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Volumn 109, Issue , 2012, Pages 113-160

Interactions of the proteasomal system with chaperones: Protein triage and protein quality control

Author keywords

Chaperones; Co Chaperones; ERAD; Heat shock proteins; Protein Quality Control; Ubiquitin Proteasome System

Indexed keywords


EID: 84862742197     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-397863-9.00004-3     Document Type: Chapter
Times cited : (49)

References (192)
  • 1
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • K. Richter, M. Haslbeck, and J. Buchner The heat shock response: life on the verge of death Mol Cell 40 2010 253 266
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 2
    • 1542396386 scopus 로고    scopus 로고
    • Heat shock and UV-B-induced DNA damage and mutagenesis in skin
    • DOI 10.1039/b301253k
    • C. Jantschitsch, and F. Trautinger Heat shock and UV-B-induced DNA damage and mutagenesis in skin Photochem Photobiol Sci 2 2003 899 903 (Pubitemid 41646637)
    • (2003) Photochemical and Photobiological Sciences , vol.2 , Issue.9 , pp. 899-903
    • Jantschitsch, C.1    Trautinger, F.2
  • 4
    • 58449101336 scopus 로고    scopus 로고
    • Ribosome biogenesis is temperature-dependent and delayed in Escherichia coli lacking the chaperones DnaK or DnaJ
    • R.A. Al, and J.H. Alix Ribosome biogenesis is temperature-dependent and delayed in Escherichia coli lacking the chaperones DnaK or DnaJ Mol Microbiol 71 2009 748 762
    • (2009) Mol Microbiol , vol.71 , pp. 748-762
    • Al, R.A.1    Alix, J.H.2
  • 6
    • 77956006894 scopus 로고    scopus 로고
    • Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function
    • S. Welker, B. Rudolph, E. Frenzel, F. Hagn, G. Liebisch, and G. Schmitz Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function Mol Cell 39 2010 507 520
    • (2010) Mol Cell , vol.39 , pp. 507-520
    • Welker, S.1    Rudolph, B.2    Frenzel, E.3    Hagn, F.4    Liebisch, G.5    Schmitz, G.6
  • 8
    • 43549102208 scopus 로고    scopus 로고
    • HSP90: The Rosetta stone for cellular protein dynamics?
    • D.C. Dezwaan, and B.C. Freeman HSP90: the Rosetta stone for cellular protein dynamics? Cell Cycle 7 2008 1006 1012 (Pubitemid 351679833)
    • (2008) Cell Cycle , vol.7 , Issue.8 , pp. 1006-1012
    • DeZwaan, D.C.1    Freeman, B.C.2
  • 10
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: Protein disaggregating machines
    • S.M. Doyle, and S. Wickner Hsp104 and ClpB: protein disaggregating machines Trends Biochem Sci 34 2009 40 48
    • (2009) Trends Biochem Sci , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 11
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • M.P. Mayer Gymnastics of molecular chaperones Mol Cell 39 2010 321 331
    • (2010) Mol Cell , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 12
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • B. Bukau, J. Weissman, and A. Horwich Molecular chaperones and protein quality control Cell 125 2006 443 451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 13
    • 0020491477 scopus 로고
    • Purification of the major mammalian heat shock proteins
    • W.J. Welch, and J.R. Feramisco Purification of the major mammalian heat shock proteins J Biol Chem 257 1982 14949 14959
    • (1982) J Biol Chem , vol.257 , pp. 14949-14959
    • Welch, W.J.1    Feramisco, J.R.2
  • 15
    • 77950224150 scopus 로고    scopus 로고
    • Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage
    • W.B. Pratt, Y. Morishima, H.M. Peng, and Y. Osawa Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage Exp Biol Med (Maywood) 235 2010 278 289
    • (2010) Exp Biol Med (Maywood) , vol.235 , pp. 278-289
    • Pratt, W.B.1    Morishima, Y.2    Peng, H.M.3    Osawa, Y.4
  • 16
    • 0037518202 scopus 로고    scopus 로고
    • Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle
    • DOI 10.1074/jbc.M213094200
    • K. Richter, P. Muschler, O. Hainzl, J. Reinstein, and J. Buchner Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle J Biol Chem 278 2003 10328 10333 (Pubitemid 36800295)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.12 , pp. 10328-10333
    • Richter, K.1    Muschler, P.2    Hainzl, O.3    Reinstein, J.4    Buchner, J.5
  • 17
    • 61949349758 scopus 로고    scopus 로고
    • Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
    • M. Hessling, K. Richter, and J. Buchner Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90 Nat Struct Mol Biol 16 2009 287 293
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 287-293
    • Hessling, M.1    Richter, K.2    Buchner, J.3
  • 18
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • DOI 10.1016/S0092-8674(00)80806-5
    • B. Bukau, E. Deuerling, C. Pfund, and E.A. Craig Getting newly synthesized proteins into shape Cell 101 2000 119 122 (Pubitemid 32004743)
    • (2000) Cell , vol.101 , Issue.2 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 19
    • 0036343904 scopus 로고    scopus 로고
    • The protein import motor of mitochondria
    • W. Neupert, and M. Brunner The protein import motor of mitochondria Nat Rev Mol Cell Biol 3 2002 555 565
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 555-565
    • Neupert, W.1    Brunner, M.2
  • 20
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • W.B. Pratt, and D.O. Toft Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery Exp Biol Med (Maywood) 228 2003 111 133 (Pubitemid 36187918)
    • (2003) Experimental Biology and Medicine , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 21
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • M.P. Mayer, and B. Bukau Hsp70 chaperones: cellular functions and molecular mechanism Cell Mol Life Sci 62 2005 670 684
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 22
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1
    • DOI 10.1093/emboj/16.20.6209
    • J. Hohfeld, and S. Jentsch GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 EMBO J 16 1997 6209 6216 (Pubitemid 27458341)
    • (1997) EMBO Journal , vol.16 , Issue.20 , pp. 6209-6216
    • Hohfeld, J.1    Jentsch, S.2
  • 23
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • DOI 10.1093/emboj/20.5.1042
    • S. Rudiger, J. Schneider-Mergener, and B. Bukau Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone EMBO J 20 2001 1042 1050 (Pubitemid 32186795)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 1042-1050
    • Rudiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 24
    • 0037470073 scopus 로고    scopus 로고
    • Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity
    • DOI 10.1074/jbc.M206867200
    • O.O. Odunuga, J.A. Hornby, C. Bies, R. Zimmermann, D.J. Pugh, and G.L. Blatch Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity J Biol Chem 278 2003 6896 6904 (Pubitemid 36800681)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , 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
  • 25
  • 27
    • 52049091847 scopus 로고    scopus 로고
    • Conserved central domains control the quaternary structure of type i and type II Hsp40 molecular chaperones
    • C.H. Ramos, C.L. Oliveira, C.Y. Fan, I.L. Torriani, and D.M. Cyr Conserved central domains control the quaternary structure of type I and type II Hsp40 molecular chaperones J Mol Biol 383 2008 155 166
    • (2008) J Mol Biol , vol.383 , pp. 155-166
