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Volumn 9, Issue 12, 2013, Pages 1937-1954

HSPA8/HSC70 chaperone protein: Structure, function, and chemical targeting

Author keywords

Autophagy; HSC70; Lupus; Nucleotide exhange factor; P140 peptide; X ray structure

Indexed keywords

1 ETHYL 2 [[3 ETHYL 5 (3 METHYLBENZOTHIAZOLIN 2 YLIDENE) 4 OXOTHIAZOLIDIN 2 YLIDENE]METHYL]PYRIDINIUM CHLORIDE; 15 DEOXYSPERGUALIN; 2 PHENYLETHYNESULFONAMIDE; ADENOSINE TRIPHOSPHATE; ANTIGEN; DIHYDROPYRIMIDINE DEHYDROGENASE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 110; P140 PEPTIDE; PEPTIDE; UNCLASSIFIED DRUG;

EID: 84890913411     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.26448     Document Type: Review
Times cited : (293)

References (249)
  • 1
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • PMID:23582321
    • Nussinov R, Tsai CJ. Allostery in disease and in drug discovery. Cell 2013; 153:293-305; PMID:23582321; http://dx.doi.org/10.1016/j.cell.2013.03.034
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.J.2
  • 2
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • PMID:15770419
    • Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 2005; 62:670-84; PMID:15770419; http://dx.doi.org/10.1007/s00018-004-4464-6
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 3
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • PMID:17544402
    • Daugaard M, Rohde M, Jäättelä M. The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions. FEBS Lett 2007; 581:3702-10; PMID:17544402; http://dx.doi.org/10.1016/j.febslet. 2007.05.039
    • (2007) FEBS Lett , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jäättelä, M.3
  • 4
    • 58849143814 scopus 로고    scopus 로고
    • From hatching to dispatching: The multiple cellular roles of the Hsp70 molecular chaperone machinery
    • PMID:18852216
    • Meimaridou E, Gooljar SB, Chapple JP. From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery. J Mol Endocrinol 2009; 42:1-9; PMID:18852216; http://dx.doi.org/10.1677/JME-08-0116
    • (2009) J Mol Endocrinol , vol.42 , pp. 1-9
    • Meimaridou, E.1    Gooljar, S.B.2    Chapple, J.P.3
  • 5
    • 77953734857 scopus 로고    scopus 로고
    • Heat shock protein 70 (hsp70) as an emerging drug target
    • PMID:20334364
    • Evans CG, Chang L, Gestwicki JE. Heat shock protein 70 (hsp70) as an emerging drug target. J Med Chem 2010; 53:4585-602; PMID:20334364; http://dx.doi.org/10.1021/jm100054f
    • (2010) J Med Chem , vol.53 , pp. 4585-4602
    • Evans, C.G.1    Chang, L.2    Gestwicki, J.E.3
  • 6
    • 84867840534 scopus 로고    scopus 로고
    • Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential
    • PMID:22960394
    • Liu T, Daniels CK, Cao S. Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential. Pharmacol Ther 2012; 136:354-74; PMID:22960394; http://dx.doi.org/10.1016/j.pharmthera.2012.08.014
    • (2012) Pharmacol Ther , vol.136 , pp. 354-374
    • Liu, T.1    Daniels, C.K.2    Cao, S.3
  • 7
    • 0028674882 scopus 로고
    • Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus
    • PMID:7704574
    • Gupta RS, Singh B. Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus. Curr Biol 1994; 4:1104-14; PMID:7704574; http://dx.doi.org/10.1016/S0960-9822(00)00249-9
    • (1994) Curr Biol , vol.4 , pp. 1104-1114
    • Gupta, R.S.1    Singh, B.2
  • 8
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70
    • PMID:3931075
    • Hunt C, Morimoto RI. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc Natl Acad Sci U S A 1985; 82:6455-9; PMID:3931075; http://dx.doi.org/10.1073/pnas.82. 19.6455
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 6455-6459
    • Hunt, C.1    Morimoto, R.I.2
  • 9
    • 0024151897 scopus 로고
    • The heat-shock proteins
    • PMID:2853609
    • Lindquist S, Craig EA. The heat-shock proteins. Annu Rev Genet 1988; 22:631-77; PMID:2853609; http://dx.doi.org/10.1146/annurev.ge.22.120188.003215
    • (1988) Annu Rev Genet , vol.22 , pp. 631-677
    • Lindquist, S.1    Craig, E.A.2
  • 10
    • 0021767876 scopus 로고
    • Hsp70 accelerates the recovery of nucleolar morphology after heat shock
    • PMID:6441707
    • Pelham HR. Hsp70 accelerates the recovery of nucleolar morphology after heat shock. EMBO J 1984; 3:3095-100; PMID:6441707
    • (1984) EMBO J , vol.3 , pp. 3095-3100
    • Pelham, H.R.1
  • 11
    • 0026073457 scopus 로고
    • Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene
    • PMID:1705702
    • Li GC, Li LG, Liu YK, Mak JY, Chen LL, Lee WM. Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene. Proc Natl Acad Sci U S A 1991; 88:1681-5; PMID:1705702; http://dx.doi.org/10.1073/pnas.88.5.1681
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 1681-1685
    • Li, G.C.1    Li, L.G.2    Liu, Y.K.3    Mak, J.Y.4    Chen, L.L.5    Lee, W.M.6
  • 12
    • 0026703222 scopus 로고
    • Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity
    • PMID:1396553
    • Jäättelä M, Wissing D, Bauer PA, Li GC. Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity. EMBO J 1992; 11:3507-12; PMID:1396553
    • (1992) EMBO J , vol.11 , pp. 3507-3512
    • Jäättelä, M.1    Wissing, D.2    Bauer, P.A.3    Li, G.C.4
  • 13
    • 0033615369 scopus 로고    scopus 로고
    • Phylogenetic analysis of the third hsp70 homolog in Escherichia coli; a novel member of the Hsc66 subfamily and its possible co-chaperone
    • PMID:10574456
    • Itoh T, Matsuda H, Mori H. Phylogenetic analysis of the third hsp70 homolog in Escherichia coli; a novel member of the Hsc66 subfamily and its possible co-chaperone. DNA Res 1999; 6:299-305; PMID:10574456; http://dx.doi.org/10.1093/dnares/6.5.299
    • (1999) DNA Res , vol.6 , pp. 299-305
    • Itoh, T.1    Matsuda, H.2    Mori, H.3
  • 14
    • 0024894102 scopus 로고
    • Expression of members of the Saccharomyces cerevisiae hsp70 multigene family
    • PMID:2698838
    • Werner-Washburne M, Craig EA. Expression of members of the Saccharomyces cerevisiae hsp70 multigene family. Genome 1989; 31:684-9; PMID:2698838; http://dx.doi.org/10.1139/g89-125
    • (1989) Genome , vol.31 , pp. 684-689
    • Werner-Washburne, M.1    Craig, E.A.2
  • 15
    • 0023375806 scopus 로고
    • Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae
    • PMID:3302682
    • Werner-Washburne M, Stone DE, Craig EA. Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae. Mol Cell Biol 1987; 7:2568-77; PMID:3302682
    • (1987) Mol Cell Biol , vol.7 , pp. 2568-2577
    • Werner-Washburne, M.1    Stone, D.E.2    Craig, E.A.3
  • 16
    • 0028036148 scopus 로고
    • Molecular evolution of the HSP70 multigene family
    • PMID:8151709
    • Boorstein WR, Ziegelhoffer T, Craig EA. Molecular evolution of the HSP70 multigene family. J Mol Evol 1994; 38:1-17; PMID:8151709; http://dx.doi.org/10. 1007/BF00175490
    • (1994) J Mol Evol , vol.38 , pp. 1-17
    • Boorstein, W.R.1    Ziegelhoffer, T.2    Craig, E.A.3
  • 18
    • 0032965580 scopus 로고    scopus 로고
    • Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution
    • PMID:10048327
    • Bertelsen EB, Zhou H, Lowry DF, Flynn GC, Dahlquist FW. Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. Protein Sci 1999; 8:343-54; PMID:10048327; http://dx.doi.org/10.1110/ps.8.2.343
    • (1999) Protein Sci , vol.8 , pp. 343-354
    • Bertelsen, E.B.1    Zhou, H.2    Lowry, D.F.3    Flynn, G.C.4    Dahlquist, F.W.5
  • 19
    • 0036177548 scopus 로고    scopus 로고
    • Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: Yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1
    • PMID:11743879
    • Qian XG, Hou WB, Zhengang L, Sha BD. Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem J 2002; 361:27-34; PMID:11743879; http://dx.doi.org/10.1042/0264-6021:3610027
    • (2002) Biochem J , vol.361 , pp. 27-34
    • Qian, X.G.1    Hou, W.B.2    Zhengang, L.3    Sha, B.D.4
  • 20
