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Volumn 62, Issue 6, 2005, Pages 670-684

Hsp70 chaperones: Cellular functions and molecular mechanism

Author keywords

Chaperones; DnaJ; DnaK; Heat shock proteins; Hsp70; Protein folding; Quality control

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BAG 1 PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70;

EID: 17044387386     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-4464-6     Document Type: Review
Times cited : (2284)

References (128)
  • 1
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • Bukau B., Deuerling E., Pfund C. and Craig E. A. (2000) Getting newly synthesized proteins into shape. Cell 101: 119-122
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 2
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F. U. and 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
  • 3
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young J. C., Barral J. M. and Ulrich Hartl F. (2003) More than folding: localized functions of cytosolic chaperones. Trends. Biochem. Sci. 28: 541-547
    • (2003) Trends. Biochem. Sci. , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich Hartl, F.3
  • 4
  • 5
    • 0035715285 scopus 로고    scopus 로고
    • Hsp70 proteins in protein translocation
    • Ryan M. T. and Pfanner N. (2002) Hsp70 proteins in protein translocation. Adv. Protein Chem. 59: 223-242
    • (2002) Adv. Protein Chem. , vol.59 , pp. 223-242
    • Ryan, M.T.1    Pfanner, N.2
  • 6
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt W. B. and Toft D. O. (2003) Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228: 111-133
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 7
    • 0001979876 scopus 로고    scopus 로고
    • Control of hormone receptor function by molecular chaperones and folding catalysts
    • Bukau B. (ed.), Harwood Academic Publishers, Amsterdam
    • Toft D. O. (1999) Control of hormone receptor function by molecular chaperones and folding catalysts. In: Molecular Chaperones and Folding Catalysts. Regulation, Cellular Function and Mechanism, pp. 313-327, Bukau B. (ed.), Harwood Academic Publishers, Amsterdam
    • (1999) Molecular Chaperones and Folding Catalysts. Regulation, Cellular Function and Mechanism , pp. 313-327
    • Toft, D.O.1
  • 8
    • 0035783169 scopus 로고    scopus 로고
    • Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • Ben-Zvi A. P. and Goloubinoff P. (2001) Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J. Struct. Biol. 135: 84-93
    • (2001) J. Struct. Biol. , vol.135 , pp. 84-93
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 10
    • 0033783190 scopus 로고    scopus 로고
    • Molecular basis for interactions of the DnaK chaperone with substrates
    • Mayer M. P., Rüdiger S. and Bukau B. (2000) Molecular basis for interactions of the DnaK chaperone with substrates. Biol. Chem. 381: 877-885
    • (2000) Biol. Chem. , vol.381 , pp. 877-885
    • Mayer, M.P.1    Rüdiger, S.2    Bukau, B.3
  • 11
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?
    • Slepenkov S. V. and Witt S. N. (2002) The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? Mol. Microbiol. 45: 1197-1206
    • (2002) Mol. Microbiol. , vol.45 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 12
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover J. R. and 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
  • 13
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P., Mogk A., Peres Ben Zvi A., Tomoyasu T. and Bukau B. (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96: 13732-13737
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Peres Ben Zvi, A.3    Tomoyasu, T.4    Bukau, B.5
  • 14
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and C1pB chaperones
    • Motohashi K., Watanabe Y., Yohda M. and Yoshida M. (1999) Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and C1pB chaperones. Proc. Natl. Acad. Sci. USA 96: 7184-7189
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 15
    • 0034647887 scopus 로고    scopus 로고
    • Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
    • Diamant S., Peres Ben-Zvi A., Bukau B. and Goloubinoff P. (2000) Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 275: 21107-21113
    • (2000) J. Biol. Chem. , vol.275 , pp. 21107-21113
    • Diamant, S.1    Peres Ben-Zvi, A.2    Bukau, B.3    Goloubinoff, P.4
  • 16
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones
    • Ben-Zvi A., De Los Rios P., Dietler G. and Goloubinoff P. (2004) Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones. J. Biol. Chem. 279: 37298-37303
    • (2004) J. Biol. Chem. , vol.279 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los Rios, P.2    Dietler, G.3    Goloubinoff, P.4
  • 17
    • 0030982641 scopus 로고    scopus 로고
    • The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase
    • Pratt W. B. (1997) The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase. Annu. Rev. Pharmacol. Toxicol. 37: 297-326
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 297-326
    • Pratt, W.B.1
  • 18
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jäättelä M. (1999) Escaping cell death: survival proteins in cancer. Exp. Cell. Res. 248: 30-43
    • (1999) Exp. Cell. Res. , vol.248 , pp. 30-43
    • Jäättelä, M.1
  • 19
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C. and Morimoto R. I. (2000) Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer. Inst. 92: 1564-1572
    • (2000) J. Natl. Cancer. Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 20
    • 0037059040 scopus 로고    scopus 로고
    • Chaperoning brain degeneration
    • Bonini N. M. (2002) Chaperoning brain degeneration. Proc. Natl. Acad. Sci. USA 99 Suppl. 4: 16407-16411
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.4 SUPPL. , pp. 16407-16411
    • Bonini, N.M.1
  • 21
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira H., Breuer P., Hayer-Hartl M. K. and Hartl F. U. (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc. Natl. Acad. Sci. USA 99 Suppl. 4: 16412-16418
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.4 SUPPL. , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 22
    • 0347122087 scopus 로고    scopus 로고
    • Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo
    • Millar D. G., Garza K. M., Odermatt B., Elford A. R., Ono N., Li, Z. et al. (2003) Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo. Nat. Med. 9: 1469-1476
    • (2003) Nat. Med. , vol.9 , pp. 1469-1476
    • Millar, D.G.1    Garza, K.M.2    Odermatt, B.3    Elford, A.R.4    Ono, N.5    Li, Z.6
  • 23
    • 17044384880 scopus 로고    scopus 로고
    • Recruitment of Hsp70 chaperones: A crucial part of viral survival strategies
    • 9 Jul. [Epub ahead of print]
    • Mayer M. P. (2004) Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies. Rev. Physiol. Biochem. Pharmacol. 9 Jul. [Epub ahead of print]
    • (2004) Rev. Physiol. Biochem. Pharmacol.