    • Ramos, C.H.1    Oliveira, C.L.2    Fan, C.Y.3    Torriani, I.L.4    Cyr, D.M.5
  • 29
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: Molecular structure and chaperone function
    • DOI 10.1007/s00018-005-5190-4
    • Y. Sun, and T.H. MacRae Small heat shock proteins: molecular structure and chaperone function Cell Mol Life Sci 62 2005 2460 2476 (Pubitemid 41801099)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.21 , pp. 2460-2476
    • Sun, Y.1    MacRae, T.H.2
  • 32
    • 70350474677 scopus 로고    scopus 로고
    • Heat shock protein 27 phosphorylation: Kinases, phosphatases, functions and pathology
    • S. Kostenko, and U. Moens Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology Cell Mol Life Sci 66 2009 3289 3307
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3289-3307
    • Kostenko, S.1    Moens, U.2
  • 33
    • 1442289304 scopus 로고    scopus 로고
    • Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae
    • DOI 10.1038/sj.emboj.7600080
    • M. Haslbeck, N. Braun, T. Stromer, B. Richter, N. Model, and S. Weinkauf Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae EMBO J 23 2004 638 649 (Pubitemid 38282395)
    • (2004) EMBO Journal , vol.23 , Issue.3 , pp. 638-649
    • Haslbeck, M.1    Braun, N.2    Stromer, T.3    Richter, B.4    Model, N.5    Weinkauf, S.6    Buchner, J.7
  • 34
    • 1542320089 scopus 로고    scopus 로고
    • The Identity of Proteins Associated with a Small Heat Shock Potein during Heat Stress in Vivo Indicates That These Chaperones Protect a Wide Range of Cellular Functions
    • DOI 10.1074/jbc.M310684200
    • E. Basha, G.J. Lee, L.A. Breci, A.C. Hausrath, N.R. Buan, and K.C. Giese The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions J Biol Chem 279 2004 7566 7575 (Pubitemid 38294635)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7566-7575
    • Basha, E.1    Lee, G.J.2    Breci, L.A.3    Hausrath, A.C.4    Buan, N.R.5    Giese, K.C.6    Vierling, E.7
  • 35
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: Implications in aging and disease
    • J. Anckar, and L. Sistonen Regulation of HSF1 function in the heat stress response: implications in aging and disease Annu Rev Biochem 80 2011 1089 1115
    • (2011) Annu Rev Biochem , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 36
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • J. Zou, Y. Guo, T. Guettouche, D.F. Smith, and R. Voellmy Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1 Cell 94 1998 471 480 (Pubitemid 28391863)
    • (1998) Cell , vol.94 , Issue.4 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 37
    • 63149154055 scopus 로고    scopus 로고
    • Heterotrimerization of heat-shock factors 1 and 2 provides a transcriptional switch in response to distinct stimuli
    • A. Sandqvist, J.K. Bjork, M. Akerfelt, Z. Chitikova, A. Grichine, and C. Vourc'h Heterotrimerization of heat-shock factors 1 and 2 provides a transcriptional switch in response to distinct stimuli Mol Biol Cell 20 2009 1340 1347
    • (2009) Mol Biol Cell , vol.20 , pp. 1340-1347
    • Sandqvist, A.1    Bjork, J.K.2    Akerfelt, M.3    Chitikova, Z.4    Grichine, A.5    Vourc'H, C.6
  • 39
    • 44049095652 scopus 로고    scopus 로고
    • Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons
    • DOI 10.1126/science.1156093
    • V. Prahlad, T. Cornelius, and R.I. Morimoto Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons Science 320 2008 811 814 (Pubitemid 351929633)
    • (2008) Science , vol.320 , Issue.5877 , pp. 811-814
    • Prahlad, V.1    Cornelius, T.2    Morimoto, R.I.3
  • 40
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • D.D. Mosser, P.T. Kotzbauer, K.D. Sarge, and R.I. Morimoto In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation Proc Natl Acad Sci USA 87 1990 3748 3752
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 41
    • 0037442768 scopus 로고    scopus 로고
    • Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress
    • DOI 10.1101/gad.1044503
    • S.G. Ahn, and D.J. Thiele Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress Genes Dev 17 2003 516 528 (Pubitemid 36258765)
    • (2003) Genes and Development , vol.17 , Issue.4 , pp. 516-528
    • Ahn, S.-G.1    Thiele, D.J.2
  • 42
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • DOI 10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2
    • H. McDonough, and C. Patterson CHIP: a link between the chaperone and proteasome systems Cell Stress Chaperones 8 2003 303 308 (Pubitemid 38222876)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.4 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 43
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • DOI 10.1074/jbc.275.7.4613
    • J. Luders, J. Demand, and J. Hohfeld The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome J Biol Chem 275 2000 4613 4617 (Pubitemid 30108845)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 4613-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 45
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • J. Jiang, C.A. Ballinger, Y. Wu, Q. Dai, D.M. Cyr, and J. Hohfeld CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation J Biol Chem 276 2001 42938 42944
    • (2001) J Biol Chem , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6
  • 46
    • 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
    • C.A. Ballinger, P. Connell, Y. Wu, Z. Hu, L.J. Thompson, and L.Y. Yin Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions Mol Cell Biol 19 1999 4535 4545 (Pubitemid 29242026)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.6 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.-Y.6    Patterson, C.7
  • 47
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • DOI 10.1093/embo-reports/kve246
    • S. Murata, Y. Minami, M. Minami, T. Chiba, and K. Tanaka CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein EMBO Rep 2 2001 1133 1138 (Pubitemid 34055961)
    • (2001) EMBO Reports , vol.2 , Issue.12 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 50
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • DOI 10.1016/S0960-9822(01)00487-0
    • J. Demand, S. Alberti, C. Patterson, and J. Hohfeld Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling Curr Biol 11 2001 1569 1577 (Pubitemid 32978521)
    • (2001) Current Biology , vol.11 , Issue.20 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 51
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • DOI 10.1074/jbc.M204196200
    • S. Alberti, J. Demand, C. Esser, N. Emmerich, H. Schild, and J. Hohfeld Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome J Biol Chem 277 2002 45920 45927 (Pubitemid 35417574)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 52
    • 0039598518 scopus 로고    scopus 로고
    • Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function
    • DOI 10.1074/jbc.275.20.14817
    • J. Luders, J. Demand, O. Papp, and J. Hohfeld Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function J Biol Chem 275 2000 14817 14823 (Pubitemid 30337193)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.20 , pp. 14817-14823
    • Luders, J.1    Demand, J.2    Papp, O.3    Hohfeld, J.4
  • 53
    • 0032489524 scopus 로고    scopus 로고
    • Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a
    • DOI 10.1074/jbc.273.10.5461
