Langer T. 1995. Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J. 14:3434-3444.
    • (1995) EMBO J. , vol.14 , pp. 3434-3444
    • Schmitt, M.1    Neupert, W.2    Langer, T.3
  • 398
    • 0029835946 scopus 로고    scopus 로고
    • The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria
    • Schmitt M, Neupert W, Langer T. 1996. The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J. Cell Biol. 134:1375-1386.
    • (1996) J. Cell Biol. , vol.134 , pp. 1375-1386
    • Schmitt, M.1    Neupert, W.2    Langer, T.3
  • 399
    • 0028132179 scopus 로고
    • Mitochondrial Hsp70/MIM44 complex facilitates protein import
    • Schneider HC, et al. 1994. Mitochondrial Hsp70/MIM44 complex facilitates protein import. Nature 371:768-774.
    • (1994) Nature , vol.371 , pp. 768-774
    • Schneider, H.C.1
  • 400
    • 0029856628 scopus 로고    scopus 로고
    • The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import
    • Schneider HC, Westermann B, Neupert W, Brunner M. 1996. The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import. EMBO J. 15:5796-5803.
    • (1996) EMBO J. , vol.15 , pp. 5796-5803
    • Schneider, H.C.1    Westermann, B.2    Neupert, W.3    Brunner, M.4
  • 401
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag JD, et al. 2001. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8:633-644.
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1
  • 402
    • 45849091944 scopus 로고    scopus 로고
    • Structure of the Hsp110:Hsc70 nucleotide exchange machine
    • Schuermann JP, et al. 2008. Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol. Cell 31:232-243.
    • (2008) Mol. Cell , vol.31 , pp. 232-243
    • Schuermann, J.P.1
  • 403
    • 0031844350 scopus 로고    scopus 로고
    • Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin
    • Schulte TW, et al. 1998. Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin. Cell Stress Chaperones 3:100-108.
    • (1998) Cell Stress Chaperones , vol.3 , pp. 100-108
    • Schulte, T.W.1
  • 404
    • 0027136175 scopus 로고
    • Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum
    • Scidmore MA, Okamura HH, Rose MD. 1993. Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum. Mol. Biol. Cell 4:1145-1159.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1145-1159
    • Scidmore, M.A.1    Okamura, H.H.2    Rose, M.D.3
  • 405
    • 0028886503 scopus 로고
    • Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance
    • Sewell AK, et al. 1995. Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance. J. Biol. Chem. 270:25079-25086.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25079-25086
    • Sewell, A.K.1
  • 406
    • 0032896994 scopus 로고    scopus 로고
    • Stress induction of HSP30, the plasma membrane heat shock protein gene of Saccharomyces cerevisiae, appears not to use known stress-regulated transcription factors
    • Seymour IJ, Piper PW. 1999. Stress induction of HSP30, the plasma membrane heat shock protein gene of Saccharomyces cerevisiae, appears not to use known stress-regulated transcription factors. Microbiology 145(Pt 1):231-239.
    • (1999) Microbiology , vol.145 , Issue.PART 1 , pp. 231-239
    • Seymour, I.J.1    Piper, P.W.2
  • 407
    • 34848840693 scopus 로고    scopus 로고
    • Negative transcriptional regulation of multidrug resistance gene expression by an Hsp70 protein
    • Shahi P, Gulshan K, Moye-Rowley WS. 2007. Negative transcriptional regulation of multidrug resistance gene expression by an Hsp70 protein. J. Biol. Chem. 282:26822-26831.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26822-26831
    • Shahi, P.1    Gulshan, K.2    Moye-Rowley, W.S.3
  • 408
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu CE, Walter P. 1996. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15:3028-3039.
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 409
    • 43349108797 scopus 로고    scopus 로고
    • The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis
    • Shaner L, Gibney PA, Morano KA. 2008. The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis. Curr. Genet. 54:1-11.
    • (2008) Curr. Genet. , vol.54 , pp. 1-11
    • Shaner, L.1    Gibney, P.A.2    Morano, K.A.3
  • 410
    • 33845587149 scopus 로고    scopus 로고
    • Characterization of hsp70 binding and nucleotide exchange by the yeast hsp110 chaperone Sse1
    • Shaner L, Sousa R, Morano KA. 2006. Characterization of hsp70 binding and nucleotide exchange by the yeast hsp110 chaperone Sse1. Biochemistry 45:15075-15084.
    • (2006) Biochemistry , vol.45 , pp. 15075-15084
    • Shaner, L.1    Sousa, R.2    Morano, K.A.3
  • 411
    • 2542435778 scopus 로고    scopus 로고
    • The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family
    • Shaner L, Trott A, Goeckeler JL, Brodsky JL, Morano KA. 2004. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. J. Biol. Chem. 279:21992-22001.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21992-22001
    • Shaner, L.1    Trott, A.2    Goeckeler, J.L.3    Brodsky, J.L.4    Morano, K.A.5
  • 412
    • 29244467709 scopus 로고    scopus 로고
    • The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb
    • Shaner L, Wegele H, Buchner J, Morano KA. 2005. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. J. Biol. Chem. 280:41262-41269.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41262-41269
    • Shaner, L.1    Wegele, H.2    Buchner, J.3    Morano, K.A.4
  • 413
    • 0035808455 scopus 로고    scopus 로고
    • Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase
    • Shao J, et al. 2001. Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase. J. Biol. Chem. 276:206-214.
    • (2001) J. Biol. Chem. , vol.276 , pp. 206-214
    • Shao, J.1
  • 414
    • 0242349780 scopus 로고    scopus 로고
    • Functional dissection of cdc37: Characterization of domain structure and amino acid residues critical for protein kinase binding
    • Shao J, Irwin A, Hartson SD, Matts RL. 2003. Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. Biochemistry 42:12577-12588.