    • Mayer, M.P.1
  • 24
    • 0036084783 scopus 로고    scopus 로고
    • Heat shock proteins: Modifying factors in physiological stress responses and acquired thermotolerance
    • Kregel K. C. (2002) Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J. Appl. Physiol. 92: 2177-2186
    • (2002) J. Appl. Physiol. , vol.92 , pp. 2177-2186
    • Kregel, K.C.1
  • 25
    • 3042662113 scopus 로고    scopus 로고
    • In silico proteome analysis to facilitate proteomics experiments using mass spectrometry
    • Cagney G., Amiri S., Premawaradena T., Lindo M. and Emili A. (2003) In silico proteome analysis to facilitate proteomics experiments using mass spectrometry. Proteome Sci 1: 5
    • (2003) Proteome Sci. , vol.1 , pp. 5
    • Cagney, G.1    Amiri, S.2    Premawaradena, T.3    Lindo, M.4    Emili, A.5
  • 26
    • 0035131701 scopus 로고    scopus 로고
    • A subset of tumor-derived mutant forms of p53 down-regulate p63 and p73 through a direct interaction with the p53 core domain
    • Gaiddon C., Lokshin M., Ahn J., Zhang T. and Prives C. (2001) A subset of tumor-derived mutant forms of p53 down-regulate p63 and p73 through a direct interaction with the p53 core domain. Mol. Cell. Biol. 21: 1874-1887
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1874-1887
    • Gaiddon, C.1    Lokshin, M.2    Ahn, J.3    Zhang, T.4    Prives, C.5
  • 27
    • 0035890265 scopus 로고    scopus 로고
    • Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53
    • King F. W., Wawrzynow A., Hohfeld J. and Zylicz M. (2001) Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53. EMBO J. 20: 6297-6305.
    • (2001) EMBO J. , vol.20 , pp. 6297-6305
    • King, F.W.1    Wawrzynow, A.2    Hohfeld, J.3    Zylicz, M.4
  • 28
    • 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., and Cyr, D. M. (1999) The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J. 18: 1492-1505
    • (1999) EMBO J. , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 29
    • 0035918258 scopus 로고    scopus 로고
    • Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis
    • Shinder G. A., Lacourse M. C., Minotti S. and Durham, H. D. (2001) Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J. Biol. Chem. 276: 12791-12796
    • (2001) J. Biol. Chem. , vol.276 , pp. 12791-12796
    • Shinder, G.A.1    Lacourse, M.C.2    Minotti, S.3    Durham, H.D.4
  • 30
    • 0032754456 scopus 로고    scopus 로고
    • Natural hyperthermia and expression of the heat shock protein Hsp70 affect developmental abnormalities in Drosophila melanogaster
    • Roberts S. P. and Feder M. E. (1999) Natural hyperthermia and expression of the heat shock protein Hsp70 affect developmental abnormalities in Drosophila melanogaster. Oecologia 121: 323-329
    • (1999) Oecologia , vol.121 , pp. 323-329
    • Roberts, S.P.1    Feder, M.E.2
  • 31
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford S. L. and Lindquist S. (1998) Hsp90 as a capacitor for morphological evolution. Nature 396: 336-342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 32
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch C., Sangster T. A. and Lindquist S. (2002) Hsp90 as a capacitor of phenotypic variation. Nature 417: 618-624
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 33
    • 0027372622 scopus 로고
    • Impaired gene transcription and nuclear protein kinase C activation in the brain and liver of aged rats
    • Rogue P. J., Ritz M. F. and Malviya A. N. (1993) Impaired gene transcription and nuclear protein kinase C activation in the brain and liver of aged rats. FEBS Lett. 334: 351-354
    • (1993) FEBS Lett. , vol.334 , pp. 351-354
    • Rogue, P.J.1    Ritz, M.F.2    Malviya, A.N.3
  • 34
    • 0035996805 scopus 로고    scopus 로고
    • Age-related decrease in the inducibility of heat-shock protein 70 in human peripheral blood mononuclear cells
