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Volumn 304, Issue 3, 2003, Pages 505-512

Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways

Author keywords

Apoptosis; Apoptosis inducing factor; Cytochrome c; Heat shock proteins; Mitochondria

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA CRYSTALLIN; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE 9; CHAPERONE; CYTOCHROME C; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; I KAPPA B; ISOPROTEIN; PROTEASOME; PROTEIN BCL 2; UBIQUITIN;

EID: 0037427476     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00623-5     Document Type: Article
Times cited : (329)

References (80)
  • 2
    • 0038668000 scopus 로고    scopus 로고
    • Escaping cell death: Survival proteins in cancer
    • Jaattela M. Escaping cell death: survival proteins in cancer. Exp. Cell Res. 248:1999;30-43.
    • (1999) Exp. Cell Res. , vol.248 , pp. 30-43
    • Jaattela, M.1
  • 3
    • 0028961801 scopus 로고
    • Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells
    • Jaattela M. Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells. Int. J. Cancer. 60:1995;689-693.
    • (1995) Int. J. Cancer , vol.60 , pp. 689-693
    • Jaattela, M.1
  • 5
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jaattela M., Wissing D., Kokholm K., Kallunki T., Egeblad M. Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 17:1998;6124-6134.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 7
    • 0032768772 scopus 로고    scopus 로고
    • Heat shock proteins as cellular lifeguards
    • Jaattela M. Heat shock proteins as cellular lifeguards. Ann. Med. 31:1999;261-271.
    • (1999) Ann. Med. , vol.31 , pp. 261-271
    • Jaattela, M.1
  • 8
    • 0025303147 scopus 로고
    • Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann R.P., Mizzen L.E., Welch W.J. Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science. 248:1990;850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 9
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70-kDa heat shock protein or its cytosolic cognate
    • Shi Y., Thomas J.O. The transport of proteins into the nucleus requires the 70-kDa heat shock protein or its cytosolic cognate. Mol. Cell. Biol. 12:1992;2186-2192.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2186-2192
    • Shi, Y.1    Thomas, J.O.2
  • 10
    • 0024268186 scopus 로고
    • 70-kDa heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria
    • Murakami H., Pain D., Blobel G. 70-kDa heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria. J. Cell Biol. 107:1988;2051-2057.
    • (1988) J. Cell Biol. , vol.107 , pp. 2051-2057
    • Murakami, H.1    Pain, D.2    Blobel, G.3
  • 12
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely P., Schnaider T., Soti C., Prohaszka Z., Nardai G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79:1998;129-168.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 13
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan D.F., Lindquist S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15:1995;3917-3925.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 14
    • 0026722373 scopus 로고
    • Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)
    • Shaknovich R., Shue G., Kohtz D.S. Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84). Mol. Cell. Biol. 12:1992;5059-5068.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5059-5068
    • Shaknovich, R.1    Shue, G.2    Kohtz, D.S.3
  • 15
    • 0028023828 scopus 로고
    • Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function
    • Hartson S.D., Matts R.L. Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function. Biochemistry. 33:1994;8912-8920.
    • (1994) Biochemistry , vol.33 , pp. 8912-8920
    • Hartson, S.D.1    Matts, R.L.2
  • 16
    • 0028227245 scopus 로고
    • The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex
    • Wartmann M., Davis R.J. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269:1994;6695-6701.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6695-6701
    • Wartmann, M.1    Davis, R.J.2
  • 17
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 18
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M., Graber S., Gaestel M., Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16:1997;221-229.
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 19
