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Volumn 16, Issue 6, 2009, Pages 623-630

Structural and functional diversity among eukaryotic Hsp70 nucleotide exchange factors

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; NUCLEOTIDE; SIGNAL PEPTIDE;

EID: 67650151030     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609788490186     Document Type: Article
Times cited : (10)

References (116)
  • 1
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer, M.P.; Bukau, B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci., 2005, 62(6), 670-684.
    • (2005) Cell. Mol. Life Sci , vol.62 , Issue.6 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 2
    • 0025100372 scopus 로고
    • Threedimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K.M.; DeLuca-Flaherty, C.; McKay, D.B. Threedimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature, 1990, 346(6285), 623-628.
    • (1990) Nature , vol.346 , Issue.6285 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 3
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • Swain, J.F.; Dinler, G.; Sivendran, R.; Montgomery, D.L.; Stotz, M.; Gierasch, L.M. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol. Cell., 2007, 26(1), 27-39.
    • (2007) Mol. Cell , vol.26 , Issue.1 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 4
    • 33846020582 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
    • Vogel, M.; Mayer, M.P.; Bukau, B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J. Biol. Chem., 2006, 281(50), 38705-38711.
    • (2006) J. Biol. Chem , vol.281 , Issue.50 , pp. 38705-38711
    • Vogel, M.1    Mayer, M.P.2    Bukau, B.3
  • 5
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D.; Baici, A.; Gehring, H.; Christen, P. Kinetics of molecular chaperone action. Science, 1994, 263(5149), 971-973.
    • (1994) Science , vol.263 , Issue.5149 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 6
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J.S.; Buchberger, A.; Reinstein, J.; Bukau, B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol., 1995, 249(1), 126-137.
    • (1995) J. Mol. Biol , vol.249 , Issue.1 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 8
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham, M.E.; Caplan, A.J. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell. Stress Chaperones, 1998, 3(1), 28-36.
    • (1998) Cell. Stress Chaperones , vol.3 , Issue.1 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 9
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley, W.L. The J-domain family and the recruitment of chaperone power. Trends Biochem. Sci., 1998, 23(6), 222-227.
    • (1998) Trends Biochem. Sci , vol.23 , Issue.6 , pp. 222-227
    • Kelley, W.L.1
  • 10
    • 4344590764 scopus 로고    scopus 로고
    • The Jprotein family: Modulating protein assembly, disassembly and translocation
    • 6
    • Walsh, P.; Bursac, D.; Law, Y.C.; Cyr, D.; Lithgow, T. The Jprotein family: modulating protein assembly, disassembly and translocation. EMBO Rep., 2004, 5(6), 567-571.
    • (2004) EMBO Rep , vol.5 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 11
    • 22344447035 scopus 로고    scopus 로고
    • Hennessy, F.; Nicoll, W.S.; Zimmermann, R.; Cheetham, M.E.; Blatch, G.L. Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci., 2005, 14(7), 1697-1709.
    • Hennessy, F.; Nicoll, W.S.; Zimmermann, R.; Cheetham, M.E.; Blatch, G.L. Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci., 2005, 14(7), 1697-1709.
  • 12
    • 33751265748 scopus 로고    scopus 로고
    • The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
    • Qiu, X.B.; Shao, Y.M.; Miao, S.; Wang, L. The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell. Mol. Life Sci., 2006, 63(22), 2560-2570.
    • (2006) Cell. Mol. Life Sci , vol.63 , Issue.22 , pp. 2560-2570
    • Qiu, X.B.1    Shao, Y.M.2    Miao, S.3    Wang, L.4
  • 13
    • 0038268566 scopus 로고    scopus 로고
    • The yeast Sls1p and Fes1p proteins define a new family of Hsp70 nucleotide exchange factors
    • Kabani, M.; Beckerich, J.M.; Brodsky, J.L. The yeast Sls1p and Fes1p proteins define a new family of Hsp70 nucleotide exchange factors. Curr. Genomics, 2003, 4(6), 465-473.
    • (2003) Curr. Genomics , vol.4 , Issue.6 , pp. 465-473
    • Kabani, M.1    Beckerich, J.M.2    Brodsky, J.L.3
  • 14
    • 0017395649 scopus 로고
    • Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12
    • Saito, H.; Uchida, H. Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12. J. Mol. Biol., 1977, 113(1), 1-25.
    • (1977) J. Mol. Biol , vol.113 , Issue.1 , pp. 1-25
    • Saito, H.1    Uchida, H.2
  • 15
    • 0018193766 scopus 로고
    • Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication
    • Yochem, J.; Uchida, H.; Sunshine, M.; Saito, H.; Georgopoulos, C.P.; Feiss, M. Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication. Mol. Gen. Genet., 1978, 164(1), 9-14.
    • (1978) Mol. Gen. Genet , vol.164 , Issue.1 , pp. 9-14
    • Yochem, J.1    Uchida, H.2    Sunshine, M.3    Saito, H.4    Georgopoulos, C.P.5    Feiss, M.6
  • 16
    • 0024978379 scopus 로고
    • Ordered assembly of nucleoprotein structures at the bacteriophage lambda replication origin during the initiation of DNA replication
    • Alfano, C.; McMacken, R. Ordered assembly of nucleoprotein structures at the bacteriophage lambda replication origin during the initiation of DNA replication. J. Biol. Chem., 1989, 264(18), 10699-10708.