    • Njemini R., Abeele M. V., Demanet C., Lambert M., Vandebosch S. and Mets T. (2002) Age-related decrease in the inducibility of heat-shock protein 70 in human peripheral blood mononuclear cells. J. Clin. Immunol. 22: 195-205
    • (2002) J. Clin. Immunol. , vol.22 , pp. 195-205
    • Njemini, R.1    Abeele, M.V.2    Demanet, C.3    Lambert, M.4    Vandebosch, S.5    Mets, T.6
  • 35
    • 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. and Cyr D. M. (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 3: 100-105
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 36
    • 3042817421 scopus 로고    scopus 로고
    • CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70
    • Urushitani M., Kurisu J., Tateno M., Hatakeyama S., Nakayama K., Kato S. et al. (2004) CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70. J. Neurochem. 90: 231-244
    • (2004) J. Neurochem. , vol.90 , pp. 231-244
    • Urushitani, M.1    Kurisu, J.2    Tateno, M.3    Hatakeyama, S.4    Nakayama, K.5    Kato, S.6
  • 37
    • 0029922120 scopus 로고    scopus 로고
    • C-terminal trimerization, but not N-terminal trimerization, of the reoviras cell attachment protein Is a posttranslational and Hsp70/ATP-dependent process
    • Leone G., Coffey M. C., Gilmore R., Duncan R., Maybaum L. and Lee P. W. (1996) C-terminal trimerization, but not N-terminal trimerization, of the reoviras cell attachment protein Is a posttranslational and Hsp70/ATP-dependent process. J. Biol. Chem. 271: 8466-8471
    • (1996) J. Biol. Chem. , vol.271 , pp. 8466-8471
    • Leone, G.1    Coffey, M.C.2    Gilmore, R.3    Duncan, R.4    Maybaum, L.5    Lee, P.W.6
  • 38
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young J. C., Hoogenraad N. J. and Hartl F. U. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112: 41-50
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 39
    • 0036479226 scopus 로고    scopus 로고
    • Co-translational folding of caspase-activated DNase with Hsp70, Hsp40 and inhibitor of caspase-activated DNase
    • Sakahira H. and Nagata S. (2002) Co-translational folding of caspase-activated DNase with Hsp70, Hsp40 and inhibitor of caspase-activated DNase. J. Biol. Chem. 277: 3364-3370
    • (2002) J. Biol. Chem. , vol.277 , pp. 3364-3370
    • Sakahira, H.1    Nagata, S.2
  • 40
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättelä M., Wissing D., Kokholm K., Kallunki T. and Egeblad M. (1998) Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 17: 6124-6134
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jäättelä, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 41
    • 0034608892 scopus 로고    scopus 로고
    • Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2
    • Nylandsted J., Rohde M., Brand K., Bastholm L., Elling F. and Jaattela M. (2000) Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2. Proc. Natl. Acad. Sci. USA 97: 7871-7876
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7871-7876
    • Nylandsted, J.1    Rohde, M.2    Brand, K.3    Bastholm, L.4    Elling, F.5    Jaattela, M.6
  • 43
    • 0032527007 scopus 로고    scopus 로고
    • The expression of heat shock protein 70 decreases with cellular senescence in vitro and in cells derived from young and old human subjects
    • Gutsmann-Conrad A., Heydari A. R., You S. and Richardson A. (1998) The expression of heat shock protein 70 decreases with cellular senescence in vitro and in cells derived from young and old human subjects. Exp. Cell. Res. 241: 404-413
    • (1998) Exp. Cell. Res. , vol.241 , pp. 404-413
    • Gutsmann-Conrad, A.1    Heydari, A.R.2    You, S.3    Richardson, A.4
  • 44
    • 6944252403 scopus 로고    scopus 로고
    • Characterization of the hsp70 response in lymphoblasts from aged and centenarian subjects and differential effects of in vitro zinc supplementation
    • Ambra R., Mocchegiani E., Giacconi R., Canali R., Rinna A., Malavolta M. et al. (2004) Characterization of the hsp70 response in lymphoblasts from aged and centenarian subjects and differential effects of in vitro zinc supplementation. Exp. Gerontol. 39: 1475-1484