    • 0036092428 scopus 로고    scopus 로고
    • Size matters: Of the small HSP27 and its large oligomers
    • Garrido C. Size matters: of the small HSP27 and its large oligomers. Cell Death Differ. 9:2002;483-485.
    • (2002) Cell Death Differ. , vol.9 , pp. 483-485
    • Garrido, C.1
  • 20
    • 0034609765 scopus 로고    scopus 로고
    • Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo
    • Bruey J.M., Paul C., Fromentin A., Hilpert S., Arrigo A.P., Solary E., Garrido C. Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo. Oncogene. 19:2000;4855-4863.
    • (2000) Oncogene , vol.19 , pp. 4855-4863
    • Bruey, J.M.1    Paul, C.2    Fromentin, A.3    Hilpert, S.4    Arrigo, A.P.5    Solary, E.6    Garrido, C.7
  • 21
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron. 29:2001;15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 22
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson M.D., Weil M., Raff M.C. Programmed cell death in animal development. Cell. 88:1997;347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 23
    • 0033820092 scopus 로고    scopus 로고
    • Positive and negative regulation of apoptotic pathways by cytotoxic agents in hematological malignancies
    • Solary E., Droin N., Bettaieb A., Corcos L., Dimanche-Boitrel M.T., Garrido C. Positive and negative regulation of apoptotic pathways by cytotoxic agents in hematological malignancies. Leukemia. 14:2000;1833-1849.
    • (2000) Leukemia , vol.14 , pp. 1833-1849
    • Solary, E.1    Droin, N.2    Bettaieb, A.3    Corcos, L.4    Dimanche-Boitrel, M.T.5    Garrido, C.6
  • 24
    • 0344348821 scopus 로고    scopus 로고
    • Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis
    • Hu Y., Benedict M.A., Ding L., Nunez G. Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 18:1999;3586-3595.
    • (1999) EMBO J. , vol.18 , pp. 3586-3595
    • Hu, Y.1    Benedict, M.A.2    Ding, L.3    Nunez, G.4
  • 25
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 29
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 102:2000;33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 30
  • 31
    • 0029979079 scopus 로고    scopus 로고
    • Inconstant association between 27-kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin-protecting effect of Hsp27
    • Garrido C., Mehlen P., Fromentin A., Hammann A., Assem M., Arrigo A.P., Chauffert B. Inconstant association between 27-kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. The doxorubicin-protecting effect of Hsp27. Eur. J. Biochem. 237:1996;653-659.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 653-659
    • Garrido, C.1    Mehlen, P.2    Fromentin, A.3    Hammann, A.4    Assem, M.5    Arrigo, A.P.6    Chauffert, B.7
  • 32
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death
    • Mehlen P., Schulze-Osthoff K., Arrigo A.P. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J. Biol. Chem. 271:1996;16510-16514.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 33
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFα-induced cell death
    • Mehlen P., Kretz-Remy C., Preville X., Arrigo A.P. Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFα-induced cell death. EMBO J. 15:1996;2695-2706.
    • (1996) EMBO J. , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Kretz-Remy, C.2    Preville, X.3    Arrigo, A.P.4
  • 34
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie J.N., Lambert H., Hickey E., Weber L.A., Landry J. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol. Cell. Biol. 15:1995;505-516.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 38
    • 0034963578 scopus 로고    scopus 로고
    • Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c
    • Concannon C.G., Orrenius S., Samali A. Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c. Gene Expr. 9:2001;195-201.
    • (2001) Gene Expr. , vol.9 , pp. 195-201
    • Concannon, C.G.1    Orrenius, S.2    Samali, A.3
  • 40
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein αB-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • Kamradt M.C., Chen F., Cryns V.L. The small heat shock protein αB-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J. Biol. Chem. 276:2001;16059-16063.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 42