    • 33748743974 scopus 로고    scopus 로고
    • Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex
    • PMID:16737444
    • Li J, Wu Y, Qian X, Sha B. Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex. Biochem J 2006; 398:353-60; PMID:16737444; http://dx.doi.org/10.1042/BJ20060618
    • (2006) Biochem J , vol.398 , pp. 353-360
    • Li, J.1    Wu, Y.2    Qian, X.3    Sha, B.4
  • 21
    • 0034803613 scopus 로고    scopus 로고
    • Characterization and regulation of the major histocompatibility complex-encoded proteins Hsp70-Hom and Hsp70-1/2
    • PMID:11599570
    • Fourie AM, Peterson PA, Yang Y. Characterization and regulation of the major histocompatibility complex-encoded proteins Hsp70-Hom and Hsp70-1/2. Cell Stress Chaperones 2001; 6:282-95; PMID:11599570; http://dx.doi.org/10.1379/1466- 1268(2001)006〈0282:CAROTM〉2.0.CO;2
    • (2001) Cell Stress Chaperones , vol.6 , pp. 282-295
    • Fourie, A.M.1    Peterson, P.A.2    Yang, Y.3
  • 22
    • 0033837992 scopus 로고    scopus 로고
    • Putative creatine kinase M-isoform in human sperm is identifiedas the 70-kilodalton heat shock protein HspA2
    • PMID:10952940
    • Huszar G, Stone K, Dix D, Vigue L. Putative creatine kinase M-isoform in human sperm is identifiedas the 70-kilodalton heat shock protein HspA2. Biol Reprod 2000; 63:925-32; PMID:10952940; http://dx.doi.org/10.1095/biolreprod63.3. 925
    • (2000) Biol Reprod , vol.63 , pp. 925-932
    • Huszar, G.1    Stone, K.2    Dix, D.3    Vigue, L.4
  • 23
    • 79956219069 scopus 로고    scopus 로고
    • Differential expression of HSPA1 and HSPA2 proteins in human tissues; tissue microarray-based immunohistochemical study
    • PMID:21373891
    • Scieglinska D, Piglowski W, Chekan M, Mazurek A, Krawczyk Z. Differential expression of HSPA1 and HSPA2 proteins in human tissues; tissue microarray-based immunohistochemical study. Histochem Cell Biol 2011; 135:337-50; PMID:21373891; http://dx.doi.org/10.1007/s00418-011-0791-5
    • (2011) Histochem Cell Biol , vol.135 , pp. 337-350
    • Scieglinska, D.1    Piglowski, W.2    Chekan, M.3    Mazurek, A.4    Krawczyk, Z.5
  • 24
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • PMID:15741319
    • Rohde M, Daugaard M, Jensen MH, Helin K, Nylandsted J, Jäättelä M. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 2005; 19:570-82; PMID:15741319; http://dx.doi.org/10.1101/gad.305405
    • (2005) Genes Dev , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5    Jäättelä, M.6
  • 25
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • PMID:10597629
    • Gething MJ. Role and regulation of the ER chaperone BiP. Semin Cell Dev Biol 1999; 10:465-72; PMID:10597629; http://dx.doi.org/10.1006/scdb.1999.0318
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 28
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • PMID:16678092
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125:443-51; PMID:16678092; http://dx.doi.org/10.1016/j.cell. 2006.04.014
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 29
    • 2442667773 scopus 로고    scopus 로고
    • Nuclear translocation of papillomavirus minor capsid protein L2 requires Hsc70
    • PMID:15140951
    • Florin L, Becker KA, Sapp C, Lambert C, Sirma H, Müller M, Streeck RE, Sapp M. Nuclear translocation of papillomavirus minor capsid protein L2 requires Hsc70. J Virol 2004; 78:5546-53; PMID:15140951; http://dx.doi.org/10. 1128/JVI.78.11.5546-5553.2004
    • (2004) J Virol , vol.78 , pp. 5546-5553
    • Florin, L.1    Becker, K.A.2    Sapp, C.3    Lambert, C.4    Sirma, H.5    Müller, M.6    Streeck, R.E.7    Sapp, M.8
  • 30
    • 0024380865 scopus 로고
    • Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein
    • PMID:2573603
    • Mizzen LA, Chang C, Garrels JI, Welch WJ. Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. J Biol Chem 1989; 264:20664-75; PMID:2573603
    • (1989) J Biol Chem , vol.264 , pp. 20664-20675
    • Mizzen, L.A.1    Chang, C.2    Garrels, J.I.3    Welch, W.J.4
  • 31
    • 0036666032 scopus 로고    scopus 로고
    • An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: What, when, and where?
    • PMID:12482206
    • Wadhwa R, Taira K, Kaul SC. An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where? Cell Stress Chaperones 2002; 7:309-16; PMID:12482206; http://dx.doi.org/10.1379/1466-1268(2002) 007〈0309:AHFCMM〉2.0.CO;2
    • (2002) Cell Stress Chaperones , vol.7 , pp. 309-316
    • Wadhwa, R.1    Taira, K.2    Kaul, S.C.3
  • 34
    • 79952273669 scopus 로고    scopus 로고
    • The chaperone network connected to human ribosome-associated complex
    • PMID:21245388
    • Jaiswal H, Conz C, Otto H, Wölfle T, Fitzke E, Mayer MP, Rospert S. The chaperone network connected to human ribosome-associated complex. Mol Cell Biol 2011; 31:1160-73; PMID:21245388; http://dx.doi.org/10.1128/MCB.00986-10
    • (2011) Mol Cell Biol , vol.31 , pp. 1160-1173
    • Jaiswal, H.1    Conz, C.2    Otto, H.3    Wölfle, T.4    Fitzke, E.5    Mayer, M.P.6    Rospert, S.7
  • 35
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • PMID:2143562
    • Flaherty KM, DeLuca-Flaherty C, McKay DB. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 1990; 346:623-8; PMID:2143562; http://dx.doi.org/10.1038/346623a0
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 36
    • 77952530199 scopus 로고    scopus 로고
    • Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78
    • PMID:20072699
    • Wisniewska M, Karlberg T, Lehtiö L, Johansson I, Kotenyova T, Moche M, Schüler H. Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78. PLoS One 2010; 5:e8625; PMID:20072699; http://dx.doi.org/10.1371/journal.pone. 0008625
    • (2010) PLoS One , vol.5
    • Wisniewska, M.1    Karlberg, T.2    Lehtiö, L.3    Johansson, I.4    Kotenyova, T.5    Moche, M.6    Schüler, H.7
  • 37
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • PMID:8658133
    • Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 1996; 272:1606-14; PMID:8658133; http://dx.doi.org/10. 1126/science.272.5268.1606
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.1    Zhao, X.2    Burkholder, W.F.3    Gragerov, A.4    Ogata, C.M.5    Gottesman, M.E.6    Hendrickson, W.A.7
  • 38
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones
    • PMID:23123194
    • Kityk R, Kopp J, Sinning I, Mayer MP. Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol Cell 2012; 48:863-74; PMID:23123194; http://dx.doi.org/10.1016/j.molcel.2012.09.023
    • (2012) Mol Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 40
    • 2442444156 scopus 로고    scopus 로고
    • The lid subdomain of DnaK is required for the stabilization of the substrate-binding site
    • PMID:14985342
    • Moro F, Fernández-Sáiz V, Muga A. The lid subdomain of DnaK is required for the stabilization of the substrate-binding site. J Biol Chem 2004; 279:19600-6; PMID:14985342; http://dx.doi.org/10.1074/jbc.M400921200
    • (2004) J Biol Chem , vol.279 , pp. 19600-19606
    • Moro, F.1    Fernández-Sáiz, V.2    Muga, A.3
  • 41
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • PMID:10786835
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000; 101:199-210; PMID:10786835; http://dx.doi.org/10.1016/S0092-8674(00)80830-2
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 42
    • 69949149115 scopus 로고    scopus 로고
    • Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: Computational analysis and protein engineering
    • PMID:19586912
    • Kajander T, Sachs JN, Goldman A, Regan L. Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering. J Biol Chem 2009; 284:25364-74; PMID:19586912; http://dx.doi.org/10.1074/jbc.M109.033894
    • (2009) J Biol Chem , vol.284 , pp. 25364-25374
    • Kajander, T.1    Sachs, J.N.2    Goldman, A.3    Regan, L.4
  • 43
    • 0037205411 scopus 로고    scopus 로고
    • Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes
    • PMID:11877417
    • Brinker A, Scheufler C, Von Der Mulbe F, Fleckenstein B, Herrmann C, Jung G, Moarefi I, Hartl FU. Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes. J Biol Chem 2002; 277:19265-75; PMID:11877417; http://dx.doi.org/10.1074/jbc.M109002200
    • (2002) J Biol Chem , vol.277 , pp. 19265-19275
    • Brinker, A.1    Scheufler, C.2    Von Der Mulbe, F.3    Fleckenstein, B.4    Herrmann, C.5    Jung, G.6    Moarefi, I.7    Hartl, F.U.8
  • 44
    • 0033578346 scopus 로고    scopus 로고
    • Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein
    • PMID:10451379
    • Johnson ER, McKay DB. Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein. Biochemistry 1999; 38:10823-30; PMID:10451379; http://dx.doi.org/10.1021/bi990816g
    • (1999) Biochemistry , vol.38 , pp. 10823-10830
    • Johnson, E.R.1    McKay, D.B.2
  • 46
    • 34848869936 scopus 로고    scopus 로고
    • Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
    • PMID:17923091
    • Liu Q, Hendrickson WA. Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell 2007; 131:106-20; PMID:17923091; http://dx.doi.org/10.1016/j.cell.2007.08.039
    • (2007) Cell , vol.131 , pp. 106-120
    • Liu, Q.1    Hendrickson, W.A.2
  • 47
    • 0032474433 scopus 로고    scopus 로고
    • NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: A preview of chaperone-protein interaction
    • PMID:9609686
    • Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER. NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Biochemistry 1998; 37:7929-40; PMID:9609686; http://dx.doi.org/10.1021/bi9800855
    • (1998) Biochemistry , vol.37 , pp. 7929-7940
    • Wang, H.1    Kurochkin, A.V.2    Pang, Y.3    Hu, W.4    Flynn, G.C.5    Zuiderweg, E.R.6
  • 48
    • 0033603631 scopus 로고    scopus 로고
    • High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70
    • PMID:10373374
    • Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER. High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70. J Mol Biol 1999; 289:1387-403; PMID:10373374; http://dx.doi.org/10.1006/jmbi.1999.2776
    • (1999) J Mol Biol , vol.289 , pp. 1387-1403
    • Morshauser, R.C.1    Hu, W.2    Wang, H.3    Pang, Y.4    Flynn, G.C.5    Zuiderweg, E.R.6
  • 49
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • PMID:7776367
    • McCarty JS, Buchberger A, Reinstein J, Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J Mol Biol 1995; 249:126-37; PMID:7776367; http://dx.doi.org/10.1006/jmbi.1995.0284
    • (1995) J Mol Biol , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 50
    • 0028584378 scopus 로고
    • ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain
    • PMID:7981225
    • Ha JH, McKay DB. ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain. Biochemistry 1994; 33:14625-35; PMID:7981225; http://dx.doi.org/10.1021/bi00252a031
    • (1994) Biochemistry , vol.33 , pp. 14625-14635
    • Ha, J.H.1    McKay, D.B.2
  • 51
    • 0028914392 scopus 로고
    • Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
    • PMID:7876226
    • Jordan R, McMacken R. Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins. J Biol Chem 1995; 270:4563-9; PMID:7876226; http://dx.doi.org/10.1074/jbc.270.9.4563
    • (1995) J Biol Chem , vol.270 , pp. 4563-4569
    • Jordan, R.1    McMacken, R.2
  • 52
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • PMID:16307916
    • Jiang J, Prasad K, Lafer EM, Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol Cell 2005; 20:513-24; PMID:16307916; http://dx.doi.org/10.1016/j.molcel.2005.09.028
    • (2005) Mol Cell , vol.20 , pp. 513-524
    • Jiang, J.1    Prasad, K.2    Lafer, E.M.3    Sousa, R.4
  • 53
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • PMID:17434124
    • Swain JF, Dinler G, Sivendran R, Montgomery DL, Stotz M, Gierasch LM. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol Cell 2007; 26:27-39; PMID:17434124; http://dx.doi.org/10.1016/j.molcel.2007.02.020
    • (2007) Mol Cell , vol.26 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 54
    • 33745183353 scopus 로고    scopus 로고
    • Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation
    • PMID:16613854
    • Rist W, Graf C, Bukau B, Mayer MP. Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. J Biol Chem 2006; 281:16493-501; PMID:16613854; http://dx.doi.org/10.1074/jbc. M600847200
    • (2006) J Biol Chem , vol.281 , pp. 16493-16501
    • Rist, W.1    Graf, C.2    Bukau, B.3    Mayer, M.P.4
  • 55
    • 33846020582 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
    • PMID:17052976
    • Vogel M, Mayer MP, Bukau B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J Biol Chem 2006; 281:38705-11; PMID:17052976; http://dx.doi.org/10.1074/jbc.M609020200
    • (2006) J Biol Chem , vol.281 , pp. 38705-38711
    • Vogel, M.1    Mayer, M.P.2    Bukau, B.3
  • 56
    • 79955565642 scopus 로고    scopus 로고
    • Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
    • PMID:21482798
    • Zhuravleva A, Gierasch LM. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc Natl Acad Sci U S A 2011; 108:6987-92; PMID:21482798; http://dx.doi.org/10.1073/pnas.1014448108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6987-6992
    • Zhuravleva, A.1    Gierasch, L.M.2
  • 57
    • 44649169371 scopus 로고    scopus 로고
    • Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation
    • PMID:18400763
    • Chang YW, Sun YJ, Wang C, Hsiao CD. Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation. J Biol Chem 2008; 283:15502-11; PMID:18400763; http://dx.doi.org/10.1074/jbc.M708992200
    • (2008) J Biol Chem , vol.283 , pp. 15502-15511
    • Chang, Y.W.1    Sun, Y.J.2    Wang, C.3    Hsiao, C.D.4
  • 58
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. Coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • PMID:19439666
    • Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S A 2009; 106:8471-6; PMID:19439666; http://dx.doi.org/10. 1073/pnas.0903503106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.4
  • 59
    • 84870916379 scopus 로고    scopus 로고
    • An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
    • PMID:23217711
    • Zhuravleva A, Clerico EM, Gierasch LM. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 2012; 151:1296-307; PMID:23217711; http://dx.doi.org/10.1016/j. cell.2012.11.002
    • (2012) Cell , vol.151 , pp. 1296-1307
    • Zhuravleva, A.1    Clerico, E.M.2    Gierasch, L.M.3
  • 60
    • 84867382657 scopus 로고    scopus 로고
    • Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones
    • PMID:22851130
    • Gillies AT, Taylor R, Gestwicki JE. Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones. Mol Biosyst 2012; 8:2901-8; PMID:22851130; http://dx.doi.org/10.1039/c2mb25248a
    • (2012) Mol Biosyst , vol.8 , pp. 2901-2908
    • Gillies, A.T.1    Taylor, R.2    Gestwicki, J.E.3
  • 61
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • PMID:20651708
    • Kampinga HH, Craig EA. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 2010; 11:579-92; PMID:20651708; http://dx.doi.org/10.1038/nrm2941
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 62
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • PMID:8764402
    • Qian YQ, Patel D, Hartl FU, McColl DJ. Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J Mol Biol 1996; 260:224-35; PMID:8764402; http://dx.doi.org/10.1006/jmbi.1996.0394
    • (1996) J Mol Biol , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.U.3    McColl, D.J.4
  • 63
    • 0028170215 scopus 로고
    • The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication
    • PMID:8106526
    • Wall D, Zylicz M, Georgopoulos C. The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. J Biol Chem 1994; 269:5446-51; PMID:8106526
    • (1994) J Biol Chem , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 64