    • (2004) Exp. Gerontol. , vol.39 , pp. 1475-1484
    • Ambra, R.1    Mocchegiani, E.2    Giacconi, R.3    Canali, R.4    Rinna, A.5    Malavolta, M.6
  • 45
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty K. M., Deluca-Flaherty C. and McKay D. B. (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
  • 46
    • 3142677815 scopus 로고    scopus 로고
    • The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains
    • Zhang Y. and Zuiderweg E. R. (2004) The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains. Proc. Natl. Acad. Sci. USA 101: 10272-10277
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10272-10277
    • Zhang, Y.1    Zuiderweg, E.R.2
  • 47
    • 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. and Mayer, M. P. (2001) Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J. Biol. Chem. 276: 32538-32544
    • (2001) J. Biol. Chem. , vol.276 , pp. 32538-32544
    • Gässler, C.S.1    Wiederkehr, T.2    Brehmer, D.3    Bukau, B.4    Mayer, M.P.5
  • 49
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai A. W. and McMacken R. (1996) A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271: 11236-11246
    • (1996) J. Biol. Chem. , vol.271 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 50
    • 0030986955 scopus 로고    scopus 로고
    • Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets
    • Barouch W., Prasad K., Greene L. and Eisenberg E. (1997) Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets. Biochemistry 36: 4303-4308
    • (1997) Biochemistry , vol.36 , pp. 4303-4308
    • Barouch, W.1    Prasad, K.2    Greene, L.3    Eisenberg, E.4
  • 52
    • 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. and Zylicz M. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88: 2874-2878
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 53
    • 0028170215 scopus 로고
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for a replication
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for A replication. J. Biol. Chem. 269: 5446-5451
    • (1994) J. Biol. Chem. , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 54
    • 0030044799 scopus 로고    scopus 로고
    • A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32
    • Gamer J., Multhaup G., Tomoyasu T., McCarty J. S., Rudiger S., Schonfeld H. J. et al. (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 15: 607-617
    • (1996) EMBO J. , vol.15 , pp. 607-617
    • Gamer, J.1    Multhaup, G.2    Tomoyasu, T.3    McCarty, J.S.4    Rudiger, S.5    Schonfeld, H.J.6
  • 56
    • 0032214832 scopus 로고    scopus 로고
    • J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
    • Misselwitz B., Staeck O. and Rapoport T. A. (1998) J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol. Cell. 2: 593-603
    • (1998) Mol. Cell. , vol.2 , pp. 593-603
    • Misselwitz, B.1    Staeck, O.2    Rapoport, T.A.3
  • 57
    • 0034678084 scopus 로고    scopus 로고
    • Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli
    • Silberg J. J. and Vickery L. E. (2000) Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 275: 7779-7786
    • (2000) J. Biol. Chem. , vol.275 , pp. 7779-7786
    • Silberg, J.J.1    Vickery, L.E.2
  • 58
    • 11144224094 scopus 로고    scopus 로고
    • Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU
    • Silberg J. J., Tapley T. L., Hoff K. G. and Vickery L. E. (2004) Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. J. Biol. Chem. 279: 53924-53931
    • (2004) J. Biol. Chem. , vol.279 , pp. 53924-53931
    • Silberg, J.J.1    Tapley, T.L.2    Hoff, K.G.3    Vickery, L.E.4
  • 60
    • 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.-U. and 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.-U.4    Kuriyan, J.5
  • 61
    • 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. and Moarefi I. (2001) Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291: 1553-1557.