    • P. Young, Q. Deveraux, R.E. Beal, C.M. Pickart, and M. Rechsteiner Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a J Biol Chem 273 1998 5461 5467 (Pubitemid 28124009)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5461-5467
    • Young, P.1    Deveraux, Q.2    Beal, R.E.3    Pickart, C.M.4    Rechsteiner, M.5
  • 54
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • DOI 10.1016/S0968-0004(97)01005-0, PII S0968000497010050
    • J. Frydman, and J. Hohfeld Chaperones get in touch: the Hip-Hop connection Trends Biochem Sci 22 1997 87 92 (Pubitemid 27107858)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.3 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 55
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70: Anti-apoptotic proteins with tumorigenic properties
    • C. Garrido, M. Brunet, C. Didelot, Y. Zermati, E. Schmitt, and G. Kroemer Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties Cell Cycle 5 2006 2592 2601 (Pubitemid 44785803)
    • (2006) Cell Cycle , vol.5 , Issue.22 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 56
    • 33845623275 scopus 로고    scopus 로고
    • HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells
    • A. Parcellier, M. Brunet, E. Schmitt, E. Col, C. Didelot, and A. Hammann HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells FASEB J 20 2006 1179 1181
    • (2006) FASEB J , vol.20 , pp. 1179-1181
    • Parcellier, A.1    Brunet, M.2    Schmitt, E.3    Col, E.4    Didelot, C.5    Hammann, A.6
  • 58
    • 70349287559 scopus 로고    scopus 로고
    • Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity
    • S.M. Brunet, T.A. De, A. Hammann, A.L. Joly, G. Bossis, and E. Fourmaux Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity Oncogene 28 2009 3332 3344
    • (2009) Oncogene , vol.28 , pp. 3332-3344
    • Brunet, S.M.1    De, T.A.2    Hammann, A.3    Joly, A.L.4    Bossis, G.5    Fourmaux, E.6
  • 59
    • 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
    • DOI 10.1006/bbrc.1998.8214
    • D.R. Joanisse, Y. Inaguma, and R.M. Tanguay 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 1998 102 109 (Pubitemid 28419907)
    • (1998) Biochemical and Biophysical Research Communications , vol.244 , Issue.1 , pp. 102-109
    • Joanisse, D.R.1    Inaguma, Y.2    Tanguay, R.M.3
  • 60
    • 0032527991 scopus 로고    scopus 로고
    • Proteasome inhibition leads to the activation of all members of the heat-shock-factor family
    • DOI 10.1046/j.1432-1327.1998.2550356.x
    • Y. Kawazoe, A. Nakai, M. Tanabe, and K. Nagata Proteasome inhibition leads to the activation of all members of the heat-shock-factor family Eur J Biochem 255 1998 356 362 (Pubitemid 28340243)
    • (1998) European Journal of Biochemistry , vol.255 , Issue.2 , pp. 356-362
    • Kawazoe, Y.1    Nakai, A.2    Tanabe, M.3    Nagata, K.4
  • 61
    • 34249062137 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a p38 mitogen-activated protein kinase (MAPK)-dependent anti-apoptotic program involving MAPK phosphatase-1 and Akt in models of breast cancer
    • Y.Y. Shi, G.W. Small, and R.Z. Orlowski Proteasome inhibitors induce a p38 mitogen-activated protein kinase (MAPK)-dependent anti-apoptotic program involving MAPK phosphatase-1 and Akt in models of breast cancer Breast Cancer Res Treat 100 2006 33 47
    • (2006) Breast Cancer Res Treat , vol.100 , pp. 33-47
    • Shi, Y.Y.1    Small, G.W.2    Orlowski, R.Z.3
  • 63
    • 77951257992 scopus 로고    scopus 로고
    • Proteasome inhibition induces hsp30 and hsp70 gene expression as well as the acquisition of thermotolerance in Xenopus laevis A6 cells
    • J.T. Young, and J.J. Heikkila Proteasome inhibition induces hsp30 and hsp70 gene expression as well as the acquisition of thermotolerance in Xenopus laevis A6 cells Cell Stress Chaperones 15 2010 323 334
    • (2010) Cell Stress Chaperones , vol.15 , pp. 323-334
    • Young, J.T.1    Heikkila, J.J.2
  • 64
    • 58149375078 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces BAG3 expression through activation of heat shock factor 1
    • Z.X. Du, H.Y. Zhang, X. Meng, Y.Y. Gao, R.L. Zou, and B.Q. Liu Proteasome inhibitor MG132 induces BAG3 expression through activation of heat shock factor 1 J Cell Physiol 218 2009 631 637
    • (2009) J Cell Physiol , vol.218 , pp. 631-637
    • Du, Z.X.1    Zhang, H.Y.2    Meng, X.3    Gao, Y.Y.4    Zou, R.L.5    Liu, B.Q.6
  • 65
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Y. Kawaguchi, J.J. Kovacs, A. McLaurin, J.M. Vance, A. Ito, and T.P. Yao The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress Cell 115 2003 727 738 (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 66
    • 26644473193 scopus 로고    scopus 로고
    • Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone
    • DOI 10.1074/jbc.M506997200
    • P.J. Murphy, Y. Morishima, J.J. Kovacs, T.P. Yao, and W.B. Pratt Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone J Biol Chem 280 2005 33792 33799 (Pubitemid 41443098)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 33792-33799
    • Murphy, P.J.M.1    Morishima, Y.2    Kovacs, J.J.3    Yao, T.-P.4    Pratt, W.B.5
  • 68
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • DOI 10.1128/MCB.21.23.8035-8044.2001
    • D. Seigneurin-Berny, A. Verdel, S. Curtet, C. Lemercier, J. Garin, and S. Rousseaux Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways Mol Cell Biol 21 2001 8035 8044 (Pubitemid 33051794)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.23 , pp. 8035-8044
    • Seigneurin-Berny, D.1    Verdel, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5    Rousseaux, S.6    Khochbin, S.7
  • 69
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    • DOI 10.1016/j.molcel.2005.12.014, PII S1097276505018976
    • S. Rumpf, and S. Jentsch Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone Mol Cell 21 2006 261 269 (Pubitemid 43099941)
    • (2006) Molecular Cell , vol.21 , Issue.2 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2
  • 70
    • 65549166880 scopus 로고    scopus 로고
    • HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling
    • V.D. Kekatpure, A.J. Dannenberg, and K. Subbaramaiah HDAC6 modulates Hsp90 chaperone activity and regulates activation of aryl hydrocarbon receptor signaling J Biol Chem 284 2009 7436 7445
    • (2009) J Biol Chem , vol.284 , pp. 7436-7445
    • Kekatpure, V.D.1    Dannenberg, A.J.2    Subbaramaiah, K.3
  • 72
    • 33846924300 scopus 로고    scopus 로고
    • How many transcription factors does it take to turn on the heme oxygenase-1 gene?
    • DOI 10.1165/rcmb.2006-0340TR
    • J. Alam, and J.L. Cook How many transcription factors does it take to turn on the heme oxygenase-1 gene? Am J Respir Cell Mol Biol 36 2007 166 174 (Pubitemid 46233469)
    • (2007) American Journal of Respiratory Cell and Molecular Biology , vol.36 , Issue.2 , pp. 166-174
    • Alam, J.1    Cook, J.L.2
  • 73
    • 33645945014 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: From basic science to therapeutic applications
    • S.W. Ryter, J. Alam, and A.M. Choi Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications Physiol Rev 86 2006 583 650
    • (2006) Physiol Rev , vol.86 , pp. 583-650
    • Ryter, S.W.1    Alam, J.2    Choi, A.M.3
  • 75
    • 35848942608 scopus 로고    scopus 로고
    • Heme oxygenase-1 in tumors: Is it a false friend?