    • (2003) Biochemistry , vol.42 , pp. 12577-12588
    • Shao, J.1    Irwin, A.2    Hartson, S.D.3    Matts, R.L.4
  • 415
    • 77954999438 scopus 로고    scopus 로고
    • Coupling temperature sensing and development: Hsp90 regulates morphogenetic signalling in Candida albicans
    • Shapiro RS, Cowen L. 2010. Coupling temperature sensing and development: Hsp90 regulates morphogenetic signalling in Candida albicans. Virulence 1:45-48.
    • (2010) Virulence , vol.1 , pp. 45-48
    • Shapiro, R.S.1    Cowen, L.2
  • 416
    • 84862556757 scopus 로고    scopus 로고
    • Reference deleted.
    • Reference deleted.
  • 417
    • 80052010587 scopus 로고    scopus 로고
    • Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p
    • Sharma D, Masison DC. 2011. Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc. Natl. Acad. Sci. U. S. A. 108:13665-13670.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 13665-13670
    • Sharma, D.1    Masison, D.C.2
  • 418
    • 0023545320 scopus 로고
    • Heat-shock proteins induced during the mycelial-to-yeast transitions of strains of Histoplasma capsulatum
    • Shearer G, Jr, Birge CH, Yuckenberg PD, Kobayashi GS, Medoff G. 1987. Heat-shock proteins induced during the mycelial-to-yeast transitions of strains of Histoplasma capsulatum. J. Gen. Microbiol. 133:3375-3382.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 3375-3382
    • Shearer Jr., G.1    Birge, C.H.2    Yuckenberg, P.D.3    Kobayashi, G.S.4    Medoff, G.5
  • 419
    • 40049109706 scopus 로고    scopus 로고
    • ATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth
    • Shimon L, Hynes GM, McCormack EA, Willison KR, Horovitz A. 2008. ATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth. J. Mol. Biol. 377:469-477.
    • (2008) J. Mol. Biol. , vol.377 , pp. 469-477
    • Shimon, L.1    Hynes, G.M.2    McCormack, E.A.3    Willison, K.R.4    Horovitz, A.5
  • 420
    • 0029960517 scopus 로고    scopus 로고
    • In vivo nuclear transport kinetics in Saccharomyces cerevisiae: A role for heat shock protein 70 during targeting and translocation
    • Shulga N, et al. 1996. In vivo nuclear transport kinetics in Saccharomyces cerevisiae: a role for heat shock protein 70 during targeting and translocation. J. Cell Biol. 135:329-339.
    • (1996) J. Cell Biol. , vol.135 , pp. 329-339
    • Shulga, N.1
  • 421
    • 16344363965 scopus 로고    scopus 로고
    • Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1
    • Sichting M, Mokranjac D, Azem A, Neupert W, Hell K. 2005. Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1. EMBO J. 24:1046-1056.
    • (2005) EMBO J. , vol.24 , pp. 1046-1056
    • Sichting, M.1    Mokranjac, D.2    Azem, A.3    Neupert, W.4    Hell, K.5
  • 422
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers K, et al. 1999. Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18:75-84.
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers, K.1
  • 423
    • 77956178634 scopus 로고    scopus 로고
    • The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner
    • Sielaff B, Tsai FT. 2010. The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J. Mol. Biol. 402:30-37.
    • (2010) J. Mol. Biol. , vol.402 , pp. 30-37
    • Sielaff, B.1    Tsai, F.T.2
  • 424
    • 0032539016 scopus 로고    scopus 로고
    • A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum
    • Silberstein S, Schlenstedt G, Silver PA, Gilmore R. 1998. A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum. J. Cell Biol. 143:921-933.
    • (1998) J. Cell Biol. , vol.143 , pp. 921-933
    • Silberstein, S.1    Schlenstedt, G.2    Silver, P.A.3    Gilmore, R.4
  • 425
    • 0037036458 scopus 로고    scopus 로고
    • Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37
    • Siligardi G, et al. 2002. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J. Biol. Chem. 277:20151-20159.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20151-20159
    • Siligardi, G.1
  • 426
    • 0033909892 scopus 로고    scopus 로고
    • Trehalose is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum but not for maintenance of membrane traffic functions after severe heat stress
    • Simola M, Hanninen AL, Stranius SM, Makarow M. 2000. Trehalose is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum but not for maintenance of membrane traffic functions after severe heat stress. Mol. Microbiol. 37:42-53.
    • (2000) Mol. Microbiol. , vol.37 , pp. 42-53
    • Simola, M.1    Hanninen, A.L.2    Stranius, S.M.3    Makarow, M.4
  • 428
    • 0029042422 scopus 로고
    • BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
    • Simons JF, Ferro-Novick S, Rose MD, Helenius A. 1995. BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell Biol. 130:41-49.
    • (1995) J. Cell Biol. , vol.130 , pp. 41-49
    • Simons, J.F.1    Ferro-Novick, S.2    Rose, M.D.3    Helenius, A.4
  • 429
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer MA, Lindquist S. 1998. Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell 1:639-648.
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 430
    • 0032213339 scopus 로고    scopus 로고
    • Thermotolerance in Saccharomyces cerevisiae: The Yin and Yang of trehalose
    • Singer MA, Lindquist S. 1998. Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose. Trends Biotechnol. 16:460-468.