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach A., Sauvageot O., Carmichael J., Diaz-Latoud C., Arrigo A.P., Rubinsztein D.C. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet. 11:2002;1137-1151.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 43
    • 0033796051 scopus 로고    scopus 로고
    • Inhibition of Daxx-mediated apoptosis by heat shock protein 27
    • Charette S.J., Lavoie J.N., Lambert H., Landry J. Inhibition of Daxx-mediated apoptosis by heat shock protein 27. Mol. Cell. Biol. 20:2000;7602-7612.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7602-7612
    • Charette, S.J.1    Lavoie, J.N.2    Lambert, H.3    Landry, J.4
  • 44
    • 0032479150 scopus 로고    scopus 로고
    • Heat shock protein 72 modulates pathways of stress-induced apoptosis
    • Buzzard K.A., Giaccia A.J., Killender M., Anderson R.L. Heat shock protein 72 modulates pathways of stress-induced apoptosis. J. Biol. Chem. 273:1998;17147-17153.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17147-17153
    • Buzzard, K.A.1    Giaccia, A.J.2    Killender, M.3    Anderson, R.L.4
  • 45
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation
    • Li C.Y., Lee J.S., Ko Y.G., Kim J.I., Seo J.S. Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J. Biol. Chem. 275:2000;25665-25671.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25665-25671
    • Li, C.Y.1    Lee, J.S.2    Ko, Y.G.3    Kim, J.I.4    Seo, J.S.5
  • 49
    • 0034713335 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits caspase-dependent and -independent apoptosis in Jurkat T cells
    • Creagh E.M., Carmody R.J., Cotter T.G. Heat shock protein 70 inhibits caspase-dependent and -independent apoptosis in Jurkat T cells. Exp. Cell Res. 257:2000;58-66.
    • (2000) Exp. Cell Res. , vol.257 , pp. 58-66
    • Creagh, E.M.1    Carmody, R.J.2    Cotter, T.G.3
  • 51
    • 0031755888 scopus 로고    scopus 로고
    • Increased expression of heat shock protein-70 protects A549 cells against hyperoxia
    • Wong H.R., Menendez I.Y., Ryan M.A., Denenberg A.G., Wispe J.R. Increased expression of heat shock protein-70 protects A549 cells against hyperoxia. Am. J. Physiol. 275:1998;L836-L841.
    • (1998) Am. J. Physiol. , vol.275
    • Wong, H.R.1    Menendez, I.Y.2    Ryan, M.A.3    Denenberg, A.G.4    Wispe, J.R.5
  • 52
    • 0035254227 scopus 로고    scopus 로고
    • Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase
    • Park H.S., Lee J.S., Huh S.H., Seo J.S., Choi E.J. Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J. 20:2001;446-456.
    • (2001) EMBO J. , vol.20 , pp. 446-456
    • Park, H.S.1    Lee, J.S.2    Huh, S.H.3    Seo, J.S.4    Choi, E.J.5
  • 53
    • 0032932192 scopus 로고    scopus 로고
    • Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: A novel pathway controlled by HSP72
    • Meriin A.B., Yaglom J.A., Gabai V.L., Zon L., Ganiatsas S., Mosser D.D., Sherman M.Y. Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72. Mol. Cell. Biol. 19:1999;2547-2555.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2547-2555
    • Meriin, A.B.1    Yaglom, J.A.2    Gabai, V.L.3    Zon, L.4    Ganiatsas, S.5    Mosser, D.D.6    Sherman, M.Y.7
  • 54
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C., Morimoto R.I. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Inst. 92:2000;1564-1572.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 55
    • 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., Morimoto R.I. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat. Cell Biol. 3:2001;276-282.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 56
    • 0030293446 scopus 로고    scopus 로고
    • Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-α and cycloheximide: A possible role in immunopathology
    • Galea-Lauri J., Richardson A.J., Latchman D.S., Katz D.R. Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-α and cycloheximide: a possible role in immunopathology. J. Immunol. 157:1996;4109-4118.
    • (1996) J. Immunol. , vol.157 , pp. 4109-4118
    • Galea-Lauri, J.1    Richardson, A.J.2    Latchman, D.S.3    Katz, D.R.4
  • 58
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-κB activation
    • Lewis J., Devin A., Miller A., Lin Y., Rodriguez Y., Neckers L., Liu Z.G. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-κB activation. J. Biol. Chem. 275:2000;10519-10526.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6    Liu, Z.G.7