    • DOI 10.1089/ars.2007.1659
    • A. Jozkowicz, H. Was, and J. Dulak Heme oxygenase-1 in tumors: is it a false friend? Antioxid Redox Signal 9 2007 2099 2117 (Pubitemid 350059009)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.12 , pp. 2099-2117
    • Jozkowicz, A.1    Was, H.2    Dulak, J.3
  • 79
    • 0034596874 scopus 로고    scopus 로고
    • Carbon monoxide generated by heme oxygenase 1 suppresses endothelial cell apoptosis
    • S. Brouard, L.E. Otterbein, J. Anrather, E. Tobiasch, F.H. Bach, and A.M. Choi Carbon monoxide generated by heme oxygenase 1 suppresses endothelial cell apoptosis J Exp Med 192 2000 1015 1026
    • (2000) J Exp Med , vol.192 , pp. 1015-1026
    • Brouard, S.1    Otterbein, L.E.2    Anrather, J.3    Tobiasch, E.4    Bach, F.H.5    Choi, A.M.6
  • 80
    • 1442326158 scopus 로고    scopus 로고
    • Antiapoptotic role of heme oxygenase (HO) and the potential of HO as a target in anticancer treatment
    • DOI 10.1023/B:APPT.0000012119.83734.4e
    • J. Fang, T. Akaike, and H. Maeda Antiapoptotic role of heme oxygenase (HO) and the potential of HO as a target in anticancer treatment Apoptosis 9 2004 27 35 (Pubitemid 38270426)
    • (2004) Apoptosis , vol.9 , Issue.1 , pp. 27-35
    • Fang, J.1    Akaike, T.2    Maeda, H.3
  • 81
    • 2542626623 scopus 로고    scopus 로고
    • Proteasome inhibitors up-regulate haem oxygenase-1 gene expression: Requirement of p38 MAPK (mitogen-activated protein kinase) activation but not of NF-kappaB (nuclear factor kappaB) inhibition
    • W.T. Wu, K.H. Chi, F.M. Ho, W.C. Tsao, and W.W. Lin Proteasome inhibitors up-regulate haem oxygenase-1 gene expression: requirement of p38 MAPK (mitogen-activated protein kinase) activation but not of NF-kappaB (nuclear factor kappaB) inhibition Biochem J 379 2004 587 593
    • (2004) Biochem J , vol.379 , pp. 587-593
    • Wu, W.T.1    Chi, K.H.2    Ho, F.M.3    Tsao, W.C.4    Lin, W.W.5
  • 82
    • 77953483653 scopus 로고    scopus 로고
    • Elevation of heme oxygenase-1 by proteasome inhibition affords dopaminergic neuroprotection
    • N. Yamamoto, Y. Izumi, T. Matsuo, S. Wakita, T. Kume, and Y. Takada-Takatori Elevation of heme oxygenase-1 by proteasome inhibition affords dopaminergic neuroprotection J Neurosci Res 88 2010 1934 1942
    • (2010) J Neurosci Res , vol.88 , pp. 1934-1942
    • Yamamoto, N.1    Izumi, Y.2    Matsuo, T.3    Wakita, S.4    Kume, T.5    Takada-Takatori, Y.6
  • 83
    • 67650229881 scopus 로고    scopus 로고
    • Nrf2-dependent upregulation of antioxidative enzymes: A novel pathway for proteasome inhibitor-mediated cardioprotection
    • H. Dreger, K. Westphal, A. Weller, G. Baumann, V. Stangl, and S. Meiners Nrf2-dependent upregulation of antioxidative enzymes: a novel pathway for proteasome inhibitor-mediated cardioprotection Cardiovasc Res 83 2009 354 361
    • (2009) Cardiovasc Res , vol.83 , pp. 354-361
    • Dreger, H.1    Westphal, K.2    Weller, A.3    Baumann, G.4    Stangl, V.5    Meiners, S.6
  • 84
    • 79955647069 scopus 로고    scopus 로고
    • Proteasome inhibition induces a p38 MAPK pathway-dependent antiapoptotic program via Nrf2 in thyroid cancer cells
    • Z.X. Du, Y. Yan, H.Y. Zhang, B.Q. Liu, Y.Y. Gao, and X.F. Niu Proteasome inhibition induces a p38 MAPK pathway-dependent antiapoptotic program via Nrf2 in thyroid cancer cells J Clin Endocrinol Metab 96 2011 E763 E771
    • (2011) J Clin Endocrinol Metab , vol.96
    • Du, Z.X.1    Yan, Y.2    Zhang, H.Y.3    Liu, B.Q.4    Gao, Y.Y.5    Niu, X.F.6
  • 85
    • 1942455887 scopus 로고    scopus 로고
    • Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles
    • DOI 10.1016/j.freeradbiomed.2004.02.075, PII S0891584904001935
    • K. Itoh, K.I. Tong, and M. Yamamoto Molecular mechanism activating Nrf2-Keap1 pathway in regulation of adaptive response to electrophiles Free Radic Biol Med 36 2004 1208 1213 (Pubitemid 38526314)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.10 , pp. 1208-1213
    • Itoh, K.1    Tong, K.I.2    Yamamoto, M.3
  • 86
    • 51049088872 scopus 로고    scopus 로고
    • HSP90 inhibitor, DMAG, synergizes with radiation of lung cancer cells by interfering with base excision and ATM-mediated DNA repair
    • T.T. Koll, S.S. Feis, M.H. Wright, M.M. Teniola, M.M. Richardson, and A.I. Robles HSP90 inhibitor, DMAG, synergizes with radiation of lung cancer cells by interfering with base excision and ATM-mediated DNA repair Mol Cancer Ther 7 2008 1985 1992
    • (2008) Mol Cancer Ther , vol.7 , pp. 1985-1992
    • Koll, T.T.1    Feis, S.S.2    Wright, M.H.3    Teniola, M.M.4    Richardson, M.M.5    Robles, A.I.6
  • 87
    • 77952167700 scopus 로고    scopus 로고
    • Heat shock proteins as targets in oncology
    • O.A. Gimenez, and S.J. Montalar Heat shock proteins as targets in oncology Clin Transl Oncol 12 2010 166 173
    • (2010) Clin Transl Oncol , vol.12 , pp. 166-173
    • Gimenez, O.A.1    Montalar, S.J.2
  • 88
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • M.A. Loo, T.J. Jensen, L. Cui, Y. Hou, X.B. Chang, and J.R. Riordan Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome EMBO J 17 1998 6879 6887 (Pubitemid 28550282)
    • (1998) EMBO Journal , vol.17 , Issue.23 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.-X.4    Chang, X.-B.5    Riordan, J.R.6
  • 89
    • 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
    • DOI 10.1016/0014-5793(94)00388-2
    • S. Tsubuki, Y. Saito, and S. Kawashima 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 (Pubitemid 24154645)
    • (1994) FEBS Letters , vol.344 , Issue.2-3 , pp. 229-233
    • Tsubuki, S.1
  • 90
    • 0028889670 scopus 로고
    • Age-dependent association of isolated bovine lens multicatalytic proteinase complex (proteasome) with heat-shock protein 90, an endogenous inhibitor
    • B.J. Wagner, and J.W. Margolis Age-dependent association of isolated bovine lens multicatalytic proteinase complex (proteasome) with heat-shock protein 90, an endogenous inhibitor Arch Biochem Biophys 323 1995 455 462
    • (1995) Arch Biochem Biophys , vol.323 , pp. 455-462
    • Wagner, B.J.1    Margolis, J.W.2
  • 91
    • 33646114761 scopus 로고    scopus 로고
    • Hsp90 inhibitors: Small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation
    • B.S. Blagg, and T.D. Kerr Hsp90 inhibitors: small molecules that transform the Hsp90 protein folding machinery into a catalyst for protein degradation Med Res Rev 26 2006 310 338
    • (2006) Med Res Rev , vol.26 , pp. 310-338
    • Blagg, B.S.1    Kerr, T.D.2
  • 92
    • 4344674482 scopus 로고    scopus 로고
    • Targeting multiple signal transduction pathways through inhibition of Hsp90
    • DOI 10.1007/s00109-004-0549-9
    • H. Zhang, and F. Burrows Targeting multiple signal transduction pathways through inhibition of Hsp90 J Mol Med (Berl) 82 2004 488 499 (Pubitemid 39149859)
    • (2004) Journal of Molecular Medicine , vol.82 , Issue.8 , pp. 488-499
    • Zhang, H.1    Burrows, F.2
  • 93
    • 79960694363 scopus 로고    scopus 로고
    • HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells
    • J.I. Leu, J. Pimkina, P. Pandey, M.E. Murphy, and D.L. George HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells Mol Cancer Res 9 2011 936 947
