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Volumn 10, Issue , 2010, Pages 1543-1552

Heat shock proteins: Cell protection through protein triage

Author keywords

Cell stress; Heat shock proteins; Proteasome; Ubiquitination process

Indexed keywords

ALPHA CRYSTALLIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEASOME; UBIQUITIN; CRYSTALLIN;

EID: 78349273136     PISSN: None     EISSN: 1537744X     Source Type: Journal    
DOI: 10.1100/tsw.2010.152     Document Type: Review
Times cited : (151)

References (59)
  • 1
    • 0037974661 scopus 로고    scopus 로고
    • A role of HSPs in apoptosis through "protein triage"?
    • Garrido, C. and Solary, E. (2003) A role of HSPs in apoptosis through "protein triage"? Cell Death Differ. 10, 619-620.
    • (2003) Cell Death Differ , vol.10 , pp. 619-620
    • Garrido, C.1    Solary, E.2
  • 2
    • 0042025074 scopus 로고    scopus 로고
    • Increased ubiquitin-dependent degradation can replace the essential requirement for heat shock protein induction
    • Friant, S., Meier, K.D., and Riezman, H. (2003) Increased ubiquitin-dependent degradation can replace the essential requirement for heat shock protein induction. EMBO J. 22, 3783-3791.
    • (2003) EMBO J , vol.22 , pp. 3783-3791
    • Friant, S.1    Meier, K.D.2    Riezman, H.3
  • 3
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • DOI 10.1038/35050618
    • Connell, P., Ballinger, C.A., Jiang, J., Wu, Y., Thompson, L.J., Hohfeld, J., and Patterson, C. (2001) The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3, 93-96. (Pubitemid 32114838)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6    Patterson, C.7
  • 4
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata, S., Minami, Y., Minami, M., Chiba, T., and Tanaka, K. (2001) CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2, 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
  • 5
    • 0035900793 scopus 로고    scopus 로고
    • CHIP Is a U-box-dependent E3 Ubiquitin Ligase: Identification of Hsc70 As a Target for Ubiquitylation
    • DOI 10.1074/jbc.M101968200
    • Jiang, J., Ballinger, C.A., Wu, Y., Dai, Q., Cyr, D.M., Hohfeld, J., and Patterson, C. (2001) CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276, 42938-42944. (Pubitemid 33691557)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.46 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 6
    • 67349084344 scopus 로고    scopus 로고
    • CHIP facilitates ubiquitination of inducible nitric oxide synthase and promotes its proteasomal degradation
    • Chen, L., Kong, X., Fu, J., Xu, Y., Fang, S., Hua, P., Luo, L., and Yin, Z. (2009) CHIP facilitates ubiquitination of inducible nitric oxide synthase and promotes its proteasomal degradation. Cell. Immunol. 258, 38-43.
    • (2009) Cell. Immunol. , vol.258 , pp. 38-43
    • Chen, L.1    Kong, X.2    Fu, J.3    Xu, Y.4    Fang, S.5    Hua, P.6    Luo, L.7    Yin, Z.8
  • 7
    • 33645293437 scopus 로고    scopus 로고
    • CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
    • Qian, S.B., McDonough, H., Boellmann, F., Cyr, D.M., and Patterson, C. (2006) CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature 440, 551-555.
    • (2006) Nature , vol.440 , pp. 551-555
    • Qian, S.B.1    McDonough, H.2    Boellmann, F.3    Cyr, D.M.4    Patterson, C.5
  • 8
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • McDonough, H. and Patterson, C. (2003) CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8, 303-308.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 9
    • 21244499845 scopus 로고    scopus 로고
    • The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways
    • Shin, Y., Klucken, J., Patterson, C., Hyman, B.T., and McLean, P.J. (2005) The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. J. Biol. Chem. 280, 23727-23734.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23727-23734
    • Shin, Y.1    Klucken, J.2    Patterson, C.3    Hyman, B.T.4    McLean, P.J.5
  • 10
    • 77952851112 scopus 로고    scopus 로고
    • Chaperone-assisted degradation: Multiple paths to destruction
    • Kettern, N., Dreiseidler, M., Tawo, R., and Hohfeld, J. (2010) Chaperone-assisted degradation: multiple paths to destruction. Biol. Chem. 391, 481-489.