    • (1989) J. Biol. Chem , vol.264 , Issue.18 , pp. 10699-10708
    • Alfano, C.1    McMacken, R.2
  • 17
    • 0024316732 scopus 로고
    • Initiation of lambda DNA replication with purified host- and bacteriophageencoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
    • Zylicz, M.; Ang, D.; Liberek, K.; Georgopoulos, C. Initiation of lambda DNA replication with purified host- and bacteriophageencoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J., 1989, 8(5), 1601-1608.
    • (1989) EMBO J , vol.8 , Issue.5 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4
  • 18
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K.; Marszalek, J.; Ang, D.; Georgopoulos, C.; Zylicz, M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA, 1991, 88(7), 2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.7 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 19
    • 0344500848 scopus 로고    scopus 로고
    • The archaeal molecular chaperone machine: Peculiarities and paradoxes
    • Macario, A.J.; de Macario, E.C. The archaeal molecular chaperone machine: peculiarities and paradoxes. Genetics, 1999, 152(4), 1277-1283.
    • (1999) Genetics , vol.152 , Issue.4 , pp. 1277-1283
    • Macario, A.J.1    de Macario, E.C.2
  • 20
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison, C.J.; Hayer-Hartl, M.; Di Liberto, M.; Hartl, F.; Kuriyan, J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science, 1997, 276(5311), 431-435.
    • (1997) Science , vol.276 , Issue.5311 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 21
    • 0035794207 scopus 로고    scopus 로고
    • Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system
    • Grimshaw, J.P.; Jelesarov, I.; Schonfeld, H.J.; Christen, P. Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J. Biol. Chem., 2001, 276(9), 6098- 6104.
    • (2001) J. Biol. Chem , vol.276 , Issue.9 , pp. 6098-6104
    • Grimshaw, J.P.1    Jelesarov, I.2    Schonfeld, H.J.3    Christen, P.4
  • 22
    • 0035900534 scopus 로고    scopus 로고
    • Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response
    • Groemping, Y.; Reinstein, J. Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. J. Mol. Biol., 2001, 314(1), 167-178.
    • (2001) J. Mol. Biol , vol.314 , Issue.1 , pp. 167-178
    • Groemping, Y.1    Reinstein, J.2
  • 23
    • 33646079874 scopus 로고    scopus 로고
    • Thermal adaptation of the yeast mitochondrial Hsp70 system is regulated by the reversible unfolding of its nucleotide exchange factor
    • Moro, F.; Muga, A. Thermal adaptation of the yeast mitochondrial Hsp70 system is regulated by the reversible unfolding of its nucleotide exchange factor. J. Mol. Biol., 2006, 358(5), 1367-1377.
    • (2006) J. Mol. Biol , vol.358 , Issue.5 , pp. 1367-1377
    • Moro, F.1    Muga, A.2
  • 24
    • 0028842615 scopus 로고    scopus 로고
    • Hohfeld, J.; Minami, Y.; Hartl, F.U. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell, 1995, 83(4), 589-598.
    • Hohfeld, J.; Minami, Y.; Hartl, F.U. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell, 1995, 83(4), 589-598.
  • 25
    • 34250871853 scopus 로고    scopus 로고
    • All in the family: Atypical Hsp70 chaperones are conserved modulators of Hsp70 activity
    • Shaner, L.; Morano, K.A. All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity. Cell. Stress Chaperones, 2007, 12(1), 1-8.
    • (2007) Cell. Stress Chaperones , vol.12 , Issue.1 , pp. 1-8
    • Shaner, L.1    Morano, K.A.2
  • 28
    • 0344039806 scopus 로고    scopus 로고
    • Hohfeld, J.; Jentsch, S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 [published erratum appears in EMBO J 1998 Feb 2;17(3):847]. EMBO J., 1997, 16(20), 6209-6216.
    • Hohfeld, J.; Jentsch, S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 [published erratum appears in EMBO J 1998 Feb 2;17(3):847]. EMBO J., 1997, 16(20), 6209-6216.
  • 29
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • Sondermann, H.; Scheufler, C.; Schneider, C.; Hohfeld, J.; Hartl, F.U.; Moarefi, I. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science, 2001, 291(5508), 1553-1557.
    • (2001) Science , vol.291 , Issue.5508 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 30
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • Takayama, S.; Reed, J.C. Molecular chaperone targeting and regulation by BAG family proteins. Nat. Cell. Biol., 2001, 3(10), E237- 241.
    • (2001) Nat. Cell. Biol , vol.3 , Issue.10
    • Takayama, S.1    Reed, J.C.2
  • 31
    • 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.; Ho, A.K.; Listenberger, L.L.; Siegers, K.; Moarefi, I.; Wente, S.R.; Hartl, F.U.; Young, J.C. Prediction of Novel Bag-1 Homologs Based on Structure/Function Analysis Identifies Snl1p as an Hsp70 Co-chaperone in Saccharomyces cerevisiae. J. Biol. Chem., 2002, 277(36), 33220-33227.
    • (2002) J. Biol. Chem , vol.277 , Issue.36 , pp. 33220-33227
    • Sondermann, H.1    Ho, A.K.2    Listenberger, L.L.3    Siegers, K.4    Moarefi, I.5    Wente, S.R.6    Hartl, F.U.7    Young, J.C.8
  • 32
    • 0035980016 scopus 로고    scopus 로고
    • Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor
    • Gässler, C.S.; Wiederkehr, T.; Brehmer, D.; Bukau, B.; Mayer, M.P. Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J. Biol. Chem., 2001, 276(35), 32538-32544.