    • (2011) Mol Cancer Res , vol.9 , pp. 936-947
    • Leu, J.I.1    Pimkina, J.2    Pandey, P.3    Murphy, M.E.4    George, D.L.5
  • 94
    • 62449124769 scopus 로고    scopus 로고
    • CHIP regulates leucine-rich repeat kinase-2 ubiquitination, degradation, and toxicity
    • H.S. Ko, R. Bailey, W.W. Smith, Z. Liu, J.H. Shin, and Y.I. Lee CHIP regulates leucine-rich repeat kinase-2 ubiquitination, degradation, and toxicity Proc Natl Acad Sci USA 106 2009 2897 2902
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2897-2902
    • Ko, H.S.1    Bailey, R.2    Smith, W.W.3    Liu, Z.4    Shin, J.H.5    Lee, Y.I.6
  • 96
    • 77955908479 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 70 improves arsenic trioxide and 17-DMAG effects on constitutive signal transducer and activator of transcription 3 activity
    • S. Ghoshal, I. Rao, J.C. Earp, W.J. Jusko, and M. Wetzler Down-regulation of heat shock protein 70 improves arsenic trioxide and 17-DMAG effects on constitutive signal transducer and activator of transcription 3 activity Cancer Chemother Pharmacol 66 2010 681 689
    • (2010) Cancer Chemother Pharmacol , vol.66 , pp. 681-689
    • Ghoshal, S.1    Rao, I.2    Earp, J.C.3    Jusko, W.J.4    Wetzler, M.5
  • 97
    • 33751111683 scopus 로고    scopus 로고
    • Hsp90 inhibition results in autophagy-mediated proteasome-independent degradation of IκB kinase (IKK)
    • DOI 10.1038/sj.cr.7310109, PII 7310109
    • G. Qing, P. Yan, and G. Xiao Hsp90 inhibition results in autophagy-mediated proteasome-independent degradation of IkappaB kinase (IKK) Cell Res 16 2006 895 901 (Pubitemid 44764199)
    • (2006) Cell Research , vol.16 , Issue.11 , pp. 895-901
    • Qing, G.1    Yan, P.2    Xiao, G.3
  • 98
    • 0034212740 scopus 로고    scopus 로고
    • Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells
    • S. Yokota, M. Kitahara, and K. Nagata Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells Cancer Res 60 2000 2942 2948 (Pubitemid 30395819)
    • (2000) Cancer Research , vol.60 , Issue.11 , pp. 2942-2948
    • Yokota, S.-I.1    Kitahara, M.2    Nagata, K.3
  • 99
    • 77952332824 scopus 로고    scopus 로고
    • Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation
    • A.M. Wang, Y. Morishima, K.M. Clapp, H.M. Peng, W.B. Pratt, and J.E. Gestwicki Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation J Biol Chem 285 2010 15714 15723
    • (2010) J Biol Chem , vol.285 , pp. 15714-15723
    • Wang, A.M.1    Morishima, Y.2    Clapp, K.M.3    Peng, H.M.4    Pratt, W.B.5    Gestwicki, J.E.6
  • 100
    • 77958019101 scopus 로고    scopus 로고
    • Targeting heat shock protein 72 enhances Hsp90 inhibitor-induced apoptosis in myeloma
    • E.L. Davenport, A. Zeisig, L.I. Aronson, H.E. Moore, S. Hockley, and D. Gonzalez Targeting heat shock protein 72 enhances Hsp90 inhibitor-induced apoptosis in myeloma Leukemia 24 2010 1804 1807
    • (2010) Leukemia , vol.24 , pp. 1804-1807
    • Davenport, E.L.1    Zeisig, A.2    Aronson, L.I.3    Moore, H.E.4    Hockley, S.5    Gonzalez, D.6
  • 101
    • 0030894162 scopus 로고    scopus 로고
    • Oxidative stress: Oxidants and antioxidants
    • H. Sies Oxidative stress: oxidants and antioxidants Exp Physiol 82 1997 291 295 (Pubitemid 27182306)
    • (1997) Experimental Physiology , vol.82 , Issue.2 , pp. 291-295
    • Sies, H.1
  • 102
    • 64149121709 scopus 로고    scopus 로고
    • Induction of heat shock proteins for protection against oxidative stress
    • B. Kalmar, and L. Greensmith Induction of heat shock proteins for protection against oxidative stress Adv Drug Deliv Rev 61 2009 310 318
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 310-318
    • Kalmar, B.1    Greensmith, L.2
  • 103
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • DOI 10.1016/S0092-8674(00)80547-4
    • U. Jakob, W. Muse, M. Eser, and J.C. Bardwell Chaperone activity with a redox switch Cell 96 1999 341 352 (Pubitemid 29077588)
    • (1999) Cell , vol.96 , Issue.3 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.A.4
  • 104
    • 84855217371 scopus 로고    scopus 로고
    • Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system
    • M. Kastle, and T. Grune Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system Curr Pharm Design 17 2011 4007 4022
    • (2011) Curr Pharm Design , vol.17 , pp. 4007-4022
    • Kastle, M.1    Grune, T.2
  • 105
    • 80052265819 scopus 로고    scopus 로고
    • HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
    • T. Grune, B. Catalgol, A. Licht, G. Ermak, A.M. Pickering, and J.K. Ngo HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress Free Radic Biol Med 51 2011 1355 1364
    • (2011) Free Radic Biol Med , vol.51 , pp. 1355-1364
    • Grune, T.1    Catalgol, B.2    Licht, A.3    Ermak, G.4    Pickering, A.M.5    Ngo, J.K.6
  • 106
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • X. Wang, J. Yen, P. Kaiser, and L. Huang Regulation of the 26S proteasome complex during oxidative stress Sci Signal 3 2010 ra88
    • (2010) Sci Signal , vol.3 , pp. 88
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 107
    • 0031105564 scopus 로고    scopus 로고
    • Proteasome inactivation upon aging and on oxidation-effect of HSP 90
    • M. Conconi, and B. Friguet Proteasome inactivation upon aging and on oxidation-effect of HSP 90 Mol Biol Rep 24 1997 45 50 (Pubitemid 27269425)
    • (1997) Molecular Biology Reports , vol.24 , Issue.1-2 , pp. 45-50
    • Conconi, M.1    Friguet, B.2
  • 109
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • D. Harman Aging: a theory based on free radical and radiation chemistry J Gerontol 11 1956 298 300
    • (1956) J Gerontol , vol.11 , pp. 298-300
    • Harman, D.1
  • 110
    • 25844494542 scopus 로고    scopus 로고
    • Sick chaperones, cellular stress, and disease
    • A.J. Macario, and M.E. Conway de Sick chaperones, cellular stress, and disease N Engl J Med 353 2005 1489 1501
    • (2005) N Engl J Med , vol.353 , pp. 1489-1501
    • MacArio, A.J.1    Conway De, M.E.2
  • 111
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • DOI 10.1016/S0531-5565(03)00185-2
    • C. Soti, and P. Csermely Aging and molecular chaperones Exp Gerontol 38 2003 1037 1040 (Pubitemid 37324414)
    • (2003) Experimental Gerontology , vol.38 , Issue.10 , pp. 1037-1040
    • Soti, C.1    Csermely, P.2
  • 112
    • 0034571008 scopus 로고    scopus 로고
    • Molecular chaperones and the aging process
    • C. Soti, and P. Csermely Molecular chaperones and the aging process Biogerontology 1 2000 225 233
    • (2000) Biogerontology , vol.1 , pp. 225-233
    • Soti, C.1    Csermely, P.2
  • 113
    • 0027511556 scopus 로고
    • The effect of age on the synthesis of two heat shock proteins in the hsp70 family
    • B. Wu, M.J. Gu, A.R. Heydari, and A. Richardson The effect of age on the synthesis of two heat shock proteins in the hsp70 family J Gerontol 48 1993 B50 B56
    • (1993) J Gerontol , vol.48
    • Wu, B.1    Gu, M.J.2    Heydari, A.R.3    Richardson, A.4
  • 114
    • 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
    • DOI 10.1006/excr.1998.4069