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 62
    • 0035069393 scopus 로고    scopus 로고
    • Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein
    • Briknarova K., Takayama S., Brive L., Havert M. L., Knee D. A., Velasco J. et al. (2001) Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Nat. Struct. Biol. 8: 349-352
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 349-352
    • Briknarova, K.1    Takayama, S.2    Brive, L.3    Havert, M.L.4    Knee, D.A.5    Velasco, J.6
  • 64
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • Takayama S. and Reed J. C. (2001) Molecular chaperone targeting and regulation by BAG family proteins. Nat. Cell. Biol. 3: E237-241
    • (2001) Nat. Cell. Biol. , vol.3
    • Takayama, S.1    Reed, J.C.2
  • 65
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Höhfeld J. and Jentsch S. (1997) GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16: 6209-6216
    • (1997) EMBO J. , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 67
    • 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. and 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
  • 68
    • 0347033285 scopus 로고    scopus 로고
    • BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP
    • Chung K. T., Shen Y. and Hendershot L. M. (2002) BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J. Biol. Chem. 277: 47557-47563
    • (2002) J. Biol. Chem. , vol.277 , pp. 47557-47563
    • Chung, K.T.1    Shen, Y.2    Hendershot, L.M.3
  • 70
    • 0030872849 scopus 로고    scopus 로고
    • A novel subfamily of Hsp70s in the endoplasmic reticulum
    • Craven R. A., Tyson J. R. and Stirling C. J. (1997) A novel subfamily of Hsp70s in the endoplasmic reticulum. Trends Cell Biol. 7: 277-282
    • (1997) Trends Cell Biol. , vol.7 , pp. 277-282
    • Craven, R.A.1    Tyson, J.R.2    Stirling, C.J.3
  • 71
    • 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. and Stirling C. J. (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
  • 72
    • 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. and Brodsky J. L. (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
  • 73
    • 0036275663 scopus 로고    scopus 로고
    • Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssalp
    • Kabani M., Beckerich J. M. and Brodsky J. L. (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssalp. 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
  • 74
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • Zhu X., Zhao X., Burkholder W. F., Gragerov A., Ogata C. M., Gottesman M. et al. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272: 1606-1614
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.1    Zhao, X.2    Burkholder, W.F.3    Gragerov, A.4    Ogata, C.M.5    Gottesman, M.6
  • 75
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüdiger S., Germeroth L., Schneider-Mergener J. and Bukau B. (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16: 1501-1507
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 76
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ chaperone as scanning factor for the DnaK chaperone
    • Rüdiger S., Schneider-Mergener J. and Bukau B. (2001) Its substrate specificity characterizes the DnaJ chaperone as scanning factor for the DnaK chaperone. EMBO J. 20: 1-9
    • (2001) EMBO J. , vol.20 , pp. 1-9
    • Rüdiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 77
    • 3142653172 scopus 로고    scopus 로고
    • Preferential substrate binding orientation by the molecular chaperone HscA
    • Tapley T. L. and Vickery L. E. (2004) Preferential substrate binding orientation by the molecular chaperone HscA. J. Biol. Chem. 279: 28435-28442
    • (2004) J. Biol. Chem. , vol.279 , pp. 28435-28442
    • Tapley, T.L.1    Vickery, L.E.2
  • 78
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • Cupp-Vickery J. R., Peterson J. C., Ta D. T. and Vickery L. E. (2004) Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. J. Mol. Biol. 342: 1265-1278
    • (2004) J. Mol. Biol. , vol.342 , pp. 1265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 81
    • 0035920236 scopus 로고    scopus 로고
    • Characterization of a lidless form of the molecular chaperone DnaK: Deletion of the lid increases peptide on- And off-rate constants
    • Buczynski G., Slepenkov S. V., Sehorn M. G. and Witt S. N. (2001) Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants. J. Biol. Chem. 276: 27231-27236
    • (2001) J. Biol. Chem. , vol.276 , pp. 27231-27236
    • Buczynski, G.1    Slepenkov, S.V.2    Sehorn, M.G.3    Witt, S.N.4
  • 82
    • 0037044301 scopus 로고    scopus 로고
    • Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state
    • Slepenkov S. V. and Witt S. N. (2002) Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state. Biochemistry 41: 12224-12235
    • (2002) Biochemistry , vol.41 , pp. 12224-12235
    • Slepenkov, S.V.1    Witt, S.N.2
  • 83
    • 0034397884 scopus 로고    scopus 로고
    • Modulation of the specificity of the Hsp70 chaperone DnaK by altering a hydrophobic arch
    • Rüdiger S., Mayer M. P., Schneider-Mergener J. and Bukau B. (2000) Modulation of the specificity of the Hsp70 chaperone DnaK by altering a hydrophobic arch. J. Mol. Biol. 304: 245-251