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • PMID:9476895
    • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998; 92:351-66; PMID:9476895; http://dx.doi.org/10.1016/S0092-8674(00)80928-9
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 65
    • 35649024724 scopus 로고    scopus 로고
    • Structural basis of J cochaperone binding and regulation of Hsp70
    • PMID:17996706
    • Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R. Structural basis of J cochaperone binding and regulation of Hsp70. Mol Cell 2007; 28:422-33; PMID:17996706; http://dx.doi.org/10.1016/j.molcel.2007.08.022
    • (2007) Mol Cell , vol.28 , pp. 422-433
    • Jiang, J.1    Maes, E.G.2    Taylor, A.B.3    Wang, L.4    Hinck, A.P.5    Lafer, E.M.6    Sousa, R.7
  • 68
    • 84863163676 scopus 로고    scopus 로고
    • The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation
    • PMID:22219199
    • Gao XC, Zhou CJ, Zhou ZR, Wu M, Cao CY, Hu HY. The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation. J Biol Chem 2012; 287:6044-52; PMID:22219199; http://dx.doi.org/10.1074/jbc. M111.294728
    • (2012) J Biol Chem , vol.287 , pp. 6044-6052
    • Gao, X.C.1    Zhou, C.J.2    Zhou, Z.R.3    Wu, M.4    Cao, C.Y.5    Hu, H.Y.6
  • 70
    • 79952364237 scopus 로고    scopus 로고
    • Mechanics of Hsp70 chaperones enables differential interaction with client proteins
    • PMID:21278757
    • Schlecht R, Erbse AH, Bukau B, Mayer MP. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol 2011; 18:345-51; PMID:21278757; http://dx.doi.org/10.1038/nsmb.2006
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 345-351
    • Schlecht, R.1    Erbse, A.H.2    Bukau, B.3    Mayer, M.P.4
  • 71
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
    • PMID:9321400
    • Höhfeld J, Jentsch S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J 1997; 16:6209-16; PMID:9321400; http://dx.doi.org/10.1093/emboj/16.20.6209
    • (1997) EMBO J , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 72
    • 79960691369 scopus 로고    scopus 로고
    • Biochemical and structural studies on the high affinity of Hsp70 for ADP
    • PMID:21608060
    • Arakawa A, Handa N, Shirouzu M, Yokoyama S. Biochemical and structural studies on the high affinity of Hsp70 for ADP. Protein Sci 2011; 20:1367-79; PMID:21608060; http://dx.doi.org/10.1002/pro.663
    • (2011) Protein Sci , vol.20 , pp. 1367-1379
    • Arakawa, A.1    Handa, N.2    Shirouzu, M.3    Yokoyama, S.4
  • 73
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • PMID:9103205
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 1997; 276:431-5; PMID:9103205; http://dx.doi.org/10.1126/science.276.5311.431
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 74
    • 84862289262 scopus 로고    scopus 로고
    • Crystal structure of DnaK protein complexed with nucleotide exchange factor GrpE in DnaK chaperone system: Insight into intermolecular communication
    • PMID:22544739
    • Wu CC, Naveen V, Chien CH, Chang YW, Hsiao CD. Crystal structure of DnaK protein complexed with nucleotide exchange factor GrpE in DnaK chaperone system: insight into intermolecular communication. J Biol Chem 2012; 287:21461-70; PMID:22544739; http://dx.doi.org/10.1074/jbc.M112.344358
    • (2012) J Biol Chem , vol.287 , pp. 21461-21470
    • Wu, C.C.1    Naveen, V.2    Chien, C.H.3    Chang, Y.W.4    Hsiao, C.D.5
  • 75
    • 0028850629 scopus 로고
    • Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins
    • PMID:8524277
    • Laloraya S, Dekker PJ, Voos W, Craig EA, Pfanner N. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins. Mol Cell Biol 1995; 15:7098-105; PMID:8524277
    • (1995) Mol Cell Biol , vol.15 , pp. 7098-7105
    • Laloraya, S.1    Dekker, P.J.2    Voos, W.3    Craig, E.A.4    Pfanner, N.5
  • 76
    • 0029020451 scopus 로고
    • The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria
    • PMID:7628446
    • Westermann B, Prip-Buus C, Neupert W, Schwarz E. The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria. EMBO J 1995; 14:3452-60; PMID:7628446
    • (1995) EMBO J , vol.14 , pp. 3452-3460
    • Westermann, B.1    Prip-Buus, C.2    Neupert, W.3    Schwarz, E.4
  • 78
    • 0347033285 scopus 로고    scopus 로고
    • BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP
    • PMID:12356756
    • Chung KT, Shen Y, Hendershot LM. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J Biol Chem 2002; 277:47557-63; PMID:12356756; http://dx.doi.org/10.1074/jbc. M208377200
    • (2002) J Biol Chem , vol.277 , pp. 47557-47563
    • Chung, K.T.1    Shen, Y.2    Hendershot, L.M.3
  • 79
    • 0037032470 scopus 로고    scopus 로고
    • HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor
    • PMID:12417338
    • Kabani M, McLellan C, Raynes DA, Guerriero V, Brodsky JL. HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett 2002; 531:339-42; PMID:12417338; http://dx.doi.org/10.1016/ S0014-5793(02)03570-6
    • (2002) FEBS Lett , vol.531 , pp. 339-342
    • Kabani, M.1    McLellan, C.2    Raynes, D.A.3    Guerriero, V.4    Brodsky, J.L.5
  • 80
  • 81
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • PMID:18555782
    • Polier S, Dragovic Z, Hartl FU, Bracher A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 2008; 133:1068-79; PMID:18555782; http://dx.doi.org/10.1016/j.cell.2008.05.022
    • (2008) Cell , vol.133 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 83
    • 43049155955 scopus 로고    scopus 로고
    • The BAG proteins: A ubiquitous family of chaperone regulators
    • PMID:18264803
    • Kabbage M, Dickman MB. The BAG proteins: a ubiquitous family of chaperone regulators. Cell Mol Life Sci 2008; 65:1390-402; PMID:18264803; http://dx.doi.org/10.1007/s00018-008-7535-2
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1390-1402
    • Kabbage, M.1    Dickman, M.B.2
  • 85
    • 0034790768 scopus 로고    scopus 로고
    • Molecular chaperone targeting and regulation by BAG family proteins
    • PMID:11584289
    • Takayama S, Reed JC. Molecular chaperone targeting and regulation by BAG family proteins. Nat Cell Biol 2001; 3:E237-41; PMID:11584289; http://dx.doi.org/10.1038/ncb1001-e237
    • (2001) Nat Cell Biol , vol.3
    • Takayama, S.1    Reed, J.C.2
  • 86
    • 0034618385 scopus 로고    scopus 로고
    • CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70
    • PMID:10980614
    • Doong H, Price J, Kim YS, Gasbarre C, Probst J, Liotta LA, Blanchette J, Rizzo K, Kohn E. CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70. Oncogene 2000; 19:4385-95; PMID:10980614; http://dx.doi.org/10.1038/sj.onc.1203797
    • (2000) Oncogene , vol.19 , pp. 4385-4395
    • Doong, H.1    Price, J.2    Kim, Y.S.3    Gasbarre, C.4    Probst, J.5    Liotta, L.A.6    Blanchette, J.7    Rizzo, K.8    Kohn, E.9
  • 87
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • PMID:11222862
    • Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 2001; 291:1553-7; PMID:11222862; http://dx.doi.org/10.1126/science.1057268
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 88
    • 57149092290 scopus 로고    scopus 로고
    • Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2
    • PMID:19029896
    • Xu Z, Page RC, Gomes MM, Kohli E, Nix JC, Herr AB, Patterson C, Misra S. Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2. Nat Struct Mol Biol 2008; 15:1309-17; PMID:19029896; http://dx.doi.org/10.1038/nsmb.1518
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1309-1317
    • Xu, Z.1    Page, R.C.2    Gomes, M.M.3    Kohli, E.4    Nix, J.C.5    Herr, A.B.6    Patterson, C.7    Misra, S.8
  • 89
    • 77649095684 scopus 로고    scopus 로고
    • The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange
    • PMID:20223214
    • Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S. The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure 2010; 18:309-19; PMID:20223214; http://dx.doi.org/10.1016/j.str.2010.01.004