    • A. Gutsmann-Conrad, A.R. Heydari, S. You, and A. Richardson 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 1998 404 413 (Pubitemid 28366566)
    • (1998) Experimental Cell Research , vol.241 , Issue.2 , pp. 404-413
    • Gutsmann-Conrad, A.1    Heydari, A.R.2    You, S.3    Richardson, A.4
  • 115
    • 0033828153 scopus 로고    scopus 로고
    • Heat shock cognate-70 gene expression declines during normal aging of the primate retina
    • S.L. Bernstein, A.M. Liu, B.C. Hansen, and R.I. Somiari Heat shock cognate-70 gene expression declines during normal aging of the primate retina Invest Ophthalmol Vis Sci 41 2000 2857 2862
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 2857-2862
    • Bernstein, S.L.1    Liu, A.M.2    Hansen, B.C.3    Somiari, R.I.4
  • 116
    • 0034630346 scopus 로고    scopus 로고
    • Age-related alterations in the activation of heat shock transcription factor 1 in rat hepatocytes
    • DOI 10.1006/excr.2000.4808
    • A.R. Heydari, S. You, R. Takahashi, A. Gutsmann-Conrad, K.D. Sarge, and A. Richardson Age-related alterations in the activation of heat shock transcription factor 1 in rat hepatocytes Exp Cell Res 256 2000 83 93 (Pubitemid 30211170)
    • (2000) Experimental Cell Research , vol.256 , Issue.1 , pp. 83-93
    • Heydari, A.R.1    You, S.2    Takahashi, R.3    Gutsmann-Conrad, A.4    Sarge, K.D.5    Richardson, A.6
  • 117
    • 0030586350 scopus 로고    scopus 로고
    • Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90
    • DOI 10.1006/abbi.1996.0303
    • M. Conconi, L.I. Szweda, R.L. Levine, E.R. Stadtman, and B. Friguet Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90 Arch Biochem Biophys 331 1996 232 240 (Pubitemid 26256072)
    • (1996) Archives of Biochemistry and Biophysics , vol.331 , Issue.2 , pp. 232-240
    • Conconi, M.1    Szweda, L.I.2    Levine, R.L.3    Stadtman, E.R.4    Friguet, B.5
  • 118
    • 33750720268 scopus 로고    scopus 로고
    • Protein oxidation and degradation during aging: Role in skin aging and neurodegeneration
    • DOI 10.1080/10715760600911154, PII W0306204J6JN1024, Free Radicals in the Aging Process - The 'Free Radical Theory of Aging' 50 years after -
    • R. Widmer, I. Ziaja, and T. Grune Protein oxidation and degradation during aging: role in skin aging and neurodegeneration Free Radic Res 40 2006 1259 1268 (Pubitemid 44698275)
    • (2006) Free Radical Research , vol.40 , Issue.12 , pp. 1259-1268
    • Widmer, R.1    Ziaja, I.2    Grune, T.3
  • 121
    • 27744605127 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Huntington's disease
    • DOI 10.1177/1073858405280639
    • A.G. Valera, M. az-Hernandez, F. Hernandez, Z. Ortega, and J.J. Lucas The ubiquitin-proteasome system in Huntington's disease Neuroscientist 11 2005 583 594 (Pubitemid 41611870)
    • (2005) Neuroscientist , vol.11 , Issue.6 , pp. 583-594
    • Valera, A.G.1    Diaz-Hernandez, M.2    Hernandez, F.3    Ortega, Z.4    Lucas, J.J.5
  • 123
    • 78650142376 scopus 로고    scopus 로고
    • Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease
    • S. Grimm, A. Hoehn, K.J. Davies, and T. Grune Protein oxidative modifications in the ageing brain: consequence for the onset of neurodegenerative disease Free Radic Res 45 2011 73 88
    • (2011) Free Radic Res , vol.45 , pp. 73-88
    • Grimm, S.1    Hoehn, A.2    Davies, K.J.3    Grune, T.4
  • 124
    • 79951925183 scopus 로고    scopus 로고
    • Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5)
    • L.V. Kalia, S.K. Kalia, H. Chau, A.M. Lozano, B.T. Hyman, and P.J. McLean Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5) PLoS One 6 2011 e14695
    • (2011) PLoS One , vol.6 , pp. 14695
    • Kalia, L.V.1    Kalia, S.K.2    Chau, H.3    Lozano, A.M.4    Hyman, B.T.5    McLean, P.J.6
  • 128
    • 23344432914 scopus 로고    scopus 로고
    • Role of molecular chaperones in neurodegenerative disorders
    • DOI 10.1080/02656730500041871, Evolving Connections Between Molecular Chaperones and Neuronal Function
    • A.B. Meriin, and M.Y. Sherman Role of molecular chaperones in neurodegenerative disorders Int J Hyperthermia 21 2005 403 419 (Pubitemid 41102940)
    • (2005) International Journal of Hyperthermia , vol.21 , Issue.5 , pp. 403-419
    • Meriin, A.B.1    Sherman, M.Y.2
  • 130
    • 3042857991 scopus 로고    scopus 로고
    • Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture
    • DOI 10.1523/JNEUROSCI.1307-04.2004
    • O. Goldbaum, and C. Richter-Landsberg Proteolytic stress causes heat shock protein induction, tau ubiquitination, and the recruitment of ubiquitin to tau-positive aggregates in oligodendrocytes in culture J Neurosci 24 2004 5748 5757 (Pubitemid 38857229)
    • (2004) Journal of Neuroscience , vol.24 , Issue.25 , pp. 5748-5757
    • Goldbaum, O.1    Richter-Landsberg, C.2
  • 131
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's Disease, and enhances its ubiquitin ligase activity
    • DOI 10.1016/S1097-2765(02)00583-X
    • Y. Imai, M. Soda, S. Hatakeyama, T. Akagi, T. Hashikawa, and K.I. Nakayama CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity Mol Cell 10 2002 55 67 (Pubitemid 34876562)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.-I.6    Takahashi, R.7
  • 132
    • 33846179357 scopus 로고    scopus 로고
    • Recommendations for the diagnosis and management of Alzheimer's disease and other disorders associated with dementia: EFNS guideline
    • G. Waldemar, B. Dubois, M. Emre, J. Georges, I.G. McKeith, and M. Rossor Recommendations for the diagnosis and management of Alzheimer's disease and other disorders associated with dementia: EFNS guideline Eur J Neurol 14 2007 e1 e26
    • (2007) Eur J Neurol , vol.14
    • Waldemar, G.1    Dubois, B.2    Emre, M.3    Georges, J.4    McKeith, I.G.5    Rossor, M.6
  • 134
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta- and gamma-secretases
    • J. Nunan, and D.H. Small Regulation of APP cleavage by alpha-, beta- and gamma-secretases FEBS Lett 483 2000 6 10
    • (2000) FEBS Lett , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 135
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • N.L. Lehman The ubiquitin proteasome system in neuropathology Acta Neuropathol 118 2009 329 347
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 136
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-β protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • DOI 10.1523/JNEUROSCI.4970-06.2007
    • G.M. Shankar, B.L. Bloodgood, M. Townsend, D.M. Walsh, D.J. Selkoe, and B.L. Sabatini Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway J Neurosci 27 2007 2866 2875 (Pubitemid 46438992)
    • (2007) Journal of Neuroscience , vol.27 , Issue.11 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 138
    • 4944267025 scopus 로고    scopus 로고
    • Cross-linking of ubiquitin, HSP27, parkin, and α-synuclein by γ-glutamyl-ε-lysine bonds in Alzheimer's neurofibrillary tangles
    • DOI 10.1096/fj.04-1493fje
    • Z. Nemes, B. Devreese, P.M. Steinert, B.J. Van, and L. Fesus Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer's neurofibrillary tangles FASEB J 18 2004 1135 1137 (Pubitemid 39561548)
    • (2004) FASEB Journal , vol.18 , Issue.10 , pp. 1135-1137
    • Nemes, Z.1    Devreese, B.2    Steinert, P.M.3    Van Beeumen, J.4    Fesus, L.5