    • (2010) Biol. Chem. , vol.391 , pp. 481-489
    • Kettern, N.1    Dreiseidler, M.2    Tawo, R.3    Hohfeld, J.4
  • 11
    • 77949328788 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: Selectivity pays off
    • Cuervo, A.M. (2009) Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol. Metab. 21, 142-150.
    • (2009) Trends Endocrinol. Metab. , vol.21 , pp. 142-150
    • Cuervo, A.M.1
  • 14
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat shock conjugate Hsc70 in the mammalian cell: The characterization of the anti-apoptotic protein BAG-1 provides novel insights
    • Hohfeld, J. (1998) Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights. Biol. Chem. 379, 269-274.
    • (1998) Biol. Chem. , vol.379 , pp. 269-274
    • Hohfeld, J.1
  • 15
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1 - A nucleotide exchange factor of Hsc70 with multiple cellular functions
    • DOI 10.1379/1466-1268(2003)008<0225:BNEFOH>2.0.CO;2
    • Alberti, S., Esser, C., and Hohfeld, J. (2003) BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones 8, 225-231. (Pubitemid 37484716)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.3 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Hohfeld, J.3
  • 16
    • 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
  • 17
    • 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., and Hohfeld, J. (2001) Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11, 1569-1577.
    • (2001) Curr. Biol. , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 18
    • 43549102208 scopus 로고    scopus 로고
    • HSP90: The Rosetta stone for cellular protein dynamics?
    • Dezwaan, D.C. and Freeman, B.C. (2008) HSP90: the Rosetta stone for cellular protein dynamics? Cell Cycle 7, 1006-1012.
    • (2008) Cell Cycle , vol.7 , pp. 1006-1012
    • Dezwaan, D.C.1    Freeman, B.C.2
  • 19
    • 36749002683 scopus 로고    scopus 로고
    • Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins
    • Didelot, C., Lanneau, D., Brunet, M., Joly, A.L., De Thonel, A., Chiosis, G., and Garrido, C. (2007) Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins. Curr. Med. Chem. 14, 2839-2847.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 2839-2847
    • Didelot, C.1    Lanneau, D.2    Brunet, M.3    Joly, A.L.4    De Thonel, A.5    Chiosis, G.6    Garrido, C.7
  • 21
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu, W., Marcu, M., Yuan, X., Mimnaugh, E., Patterson, C., and Neckers, L. (2002) Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. U. S. A. 99, 12847-12852.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 22
    • 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
  • 23
    • 77950473770 scopus 로고    scopus 로고
    • Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1alpha but Not HIF-2alpha
    • Luo, W., Zhong, J., Chang, R., Hu, H., Pandey, A., and Semenza, G.L. (2010) Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1alpha but Not HIF-2alpha. J. Biol. Chem. 285, 3651-3663.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3651-3663
    • Luo, W.1    Zhong, J.2    Chang, R.3    Hu, H.4    Pandey, A.5    Semenza, G.L.6
  • 24
    • 22844447871 scopus 로고    scopus 로고
    • The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation
    • DOI 10.1074/jbc.M501574200
    • Esser, C., Scheffner, M., and Hohfeld, J. (2005) The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J. Biol. Chem. 280, 27443-27448. (Pubitemid 41040787)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 27443-27448
    • Esser, C.1    Scheffner, M.2    Hohfeld, J.3
  • 25
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • Pearl, L.H., Prodromou, C., and Workman, P. (2008) The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem. J. 410, 439-453.
    • (2008) Biochem. J. , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 26
    • 33845926057 scopus 로고    scopus 로고
    • Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding
    • Fearns, C., Pan, Q., Mathison, J.C., and Chuang, T.H. (2006) Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding. J. Biol. Chem. 281, 34592-34600.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34592-34600
    • Fearns, C.1    Pan, Q.2    Mathison, J.C.3    Chuang, T.H.4