    • (2001) J. Biol. Chem , vol.276 , Issue.35 , pp. 32538-32544
    • Gässler, C.S.1    Wiederkehr, T.2    Brehmer, D.3    Bukau, B.4    Mayer, M.P.5
  • 33
    • 17544365200 scopus 로고    scopus 로고
    • Sls1p, an endoplasmic reticulum component, is involved in the protein translocation process in the yeast Yarrowia lipolytica
    • Boisrame, A.; Beckerich, J.M.; Gaillardin, C. Sls1p, an endoplasmic reticulum component, is involved in the protein translocation process in the yeast Yarrowia lipolytica. J. Biol. Chem., 1996, 271(20), 11668-11675.
    • (1996) J. Biol. Chem , vol.271 , Issue.20 , pp. 11668-11675
    • Boisrame, A.1    Beckerich, J.M.2    Gaillardin, C.3
  • 34
    • 0032553527 scopus 로고    scopus 로고
    • Interaction of Kar2p and Sls1p is required for efficient co- translational translocation of secreted proteins in the yeast Yarrowia lipolytica
    • Boisrame, A.; Kabani, M.; Beckerich, J.M.; Hartmann, E.; Gaillardin, C. Interaction of Kar2p and Sls1p is required for efficient co- translational translocation of secreted proteins in the yeast Yarrowia lipolytica. J. Biol. Chem., 1998, 273(47), 30903-30908.
    • (1998) J. Biol. Chem , vol.273 , Issue.47 , pp. 30903-30908
    • Boisrame, A.1    Kabani, M.2    Beckerich, J.M.3    Hartmann, E.4    Gaillardin, C.5
  • 35
    • 0033988715 scopus 로고    scopus 로고
    • A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica
    • Kabani, M.; Boisrame, A.; Beckerich, J.M.; Gaillardin, C. A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica. Gene, 2000, 241(2), 309-315.
    • (2000) Gene , vol.241 , Issue.2 , pp. 309-315
    • Kabani, M.1    Boisrame, A.2    Beckerich, J.M.3    Gaillardin, C.4
  • 36
    • 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, J.M.; Gaillardin, C. Sls1p Stimulates Sec63p-Mediated Activation of Kar2p in a Conformation- Dependent Manner in the Yeast Endoplasmic Reticulum. Mol. Cell. Biol., 2000, 20(18), 6923-6934.
    • (2000) Mol. Cell. Biol , vol.20 , Issue.18 , pp. 6923-6934
    • Kabani, M.1    Beckerich, J.M.2    Gaillardin, C.3
  • 37
    • 0034388026 scopus 로고    scopus 로고
    • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
    • Tyson, J.R.; Stirling, C.J. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J., 2000, 19(23), 6440-6452.
    • (2000) EMBO J , vol.19 , Issue.23 , pp. 6440-6452
    • Tyson, J.R.1    Stirling, C.J.2
  • 38
    • 0347033285 scopus 로고    scopus 로고
    • Chung, K.T.; Shen, Y.; Hendershot, L.M. BAP, a Mammalian BiPassociated Protein, Is a Nucleotide Exchange Factor That Regulates the ATPase Activity of BiP. J. Biol. Chem., 2002, 277(49), 47557- 47563.
    • Chung, K.T.; Shen, Y.; Hendershot, L.M. BAP, a Mammalian BiPassociated Protein, Is a Nucleotide Exchange Factor That Regulates the ATPase Activity of BiP. J. Biol. Chem., 2002, 277(49), 47557- 47563.
  • 39
    • 0036275663 scopus 로고    scopus 로고
    • Nucleotide exchange factor for the yeast hsp70 molecular chaperone ssa1p
    • Kabani, M.; Beckerich, J.M.; Brodsky, J.L. Nucleotide exchange factor for the yeast hsp70 molecular chaperone ssa1p. Mol. Cell. Biol., 2002, 22(13), 4677-4689.
    • (2002) Mol. Cell. Biol , vol.22 , Issue.13 , pp. 4677-4689
    • Kabani, M.1    Beckerich, J.M.2    Brodsky, J.L.3
  • 40
    • 33751517708 scopus 로고    scopus 로고
    • Fes1p acts as a nucleotide exchange factor for the ribosomeassociated molecular chaperone Ssb1p
    • Dragovic, Z.; Shomura, Y.; Tzvetkov, N.; Hartl, F.U.; Bracher, A. Fes1p acts as a nucleotide exchange factor for the ribosomeassociated molecular chaperone Ssb1p. Biol. Chem., 2006, 387(12), 1593-1600.
    • (2006) Biol. Chem , vol.387 , Issue.12 , pp. 1593-1600
    • Dragovic, Z.1    Shomura, Y.2    Tzvetkov, N.3    Hartl, F.U.4    Bracher, A.5
  • 41
    • 0032483996 scopus 로고    scopus 로고
    • Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein
    • Raynes, D.A.; Guerriero, V.; Jr. Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein. J. Biol. Chem., 1998, 273(49), 32883-32888.
    • (1998) J. Biol. Chem , vol.273 , Issue.49 , pp. 32883-32888
    • Raynes, D.A.1    Guerriero Jr., V.2
  • 42
    • 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, D.A.; Guerriero, V.; Brodsky, J.L. HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett., 2002, 531(2), 339-342.