    • (2010) Structure , vol.18 , pp. 309-319
    • Arakawa, A.1    Handa, N.2    Ohsawa, N.3    Shida, M.4    Kigawa, T.5    Hayashi, F.6    Shirouzu, M.7    Yokoyama, S.8
  • 90
    • 3142677815 scopus 로고    scopus 로고
    • The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains
    • PMID:15232009
    • Zhang Y, Zuiderweg ER. The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains. Proc Natl Acad Sci U S A 2004; 101:10272-7; PMID:15232009; http://dx.doi.org/10.1073/pnas.0401313101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10272-10277
    • Zhang, Y.1    Zuiderweg, E.R.2
  • 91
    • 64649089001 scopus 로고    scopus 로고
    • Allostery in Hsp70 chaperones is transduced by subdomain rotations
    • PMID:19361428
    • Bhattacharya A, Kurochkin AV, Yip GN, Zhang Y, Bertelsen EB, Zuiderweg ER. Allostery in Hsp70 chaperones is transduced by subdomain rotations. J Mol Biol 2009; 388:475-90; PMID:19361428; http://dx.doi.org/10.1016/j.jmb.2009.01. 062
    • (2009) J Mol Biol , vol.388 , pp. 475-490
    • Bhattacharya, A.1    Kurochkin, A.V.2    Yip, G.N.3    Zhang, Y.4    Bertelsen, E.B.5    Zuiderweg, E.R.6
  • 92
    • 0021471706 scopus 로고
    • Dissociation of clathrin coats coupled to the hydrolysis of ATP: Role of an uncoating ATPase
    • PMID:6146631
    • Braell WA, Schlossman DM, Schmid SL, Rothman JE. Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase. J Cell Biol 1984; 99:734-41; PMID:6146631; http://dx.doi.org/10.1083/jcb.99.2.734
    • (1984) J Cell Biol , vol.99 , pp. 734-741
    • Braell, W.A.1    Schlossman, D.M.2    Schmid, S.L.3    Rothman, J.E.4
  • 93
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • PMID:6146630
    • Schlossman DM, Schmid SL, Braell WA, Rothman JE. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol 1984; 99:723-33; PMID:6146630; http://dx.doi.org/10.1083/jcb.99.2.723
    • (1984) J Cell Biol , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 94
    • 0022427782 scopus 로고
    • The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles
    • PMID:2868889
    • Ungewickell E. The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J 1985; 4(13A):3385-91; PMID:2868889
    • (1985) EMBO J , vol.4 , Issue.13 , pp. 3385-3391
    • Ungewickell, E.1
  • 95
    • 0022531954 scopus 로고
    • Uncoating ATPase is a member of the 70 kilodalton family of stress proteins
    • PMID:2937542
    • Chappell TG, Welch WJ, Schlossman DM, Palter KB, Schlesinger MJ, Rothman JE. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins. Cell 1986; 45:3-13; PMID:2937542; http://dx.doi.org/10.1016/0092-8674(86)90532- 5
    • (1986) Cell , vol.45 , pp. 3-13
    • Chappell, T.G.1    Welch, W.J.2    Schlossman, D.M.3    Palter, K.B.4    Schlesinger, M.J.5    Rothman, J.E.6
  • 96
    • 67650711138 scopus 로고    scopus 로고
    • Mechanisms of endocytosis
    • PMID:19317650
    • Doherty GJ, McMahon HT. Mechanisms of endocytosis. Annu Rev Biochem 2009; 78:857-902; PMID:19317650; http://dx.doi.org/10.1146/annurev.biochem.78.081307. 110540
    • (2009) Annu Rev Biochem , vol.78 , pp. 857-902
    • Doherty, G.J.1    McMahon, H.T.2
  • 97
    • 0027358782 scopus 로고
    • A protein cofactor is required for uncoating of clathrin baskets by uncoating ATPase
    • PMID:8226905
    • Prasad K, Barouch W, Greene L, Eisenberg E. A protein cofactor is required for uncoating of clathrin baskets by uncoating ATPase. J Biol Chem 1993; 268:23758-61; PMID:8226905
    • (1993) J Biol Chem , vol.268 , pp. 23758-23761
    • Prasad, K.1    Barouch, W.2    Greene, L.3    Eisenberg, E.4
  • 99
    • 0031023433 scopus 로고    scopus 로고
    • GAK: A cyclin G associated kinase contains a tensin/auxilin-like domain
    • PMID:9013862
    • Kanaoka Y, Kimura SH, Okazaki I, Ikeda M, Nojima H. GAK: a cyclin G associated kinase contains a tensin/auxilin-like domain. FEBS Lett 1997; 402:73-80; PMID:9013862; http://dx.doi.org/10.1016/S0014-5793(96)01484-6
    • (1997) FEBS Lett , vol.402 , pp. 73-80
    • Kanaoka, Y.1    Kimura, S.H.2    Okazaki, I.3    Ikeda, M.4    Nojima, H.5
  • 100
    • 0033978513 scopus 로고    scopus 로고
    • Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells
    • PMID:10625686
    • Greener T, Zhao X, Nojima H, Eisenberg E, Greene LE. Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells. J Biol Chem 2000; 275:1365-70; PMID:10625686; http://dx.doi.org/10.1074/ jbc.275.2.1365
    • (2000) J Biol Chem , vol.275 , pp. 1365-1370
    • Greener, T.1    Zhao, X.2    Nojima, H.3    Eisenberg, E.4    Greene, L.E.5
  • 101
    • 0025231301 scopus 로고
    • Dissociation of clathrin from coated vesicles by the uncoating ATPase
    • PMID:1969864
    • Greene LE, Eisenberg E. Dissociation of clathrin from coated vesicles by the uncoating ATPase. J Biol Chem 1990; 265:6682-7; PMID:1969864
    • (1990) J Biol Chem , vol.265 , pp. 6682-6687
    • Greene, L.E.1    Eisenberg, E.2
  • 102
    • 0027973055 scopus 로고
    • ATPase activity associated with the uncoating of clathrin baskets by Hsp70
    • PMID:7961802
    • Barouch W, Prasad K, Greene LE, Eisenberg E. ATPase activity associated with the uncoating of clathrin baskets by Hsp70. J Biol Chem 1994; 269:28563-8; PMID:7961802
    • (1994) J Biol Chem , vol.269 , pp. 28563-28568
    • Barouch, W.1    Prasad, K.2    Greene, L.E.3    Eisenberg, E.4
  • 103
    • 10344227184 scopus 로고    scopus 로고
    • Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating
    • PMID:15502813
    • Fotin A, Cheng Y, Grigorieff N, Walz T, Harrison SC, Kirchhausen T. Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature 2004; 432:649-53; PMID:15502813; http://dx.doi.org/10.1038/nature03078
    • (2004) Nature , vol.432 , pp. 649-653
    • Fotin, A.1    Cheng, Y.2    Grigorieff, N.3    Walz, T.4    Harrison, S.C.5    Kirchhausen, T.6
  • 104
    • 14844331402 scopus 로고    scopus 로고
    • Visualization of the binding of Hsc70 ATPase to clathrin baskets: Implications for an uncoating mechanism
    • PMID:15596443
    • Heymann JB, Iwasaki K, Yim YI, Cheng N, Belnap DM, Greene LE, Eisenberg E, Steven AC. Visualization of the binding of Hsc70 ATPase to clathrin baskets: implications for an uncoating mechanism. J Biol Chem 2005; 280:7156-61; PMID:15596443; http://dx.doi.org/10.1074/jbc.M411712200
    • (2005) J Biol Chem , vol.280 , pp. 7156-7161
    • Heymann, J.B.1    Iwasaki, K.2    Yim, Y.I.3    Cheng, N.4    Belnap, D.M.5    Greene, L.E.6    Eisenberg, E.7    Steven, A.C.8
  • 105
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • PMID:2188360
    • Beckmann RP, Mizzen LE, Welch WJ. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 1990; 248:850-4; PMID:2188360; http://dx.doi.org/10.1126/science.2188360
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 106
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
    • PMID:8633246
    • Frydman J, Hartl FU. Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science 1996; 272:1497-502; PMID:8633246; http://dx.doi.org/10.1126/science.272.5267.1497
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F.U.2
  • 107
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • PMID:9878053
    • Thulasiraman V, Yang CF, Frydman J. In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J 1999; 18:85-95; PMID:9878053; http://dx.doi.org/10.1093/emboj/18.1.85
    • (1999) EMBO J , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 108
    • 0030798979 scopus 로고    scopus 로고
    • The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator
    • PMID:9325249
    • Strickland E, Qu BH, Millen L, Thomas PJ. The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 1997; 272:25421-4; PMID:9325249; http://dx.doi.org/10.1074/jbc.272.41.25421
    • (1997) J Biol Chem , vol.272 , pp. 25421-25424
    • Strickland, E.1    Qu, B.H.2    Millen, L.3    Thomas, P.J.4