  • 28
  • 29
    • 70350474677 scopus 로고    scopus 로고
    • Heat shock protein 27 phosphorylation: Kinases, phosphatases, functions and pathology
    • Kostenko, S. and Moens, U. (2009) Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology. Cell. Mol. Life Sci. 66, 3289-3307.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3289-3307
    • Kostenko, S.1    Moens, U.2
  • 30
    • 0032561079 scopus 로고    scopus 로고
    • Phosphorylation of alphaB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation
    • Kato, K., Ito, H., Kamei, K., Inaguma, Y., Iwamoto, I., and Saga, S. (1998) Phosphorylation of alphaB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J. Biol. Chem. 273, 28346-28354.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28346-28354
    • Kato, K.1    Ito, H.2    Kamei, K.3    Inaguma, Y.4    Iwamoto, I.5    Saga, S.6
  • 31
    • 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., and Kroemer, G. (2006) Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties. Cell Cycle 5, 2592-2601.
    • (2006) Cell Cycle , vol.5 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 34
    • 0141953292 scopus 로고    scopus 로고
    • Blockade of Hsp27 overcomes bortezomib/proteasome inhibitor PS-341 resistance in lymphoma cells
    • Chauhan, D., Li, G., Shringarpure, R., Podar, K., Ohtake, Y., Hideshima, T., and Anderson, K.C. (2003) Blockade of Hsp27 overcomes bortezomib/proteasome inhibitor PS-341 resistance in lymphoma cells. Cancer Res. 63, 6174-6177.
    • (2003) Cancer Res. , vol.63 , pp. 6174-6177
    • Chauhan, D.1    Li, G.2    Shringarpure, R.3    Podar, K.4    Ohtake, Y.5    Hideshima, T.6    Anderson, K.C.7
  • 39
    • 0032489328 scopus 로고    scopus 로고
    • Cloning and developmental expression of a nuclear ubiquitin-conjugating enzyme (DmUbc9) that interacts with small heat shock proteins in Drosophila melanogaster
    • Joanisse, D.R., Inaguma, Y., and Tanguay, R.M. (1998) Cloning and developmental expression of a nuclear ubiquitin-conjugating enzyme (DmUbc9) that interacts with small heat shock proteins in Drosophila melanogaster. Biochem. Biophys. Res. Commun. 244, 102-109.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 102-109
    • Joanisse, D.R.1    Inaguma, Y.2    Tanguay, R.M.3
  • 40
    • 0035847115 scopus 로고    scopus 로고
    • Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7
    • Boelens, W.C., Croes, Y., and de Jong, W.W. (2001) Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7. Biochim. Biophys. Acta 1544, 311-319.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 311-319
    • Boelens, W.C.1    Croes, Y.2    De Jong, W.W.3
  • 41
    • 0037648469 scopus 로고    scopus 로고
    • The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination
    • den Engelsman, J., Keijsers, V., de Jong, W.W., and Boelens, W.C. (2003) The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination. J. Biol. Chem. 278, 4699-4704.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4699-4704
    • Den Engelsman, J.1    Keijsers, V.2    De Jong, W.W.3    Boelens, W.C.4
  • 43
    • 34248349948 scopus 로고    scopus 로고
    • SCF Fbx4/alphaB-crystallin cyclin D1 ubiquitin ligase: A license to destroy
    • Barbash, O., Lin, D.I., and Diehl, J.A. (2007) SCF Fbx4/alphaB-crystallin cyclin D1 ubiquitin ligase: a license to destroy. Cell Div. 2, 2.
    • (2007) Cell Div. , vol.2 , pp. 2
    • Barbash, O.1    Lin, D.I.2    Diehl, J.A.3
  • 44
    • 53649106818 scopus 로고    scopus 로고
    • SCF(Fbx4/alphaB-crystallin) E3 ligase: When one is not enough
    • Barbash, O. and Diehl, J.A. (2008) SCF(Fbx4/alphaB-crystallin) E3 ligase: when one is not enough. Cell Cycle 7, 2983-2986.
    • (2008) Cell Cycle , vol.7 , pp. 2983-2986
    • Barbash, O.1    Diehl, J.A.2
  • 45
    • 77649272915 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-mediated degradation and synthesis of MyoD is modulated by alphaB-crystallin, a small heat shock protein, during muscle differentiation
    • Singh, B.N., Rao, K.S., and Rao Ch.M. (2009) Ubiquitin-proteasome- mediated degradation and synthesis of MyoD is modulated by alphaB-crystallin, a small heat shock protein, during muscle differentiation. Biochim. Biophys. Acta 1803, 288-299.