    • (1998) Trends Biotechnol. , vol.16 , pp. 460-468
    • Singer, M.A.1    Lindquist, S.2
  • 431
    • 0023114146 scopus 로고
    • Transcriptional regulation of an hsp70 heat shock gene in the yeast Saccharomyces cerevisiae
    • Slater MR, Craig EA. 1987. Transcriptional regulation of an hsp70 heat shock gene in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 7:1906-1916.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1906-1916
    • Slater, M.R.1    Craig, E.A.2
  • 432
    • 0026342691 scopus 로고
    • A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle
    • Smith BJ, Yaffe MP. 1991. A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle. Mol. Cell. Biol. 11:2647-2655.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2647-2655
    • Smith, B.J.1    Yaffe, M.P.2
  • 433
    • 0036461599 scopus 로고    scopus 로고
    • The eukaryote chaperonin CCT is a cold shock protein in Saccharomyces cerevisiae
    • Somer L, Shmulman O, Dror T, Hashmueli S, Kashi Y. 2002. The eukaryote chaperonin CCT is a cold shock protein in Saccharomyces cerevisiae. Cell Stress Chaperones 7:47-54.
    • (2002) Cell Stress Chaperones , vol.7 , pp. 47-54
    • Somer, L.1    Shmulman, O.2    Dror, T.3    Hashmueli, S.4    Kashi, Y.5
  • 434
    • 0037031902 scopus 로고    scopus 로고
    • Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae
    • Sondermann H, et al. 2002. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. J. Biol. Chem. 277:33220-33227.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33220-33227
    • Sondermann, H.1
  • 435
    • 0029058524 scopus 로고
    • Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese
    • Song JL, Wang CC. 1995. Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese. Eur. J. Biochem. 231:312-316.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 312-316
    • Song, J.L.1    Wang, C.C.2
  • 436
    • 0035660414 scopus 로고    scopus 로고
    • Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes
    • Song Y, et al. 2001. Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes. J. Biochem. 130:757-764.
    • (2001) J. Biochem. , vol.130 , pp. 757-764
    • Song, Y.1
  • 437
    • 0024989583 scopus 로고
    • Yeast heat shock factor contains separable transient and sustained response transcriptional activators
    • Sorger PK. 1990. Yeast heat shock factor contains separable transient and sustained response transcriptional activators. Cell 62:793-805.
    • (1990) Cell , vol.62 , pp. 793-805
    • Sorger, P.K.1
  • 438
    • 0023643235 scopus 로고
    • Heat shock factor is regulated differently in yeast and HeLa cells
    • Sorger PK, Lewis MJ, Pelham HRB. 1987. Heat shock factor is regulated differently in yeast and HeLa cells. Nature 329:81-84.
    • (1987) Nature , vol.329 , pp. 81-84
    • Sorger, P.K.1    Lewis, M.J.2    Pelham, H.R.B.3
  • 439
    • 0024852809 scopus 로고
    • Trimerization of a yeast transcriptional activator via a coiled-coil motif
    • Sorger PK, Nelson HCM. 1989. Trimerization of a yeast transcriptional activator via a coiled-coil motif. Cell 59:807-813.
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.M.2
  • 440
    • 0023427519 scopus 로고
    • Purification and characterization of a heat-shock element binding protein from yeast
    • Sorger PK, Pelham HR. 1987. Purification and characterization of a heat-shock element binding protein from yeast. EMBO J. 6:3035-3041.
    • (1987) EMBO J. , vol.6 , pp. 3035-3041
    • Sorger, P.K.1    Pelham, H.R.2
  • 441
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger PK, Pelham HR. 1988. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54:855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.2
  • 442
    • 0029862454 scopus 로고    scopus 로고
    • Identification, characterization, and expression of the BiP endoplasmic reticulum resident chaperonins in Pneumocystis carinii
    • Stedman TT, Buck GA. 1996. Identification, characterization, and expression of the BiP endoplasmic reticulum resident chaperonins in Pneumocystis carinii. Infect. Immun. 64:4463-4471.
    • (1996) Infect. Immun. , vol.64 , pp. 4463-4471
    • Stedman, T.T.1    Buck, G.A.2
  • 444
    • 33646381898 scopus 로고    scopus 로고
    • PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates
    • Stirling PC, et al. 2006. PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates. J. Biol. Chem. 281:7012-7021.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7012-7021
    • Stirling, P.C.1
  • 445
    • 0029884589 scopus 로고    scopus 로고
    • The Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts
    • Stoldt V, et al. 1996. The Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Yeast 12:523-529.
    • (1996) Yeast , vol.12 , pp. 523-529
    • Stoldt, V.1
  • 446
    • 0032553445 scopus 로고    scopus 로고
    • Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly
    • Strain J, et al. 1998. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J. Biol. Chem. 273:31138-31144.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31138-31144
    • Strain, J.1
  • 447
    • 0038043235 scopus 로고    scopus 로고
    • Analysis of the interaction of small heat shock proteins with unfolding proteins
    • Stromer T, Ehrnsperger M, Gaestel M, Buchner J. 2003. Analysis of the interaction of small heat shock proteins with unfolding proteins. J. Biol. Chem. 278:18015-18021.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18015-18021
    • Stromer, T.1    Ehrnsperger, M.2    Gaestel, M.3    Buchner, J.4
  • 448
    • 1642524277 scopus 로고    scopus 로고
    • Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins
    • Stromer T, Fischer E, Richter K, Haslbeck M, Buchner J. 2004. Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domain is important for oligomer assembly and the binding of unfolding proteins. J. Biol. Chem. 279:11222-11228.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11222-11228
    • Stromer, T.1    Fischer, E.2    Richter, K.3    Haslbeck, M.4    Buchner, J.5
  • 449
    • 3042521076 scopus 로고    scopus 로고
    • The distinct morphogenic states of Candida albicans
    • Sudbery P, Gow N, Berman J. 2004. The distinct morphogenic states of Candida albicans. Trends Microbiol. 12:317-324.