  • 109
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • PMID:10075921
    • Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM. The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J 1999; 18:1492-505; PMID:10075921; http://dx.doi.org/10.1093/emboj/18.6.1492
    • (1999) EMBO J , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 110
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • PMID:10942430
    • Jana NR, Tanaka M, Wang Gh, Nukina N. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 2000; 9:2009-18; PMID:10942430; http://dx.doi.org/10.1093/hmg/9.13. 2009
    • (2000) Hum Mol Genet , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Gh, W.3    Nukina, N.4
  • 111
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • PMID:11741389
    • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis 2001; 8:933-41; PMID:11741389; http://dx.doi.org/10.1006/nbdi.2001.0443
    • (2001) Neurobiol Dis , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 113
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • PMID:9857172
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J 1998; 17:7151-60; PMID:9857172; http://dx.doi.org/10.1093/ emboj/17.24.7151
    • (1998) EMBO J , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 114
    • 0031004769 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70
    • PMID:9083024
    • Bercovich B, Stancovski I, Mayer A, Blumenfeld N, Laszlo A, Schwartz AL, Ciechanover A. Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70. J Biol Chem 1997; 272:9002-10; PMID:9083024; http://dx.doi.org/10.1074/jbc.272.14.9002
    • (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
  • 115
    • 0031585998 scopus 로고    scopus 로고
    • Maturation of mammalian 20 S proteasome: Purification and characterization of 13 S and 16 S proteasome precursor complexes
    • PMID:9149144
    • Schmidtke G, Schmidt M, Kloetzel PM. Maturation of mammalian 20 S proteasome: purification and characterization of 13 S and 16 S proteasome precursor complexes. J Mol Biol 1997; 268:95-106; PMID:9149144; http://dx.doi.org/10.1006/jmbi.1997.0947
    • (1997) J Mol Biol , vol.268 , pp. 95-106
    • Schmidtke, G.1    Schmidt, M.2    Kloetzel, P.M.3
  • 116
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • PMID:11146634
    • Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 2001; 3:100-5; PMID:11146634; http://dx.doi.org/10.1038/35050509
    • (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
  • 117
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • PMID:11743028
    • Murata S, Minami Y, Minami M, Chiba T, Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep 2001; 2:1133-8; PMID:11743028; http://dx.doi.org/10.1093/embo-reports/kve246
    • (2001) EMBO Rep , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 118
    • 3042817421 scopus 로고    scopus 로고
    • CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70
    • PMID:15198682
    • Urushitani M, Kurisu J, Tateno M, Hatakeyama S, Nakayama K, Kato S, Takahashi R. CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70. J Neurochem 2004; 90:231-44; PMID:15198682; http://dx.doi.org/10.1111/j.1471-4159.2004.02486.x
    • (2004) J Neurochem , vol.90 , pp. 231-244
    • Urushitani, M.1    Kurisu, J.2    Tateno, M.3    Hatakeyama, S.4    Nakayama, K.5    Kato, S.6    Takahashi, R.7
  • 119
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • PMID:10671488
    • Lüders J, Demand J, Höhfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J Biol Chem 2000; 275:4613-7; PMID:10671488; http://dx.doi.org/10.1074/jbc.275. 7.4613
    • (2000) J Biol Chem , vol.275 , pp. 4613-4617
    • Lüders, J.1    Demand, J.2    Höhfeld, J.3
  • 120
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • PMID:11676916
    • Demand J, Alberti S, Patterson C, Höhfeld J. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr Biol 2001; 11:1569-77; PMID:11676916; http://dx.doi.org/10.1016/ S0960-9822(01)00487-0
    • (2001) Curr Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Höhfeld, J.4
  • 121
    • 0035980094 scopus 로고    scopus 로고
    • U box proteins as a new family of ubiquitin-protein ligases
    • PMID:11435423
    • Hatakeyama S, Yada M, Matsumoto M, Ishida N, Nakayama KI. U box proteins as a new family of ubiquitin-protein ligases. J Biol Chem 2001; 276:33111-20; PMID:11435423; http://dx.doi.org/10.1074/jbc.M102755200
    • (2001) J Biol Chem , vol.276 , pp. 33111-33120
    • Hatakeyama, S.1    Yada, M.2    Matsumoto, M.3    Ishida, N.4    Nakayama, K.I.5
  • 122
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • PMID:11557750
    • Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Höhfeld J, Patterson C. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J Biol Chem 2001; 276:42938-44; PMID:11557750; http://dx.doi.org/10.1074/jbc.M101968200
    • (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    Höhfeld, J.6    Patterson, C.7
  • 123
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • PMID:12297498
    • Alberti S, Demand J, Esser C, Emmerich N, Schild H, Hohfeld J. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J Biol Chem 2002; 277:45920-7; PMID:12297498; http://dx.doi.org/10.1074/jbc.M204196200
    • (2002) J Biol Chem , vol.277 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 124
    • 0025052137 scopus 로고
    • Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope
    • PMID:2229173
    • Mandell RB, Feldherr CM. Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope. J Cell Biol 1990; 111:1775-83; PMID:2229173; http://dx.doi.org/10.1083/jcb.111.5. 1775
    • (1990) J Cell Biol , vol.111 , pp. 1775-1783
    • Mandell, R.B.1    Feldherr, C.M.2
  • 125
    • 25444440843 scopus 로고    scopus 로고
    • Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70
    • PMID:15930140
    • Kodiha M, Chu A, Lazrak O, Stochaj U. Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70. Am J Physiol Cell Physiol 2005; 289:C1034-41; PMID:15930140; http://dx.doi.org/10.1152/ajpcell.00590.2004
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Kodiha, M.1    Chu, A.2    Lazrak, O.3    Stochaj, U.4
  • 126
    • 0026468193 scopus 로고
    • Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins
    • PMID:1332978
    • Imamoto N, Matsuoka Y, Kurihara T, Kohno K, Miyagi M, Sakiyama F, Okada Y, Tsunasawa S, Yoneda Y. Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins. J Cell Biol 1992; 119:1047-61; PMID:1332978; http://dx.doi.org/10.1083/jcb.119.5.1047
    • (1992) J Cell Biol , vol.119 , pp. 1047-1061
    • Imamoto, N.1    Matsuoka, Y.2    Kurihara, T.3    Kohno, K.4    Miyagi, M.5    Sakiyama, F.6    Okada, Y.7    Tsunasawa, S.8    Yoneda, Y.9
  • 127
    • 0027315529 scopus 로고
    • 70-kDa heat-shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro
    • PMID:8482354
    • Okuno Y, Imamoto N, Yoneda Y. 70-kDa heat-shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro. Exp Cell Res 1993; 206:134-42; PMID:8482354; http://dx.doi.org/10.1006/ excr.1993.1129
    • (1993) Exp Cell Res , vol.206 , pp. 134-142
    • Okuno, Y.1    Imamoto, N.2    Yoneda, Y.3
  • 129
    • 0024431720 scopus 로고
    • Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins
    • PMID:2553699
    • Dang CV, Lee WM. Nuclear and nucleolar targeting sequences of c-erb-A, c-myb, N-myc, p53, HSP70, and HIV tat proteins. J Biol Chem 1989; 264:18019-23; PMID:2553699
    • (1989) J Biol Chem , vol.264 , pp. 18019-18023
    • Dang, C.V.1    Lee, W.M.2
  • 130
    • 0030579097 scopus 로고    scopus 로고
    • Evidence for the existence of a novel mechanism for the nuclear import of Hsc70
    • PMID:8892974
    • Lamian V, Small GM, Feldherr CM. Evidence for the existence of a novel mechanism for the nuclear import of Hsc70. Exp Cell Res 1996; 228:84-91; PMID:8892974; http://dx.doi.org/10.1006/excr.1996.0302