    • (2000) J. Mol. Biol. , vol.304 , pp. 245-251
    • Rüdiger, S.1    Mayer, M.P.2    Schneider-Mergener, J.3    Bukau, B.4
  • 84
    • 0032474433 scopus 로고    scopus 로고
    • NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: A preview of chaperone-protein interaction
    • Wang H., Kurochkin A. V., Pang Y., Hu W., Flynn G. C. and Zuiderweg E. R. P. (1998) NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Biochemistry 37: 7929-7940
    • (1998) Biochemistry , vol.37 , pp. 7929-7940
    • Wang, H.1    Kurochkin, A.V.2    Pang, Y.3    Hu, W.4    Flynn, G.C.5    Zuiderweg, E.R.P.6
  • 85
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn G. C., Chappell T. G. and Rothman J. E. (1989) Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245: 385-390
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 87
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid D., Baici A., Gehring H. and Christen P. (1994) Kinetics of molecular chaperone action. Science 263: 971-973
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 88
    • 0032564386 scopus 로고    scopus 로고
    • Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ
    • Pierpaoli E. V., Gisler S. M. and Christen P. (1998) Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ. Biochemistry 37: 16741-16748
    • (1998) Biochemistry , vol.37 , pp. 16741-16748
    • Pierpaoli, E.V.1    Gisler, S.M.2    Christen, P.3
  • 89
    • 0029911568 scopus 로고    scopus 로고
    • Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone
    • Takeda S. and McKay D. B. (1996) Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone. Biochemistry 35: 4636-4644
    • (1996) Biochemistry , vol.35 , pp. 4636-4644
    • Takeda, S.1    McKay, D.B.2
  • 90
    • 0032480794 scopus 로고    scopus 로고
    • The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change
    • Sousa M. C. and McKay D. B. (1998) The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change. Biochemistry 37: 15392-15399
    • (1998) Biochemistry , vol.37 , pp. 15392-15399
    • Sousa, M.C.1    McKay, D.B.2
  • 91
    • 0033594405 scopus 로고    scopus 로고
    • Molecular chaperones: How J domains turn on Hsp70s
    • Kelley W. L. (1999) Molecular chaperones: how J domains turn on Hsp70s. Curr. Biol. 9: R305-308
    • (1999) Curr. Biol. , vol.9
    • Kelley, W.L.1
  • 92
    • 0032103439 scopus 로고    scopus 로고
    • The J-domain family and the recruitment of chaperone power
    • Kelley W. L. (1998) The J-domain family and the recruitment of chaperone power. Trends Biochem. Sci. 23: 222-227
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 222-227
    • Kelley, W.L.1
  • 93
    • 0031925150 scopus 로고    scopus 로고
    • Hsp70 Chaperone systems: Diversity of cellular functions and mechanism of action
    • Mayer M. and Bukau B. (1998) Hsp70 Chaperone systems: diversity of cellular functions and mechanism of action. Biol. Chem. 379: 261-268
    • (1998) Biol. Chem. , vol.379 , pp. 261-268
    • Mayer, M.1    Bukau, B.2
  • 94
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham M. I. E. and Caplan A. J. (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chap. 3: 28-36
    • (1998) Cell Stress Chap. , vol.3 , pp. 28-36
    • Cheetham, M.I.E.1    Caplan, A.J.2
  • 95
    • 0242414663 scopus 로고    scopus 로고
    • The roles of the two zinc binding sites in DnaJ
    • Linke K., Wolfram T., Bussemer J. and Jakob U. (2003) The roles of the two zinc binding sites in DnaJ. J. Biol. Chem. 278: 44457-44466
    • (2003) J. Biol. Chem. , vol.278 , pp. 44457-44466
    • Linke, K.1    Wolfram, T.2    Bussemer, J.3    Jakob, U.4
  • 96
    • 0030935256 scopus 로고    scopus 로고
    • The T/t common exon of simian virus 40, JC and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone
    • Kelley W. L. and Georgopoulos C. (1997) The T/t common exon of simian virus 40, JC and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone. Proc. Natl. Acad. Sci. USA 94: 3679-3684
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3679-3684
    • Kelley, W.L.1    Georgopoulos, C.2
  • 97
    • 0033534588 scopus 로고    scopus 로고
    • An evohitionarily conserved family of Hsp70/Ffsc70 molecular chaperone regulators
    • Takayama S., Xie Z. and Reed J. C. (1999) An evohitionarily conserved family of Hsp70/Ffsc70 molecular chaperone regulators. J. Biol. Chem. 274: 781-786
    • (1999) J. Biol. Chem. , vol.274 , pp. 781-786
    • Takayama, S.1    Xie, Z.2    Reed, J.C.3
  • 98
    • 0035282773 scopus 로고    scopus 로고
    • Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper
    • Thress K., Song J., Morimoto R. I. and Kornbluth S. (2001) Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper. EMBO J. 20: 1033-1041
    • (2001) EMBO J. , vol.20 , pp. 1033-1041
    • Thress, K.1    Song, J.2    Morimoto, R.I.3    Kornbluth, S.4
  • 99
    • 0036208624 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain
    • Miki K. and Eddy E. M. (2002) Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain. Mol. Cell. Biol. 22: 2536-2543
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2536-2543
    • Miki, K.1    Eddy, E.M.2
  • 100
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1 - A nucleotide exchange factor of Hsc70 with multiple cellular functions