    • (2009) Biochim. Biophys. Acta , vol.1803 , pp. 288-299
    • Singh, B.N.1    Rao, K.S.2    Rao, Ch.M.3
  • 46
    • 0027407247 scopus 로고
    • Ubiquitin in neurodegenerative diseases
    • Lowe, J., Mayer, R.J., and Landon, M. (1993) Ubiquitin in neurodegenerative diseases. Brain Pathol. 3, 55-65.
    • (1993) Brain Pathol. , vol.3 , pp. 55-65
    • Lowe, J.1    Mayer, R.J.2    Landon, M.3
  • 47
    • 0026539546 scopus 로고
    • Accumulation of alpha B-crystallin in central nervous system glia and neurons in pathologic conditions
    • Iwaki, T., Wisniewski, T., Iwaki, A., Corbin, E., Tomokane, N., Tateishi, J., and Goldman, J.E. (1992) Accumulation of alpha B-crystallin in central nervous system glia and neurons in pathologic conditions. Am. J. Pathol. 140, 345-356.
    • (1992) Am. J. Pathol. , vol.140 , pp. 345-356
    • Iwaki, T.1    Wisniewski, T.2    Iwaki, A.3    Corbin, E.4    Tomokane, N.5    Tateishi, J.6    Goldman, J.E.7
  • 48
    • 0024521440 scopus 로고
    • Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki, T., Kume-Iwaki, A., Liem, R.K., and Goldman, J.E. (1989) Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57, 71-78.
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.3    Goldman, J.E.4
  • 50
    • 0026570931 scopus 로고
    • Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II
    • Landry, J., Lambert, H., Zhou, M., Lavoie, J.N., Hickey, E., Weber, L.A., and Anderson, C.W. (1992) Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II. J. Biol. Chem. 267, 794-803.
    • (1992) J. Biol. Chem. , vol.267 , pp. 794-803
    • Landry, J.1    Lambert, H.2    Zhou, M.3    Lavoie, J.N.4    Hickey, E.5    Weber, L.A.6    Anderson, C.W.7
  • 52
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski, P.J. and Wacker, J.L. (2005) Modulation of neurodegeneration by molecular chaperones. Nat. Rev. 6, 11-22.
    • (2005) Nat. Rev. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 53
    • 2342444942 scopus 로고    scopus 로고
    • Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival
    • Shimura, H., Miura-Shimura, Y., and Kosik, K.S. (2004) Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. J. Biol. Chem. 279, 17957-17962.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17957-17962
    • Shimura, H.1    Miura-Shimura, Y.2    Kosik, K.S.3
  • 54
    • 2942708228 scopus 로고    scopus 로고
    • Mechanism of neurodegenerative disease: Role of the ubiquitin proteasome system
    • Petrucelli, L. and Dawson, T.M. (2004) Mechanism of neurodegenerative disease: role of the ubiquitin proteasome system. Ann. Med. 36, 315-320.
    • (2004) Ann. Med. , vol.36 , pp. 315-320
    • Petrucelli, L.1    Dawson, T.M.2
  • 56
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents alphasynuclein aggregation and toxicity in vitro
    • McLean, P.J., Klucken, J., Shin, Y., and Hyman, B.T. (2004) Geldanamycin induces Hsp70 and prevents alphasynuclein aggregation and toxicity in vitro. Biochem. Biophys. Res. Commun. 321, 665-669.
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 57
  • 58
    • 0031004769 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70
    • Bercovich, B., Stancovski, I., Mayer, A., Blumenfeld, N., Laszlo, A., Schwartz, A.L., and Ciechanover, A. (1997) Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70. J. Biol. Chem. 272, 9002-9010.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9002-9010
    • Bercovich, B.1    Stancovski, I.2    Mayer, A.3    Blumenfeld, N.4    Laszlo, A.5    Schwartz, A.L.6    Ciechanover, A.7
  • 59
    • 2342625412 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino-demethoxygeldanamycin: Role of the cochaperone carboxyl heat shock protein 70-interacting protein
    • Bonvini, P., Dalla Rosa, H., Vignes, N., and Rosolen, A. (2004) Ubiquitination and proteasomal degradation of nucleophosmin-anaplastic lymphoma kinase induced by 17-allylamino-demethoxygeldanamycin: role of the cochaperone carboxyl heat shock protein 70-interacting protein. Cancer Res. 64, 3256-3264.
    • (2004) Cancer Res , vol.64 , pp. 3256-3264
    • Bonvini, P.1    Dalla Rosa, H.2    Vignes, N.3    Rosolen, A.4


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