    • (1996) Exp Cell Res , vol.228 , pp. 84-91
    • Lamian, V.1    Small, G.M.2    Feldherr, C.M.3
  • 131
    • 26444491096 scopus 로고    scopus 로고
    • The 70-kD heat shock cognate protein (hsc70) facilitates the nuclear export of the import receptors
    • PMID:16203861
    • Kose S, Furuta M, Koike M, Yoneda Y, Imamoto N. The 70-kD heat shock cognate protein (hsc70) facilitates the nuclear export of the import receptors. J Cell Biol 2005; 171:19-25; PMID:16203861; http://dx.doi.org/10.1083/jcb. 200506074
    • (2005) J Cell Biol , vol.171 , pp. 19-25
    • Kose, S.1    Furuta, M.2    Koike, M.3    Yoneda, Y.4    Imamoto, N.5
  • 132
    • 1542275420 scopus 로고    scopus 로고
    • Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70
    • PMID:14684748
    • Tsukahara F, Maru Y. Identification of novel nuclear export and nuclear localization-related signals in human heat shock cognate protein 70. J Biol Chem 2004; 279:8867-72; PMID:14684748; http://dx.doi.org/10.1074/jbc.M308848200
    • (2004) J Biol Chem , vol.279 , pp. 8867-8872
    • Tsukahara, F.1    Maru, Y.2
  • 133
    • 62649092442 scopus 로고    scopus 로고
    • Heat shock cognate protein 70 controls Borna disease virus replication via interaction with the viral non-structural protein X
    • PMID:19397879
    • Hayashi Y, Horie M, Daito T, Honda T, Ikuta K, Tomonaga K. Heat shock cognate protein 70 controls Borna disease virus replication via interaction with the viral non-structural protein X. Microbes Infect 2009; 11:394-402; PMID:19397879; http://dx.doi.org/10.1016/j.micinf.2009.01.006
    • (2009) Microbes Infect , vol.11 , pp. 394-402
    • Hayashi, Y.1    Horie, M.2    Daito, T.3    Honda, T.4    Ikuta, K.5    Tomonaga, K.6
  • 134
    • 33749338927 scopus 로고    scopus 로고
    • Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle
    • PMID:17022977
    • Watanabe K, Fuse T, Asano I, Tsukahara F, Maru Y, Nagata K, Kitazato K, Kobayashi N. Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle. FEBS Lett 2006; 580:5785-90; PMID:17022977; http://dx.doi.org/10.1016/j.febslet.2006.09.040
    • (2006) FEBS Lett , vol.580 , pp. 5785-5790
    • Watanabe, K.1    Fuse, T.2    Asano, I.3    Tsukahara, F.4    Maru, Y.5    Nagata, K.6    Kitazato, K.7    Kobayashi, N.8
  • 135
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • PMID:3282179
    • Chirico WJ, Waters MG, Blobel G. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 1988; 332:805-10; PMID:3282179; http://dx.doi.org/10.1038/332805a0
    • (1988) Nature , vol.332 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 136
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • PMID:3282178
    • Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 1988; 332:800-5; PMID:3282178; http://dx.doi.org/10.1038/332800a0
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 137
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • PMID:12526792
    • Young JC, Hoogenraad NJ, Hartl FU. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 2003;
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 138
    • 0025295174 scopus 로고
    • Mitochondrial precursor protein. Effects of 70-kilodalton heat shock protein on polypeptide folding, aggregation, and import competence
    • PMID:2193031
    • Sheffield WP, Shore GC, Randall SK. Mitochondrial precursor protein. Effects of 70-kilodalton heat shock protein on polypeptide folding, aggregation, and import competence. J Biol Chem 1990; 265:11069-76; PMID:2193031
    • (1990) J Biol Chem , vol.265 , pp. 11069-11076
    • Sheffield, W.P.1    Shore, G.C.2    Randall, S.K.3
  • 139
    • 0029845194 scopus 로고    scopus 로고
    • The requirement of heat shock cognate 70 protein for mitochondrial import varies among precursor proteins and depends on precursor length
    • PMID:8887640
    • Terada K, Ueda I, Ohtsuka K, Oda T, Ichiyama A, Mori M. The requirement of heat shock cognate 70 protein for mitochondrial import varies among precursor proteins and depends on precursor length. Mol Cell Biol 1996; 16:6103-9; PMID:8887640
    • (1996) Mol Cell Biol , vol.16 , pp. 6103-6109
    • Terada, K.1    Ueda, I.2    Ohtsuka, K.3    Oda, T.4    Ichiyama, A.5    Mori, M.6
  • 140
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • PMID:21801011
    • Shao S, Hegde RS. Membrane protein insertion at the endoplasmic reticulum. Annu Rev Cell Dev Biol 2011; 27:25-56; PMID:21801011; http://dx.doi.org/10.1146/annurev-cellbio-092910-154125
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 141
    • 3543016171 scopus 로고    scopus 로고
    • Signal recognition particle mediates post-translational targeting in eukaryotes
    • PMID:15229647
    • Abell BM, Pool MR, Schlenker O, Sinning I, High S. Signal recognition particle mediates post-translational targeting in eukaryotes. EMBO J 2004; 23:2755-64; PMID:15229647; http://dx.doi.org/10.1038/sj.emboj.7600281
    • (2004) EMBO J , vol.23 , pp. 2755-2764
    • Abell, B.M.1    Pool, M.R.2    Schlenker, O.3    Sinning, I.4    High, S.5
  • 142
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • PMID:17382883
    • Stefanovic S, Hegde RS. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 2007; 128:1147-59; PMID:17382883; http://dx.doi.org/10.1016/j.cell.2007.01.036
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 143
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • PMID:17456552
    • Abell BM, Rabu C, Leznicki P, Young JC, High S. Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones. J Cell Sci 2007; 120:1743-51; PMID:17456552; http://dx.doi.org/10. 1242/jcs.002410
    • (2007) J Cell Sci , vol.120 , pp. 1743-1751
    • Abell, B.M.1    Rabu, C.2    Leznicki, P.3    Young, J.C.4    High, S.5
  • 144
    • 55549102665 scopus 로고    scopus 로고
    • A precursor-specific role for Hsp40/Hsc70 during tail-anchored protein integration at the endoplasmic reticulum
    • PMID:18667436
    • Rabu C, Wipf P, Brodsky JL, High S. A precursor-specific role for Hsp40/Hsc70 during tail-anchored protein integration at the endoplasmic reticulum. J Biol Chem 2008; 283:27504-13; PMID:18667436; http://dx.doi.org/10. 1074/jbc.M804591200
    • (2008) J Biol Chem , vol.283 , pp. 27504-27513
    • Rabu, C.1    Wipf, P.2    Brodsky, J.L.3    High, S.4
  • 145
    • 84875510924 scopus 로고    scopus 로고
    • Pathways of antigen processing
    • PMID:23298205
    • Blum JS, Wearsch PA, Cresswell P. Pathways of antigen processing. Annu Rev Immunol 2013; 31:443-73; PMID:23298205; http://dx.doi.org/10.1146/annurev- immunol-032712-095910
    • (2013) Annu Rev Immunol , vol.31 , pp. 443-473
    • Blum, J.S.1    Wearsch, P.A.2    Cresswell, P.3
  • 146
    • 51449098448 scopus 로고    scopus 로고
    • Disruption of the association of 73 kDa heat shock cognate protein with transporters associated with antigen processing (TAP) decreases TAP-dependent translocation of antigenic peptides into the endoplasmic reticulum
    • PMID:18380807
    • Kamiguchi K, Torigoe T, Fujiwara O, Ohshima S, Hirohashi Y, Sahara H, Hirai I, Kohgo Y, Sato N. Disruption of the association of 73 kDa heat shock cognate protein with transporters associated with antigen processing (TAP) decreases TAP-dependent translocation of antigenic peptides into the endoplasmic reticulum. Microbiol Immunol 2008; 52:94-106; PMID:18380807; http://dx.doi.org/10.1111/j.1348-0421.2008.00017.x
    • (2008) Microbiol Immunol , vol.52 , pp. 94-106
    • Kamiguchi, K.1    Torigoe, T.2    Fujiwara, O.3    Ohshima, S.4    Hirohashi, Y.5    Sahara, H.6    Hirai, I.7    Kohgo, Y.8    Sato, N.9
  • 147
    • 0034086882 scopus 로고    scopus 로고
    • Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport
    • PMID:10848636
    • Tsai MY, Morfini G, Szebenyi G, Brady ST. Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport. Mol Biol Cell 2000; 11:2161-73; PMID:10848636; http://dx.doi.org/10.1091/mbc.11.6.2161