    • Alberti S., Esser C. and Hollfeld J. (2003) BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chap. 8: 225-231
    • (2003) Cell Stress Chap. , vol.8 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Hollfeld, J.3
  • 101
    • 0842281543 scopus 로고    scopus 로고
    • The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains
    • Brockmann C., Leitner D., Labudde D., Diehl A., Sievert V., Bussow K. et al. (2004) The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains. FEBS Lett. 558: 101-106
    • (2004) FEBS Lett. , vol.558 , pp. 101-106
    • Brockmann, C.1    Leitner, D.2    Labudde, D.3    Diehl, A.4    Sievert, V.5    Bussow, K.6
  • 102
    • 1642527873 scopus 로고    scopus 로고
    • Biological activities of HAP46/BAG-1. The HAP46/BAG-1 protein: Regulator of HSP70 chaperones, DNA-binding protein and stimulator of transcription
    • Gehring U. (2004) Biological activities of HAP46/BAG-1. The HAP46/BAG-1 protein: regulator of HSP70 chaperones, DNA-binding protein and stimulator of transcription. EMBO Rep. 5: 148-153
    • (2004) EMBO Rep. , vol.5 , pp. 148-153
    • Gehring, U.1
  • 103
    • 0037114358 scopus 로고    scopus 로고
    • What's in the 'BAG'? - A functional domain analysis of the BAG-family proteins
    • Doong H., Vrailas A. and Kolm E. C. (2002) What's in the 'BAG'? - a functional domain analysis of the BAG-family proteins. Cancer Lett. 188: 25-32
    • (2002) Cancer Lett. , vol.188 , pp. 25-32
    • Doong, H.1    Vrailas, A.2    Kolm, E.C.3
  • 104
    • 0032527616 scopus 로고    scopus 로고
    • Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines
    • Takayama S., Krajewski S., Krajewski M., Kitada S., Zapata J. M., Kochel K. et al. (1998) Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines. Cancer Res. 58: 3116-3131
    • (1998) Cancer Res. , vol.58 , pp. 3116-3131
    • Takayama, S.1    Krajewski, S.2    Krajewski, M.3    Kitada, S.4    Zapata, J.M.5    Kochel, K.6
  • 105
    • 0039598518 scopus 로고    scopus 로고
    • Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function
    • Lüders J., Demand J., Papp O. and Hohfeld J. (2000) Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function. J. Biol. Chem. 275: 14817-14823
    • (2000) J. Biol. Chem. , vol.275 , pp. 14817-14823
    • Lüders, J.1    Demand, J.2    Papp, O.3    Hohfeld, J.4
  • 106
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Luders J., Demand J. and Hohfeld J. (2000) The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275: 4613-4617
    • (2000) J. Biol. Chem. , vol.275 , pp. 4613-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 107
    • 0034745354 scopus 로고    scopus 로고
    • Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth
    • Song J., Takeda M. and Morimoto R. I. (2001) Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat. Cell Biol. 3: 276-282
    • (2001) Nat. Cell Biol. , vol.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 108
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Höhfeld J., Minami Y. and Hartl F. U. (1995) Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589-598
    • (1995) Cell , vol.83 , pp. 589-598
    • Höhfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 109
    • 0030671388 scopus 로고    scopus 로고
    • Proteins interacting with the molecular chaperone hsp70/hsc70: Physical associations and effects on refolding activity
    • Gebauer M., Zeiner M. and Gehring U. (1997) Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity. FEBS Lett. 417: 109-113
    • (1997) FEBS Lett. , vol.417 , pp. 109-113
    • Gebauer, M.1    Zeiner, M.2    Gehring, U.3
  • 110
    • 0034700318 scopus 로고    scopus 로고
    • hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1
    • Kanelakis K. C., Murphy P. J., Galigniana M. D., Morishima Y., Takayama S., Reed J. C. et al. (2000) hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1. Biochemistry 39: 14314-14321
    • (2000) Biochemistry , vol.39 , pp. 14314-14321
    • Kanelakis, K.C.1    Murphy, P.J.2    Galigniana, M.D.3    Morishima, Y.4    Takayama, S.5    Reed, J.C.6
  • 111
    • 0038642094 scopus 로고    scopus 로고
    • Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation
    • Lambert C. and Prange R. (2003) Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation. Proc. Natl. Acad. Sci. USA 100: 5199-5204
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5199-5204
    • Lambert, C.1    Prange, R.2
  • 112
    • 3042748160 scopus 로고    scopus 로고
    • The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor
    • Nelson G. M., Prapapanich V. Carrigan P. E., Roberts P. J., Riggs D. L. and Smith D. F. (2004) The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor. Mol. Endocrinol. 18: 1620-1630
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1620-1630
    • Nelson, G.M.1    Prapapanich, V.2    Carrigan, P.E.3    Roberts, P.J.4    Riggs, D.L.5    Smith, D.F.6
  • 114
    • 0024469206 scopus 로고
    • Isolation and characterization of STIl, a stress-inducible gene from Saccharomyces cerevisiae
    • Nicolet C. and Craig E. (1989) Isolation and characterization of STIl, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9: 3638-3646