  • 139
  • 144
    • 21244499845 scopus 로고    scopus 로고
    • The Co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates α-synuclein degradation decisions between proteasomal and lysosomal pathways
    • DOI 10.1074/jbc.M503326200
    • Y. Shin, J. Klucken, C. Patterson, B.T. Hyman, and P.J. McLean The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways J Biol Chem 280 2005 23727 23734 (Pubitemid 40884855)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23727-23734
    • Shin, Y.1    Klucken, J.2    Patterson, C.3    Hyman, B.T.4    McLean, P.J.5
  • 145
    • 0038689039 scopus 로고    scopus 로고
    • Protein aggregation and the ubiquitin proteasome pathway: Gaining the UPPer hand on neurodegeneration
    • DOI 10.1016/S0959-437X(03)00053-4
    • S.J. Berke, and H.L. Paulson Protein aggregation and the ubiquitin proteasome pathway: gaining the UPPer hand on neurodegeneration Curr Opin Genet Dev 13 2003 253 261 (Pubitemid 36645088)
    • (2003) Current Opinion in Genetics and Development , vol.13 , Issue.3 , pp. 253-261
    • Berke, S.J.S.1    Paulson, H.L.2
  • 148
    • 2442515965 scopus 로고    scopus 로고
    • Proteasome function in antigen presentation: Immunoproteasome complexes, peptide production, and interactions with viral proteins
    • DOI 10.2174/1389203043379774
    • A.J. Rivett, and A.R. Hearn Proteasome function in antigen presentation: immunoproteasome complexes, peptide production, and interactions with viral proteins Curr Protein Pept Sci 5 2004 153 161 (Pubitemid 38647468)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.3 , pp. 153-161
    • Rivett, A.J.1    Hearn, A.R.2
  • 150
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • S.I. Nishikawa, S.W. Fewell, Y. Kato, J.L. Brodsky, and T. Endo Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation J Cell Biol 153 2001 1061 1070
    • (2001) J Cell Biol , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 152
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • DOI 10.1038/nature06384, PII NATURE06384
    • T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669 (Pubitemid 350207698)
    • (2007) Nature , vol.450 , Issue.7170 , pp. 663-669
    • Rapoport, T.A.1
  • 155
    • 33748795800 scopus 로고    scopus 로고
    • EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation
    • DOI 10.1016/j.bbrc.2006.08.186, PII S0006291X06019887
    • S. Olivari, T. Cali, K.E. Salo, P. Paganetti, L.W. Ruddock, and M. Molinari EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation Biochem Biophys Res Commun 349 2006 1278 1284 (Pubitemid 44416396)
    • (2006) Biochemical and Biophysical Research Communications , vol.349 , Issue.4 , pp. 1278-1284
    • Olivari, S.1    Cali, T.2    Salo, K.E.H.3    Paganetti, P.4    Ruddock, L.W.5    Molinari, M.6
  • 156
    • 0036019901 scopus 로고    scopus 로고
    • The specificity of the yeast and human class I ER α1,2-mannosidases involved in ER quality control is not as strict as previously reported
    • A. Herscovics, P.A. Romero, and L.O. Tremblay The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported Glycobiology 12 2002 14G 15G (Pubitemid 34760065)
    • (2002) Glycobiology , vol.12 , Issue.4
    • Herscovics, A.1    Romero, P.A.2    Tremblay, L.O.3
  • 158
    • 13244265787 scopus 로고    scopus 로고
    • A novel stress-induced EDEM Variant regulating endoplasmic reticulum-associated glycoprotein degradation
    • DOI 10.1074/jbc.C400534200
    • S. Olivari, C. Galli, H. Alanen, L. Ruddock, and M. Molinari A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation J Biol Chem 280 2005 2424 2428 (Pubitemid 40189341)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2424-2428
    • Olivari, S.1    Galli, C.2    Alanen, H.3    Ruddock, L.4    Molinari, M.5
  • 159
    • 0033605219 scopus 로고    scopus 로고
    • Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
    • DOI 10.1074/jbc.274.9.5861
    • Y. Liu, P. Choudhury, C.M. Cabral, and R.N. Sifers Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome J Biol Chem 274 1999 5861 5867 (Pubitemid 29109243)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.9 , pp. 5861-5867
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 160
    • 0037157856 scopus 로고    scopus 로고
    • Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
    • M. Molinari, C. Galli, V. Piccaluga, M. Pieren, and P. Paganetti Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER J Cell Biol 158 2002 247 257
    • (2002) J Cell Biol , vol.158 , pp. 247-257
    • Molinari, M.1    Galli, C.2    Piccaluga, V.3    Pieren, M.4    Paganetti, P.5
  • 161
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • DOI 10.1126/science.1079474
    • M. Molinari, V. Calanca, C. Galli, P. Lucca, and P. Paganetti Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle Science 299 2003 1397 1400 (Pubitemid 36254653)
    • (2003) Science , vol.299 , Issue.5611 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 162
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • C. Hwang, A.J. Sinskey, and H.F. Lodish Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 164
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation
    • J. Hoseki, R. Ushioda, and K. Nagata Mechanism and components of endoplasmic reticulum-associated degradation J Biochem 147 2010 19 25
    • (2010) J Biochem , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 165
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: Versatility packed into a single fold
    • C. Appenzeller-Herzog, and L. Ellgaard The human PDI family: versatility packed into a single fold Biochim Biophys Acta 1783 2008 535 548
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 166
    • 24744471839 scopus 로고    scopus 로고
    • Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities
    • DOI 10.1074/jbc.M503377200
    • T. Kimura, Y. Hosoda, Y. Sato, Y. Kitamura, T. Ikeda, and T. Horibe Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities J Biol Chem 280 2005 31438 31441 (Pubitemid 41291885)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31438-31441
    • Kimura, T.1    Hosoda, Y.2    Sato, Y.3    Kitamura, Y.4    Ikeda, T.5    Horibe, T.6    Kikuchi, M.7
  • 167
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • DOI 10.1016/j.ceb.2004.06.012, PII S095506740400081X
    • B. Kleizen, and I. Braakman Protein folding and quality control in the endoplasmic reticulum Curr Opin Cell Biol 16 2004 343 349 (Pubitemid 38903139)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 168
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • R. Ushioda, J. Hoseki, K. Araki, G. Jansen, D.Y. Thomas, and K. Nagata ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER Science 321 2008 569 572
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 169
    • 66449089339 scopus 로고    scopus 로고
    • Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation
    • M. Sakoh-Nakatogawa, S. Nishikawa, and T. Endo Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation J Biol Chem 284 2009 11815 11825
    • (2009) J Biol Chem , vol.284 , pp. 11815-11825
    • Sakoh-Nakatogawa, M.1    Nishikawa, S.2    Endo, T.3
  • 170