    • (2004) Trends Microbiol. , vol.12 , pp. 317-324
    • Sudbery, P.1    Gow, N.2    Berman, J.3
  • 451
    • 0028876053 scopus 로고
    • Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans
    • Swoboda RK, et al. 1995. Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans. Infect. Immun. 63:4506-4514.
    • (1995) Infect. Immun. , vol.63 , pp. 4506-4514
    • Swoboda, R.K.1
  • 452
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana C, Stevens TH. 1992. The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12:4601-4611.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 453
    • 0031590425 scopus 로고    scopus 로고
    • Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner
    • Tachikawa H, et al. 1997. Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem. Biophys. Res. Commun. 239:710-714.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 710-714
    • Tachikawa, H.1
  • 454
    • 0025822385 scopus 로고
    • Molecular structure of a yeast gene, PDI1, encoding protein disulfide isomerase that is essential for cell growth
    • Tachikawa H, Miura T, Katakura Y, Mizunaga T. 1991. Molecular structure of a yeast gene, PDI1, encoding protein disulfide isomerase that is essential for cell growth. J. Biochem. 110:306-313.
    • (1991) J. Biochem. , vol.110 , pp. 306-313
    • Tachikawa, H.1    Miura, T.2    Katakura, Y.3    Mizunaga, T.4
  • 455
    • 0029115691 scopus 로고
    • Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion
    • Tachikawa H, et al. 1995. Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett. 369:212-216.
    • (1995) FEBS Lett. , vol.369 , pp. 212-216
    • Tachikawa, H.1
  • 456
    • 0027940568 scopus 로고
    • Heat shock transcription factor activates yeast metallothionein gene expression in response to heat and glucose starvation via distinct signalling pathways
    • Tamai KT, Liu X, Silar P, Sosinowski T, Thiele DJ. 1994. Heat shock transcription factor activates yeast metallothionein gene expression in response to heat and glucose starvation via distinct signalling pathways. Mol. Cell. Biol. 14:8155-8165.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8155-8165
    • Tamai, K.T.1    Liu, X.2    Silar, P.3    Sosinowski, T.4    Thiele, D.J.5
  • 457
    • 0033804841 scopus 로고    scopus 로고
    • Targeted disruption of sti35, a stress-responsive gene in phytopathogenic fungus Fusarium oxysporum
    • Thanonkeo P, Akiyama K, Jain S, Takata R. 2000. Targeted disruption of sti35, a stress-responsive gene in phytopathogenic fungus Fusarium oxysporum. Curr. Microbiol. 41:284-289.
    • (2000) Curr. Microbiol. , vol.41 , pp. 284-289
    • Thanonkeo, P.1    Akiyama, K.2    Jain, S.3    Takata, R.4
  • 458
    • 0030707562 scopus 로고    scopus 로고
    • TOR signalling and control of cell growth
    • Thomas G, Hall MN. 1997. TOR signalling and control of cell growth. Curr. Opin. Cell Biol. 9:782-787.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 782-787
    • Thomas, G.1    Hall, M.N.2
  • 459
    • 34347249238 scopus 로고    scopus 로고
    • The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation
    • Toogun OA, Zeiger W, Freeman BC. 2007. The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc. Natl. Acad. Sci. U. S. A. 104:5765-5770.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5765-5770
    • Toogun, O.A.1    Zeiger, W.2    Freeman, B.C.3
  • 460
    • 0029117426 scopus 로고
    • Genetic identification of the site of DNA contact in the yeast heat shock transcription factor
    • Torres FA, Bonner JJ. 1995. Genetic identification of the site of DNA contact in the yeast heat shock transcription factor. Mol. Cell. Biol. 15:5063-5070.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5063-5070
    • Torres, F.A.1    Bonner, J.J.2
  • 461
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, et al. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1
  • 462
    • 0032481247 scopus 로고    scopus 로고
    • Functional analysis of the stress response element and its role in the multistress response of Saccharomyces cerevisiae
    • Treger JM, Magee TR, McEntee K. 1998. Functional analysis of the stress response element and its role in the multistress response of Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 243:13-19.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 13-19
    • Treger, J.M.1    Magee, T.R.2    McEntee, K.3
  • 463
    • 0032500690 scopus 로고    scopus 로고
    • Transcriptional factor mutations reveal regulatory complexities of heat shock and newly identified stress genes in Saccharomyces cerevisiae
    • Treger JM, Schmitt AP, Simon JR, McEntee K. 1998. Transcriptional factor mutations reveal regulatory complexities of heat shock and newly identified stress genes in Saccharomyces cerevisiae. J. Biol. Chem. 273:26875-26879.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26875-26879
    • Treger, J.M.1    Schmitt, A.P.2    Simon, J.R.3    McEntee, K.4
  • 464
    • 23344432378 scopus 로고    scopus 로고
    • The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae
    • Trott A, Shaner L, Morano KA. 2005. The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae. Genetics 170:1009-1021.