  • 59
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S., Fujita N., Tsuruo T. Modulation of Akt kinase activity by binding to Hsp90. Proc. Natl. Acad. Sci. USA. 97:2000;10832-10837.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 61
    • 0033517189 scopus 로고    scopus 로고
    • NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes O.N., Mayo L.D., Gustin J.A., Pfeffer S.R., Pfeffer L.M., Donner D.B. NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature. 401:1999;82-85.
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5    Donner, D.B.6
  • 62
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells
    • Samali A., Cai J., Zhivotovsky B., Jones D.P., Orrenius S. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J. 18:1999;2040-2048.
    • (1999) EMBO J. , vol.18 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 64
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • Lin K.M., Lin B., Lian I.Y., Mestril R., Scheffler I.E., Dillmann W.H. Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation. 103:2001;1787-1792.
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 65
    • 0037129860 scopus 로고    scopus 로고
    • Cytosolic heat shock protein 60, apoptosis, and myocardial injury
    • Kirchhoff S.R., Gupta S., Knowlton A.A. Cytosolic heat shock protein 60, apoptosis, and myocardial injury. Circulation. 105:2002;2899-2904.
    • (2002) Circulation , vol.105 , pp. 2899-2904
    • Kirchhoff, S.R.1    Gupta, S.2    Knowlton, A.A.3
  • 66
    • 0037137296 scopus 로고    scopus 로고
    • Cytosolic heat shock protein 60, hypoxia, and apoptosis
    • Gupta S., Knowlton A.A. Cytosolic heat shock protein 60, hypoxia, and apoptosis. Circulation. 106:2002;2727-2733.
    • (2002) Circulation , vol.106 , pp. 2727-2733
    • Gupta, S.1    Knowlton, A.A.2
  • 67
    • 0034595066 scopus 로고    scopus 로고
    • An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties
    • Guo Z., Cooper L.F. An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties. Biochem. Biophys. Res. Commun. 270:2000;183-189.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 183-189
    • Guo, Z.1    Cooper, L.F.2
  • 68
    • 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. 276:2001;24891-24900.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24891-24900
    • Gusarova, V.1    Caplan, A.J.2    Brodsky, J.L.3    Fisher, E.A.4
  • 69
    • 0028352980 scopus 로고
    • Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90
    • Tsubuki S., Saito Y., Kawashima S. Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90. FEBS Lett. 344:1994;229-233.
    • (1994) FEBS Lett. , vol.344 , pp. 229-233
    • Tsubuki, S.1    Saito, Y.2    Kawashima, S.3
  • 70
    • 0032527963 scopus 로고    scopus 로고
    • Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90
    • Conconi M., Petropoulos I., Emod I., Turlin E., Biville F., Friguet B. Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90. Biochem. J. 333:1998;407-415.
    • (1998) Biochem. J. , vol.333 , pp. 407-415
    • Conconi, M.1    Petropoulos, I.2    Emod, I.3    Turlin, E.4    Biville, F.5    Friguet, B.6
  • 72
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata S., Minami Y., Minami M., Chiba T., Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2:2001;1133-1138.
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 73
    • 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. 3:2001;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
  • 74
    • 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., Hohfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275:2000;4613-4617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4613-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 75
    • 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. 11:2001;1569-1577.
    • (2001) Curr. Biol. , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 77
    • 0035847115 scopus 로고    scopus 로고
    • Interaction between αB-crystallin and the human 20S proteasomal subunit C8/α7
    • Boelens W.C., Croes Y., de Jong W.W. Interaction between αB-crystallin and the human 20S proteasomal subunit C8/α7. Biochim. Biophys. Acta. 1544:2001;311-319.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 311-319
    • Boelens, W.C.1    Croes, Y.2    De Jong, W.W.3


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