    • (2002) FEBS Lett , vol.531 , Issue.2 , pp. 339-342
    • Kabani, M.1    McLellan, C.2    Raynes, D.A.3    Guerriero, V.4    Brodsky, J.L.5
  • 43
    • 13244278043 scopus 로고    scopus 로고
    • Regulation of Hsp70 function by HspBP1: Structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
    • Shomura, Y.; Dragovic, Z.; Chang, H.C.; Tzvetkov, N.; Young, J.C.; Brodsky, J.L.; Guerriero, V.; Hartl, F.U.; Bracher, A. Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol. Cell., 2005, 17(3), 367-379.
    • (2005) Mol. Cell , vol.17 , Issue.3 , pp. 367-379
    • Shomura, Y.1    Dragovic, Z.2    Chang, H.C.3    Tzvetkov, N.4    Young, J.C.5    Brodsky, J.L.6    Guerriero, V.7    Hartl, F.U.8    Bracher, A.9
  • 44
    • 34848869936 scopus 로고    scopus 로고
    • Insights into hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
    • Liu, Q.; Hendrickson, W.A. Insights into hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell, 2007, 131(1), 106-120.
    • (2007) Cell , vol.131 , Issue.1 , pp. 106-120
    • Liu, Q.1    Hendrickson, W.A.2
  • 45
    • 0001133526 scopus 로고    scopus 로고
    • Hsp110 protects heat-denatured proteins and confers cellular thermoresistance
    • Oh, H.J.; Chen, X.; Subjeck, J.R. Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. J. Biol. Chem., 1997, 272(50), 31636-31640.
    • (1997) J. Biol. Chem , vol.272 , Issue.50 , pp. 31636-31640
    • Oh, H.J.1    Chen, X.2    Subjeck, J.R.3
  • 46
    • 0000905027 scopus 로고    scopus 로고
    • The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions
    • Oh, H.J.; Easton, D.; Murawski, M.; Kaneko, Y.; Subjeck, J.R. The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions. J. Biol. Chem., 1999, 274(22), 15712-15718.
    • (1999) J. Biol. Chem , vol.274 , Issue.22 , pp. 15712-15718
    • Oh, H.J.1    Easton, D.2    Murawski, M.3    Kaneko, Y.4    Subjeck, J.R.5
  • 47
    • 0346727523 scopus 로고    scopus 로고
    • Coordinated activation of Hsp70 chaperones
    • Steel, G.J.; Fullerton, D.M.; Tyson, J.R.; Stirling, C.J. Coordinated activation of Hsp70 chaperones. Science, 2004, 303(5654), 98-101.
    • (2004) Science , vol.303 , Issue.5654 , pp. 98-101
    • Steel, G.J.1    Fullerton, D.M.2    Tyson, J.R.3    Stirling, C.J.4
  • 48
    • 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, K.A. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. J. Biol. Chem., 2005, 280(50), 41262-41269.
    • (2005) J. Biol. Chem , vol.280 , Issue.50 , pp. 41262-41269
    • Shaner, L.1    Wegele, H.2    Buchner, J.3    Morano, K.A.4
  • 49
    • 29244432181 scopus 로고    scopus 로고
    • Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
    • Yam, A.Y.; Albanese, V.; Lin, H.T.; Frydman, J. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J. Biol. Chem., 2005, 280(50), 41252-41261.
    • (2005) J. Biol. Chem , vol.280 , Issue.50 , pp. 41252-41261
    • Yam, A.Y.1    Albanese, V.2    Lin, H.T.3    Frydman, J.4
  • 50
    • 4744370912 scopus 로고    scopus 로고
    • Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity
    • Yamagishi, N.; Ishihara, K.; Hatayama, T. Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity. J. Biol. Chem., 2004, 279(40), 41727-41733.
    • (2004) J. Biol. Chem , vol.279 , Issue.40 , pp. 41727-41733
    • Yamagishi, N.1    Ishihara, K.2    Hatayama, T.3
  • 51
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic, Z.; Broadley, S.A.; Shomura, Y.; Bracher, A.; Hartl, F.U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J., 2006, 25(11), 2519-2528.
    • (2006) EMBO J , vol.25 , Issue.11 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 52
    • 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, M.P.; Bukau, B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J., 2006, 25(11), 2510- 2518.
    • (2006) EMBO J , vol.25 , Issue.11 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 53
    • 44049083594 scopus 로고    scopus 로고
    • Hsp110 Is a Nucleotide-activated Exchange Factor for Hsp70
    • Andreasson, C.; Fiaux, J.; Rampelt, H.; Mayer, M.P.; Bukau, B. Hsp110 Is a Nucleotide-activated Exchange Factor for Hsp70. J. Biol. Chem., 2008, 283(14), 8877-8884.
    • (2008) J. Biol. Chem , vol.283 , Issue.14 , pp. 8877-8884
    • Andreasson, C.1    Fiaux, J.2    Rampelt, H.3    Mayer, M.P.4    Bukau, B.5
  • 54
    • 33845587149 scopus 로고    scopus 로고
    • Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1
    • Shaner, L.; Sousa, R.; Morano, K.A. Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. Biochemistry, 2006, 45(50), 15075-15084.
    • (2006) Biochemistry , vol.45 , Issue.50 , pp. 15075-15084
    • Shaner, L.1    Sousa, R.2    Morano, K.A.3
  • 55
    • 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, J.L.; Brodsky, J.L.; Morano, K.A. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. J. Biol. Chem., 2004, 279(21), 21992-22001.
    • (2004) J. Biol. Chem , vol.279 , Issue.21 , pp. 21992-22001
    • Shaner, L.1    Trott, A.2    Goeckeler, J.L.3    Brodsky, J.L.4    Morano, K.A.5
  • 56
    • 46149116088 scopus 로고    scopus 로고
    • Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities
    • Sadlish, H.; Rampelt, H.; Shorter, J.; Wegrzyn, R.D.; Andreasson, C.; Lindquist, S.; Bukau, B. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE, 2008, 3(3), e1763.