    • (2005) Genetics , vol.170 , pp. 1009-1021
    • Trott, A.1    Shaner, L.2    Morano, K.A.3
  • 465
    • 41649104650 scopus 로고    scopus 로고
    • Activation of heat shock and antioxidant responses by the natural product celastrol: Transcriptional signatures of a thioltargeted molecule
    • Trott A, et al. 2008. Activation of heat shock and antioxidant responses by the natural product celastrol: transcriptional signatures of a thioltargeted molecule. Mol. Biol. Cell 19:1104-1112.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1104-1112
    • Trott, A.1
  • 466
    • 0035912730 scopus 로고    scopus 로고
    • Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in Saccharomyces cerevisiae
    • Trotter EW, Berenfeld L, Krause SA, Petsko GA, Gray JV. 2001. Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 98:7313-7318.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7313-7318
    • Trotter, E.W.1    Berenfeld, L.2    Krause, S.A.3    Petsko, G.A.4    Gray, J.V.5
  • 467
    • 0346736509 scopus 로고    scopus 로고
    • Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae
    • Trotter EW, et al. 2002. Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 277:44817-44825.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44817-44825
    • Trotter, E.W.1
  • 468
    • 34247892293 scopus 로고    scopus 로고
    • In the yeast heat shock response, Hsf1-directed induction of Hsp90 facilitates the activation of the Slt2 (Mpk1) mitogen-activated protein kinase required for cell integrity
    • Truman AW, et al. 2007. In the yeast heat shock response, Hsf1-directed induction of Hsp90 facilitates the activation of the Slt2 (Mpk1) mitogen-activated protein kinase required for cell integrity. Eukaryot. Cell 6:744-752.
    • (2007) Eukaryot. Cell , vol.6 , pp. 744-752
    • Truman, A.W.1
  • 469
    • 10744228445 scopus 로고    scopus 로고
    • A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria
    • Truscott KN, et al. 2003. A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria. J. Cell Biol. 163:707-713.
    • (2003) J. Cell Biol. , vol.163 , pp. 707-713
    • Truscott, K.N.1
  • 470
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai J, Douglas MG. 1996. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271:9347-9354.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 471
    • 0034388026 scopus 로고    scopus 로고
    • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
    • Tyson JR, Stirling CJ. 2000. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J. 19:6440-6452.
    • (2000) EMBO J. , vol.19 , pp. 6440-6452
    • Tyson, J.R.1    Stirling, C.J.2
  • 472
    • 79959498194 scopus 로고    scopus 로고
    • Gametogenesis eliminates age-induced cellular damage and resets life span in yeast
    • Unal E, Kinde B, Amon A. 2011. Gametogenesis eliminates age-induced cellular damage and resets life span in yeast. Science 332:1554-1557.
    • (2011) Science , vol.332 , pp. 1554-1557
    • Unal, E.1    Kinde, B.2    Amon, A.3
  • 473
    • 0031452228 scopus 로고    scopus 로고
    • Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed Ssa mutants
    • Unno K, Kishido T, Hosaka M, Okada S. 1997. Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed Ssa mutants. Biol. Pharm. Bull. 20:1240-1244.
    • (1997) Biol. Pharm. Bull. , vol.20 , pp. 1240-1244
    • Unno, K.1    Kishido, T.2    Hosaka, M.3    Okada, S.4
  • 475
    • 0028049082 scopus 로고
    • PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae
    • Van Dyck L, Pearce DA, Sherman F. 1994. PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 269:238-242.
    • (1994) J. Biol. Chem. , vol.269 , pp. 238-242
    • Van Dyck, L.1    Pearce, D.A.2    Sherman, F.3
  • 476
  • 478
    • 0031442669 scopus 로고    scopus 로고
    • A family of genes required for maintenance of cell wall integrity and for the stress response in Saccharomyces cerevisiae
    • Verna J, Lodder A, Lee K, Vagts A, Ballester R. 1997. A family of genes required for maintenance of cell wall integrity and for the stress response in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 94:13804-13809.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13804-13809
    • Verna, J.1    Lodder, A.2    Lee, K.3    Vagts, A.4    Ballester, R.5
  • 479
    • 0028587244 scopus 로고
    • A yeast TCP-1-like protein is required for actin function in vivo
    • Vinh DB, Drubin DG. 1994. A yeast TCP-1-like protein is required for actin function in vivo. Proc. Natl. Acad. Sci. U. S. A. 91:9116-9120.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9116-9120
    • Vinh, D.B.1    Drubin, D.G.2
  • 480
    • 3542991477 scopus 로고    scopus 로고
    • On mechanisms that control heat shock transcription factor activity in metazoan cells
    • Voellmy R. 2004. On mechanisms that control heat shock transcription factor activity in metazoan cells. Cell Stress Chaperones 9:122-133.
    • (2004) Cell Stress Chaperones , vol.9 , pp. 122-133
    • Voellmy, R.1
  • 481
    • 84934440933 scopus 로고    scopus 로고
    • Chaperone regulation of the heat shock protein response
    • Voellmy R, Boellmann F. 2007. Chaperone regulation of the heat shock protein response. Adv. Exp. Med. Biol. 594:89-99.
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 89-99
    • Voellmy, R.1    Boellmann, F.2
  • 482
    • 0025339295 scopus 로고
    • Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
    • Vogel JP, Misra LM, Rose MD. 1990. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110:1885-1895.
    • (1990) J. Cell Biol. , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 483
    • 31544442176 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones by a proline switch
    • Vogel M, Bukau B, Mayer MP. 2006. Allosteric regulation of Hsp70 chaperones by a proline switch. Mol. Cell 21:359-367.