    • 78149482323 scopus 로고    scopus 로고
    • Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p
    • P. Carvalho, A.M. Stanley, and T.A. Rapoport Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p Cell 143 2010 579 591
    • (2010) Cell , vol.143 , pp. 579-591
    • Carvalho, P.1    Stanley, A.M.2    Rapoport, T.A.3
  • 171
    • 33746228127 scopus 로고    scopus 로고
    • Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins
    • DOI 10.1016/j.cell.2006.05.043, PII S0092867406008579
    • P. Carvalho, V. Goder, and T.A. Rapoport Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins Cell 126 2006 361 373 (Pubitemid 44092963)
    • (2006) Cell , vol.126 , Issue.2 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 172
    • 57749114774 scopus 로고    scopus 로고
    • Sec61p is required for ERAD-L: Genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY
    • M. Willer, G.M. Forte, and C.J. Stirling Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY J Biol Chem 283 2008 33883 33888
    • (2008) J Biol Chem , vol.283 , pp. 33883-33888
    • Willer, M.1    Forte, G.M.2    Stirling, C.J.3
  • 173
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • DOI 10.1016/S0092-8674(01)00289-6
    • B. Tsai, C. Rodighiero, W.I. Lencer, and T.A. Rapoport Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin Cell 104 2001 937 948 (Pubitemid 32289285)
    • (2001) Cell , vol.104 , Issue.6 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 174
    • 27144535945 scopus 로고    scopus 로고
    • Ubx2 links the Cdc48 complex to ER-associated protein degradation
    • DOI 10.1038/ncb1298, PII N1298
    • O. Neuber, E. Jarosch, C. Volkwein, J. Walter, and T. Sommer Ubx2 links the Cdc48 complex to ER-associated protein degradation Nat Cell Biol 7 2005 993 998 (Pubitemid 41486273)
    • (2005) Nature Cell Biology , vol.7 , Issue.10 , pp. 993-998
    • Neuber, O.1    Jarosch, E.2    Volkwein, C.3    Walter, J.4    Sommer, T.5
  • 175
    • 36249022073 scopus 로고    scopus 로고
    • Ubiquitin receptors and ERAD: A network of pathways to the proteasome
    • DOI 10.1016/j.semcdb.2007.09.008, PII S1084952107001462, Degredation of Misfolded Glycoproteins
    • S. Raasi, and D.H. Wolf Ubiquitin receptors and ERAD: a network of pathways to the proteasome Semin Cell Dev Biol 18 2007 780 791 (Pubitemid 350138450)
    • (2007) Seminars in Cell and Developmental Biology , vol.18 , Issue.6 , pp. 780-791
    • Raasi, S.1    Wolf, D.H.2
  • 177
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • DOI 10.1038/sj.emboj.7600946, PII 7600946
    • T. Ravid, S.G. Kreft, and M. Hochstrasser Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways EMBO J 25 2006 533 543 (Pubitemid 43237660)
    • (2006) EMBO Journal , vol.25 , Issue.3 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 179
    • 33846008398 scopus 로고    scopus 로고
    • Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants
    • DOI 10.1074/jbc.M607085200
    • F. Sun, R. Zhang, X. Gong, X. Geng, P.F. Drain, and R.A. Frizzell Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants J Biol Chem 281 2006 36856 36863 (Pubitemid 46042153)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36856-36863
    • Sun, F.1    Zhang, R.2    Gong, X.3    Geng, X.4    Drain, P.F.5    Frizzell, R.A.6
  • 180
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1?SEL1L ubiquitin ligase complex for ERAD
    • DOI 10.1038/ncb1689, PII NCB1689
    • J.C. Christianson, T.A. Shaler, R.E. Tyler, and R.R. Kopito OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD Nat Cell Biol 10 2008 272 282 (Pubitemid 351331014)
    • (2008) Nature Cell Biology , vol.10 , Issue.3 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 181
    • 51049121849 scopus 로고    scopus 로고
    • Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    • N. Hosokawa, I. Wada, K. Nagasawa, T. Moriyama, K. Okawa, and K. Nagata Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP J Biol Chem 283 2008 20914 20924
    • (2008) J Biol Chem , vol.283 , pp. 20914-20924
    • Hosokawa, N.1    Wada, I.2    Nagasawa, K.3    Moriyama, T.4    Okawa, K.5    Nagata, K.6
  • 183
    • 0034651604 scopus 로고    scopus 로고
    • Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system
    • K. Hill, and A.A. Cooper Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system EMBO J 19 2000 550 561 (Pubitemid 30093728)
    • (2000) EMBO Journal , vol.19 , Issue.4 , pp. 550-561
    • Hill, K.1    Cooper, A.A.2
  • 184
    • 0037043340 scopus 로고    scopus 로고
    • An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport
    • C.M. Haynes, S. Caldwell, and A.A. Cooper An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport J Cell Biol 158 2002 91 101
    • (2002) J Cell Biol , vol.158 , pp. 91-101
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3
  • 186
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death
    • DOI 10.1016/j.molcel.2004.08.025, PII S1097276504005118
    • C.M. Haynes, E.A. Titus, and A.A. Cooper Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death Mol Cell 15 2004 767 776 (Pubitemid 39194906)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 187
    • 74849136799 scopus 로고    scopus 로고
    • Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia
    • T. Rzymski, M. Milani, D.C. Singleton, and A.L. Harris Role of ATF4 in regulation of autophagy and resistance to drugs and hypoxia Cell Cycle 8 2009 3838 3847
    • (2009) Cell Cycle , vol.8 , pp. 3838-3847
    • Rzymski, T.1    Milani, M.2    Singleton, D.C.3    Harris, A.L.4
  • 188
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • DOI 10.1182/blood-2005-08-3531
    • E.A. Obeng, L.M. Carlson, D.M. Gutman, W.J. Harrington Jr., K.P. Lee, and L.H. Boise Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells Blood 107 2006 4907 4916 (Pubitemid 43882644)
    • (2006) Blood , vol.107 , Issue.12 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, L.H.6
  • 189
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • DOI 10.1083/jcb.200311055
    • B.P. Tu, and J.S. Weissman Oxidative protein folding in eukaryotes: mechanisms and consequences J Cell Biol 164 2004 341 346 (Pubitemid 38174761)
    • (2004) Journal of Cell Biology , vol.164 , Issue.3 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 190
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent Activation of Nrf2 Contributes to Redox Homeostasis and Cell Survival following Endoplasmic Reticulum Stress
    • DOI 10.1074/jbc.M314219200
    • S.B. Cullinan, and J.A. Diehl PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress J Biol Chem 279 2004 20108 20117 (Pubitemid 38623455)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 192
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state
    • DOI 10.1128/MCB.21.4.1249-1259.2001
    • K.D. McCullough, J.L. Martindale, L.O. Klotz, T.Y. Aw, and N.J. Holbrook Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state Mol Cell Biol 21 2001 1249 1259 (Pubitemid 32114973)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.4 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.-O.3    Aw, T.-Y.4    Holbrook, N.J.5


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