    • (2008) PLoS ONE , vol.3 , Issue.3
    • Sadlish, H.1    Rampelt, H.2    Shorter, J.3    Wegrzyn, R.D.4    Andreasson, C.5    Lindquist, S.6    Bukau, B.7
  • 57
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • Jiang, J.; Prasad, K.; Lafer, E.M.; Sousa, R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol. Cell, 2005, 20(4), 513-524.
    • (2005) Mol. Cell , vol.20 , Issue.4 , pp. 513-524
    • Jiang, J.1    Prasad, K.2    Lafer, E.M.3    Sousa, R.4
  • 58
    • 37249072739 scopus 로고    scopus 로고
    • Flo11p-independent control of "mat" formation by hsp70 molecular chaperones and nucleotide exchange factors in yeast
    • Martineau, C.N.; Beckerich, J.M.; Kabani, M. Flo11p-independent control of "mat" formation by hsp70 molecular chaperones and nucleotide exchange factors in yeast. Genetics, 2007, 177(3), 1679- 1689.
    • (2007) Genetics , vol.177 , Issue.3 , pp. 1679-1689
    • Martineau, C.N.1    Beckerich, J.M.2    Kabani, M.3
  • 59
    • 36248973177 scopus 로고    scopus 로고
    • The activities and function of molecular chaperones in the endoplasmic reticulum
    • Buck, T.M.; Wright, C.M.; Brodsky, J.L. The activities and function of molecular chaperones in the endoplasmic reticulum. Semin. Cell. Dev. Biol., 2007, 18(6), 751-761.
    • (2007) Semin. Cell. Dev. Biol , vol.18 , Issue.6 , pp. 751-761
    • Buck, T.M.1    Wright, C.M.2    Brodsky, J.L.3
  • 60
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ERassociated degradation
    • Travers, K.J.; Patil, C.K.; Wodicka, L.; Lockhart, D.J.; Weissman, J.S.; Walter, P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ERassociated degradation. Cell, 2000, 101(3), 249-258.
    • (2000) Cell , vol.101 , Issue.3 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 61
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao, L.; Longo-Guess, C.; Harris, B.S.; Lee, J.W.; Ackerman, S.L. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet., 2005, 37(9), 974-979.
    • (2005) Nat. Genet , vol.37 , Issue.9 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5
  • 63
    • 28444497039 scopus 로고    scopus 로고
    • Senderek, J.; Krieger, M.; Stendel, C.; Bergmann, C.; Moser, M.; Breitbach-Faller, N.; Rudnik-Schoneborn, S.; Blaschek, A.; Wolf, N.I.; Harting, I.; North, K.; Smith, J.; Muntoni, F.; Brockington, M.; Quijano-Roy, S.; Renault, F.; Herrmann, R.; Hendershot, L.M.; Schroder, J.M.; Lochmuller, H.; Topaloglu, H.; Voit, T.; Weis, J.; Ebinger, F.; Zerres, K. Mutations in SIL1 cause Marinesco-Sjogren syndrome, a cerebellar ataxia with cataract and myopathy. Nat. Genet., 2005, 37(12), 1312-1314.
    • Senderek, J.; Krieger, M.; Stendel, C.; Bergmann, C.; Moser, M.; Breitbach-Faller, N.; Rudnik-Schoneborn, S.; Blaschek, A.; Wolf, N.I.; Harting, I.; North, K.; Smith, J.; Muntoni, F.; Brockington, M.; Quijano-Roy, S.; Renault, F.; Herrmann, R.; Hendershot, L.M.; Schroder, J.M.; Lochmuller, H.; Topaloglu, H.; Voit, T.; Weis, J.; Ebinger, F.; Zerres, K. Mutations in SIL1 cause Marinesco-Sjogren syndrome, a cerebellar ataxia with cataract and myopathy. Nat. Genet., 2005, 37(12), 1312-1314.
  • 64
    • 38449087466 scopus 로고    scopus 로고
    • The role of the UPS in cystic fibrosis
    • Turnbull, E.L.; Rosser, M.F.; Cyr, D.M. The role of the UPS in cystic fibrosis. BMC Biochem., 2007, 8 (Suppl. 1), S11.
    • (2007) BMC Biochem , vol.8 , Issue.SUPPL. 1
    • Turnbull, E.L.1    Rosser, M.F.2    Cyr, D.M.3
  • 65
    • 0037106481 scopus 로고    scopus 로고
    • The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70
    • Farinha, C.M.; Nogueira, P.; Mendes, F.; Penque, D.; Amaral, M.D. The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70. Biochem. J., 2002, 366(Pt 3), 797-806.
    • (2002) Biochem. J , vol.366 , Issue.PART 3 , pp. 797-806
    • Farinha, C.M.1    Nogueira, P.2    Mendes, F.3    Penque, D.4    Amaral, M.D.5
  • 66
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo, M.A.; Jensen, T.J.; Cui, L.; Hou, Y.; Chang, X.B.; Riordan, J.R. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J., 1998, 17(23), 6879-6887.
    • (1998) EMBO J , vol.17 , Issue.23 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 67
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham, G.C.; Lu, Z.; King, S.; Sorscher, E.; Tousson, A.; Cyr, D.M. The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J., 1999, 18(6), 1492-1505.