    • (2006) Mol. Cell , vol.21 , pp. 359-367
    • Vogel, M.1    Bukau, B.2    Mayer, M.P.3
  • 484
    • 33846020582 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
    • Vogel M, Mayer MP, Bukau B. 2006. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J. Biol. Chem. 281:38705-38711.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38705-38711
    • Vogel, M.1    Mayer, M.P.2    Bukau, B.3
  • 485
    • 0035852737 scopus 로고    scopus 로고
    • Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae
    • Voisine C, et al. 2001. Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 98:1483-1488.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1483-1488
    • Voisine, C.1
  • 486
    • 33644951058 scopus 로고    scopus 로고
    • The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress
    • von Janowsky B, Major T, Knapp K, Voos W. 2006. The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J. Mol. Biol. 357:793-807.
    • (2006) J. Mol. Biol. , vol.357 , pp. 793-807
    • Von Janowsky, B.1    Major, T.2    Knapp, K.3    Voos, W.4
  • 487
    • 69749111488 scopus 로고    scopus 로고
    • The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase network
    • von Plehwe U, et al. 2009. The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase network. Genes Dev. 23:2102-2115.
    • (2009) Genes Dev. , vol.23 , pp. 2102-2115
    • Von Plehwe, U.1
  • 488
    • 0027362778 scopus 로고
    • Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
    • Voos W, Gambill BD, Guiard B, Pfanner N, Craig EA. 1993. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix. J. Cell Biol. 123:119-126.
    • (1993) J. Cell Biol. , vol.123 , pp. 119-126
    • Voos, W.1    Gambill, B.D.2    Guiard, B.3    Pfanner, N.4    Craig, E.A.5
  • 489
    • 0027994692 scopus 로고
    • Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
    • Voos W, et al. 1994. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes. Mol. Cell. Biol. 14:6627-6634.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6627-6634
    • Voos, W.1
  • 490
    • 0037009130 scopus 로고    scopus 로고
    • Molecular chaperones as essential mediators of mitochondrial biogenesis
    • Voos W, Rottgers K. 2002. Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim. Biophys. Acta 1592:51-62.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 51-62
    • Voos, W.1    Rottgers, K.2
  • 491
    • 29944442714 scopus 로고    scopus 로고
    • Distinct antifungal mechanisms: Beta-defensins require Candida albicans Ssa1 protein, while Trk1p mediates activity of cysteine-free cationic peptides
    • Vylkova S, Li XS, Berner JC, Edgerton M. 2006. Distinct antifungal mechanisms: beta-defensins require Candida albicans Ssa1 protein, while Trk1p mediates activity of cysteine-free cationic peptides. Antimicrob. Agents Chemother. 50:324-331.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 324-331
    • Vylkova, S.1    Li, X.S.2    Berner, J.C.3    Edgerton, M.4
  • 492
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner I, Arlt H, van Dyck L, Langer T, Neupert W. 1994. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13:5135-5145.
    • (1994) EMBO J. , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    Van Dyck, L.3    Langer, T.4    Neupert, W.5
  • 493
    • 0030061006 scopus 로고    scopus 로고
    • Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine
    • Walker KW, Lyles MM, Gilbert HF. 1996. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35:1972-1980.
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 495
    • 31444454302 scopus 로고    scopus 로고
    • The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
    • Wandinger SK, Suhre MH, Wegele H, Buchner J. 2006. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. 25:367-376.
    • (2006) EMBO J. , vol.25 , pp. 367-376
    • Wandinger, S.K.1    Suhre, M.H.2    Wegele, H.3    Buchner, J.4
  • 496
    • 0033230434 scopus 로고    scopus 로고
    • Eps1, a novel PDI-related protein involved in ER quality control in yeast
    • Wang Q, Chang A. 1999. Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 18:5972-5982.
    • (1999) EMBO J. , vol.18 , pp. 5972-5982
    • Wang, Q.1    Chang, A.2
  • 498
    • 33748776034 scopus 로고    scopus 로고
    • The nucleotide exchange factor activity of Grp170 may explain the non-lethal phenotype of loss of Sil1 function in man and mouse
    • Weitzmann A, Volkmer J, Zimmermann R. 2006. The nucleotide exchange factor activity of Grp170 may explain the non-lethal phenotype of loss of Sil1 function in man and mouse. FEBS Lett. 580:5237-5240.
    • (2006) FEBS Lett. , vol.580 , pp. 5237-5240
    • Weitzmann, A.1    Volkmer, J.2    Zimmermann, R.3
  • 499
    • 77956006894 scopus 로고    scopus 로고
    • Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function
    • Welker S, et al. 2010. Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Mol. Cell 39:507-520.
    • (2010) Mol. Cell , vol.39 , pp. 507-520
    • Welker, S.1
  • 500
    • 0032571231 scopus 로고    scopus 로고
    • Heat-induced elevation of ceramide in Saccharomyces cerevisiae via de novo synthesis
    • Wells GB, Dickson RC, Lester RL. 1998. Heat-induced elevation of ceramide in Saccharomyces cerevisiae via de novo synthesis. J. Biol. Chem. 273:7235-7243.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7235-7243
    • Wells, G.B.1    Dickson, R.C.2    Lester, R.L.3
  • 501
    • 37449008520 scopus 로고    scopus 로고
    • Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104
    • Wendler P, et al. 2007. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 131:1366-1377.
    • (2007) Cell , vol.131 , pp. 1366-1377
    • Wendler, P.1
  • 502
    • 63849263045 scopus 로고    scopus 로고
    • Motor mechanism for protein threading through Hsp104
    • Wendler P, et al. 2009. Motor mechanism for protein threading through Hsp104. Mol. Cell 34:81-92.