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3638-3646
    • Nicolet, C.1    Craig, E.2
  • 115
    • 0027439595 scopus 로고
    • Identification of a 60-Kilodalton Stress-Related Protein, p60, which interacts with hsp90 and hsp70
    • Smith D. F., Sullivan W. P., Marion T. N., Zaitsu K., Madden B., McCormick, D. J. et al. (1993) Identification of a 60-Kilodalton Stress-Related Protein, p60, which interacts with hsp90 and hsp70. Mol. Cell. Biol. 13: 869-876
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 869-876
    • Smith, D.F.1    Sullivan, W.P.2    Marion, T.N.3    Zaitsu, K.4    Madden, B.5    McCormick, D.J.6
  • 116
    • 0034646511 scopus 로고    scopus 로고
    • Struture of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., et al. (2000) Struture 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    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6
  • 117
    • 0037470073 scopus 로고    scopus 로고
    • Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity
    • Odunuga O. O., Hornby J. A., Bies C., Zimmermann R., Pugh, D. J. and Blatch G. L. (2003) Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity. J Biol. Chem. 278: 6896-6904
    • (2003) J. Biol. Chem. , vol.278 , pp. 6896-6904
    • Odunuga, O.O.1    Hornby, J.A.2    Bies, C.3    Zimmermann, R.4    Pugh, D.J.5    Blatch, G.L.6
  • 118
    • 0034629150 scopus 로고    scopus 로고
    • The Hsp organizer protein Hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system
    • Morishima Y., Kanelakis K. C., Silverstein A. M., Dittmar K. D., Estrada L. and Pratt W. B. (2000) The Hsp organizer protein Hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system. J. Biol. Chem. 275: 6894-6900
    • (2000) J. Biol. Chem. , vol.275 , pp. 6894-6900
    • Morishima, Y.1    Kanelakis, K.C.2    Silverstein, A.M.3    Dittmar, K.D.4    Estrada, L.5    Pratt, W.B.6
  • 120
    • 0042815093 scopus 로고    scopus 로고
    • Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
    • Brychzy A., Rein T., Winklhofer K. F., Hartl F. U., Young J. C. and Obermann W. M. (2003) Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J. 22: 3613-3623
    • (2003) EMBO J. , vol.22 , pp. 3613-3623
    • Brychzy, A.1    Rein, T.2    Winklhofer, K.F.3    Hartl, F.U.4    Young, J.C.5    Obermann, W.M.6
  • 121
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C. A., Connell P., Wu Y., Hu Z., Thompson L. J., Yin, L. Y. et al. (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19: 4535-4545
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6
  • 122
    • 1642576077 scopus 로고    scopus 로고
    • Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity
    • Nikolay R., Wiederkehr T., Rist W., Kramer G., Mayer M. P. and Bukau B. (2004) Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J. Biol. Chem. 279: 2673-2678
    • (2004) J. Biol. Chem. , vol.279 , pp. 2673-2678
    • Nikolay, R.1    Wiederkehr, T.2    Rist, W.3    Kramer, G.4    Mayer, M.P.5    Bukau, B.6
  • 123
    • 0034756104 scopus 로고    scopus 로고
    • From the cradle to the grave: Molecular chaperones that may choose between folding and degradation
    • Höhfeld J., Cyr D. M. and Patterson C. (2001) From the cradle to the grave: molecular chaperones that may choose between folding and degradation. EMBO Rep. 2: 885-890
    • (2001) EMBO Rep. , vol.2 , pp. 885-890
    • Höhfeld, J.1    Cyr, D.M.2    Patterson, C.3
  • 124
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell P., Ballinger C. A., Jiang J., Wu Y., Thompson L. J., Hohfeld J. et al. (2001) The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell. Biol. 3: 93-96
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6
  • 125
    • 1542782162 scopus 로고    scopus 로고
    • Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP
    • Jiang J., Cyr D., Babbitt R. W., Sessa W. C. and Patterson C. (2003) Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP. J. Biol. Chem. 278: 49332-49341
    • (2003) J. Biol. Chem. , vol.278 , pp. 49332-49341
    • Jiang, J.1    Cyr, D.2    Babbitt, R.W.3    Sessa, W.C.4    Patterson, C.5
  • 126
    • 10744223839 scopus 로고    scopus 로고
    • CHIP activates HSF1 and confers protection against apoptosis and cellular stress
    • Dai Q., Zhang C., Wu Y., McDonough H., Whaley R. A., Godfrey V. et al. (2003) CHIP activates HSF1 and confers protection against apoptosis and cellular stress. EMBO J. 22: 5446-5458
    • (2003) EMBO J. , vol.22 , pp. 5446-5458
    • Dai, Q.1    Zhang, C.2    Wu, Y.3    McDonough, H.4    Whaley, R.A.5    Godfrey, V.6
  • 127
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia M., Szyperski T., Wall D., Georgopoulos C. and Wüthrich K. (1996) NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J. Mol. Biol. 260: 236-250
    • (1996) J. Mol. Biol. , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 128
    • 0345299781 scopus 로고    scopus 로고
    • The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
    • Li J., Qian X. and Sha B. (2003) The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 11: 1475-1483
    • (2003) Structure , vol.11 , pp. 1475-1483
    • Li, J.1    Qian, X.2    Sha, B.3


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