    • (1999) EMBO J , vol.18 , Issue.6 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 69
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang, Y.; Janich, S.; Cohn, J.A.; Wilson, J.M. The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc. Natl. Acad. Sci. USA, 1993, 90(20), 9480-9484.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , Issue.20 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4
  • 70
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G.C.; Patterson, C.; Zhang, W.; Younger, J.M.; Cyr, D.M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell. Biol., 2001, 3(1), 100-105.
    • (2001) Nat. Cell. Biol , vol.3 , Issue.1 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 71
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • Younger, J.M.; Ren, H.Y.; Chen, L.; Fan, C.Y.; Fields, A.; Patterson, C.; Cyr, D.M. A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. J. Cell. Biol., 2004, 167(6), 1075-1085.
    • (2004) J. Cell. Biol , vol.167 , Issue.6 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.Y.2    Chen, L.3    Fan, C.Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 72
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/ proteasome coupling
    • Demand, J.; Alberti, S.; Patterson, C.; Hohfeld, J. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/ proteasome coupling. Curr. Biol., 2001, 11(20), 1569-1577.
    • (2001) Curr. Biol , vol.11 , Issue.20 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 73
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • Alberti, S.; Bohse, K.; Arndt, V.; Schmitz, A.; Hohfeld, J. The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol. Biol. Cell., 2004, 15(9), 4003-4010.
    • (2004) Mol. Biol. Cell , vol.15 , Issue.9 , pp. 4003-4010
    • Alberti, S.1    Bohse, K.2    Arndt, V.3    Schmitz, A.4    Hohfeld, J.5
  • 74
    • 28644442088 scopus 로고    scopus 로고
    • BAG-2 Acts as an Inhibitor of the Chaperone-associated Ubiquitin Ligase CHIP
    • Arndt, V.; Daniel, C.; Nastainczyk, W.; Alberti, S.; Hohfeld, J. BAG-2 Acts as an Inhibitor of the Chaperone-associated Ubiquitin Ligase CHIP. Mol. Biol. Cell., 2005, 16(12), 5891-5900.
    • (2005) Mol. Biol. Cell , vol.16 , Issue.12 , pp. 5891-5900
    • Arndt, V.1    Daniel, C.2    Nastainczyk, W.3    Alberti, S.4    Hohfeld, J.5
  • 76
    • 0035816574 scopus 로고    scopus 로고
    • Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70
    • Gusarova, V.; Caplan, A.J.; Brodsky, J.L.; Fisher, E.A. Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70. J. Biol. Chem., 2001, 276(27), 24891-24900.
    • (2001) J. Biol. Chem , vol.276 , Issue.27 , pp. 24891-24900
    • Gusarova, V.1    Caplan, A.J.2    Brodsky, J.L.3    Fisher, E.A.4
  • 77
    • 36349015924 scopus 로고    scopus 로고
    • The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)
    • Hrizo, S.L.; Gusarova, V.; Habiel, D.M.; Goeckeler, J.L.; Fisher, E.A.; Brodsky, J.L. The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD). J. Biol. Chem., 2007, 282(45), 32665-32675.
    • (2007) J. Biol. Chem , vol.282 , Issue.45 , pp. 32665-32675
    • Hrizo, S.L.1    Gusarova, V.2    Habiel, D.M.3    Goeckeler, J.L.4    Fisher, E.A.5    Brodsky, J.L.6
  • 78
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70: Anti-apoptotic proteins with tumorigenic properties
    • Garrido, C.; Brunet, M.; Didelot, C.; Zermati, Y.; Schmitt, E.; Kroemer, G. Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties. Cell Cycle, 2006, 5(22), 2592-2601.
    • (2006) Cell Cycle , vol.5 , Issue.22 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 79
  • 80
    • 37249017924 scopus 로고    scopus 로고
    • Anticancer drugs up-regulate HspBP1 and thereby antagonize the prosurvival function of Hsp70 in tumor cells
    • Tanimura, S.; Hirano, A.I.; Hashizume, J.; Yasunaga, M.; Kawabata, T.; Ozaki, K.; Kohno, M. Anticancer drugs up-regulate HspBP1 and thereby antagonize the prosurvival function of Hsp70 in tumor cells. J. Biol. Chem., 2007, 282(49), 35430-35439.
    • (2007) J. Biol. Chem , vol.282 , Issue.49 , pp. 35430-35439
    • Tanimura, S.1    Hirano, A.I.2    Hashizume, J.3    Yasunaga, M.4    Kawabata, T.5    Ozaki, K.6    Kohno, M.7
  • 81
    • 0038482018 scopus 로고    scopus 로고
    • HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain
    • McLellan, C.A.; Raynes, D.A.; Guerriero, V. HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domain. J. Biol. Chem., 2003, 278(21), 19017-19022.
    • (2003) J. Biol. Chem , vol.278 , Issue.21 , pp. 19017-19022
    • McLellan, C.A.1    Raynes, D.A.2    Guerriero, V.3
  • 82
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity
    • Takayama, S.; Sato, T.; Krajewski, S.; Kochel, K.; Irie, S.; Millan, J.A.; Reed, J.C. Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity. Cell, 1995, 80(2), 279-284.
    • (1995) Cell , vol.80 , Issue.2 , pp. 279-284
    • Takayama, S.1    Sato, T.2    Krajewski, S.3    Kochel, K.4    Irie, S.5    Millan, J.A.6    Reed, J.C.7
  • 83
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: The story of [PIN(+)]
    • Derkatch, I.L.; Bradley, M.E.; Hong, J.Y.; Liebman, S.W. Prions affect the appearance of other prions: the story of [PIN(+)]. Cell, 2001, 106(2), 171-182.