    • (2009) Mol. Cell , vol.34 , pp. 81-92
    • Wendler, P.1
  • 503
    • 0033229937 scopus 로고    scopus 로고
    • Opposite roles of trehalase activity in heat-shock recovery and heatshock survival in Saccharomyces cerevisiae
    • Wera S, De Schrijver E, Geyskens I, Nwaka S, Thevelein JM. 1999. Opposite roles of trehalase activity in heat-shock recovery and heatshock survival in Saccharomyces cerevisiae. Biochem. J. 343(Pt. 3):621-626.
    • (1999) Biochem. J. , vol.343 , Issue.PART 3 , pp. 621-626
    • Wera, S.1    De Schrijver, E.2    Geyskens, I.3    Nwaka, S.4    Thevelein, J.M.5
  • 504
    • 0024670024 scopus 로고
    • Yeast Hsp70 RNA levels vary in response to the physiological status of the cell
    • Werner-Washburne M, Becker J, Kosic-Smithers J, Craig EA. 1989. Yeast Hsp70 RNA levels vary in response to the physiological status of the cell. J. Bacteriol. 171:2680-2688.
    • (1989) J. Bacteriol. , vol.171 , pp. 2680-2688
    • Werner-Washburne, M.1    Becker, J.2    Kosic-Smithers, J.3    Craig, E.A.4
  • 505
    • 0024894102 scopus 로고
    • Expression of members of the Saccharomyces cerevisiae hsp70 multigene family
    • Werner-Washburne M, Craig EA. 1989. Expression of members of the Saccharomyces cerevisiae hsp70 multigene family. Genome 31:684-689.
    • (1989) Genome , vol.31 , pp. 684-689
    • Werner-Washburne, M.1    Craig, E.A.2
  • 506
    • 0023375806 scopus 로고
    • Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae
    • Werner-Washburne M, Stone DE, Craig EA. 1987. Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 7:2568-2577.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2568-2577
    • Werner-Washburne, M.1    Stone, D.E.2    Craig, E.A.3
  • 507
    • 19944426695 scopus 로고    scopus 로고
    • Celastrols as inducers of the heat shock response and cytoprotection
    • Westerheide SD, et al. 2004. Celastrols as inducers of the heat shock response and cytoprotection. J. Biol. Chem. 279:56053-56060.
    • (2004) J. Biol. Chem. , vol.279 , pp. 56053-56060
    • Westerheide, S.D.1
  • 508
    • 0029860683 scopus 로고    scopus 로고
    • Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins
    • Westermann B, Gaume B, Herrmann JM, Neupert W, Schwarz E. 1996. Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol. Cell. Biol. 16: 7063-7071.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7063-7071
    • Westermann, B.1    Gaume, B.2    Herrmann, J.M.3    Neupert, W.4    Schwarz, E.5
  • 509
    • 0031551576 scopus 로고    scopus 로고
    • Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae
    • Westermann B, Neupert W. 1997. Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae. J. Mol. Biol. 272:477-483.
    • (1997) J. Mol. Biol. , vol.272 , pp. 477-483
    • Westermann, B.1    Neupert, W.2
  • 510
    • 0025955517 scopus 로고
    • Stress-induced oligomerization and chromosomal relocalization of heat-shock factor
    • Westwood JT, Clos J, Wu C. 1991. Stress-induced oligomerization and chromosomal relocalization of heat-shock factor. Nature 353:822-827.
    • (1991) Nature , vol.353 , pp. 822-827
    • Westwood, J.T.1    Clos, J.2    Wu, C.3
  • 511
    • 0024282788 scopus 로고
    • Isolation of the gene encoding the S. cerevisiae heat shock transcription factor
    • Wiederrecht G, Seto D, Parker CS. 1988. Isolation of the gene encoding the S. cerevisiae heat shock transcription factor. Cell 54:841-853.
    • (1988) Cell , vol.54 , pp. 841-853
    • Wiederrecht, G.1    Seto, D.2    Parker, C.S.3
  • 512
    • 0025862421 scopus 로고
    • Heat shock factor-independent heat control of transcription of the CTT1 gene encoding the cytosolic catalase T of Saccharomyces cerevisiae
    • Wieser R, et al. 1991. Heat shock factor-independent heat control of transcription of the CTT1 gene encoding the cytosolic catalase T of Saccharomyces cerevisiae. J. Biol. Chem. 266:12406-12411.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12406-12411
    • Wieser, R.1
  • 513
    • 0036548318 scopus 로고    scopus 로고
    • Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress
    • Winkler A, et al. 2002. Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress. Eukaryot. Cell 1:163-173.
    • (2002) Eukaryot. Cell , vol.1 , pp. 163-173
    • Winkler, A.1
  • 514
    • 3943093972 scopus 로고    scopus 로고
    • Nosocomial bloodstream infections in US hospitals: Analysis of 24,179 cases from a prospective nationwide surveillance study
    • Wisplinghoff H, et al. 2004. Nosocomial bloodstream infections in US hospitals: analysis of 24,179 cases from a prospective nationwide surveillance study. Clin. Infect. Dis. 39:309-317.
    • (2004) Clin. Infect. Dis. , vol.39 , pp. 309-317
    • Wisplinghoff, H.1
  • 515
    • 0030053217 scopus 로고    scopus 로고
    • Multimerization of Hsp42p, a novel heat shock protein of Saccharomyces cerevisiae, is dependent on a conserved carboxyl-terminal sequence
    • Wotton D, Freeman K, Shore D. 1996. Multimerization of Hsp42p, a novel heat shock protein of Saccharomyces cerevisiae, is dependent on a conserved carboxyl-terminal sequence. J. Biol. Chem. 271:2717-2723.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2717-2723
    • Wotton, D.1    Freeman, K.2    Shore, D.3
  • 516
    • 33947139005 scopus 로고    scopus 로고
    • The hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae
    • Wright CM, et al. 2007. The hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae. Genetics 175:1649-1664.
    • (2007) Genetics , vol.175 , pp. 1649-1664
    • Wright, C.M.1
  • 517
    • 33745608086 scopus 로고    scopus 로고
    • Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo
    • Xiao J, Kim LS, Graham TR. 2006. Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo. Mol. Biol. Cell 17:3281-3290.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3281-3290
    • Xiao, J.1    Kim, L.S.2    Graham, T.R.3
  • 518
    • 3142610777 scopus 로고    scopus 로고
    • P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue
    • Xu X, Azakami H, Kato A. 2004. P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett. 570:155-160.
    • (2004) FEBS Lett. , vol.570 , pp. 155-160
    • Xu, X.1    Azakami, H.2    Kato, A.3
  • 519
    • 3042838324 scopus 로고    scopus 로고
    • Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue
    • Xu X, Kanbara K, Azakami H, Kato A. 2004. Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J. Biochem. 135:615-618.
    • (2004) J. Biochem. , vol.135 , pp. 615-618
    • Xu, X.1    Kanbara, K.2    Azakami, H.3    Kato, A.4
  • 520
    • 0033524442 scopus 로고    scopus 로고
    • Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90
    • Xu Y, Singer MA, Lindquist S. 1999. Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc. Natl. Acad. Sci. U. S. A. 96:109-114.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 109-114
    • Xu, Y.1    Singer, M.A.2    Lindquist, S.3
  • 521
    • 29244432181 scopus 로고    scopus 로고
    • Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
    • Yam AY, Albanese V, Lin HT, Frydman J. 2005. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J. Biol. Chem. 280:41252-41261.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41252-41261
    • Yam, A.Y.1    Albanese, V.2    Lin, H.T.3    Frydman, J.4
  • 522
    • 62149093857 scopus 로고    scopus 로고
    • Differential recognition of heat shock elements by members of the heat shock transcription factor family
    • Yamamoto N, Takemori Y, Sakurai M, Sugiyama K, Sakurai H. 2009. Differential recognition of heat shock elements by members of the heat shock transcription factor family. FEBS J. 276:1962-1974.
    • (2009) FEBS J. , vol.276 , pp. 1962-1974
    • Yamamoto, N.1    Takemori, Y.2    Sakurai, M.3    Sugiyama, K.4    Sakurai, H.5
  • 523
    • 0031034725 scopus 로고    scopus 로고
    • Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2
    • Yao Y, Zhou Y, Wang C. 1997. Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2. EMBO J. 16:651-658.
    • (1997) EMBO J. , vol.16 , pp. 651-658
    • Yao, Y.1    Zhou, Y.2    Wang, C.3
  • 524
    • 6344275303 scopus 로고    scopus 로고
    • Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
    • Youker RT, Walsh P, Beilharz T, Lithgow T, Brodsky JL. 2004. Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol. Biol. Cell 15:4787-4797.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4787-4797
    • Youker, R.T.1    Walsh, P.2    Beilharz, T.3    Lithgow, T.4    Brodsky, J.L.5
  • 525
    • 0030779154 scopus 로고    scopus 로고
    • A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication
    • Zarzov P, Boucherie H, Mann C. 1997. A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication. J. Cell Sci. 110:1879-1891.
    • (1997) J. Cell Sci. , vol.110 , pp. 1879-1891
    • Zarzov, P.1    Boucherie, H.2    Mann, C.3
  • 526
    • 0031806619 scopus 로고    scopus 로고
    • Molecular mechanism governing heme signaling in yeast: A higher-order complex mediates heme regulation of the transcriptional activator HAP1
    • Zhang L, Hach A, Wang C. 1998. Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1. Mol. Cell. Biol. 18:3819-3828.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3819-3828
    • Zhang, L.1    Hach, A.2    Wang, C.3
  • 527
    • 3042598511 scopus 로고    scopus 로고
    • Biochemical and structural studies of the interaction of Cdc37 with Hsp90
    • Zhang W, et al. 2004. Biochemical and structural studies of the interaction of Cdc37 with Hsp90. J. Mol. Biol. 340:891-907.
    • (2004) J. Mol. Biol. , vol.340 , pp. 891-907
    • Zhang, W.1
  • 528
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • Zhao R, et al. 2005. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120:715-727.
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1
  • 529
    • 0027256768 scopus 로고
    • The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation
    • Zhong T, Arndt KT. 1993. The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation. Cell 73:1175-1186.
    • (1993) Cell , vol.73 , pp. 1175-1186
    • Zhong, T.1    Arndt, K.T.2
  • 530
    • 81855227611 scopus 로고    scopus 로고
    • Motility and segregation of hsp104-associated protein aggregates in budding yeast
    • Zhou C, et al. 2011. Motility and segregation of hsp104-associated protein aggregates in budding yeast. Cell 147:1186-1196.
    • (2011) Cell , vol.147 , pp. 1186-1196
    • Zhou, C.1
  • 531
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. 1998. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94:471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 532
    • 0034885773 scopus 로고    scopus 로고
    • Mutations in WSC genes for putative stress receptors result in sensitivity to multiple stress conditions and impairment of Rlm1-dependent gene expression in Saccharomyces cerevisiae
    • Zu T, Verna J, Ballester R. 2001. Mutations in WSC genes for putative stress receptors result in sensitivity to multiple stress conditions and impairment of Rlm1-dependent gene expression in Saccharomyces cerevisiae. Mol. Genet. Genomics 266:142-155.
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 142-155
    • Zu, T.1    Verna, J.2    Ballester, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.