    • (2001) Cell , vol.106 , Issue.2 , pp. 171-182
    • Derkatch, I.L.1    Bradley, M.E.2    Hong, J.Y.3    Liebman, S.W.4
  • 84
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • Sondheimer, N.; Lindquist, S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell., 2000, 5(1), 163-172.
    • (2000) Mol. Cell , vol.5 , Issue.1 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 85
    • 0028308104 scopus 로고
    • URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner, R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science, 1994, 264(5158), 566-569.
    • (1994) Science , vol.264 , Issue.5158 , pp. 566-569
    • Wickner, R.B.1
  • 86
    • 0029888121 scopus 로고    scopus 로고
    • Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • Paushkin, S.V.; Kushnirov, V.V.; Smirnov, V.N.; Ter-Avanesyan, M.D. Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J., 1996, 15(12), 3127-3134.
    • (1996) EMBO J , vol.15 , Issue.12 , pp. 3127-3134
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 87
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
    • Glover, J.R.; Kowal, A.S.; Schirmer, E.C.; Patino, M.M.; Liu, J.J.; Lindquist, S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell, 1997, 89(5), 811-819.
    • (1997) Cell , vol.89 , Issue.5 , pp. 811-819
    • Glover, J.R.1    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5    Lindquist, S.6
  • 88
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King, C.Y.; Tittmann, P.; Gross, H.; Gebert, R.; Aebi, M.; Wuthrich, K. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. USA, 1997, 94(13), 6618-6622.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.13 , pp. 6618-6622
    • King, C.Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wuthrich, K.6
  • 89
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor, K.L.; Cheng, N.; Williams, R.W.; Steven, A.C.; Wickner, R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science., 1999, 283(5406), 1339-1343.
    • (1999) Science , vol.283 , Issue.5406 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 91
    • 33645728523 scopus 로고    scopus 로고
    • Neurodegenerative diseases: New concepts of pathogenesis and their therapeutic implications
    • Skovronsky, D.M.; Lee, V.M.; Trojanowski, J.Q. Neurodegenerative diseases: new concepts of pathogenesis and their therapeutic implications. Annu. Rev. Pathol., 2006, 1, 151-170.
    • (2006) Annu. Rev. Pathol , vol.1 , pp. 151-170
    • Skovronsky, D.M.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 92
  • 93
    • 34447526217 scopus 로고    scopus 로고
    • Stress and prions: Lessons from the yeast model
    • Chernoff, Y.O. Stress and prions: lessons from the yeast model. FEBS Lett., 2007, 581(19), 3695-3701.
    • (2007) FEBS Lett , vol.581 , Issue.19 , pp. 3695-3701
    • Chernoff, Y.O.1
  • 94
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J.R.; Lindquist, S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell, 1998, 94(1), 73-82.
    • (1998) Cell , vol.94 , Issue.1 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 95
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff, Y.O.; Lindquist, S.L.; Ono, B.; Inge-Vechtomov, S.G.; Liebman, S.W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science, 1995, 268(5212), 880-884.
    • (1995) Science , vol.268 , Issue.5212 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 96
    • 0034462603 scopus 로고    scopus 로고
    • URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • Moriyama, H.; Edskes, H.K.; Wickner, R.B. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cell. Biol., 2000, 20(23), 8916-8922.
    • (2000) Mol. Cell. Biol , vol.20 , Issue.23 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 97
    • 0034932879 scopus 로고    scopus 로고
    • The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation
    • Ferreira, P.C.; Ness, F.; Edwards, S.R.; Cox, B.S.; Tuite, M.F. The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol. Microbiol., 2001, 40(6), 1357-1369.
    • (2001) Mol. Microbiol , vol.40 , Issue.6 , pp. 1357-1369
    • Ferreira, P.C.1    Ness, F.2    Edwards, S.R.3    Cox, B.S.4    Tuite, M.F.5
  • 98
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp104 activity in vivo: A possible explanation for its effect in curing yeast prions
    • Jung, G.; Masison, D.C. Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr. Microbiol., 2001, 43(1), 7-10.
    • (2001) Curr. Microbiol , vol.43 , Issue.1 , pp. 7-10
    • Jung, G.1    Masison, D.C.2
  • 99
    • 1542782213 scopus 로고    scopus 로고
    • Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
    • Kryndushkin, D.S.; Alexandrov, I.M.; Ter-Avanesyan, M.D.; Kushnirov, V.V. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem., 2003, 278(49), 49636-49643.
    • (2003) J. Biol. Chem , vol.278 , Issue.49 , pp. 49636-49643
    • Kryndushkin, D.S.1    Alexandrov, I.M.2    Ter-Avanesyan, M.D.3    Kushnirov, V.V.4
  • 101
    • 33846973006 scopus 로고    scopus 로고
    • Hsp104- dependent remodeling of prion complexes mediates protein-only inheritance
    • Satpute-Krishnan, P.; Langseth, S.X.; Serio, T.R. Hsp104- dependent remodeling of prion complexes mediates protein-only inheritance. PLoS Biol., 2007, 5(2), e24.
    • (2007) PLoS Biol , vol.5 , Issue.2
    • Satpute-Krishnan, P.1    Langseth, S.X.2    Serio, T.R.3
  • 102
    • 0033786333 scopus 로고    scopus 로고
    • A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress
    • Jung, G.; Jones, G.; Wegrzyn, R.D.; Masison, D.C. A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress. Genetics, 2000, 156(2), 559-570.
    • (2000) Genetics , vol.156 , Issue.2 , pp. 559-570
    • Jung, G.1    Jones, G.2    Wegrzyn, R.D.3    Masison, D.C.4
  • 103
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newnam, G.P.; Wegrzyn, R.D.; Lindquist, S.L.; Chernoff, Y.O. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol., 1999, 19(2), 1325-1333.
    • (1999) Mol. Cell. Biol , vol.19 , Issue.2 , pp. 1325-1333
    • Newnam, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 104
    • 0036096777 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p
    • Schwimmer, C.; Masison, D.C. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. Mol. Cell. Biol., 2002, 22(11), 3590-3598.
    • (2002) Mol. Cell. Biol , vol.22 , Issue.11 , pp. 3590-3598
    • Schwimmer, C.1    Masison, D.C.2
  • 105
    • 1242296312 scopus 로고    scopus 로고
    • URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast
    • Roberts, B.T.; Moriyama, H.; Wickner, R.B. [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast, 2004, 21(2), 107-117.
    • (2004) Yeast , vol.21 , Issue.2 , pp. 107-117
    • Roberts, B.T.1    Moriyama, H.2    Wickner, R.B.3
  • 106
    • 0035873740 scopus 로고    scopus 로고
    • The role of Sis1 in the maintenance of the [RNQ+] prion
    • Sondheimer, N.; Lopez, N.; Craig, E.A.; Lindquist, S. The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J., 2001, 20(10), 2435-2442.
    • (2001) EMBO J , vol.20 , Issue.10 , pp. 2435-2442
    • Sondheimer, N.1    Lopez, N.2    Craig, E.A.3    Lindquist, S.4
  • 107
    • 1942518319 scopus 로고    scopus 로고
    • Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding
    • Jones, G.; Song, Y.; Chung, S.; Masison, D.C. Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol. Cell. Biol., 2004, 24(9), 3928-3937.
    • (2004) Mol. Cell. Biol , vol.24 , Issue.9 , pp. 3928-3937
    • Jones, G.1    Song, Y.2    Chung, S.3    Masison, D.C.4
  • 108
    • 34250311267 scopus 로고    scopus 로고
    • Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae
    • Kryndushkin, D.; Wickner, R.B. Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae. Mol. Biol. Cell., 2007, 18(6), 2149-2154.
    • (2007) Mol. Biol. Cell , vol.18 , Issue.6 , pp. 2149-2154
    • Kryndushkin, D.1    Wickner, R.B.2
  • 109
    • 34249689651 scopus 로고    scopus 로고
    • Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils
    • Lian, H.Y.; Zhang, H.; Zhang, Z.R.; Loovers, H.M.; Jones, G.W.; Rowling, P.J.; Itzhaki, L.S.; Zhou, J.M.; Perrett, S. Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils. J. Biol. Chem., 2007, 282(16), 11931-11940.
    • (2007) J. Biol. Chem , vol.282 , Issue.16 , pp. 11931-11940
    • Lian, H.Y.1    Zhang, H.2    Zhang, Z.R.3    Loovers, H.M.4    Jones, G.W.5    Rowling, P.J.6    Itzhaki, L.S.7    Zhou, J.M.8    Perrett, S.9
  • 110
    • 37249063043 scopus 로고    scopus 로고
    • The role of Sse1 in the de Novo formation and variant determination of the [PSI+] prion
    • Fan, Q.; Park, K.W.; Du, Z.; Morano, K.A.; Li, L. The role of Sse1 in the de Novo formation and variant determination of the [PSI+] prion. Genetics, 2007, 177(3), 1583-1593.
    • (2007) Genetics , vol.177 , Issue.3 , pp. 1583-1593
    • Fan, Q.1    Park, K.W.2    Du, Z.3    Morano, K.A.4    Li, L.5
  • 111
    • 33644555537 scopus 로고    scopus 로고
    • Molecular chaperones and the assembly of the prion Sup35p, an in vitro study
    • Krzewska, J.; Melki, R. Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J., 2006, 25(4), 822- 833.
    • (2006) EMBO J , vol.25 , Issue.4 , pp. 822-833
    • Krzewska, J.1    Melki, R.2
  • 112
    • 33746405081 scopus 로고    scopus 로고
    • Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
    • Shorter, J.; Lindquist, S. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol. Cell., 2006, 23(3), 425-438.
    • (2006) Mol. Cell , vol.23 , Issue.3 , pp. 425-438
    • Shorter, J.1    Lindquist, S.2
  • 113
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • Polier, S.; Dragovic, Z.; Hartl, F.U.; Bracher, A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell, 2008, 133(6), 1068-1079.
    • (2008) Cell , vol.133 , Issue.6 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 115
    • 55949092734 scopus 로고    scopus 로고
    • Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity
    • Andreasson, C.; Fiaux, J.; Rampelt, H.; Druffel-Augustin, S.; Bukau, B. Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc. Natl. Acad. Sci. US A, 2008, 105(43), 16519-16524.
    • (2008) Proc. Natl. Acad. Sci. US A , vol.105 , Issue.43 , pp. 16519-16524
    • Andreasson, C.1    Fiaux, J.2    Rampelt, H.3    Druffel-Augustin, S.4    Bukau, B.5
  • 116
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B.; Weissman, J.; Horwich, A. Molecular chaperones and protein quality control. Cell, 2006, 125(3), 443-451.
    • (2006) Cell , vol.125 , Issue.3 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3


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