    • (2000) Mol Biol Cell , vol.11 , pp. 2161-2173
    • Tsai, M.Y.1    Morfini, G.2    Szebenyi, G.3    Brady, S.T.4
  • 148
    • 77149135259 scopus 로고    scopus 로고
    • Kinesin-1/Hsc70-dependent mechanism of slow axonal transport and its relation to fast axonal transport
    • PMID:20111006
    • Terada S, Kinjo M, Aihara M, Takei Y, Hirokawa N. Kinesin-1/Hsc70- dependent mechanism of slow axonal transport and its relation to fast axonal transport. EMBO J 2010; 29:843-54; PMID:20111006; http://dx.doi.org/10.1038/ emboj.2009.389
    • (2010) EMBO J , vol.29 , pp. 843-854
    • Terada, S.1    Kinjo, M.2    Aihara, M.3    Takei, Y.4    Hirokawa, N.5
  • 149
    • 0037783960 scopus 로고    scopus 로고
    • Stress-induced release of HSC70 from human tumors
    • PMID:12826079
    • Barreto A, Gonzalez JM, Kabingu E, Asea A, Fiorentino S. Stress-induced release of HSC70 from human tumors. Cell Immunol 2003; 222:97-104; PMID:12826079; http://dx.doi.org/10.1016/S0008-8749(03)00115-1
    • (2003) Cell Immunol , vol.222 , pp. 97-104
    • Barreto, A.1    Gonzalez, J.M.2    Kabingu, E.3    Asea, A.4    Fiorentino, S.5
  • 150
    • 77957344304 scopus 로고    scopus 로고
    • Secretion of the heat shock proteins HSP70 and HSC70 by baby hamster kidney (BHK-21) cells
    • PMID:20486902
    • Evdokimovskaya Y, Skarga Y, Vrublevskaya V, Morenkov O. Secretion of the heat shock proteins HSP70 and HSC70 by baby hamster kidney (BHK-21) cells. Cell Biol Int 2010; 34:985-90; PMID:20486902; http://dx.doi.org/10.1042/CBI20100147
    • (2010) Cell Biol Int , vol.34 , pp. 985-990
    • Evdokimovskaya, Y.1    Skarga, Y.2    Vrublevskaya, V.3    Morenkov, O.4
  • 151
    • 73849088641 scopus 로고    scopus 로고
    • Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells
    • PMID:19802014
    • Nirdé P, Derocq D, Maynadier M, Chambon M, Basile I, Gary-Bobo M, Garcia M. Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells. Oncogene 2010; 29:117-27; PMID:19802014; http://dx.doi.org/10. 1038/onc.2009.311
    • (2010) Oncogene , vol.29 , pp. 117-127
    • Nirdé, P.1    Derocq, D.2    Maynadier, M.3    Chambon, M.4    Basile, I.5    Gary-Bobo, M.6    Garcia, M.7
  • 152
    • 24944495594 scopus 로고    scopus 로고
    • Induction of heat shock proteins in B-cell exosomes
    • PMID:16046478
    • Clayton A, Turkes A, Navabi H, Mason MD, Tabi Z. Induction of heat shock proteins in B-cell exosomes. J Cell Sci 2005; 118:3631-8; PMID:16046478; http://dx.doi.org/10.1242/jcs.02494
    • (2005) J Cell Sci , vol.118 , pp. 3631-3638
    • Clayton, A.1    Turkes, A.2    Navabi, H.3    Mason, M.D.4    Tabi, Z.5
  • 153
    • 7744222195 scopus 로고    scopus 로고
    • Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability
    • PMID:15522909
    • Arispe N, Doh M, Simakova O, Kurganov B, De Maio A. Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J 2004; 18:1636-45; PMID:15522909; http://dx.doi.org/10.1096/fj.04-2088com
    • (2004) FASEB J , vol.18 , pp. 1636-1645
    • Arispe, N.1    Doh, M.2    Simakova, O.3    Kurganov, B.4    De Maio, A.5
  • 155
    • 38149065825 scopus 로고    scopus 로고
    • Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress
    • PMID:17918243
    • Robinson MB, Taylor AR, Gifondorwa DJ, Tytell M, Milligan CE. Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress. Dev Neurobiol 2008; 68:1-17; PMID:17918243; http://dx.doi.org/10.1002/dneu.20550
    • (2008) Dev Neurobiol , vol.68 , pp. 1-17
    • Robinson, M.B.1    Taylor, A.R.2    Gifondorwa, D.J.3    Tytell, M.4    Milligan, C.E.5
  • 156
    • 0027997530 scopus 로고
    • Monoclonal antibody specifically reacting against 73-kilodalton heat shock cognate protein: Possible expression on mammalian cell surface
    • PMID:7860094
    • Tsuboi N, Ishikawa M, Tamura Y, Takayama S, Tobioka H, Matsuura A, Hirayoshi K, Nagata K, Sato N, Kikuchi K. Monoclonal antibody specifically reacting against 73-kilodalton heat shock cognate protein: possible expression on mammalian cell surface. Hybridoma 1994; 13:373-81; PMID:7860094; http://dx.doi.org/10.1089/hyb.1994.13.373
    • (1994) Hybridoma , vol.13 , pp. 373-381
    • Tsuboi, N.1    Ishikawa, M.2    Tamura, Y.3    Takayama, S.4    Tobioka, H.5    Matsuura, A.6    Hirayoshi, K.7    Nagata, K.8    Sato, N.9    Kikuchi, K.10
  • 157
    • 0034879081 scopus 로고    scopus 로고
    • Contribution of heat shock proteins to cell protection from complement-mediated lysis
    • PMID:11470768
    • Fishelson Z, Hochman I, Greene LE, Eisenberg E. Contribution of heat shock proteins to cell protection from complement-mediated lysis. Int Immunol 2001; 13:983-91; PMID:11470768; http://dx.doi.org/10.1093/intimm/13.8.983
    • (2001) Int Immunol , vol.13 , pp. 983-991
    • Fishelson, Z.1    Hochman, I.2    Greene, L.E.3    Eisenberg, E.4
  • 158
    • 79953317423 scopus 로고    scopus 로고
    • HSC70 blockade by the therapeutic peptide P140 affects autophagic processes and endogenous MHCII presentation in murine lupus
    • PMID:21173017
    • Page N, Gros F, Schall N, Décossas M, Bagnard D, Briand JP, Muller S. HSC70 blockade by the therapeutic peptide P140 affects autophagic processes and endogenous MHCII presentation in murine lupus. Ann Rheum Dis 2011; 70:837-43; PMID:21173017; http://dx.doi.org/10.1136/ard.2010.139832
    • (2011) Ann Rheum Dis , vol.70 , pp. 837-843
    • Page, N.1    Gros, F.2    Schall, N.3    Décossas, M.4    Bagnard, D.5    Briand, J.P.6    Muller, S.7
  • 159
  • 160
    • 0031964682 scopus 로고    scopus 로고
    • 71-kilodalton heat shock cognate protein acts as a cellular receptor for syncytium formation induced by human T-cell lymphotropic virus type 1
    • PMID:9420256
    • Sagara Y, Ishida C, Inoue Y, Shiraki H, Maeda Y. 71-kilodalton heat shock cognate protein acts as a cellular receptor for syncytium formation induced by human T-cell lymphotropic virus type 1. J Virol 1998; 72:535-41; PMID:9420256
    • (1998) J Virol , vol.72 , pp. 535-541
    • Sagara, Y.1    Ishida, C.2    Inoue, Y.3    Shiraki, H.4    Maeda, Y.5
  • 161
    • 84862240352 scopus 로고    scopus 로고
    • Rotavirus receptor proteins Hsc70 and integrin αvβ3 are located in the lipid microdomains of animal intestinal cells
    • PMID:22404611
    • Guerrero CA, Moreno LP. Rotavirus receptor proteins Hsc70 and integrin αvβ3 are located in the lipid microdomains of animal intestinal cells. Acta Virol 2012; 56:63-70; PMID:22404611; http://dx.doi.org/10.4149/av- 2012-01-63
    • (2012) Acta Virol , vol.56 , pp. 63-70
    • Guerrero, C.A.1    Moreno, L.P.2
  • 162
    • 0026749295 scopus 로고
    • Unusual expression and localization of heat-shock proteins in human tumor cells
    • PMID:1601523
    • Ferrarini M, Heltai S, Zocchi MR, Rugarli C. Unusual expression and localization of heat-shock proteins in human tumor cells. Int J Cancer 1992; 51:613-9; PMID:1601523; http://dx.doi.org/10.1002/ijc.2910510418
    • (1992) Int J Cancer , vol.51 , pp. 613-619
    • Ferrarini, M.1    Heltai, S.2    Zocchi, M.R.3    Rugarli, C.4
  • 165
    • 0023551778 scopus 로고
    • Heat-shock protein synthesis by human peripheral mononuclear cells from SLE patients
    • PMID:3689384
    • Deguchi Y, Negoro S, Kishimoto S. Heat-shock protein synthesis by human peripheral mononuclear cells from SLE patients. Biochem Biophys Res Commun 1987; 148:1063-8; PMID:3689384; http://dx.doi.org/10.1016/S0006-291X(87)80239-5
    • (1987) Biochem Biophys Res Commun , vol.148 , pp. 1063-1068
    • Deguchi, Y.1    Negoro, S.2    Kishimoto, S.3
  • 166
    • 0024645048 scopus 로고
    • Elevated levels of the 90 kd heat shock protein in a proportion of SLE patients with active disease
    • PMID:2765096
    • Norton PM, Isenberg DA, Latchman DS. Elevated levels of the 90 kd heat shock protein in a proportion of SLE patients with active disease. J Autoimmun 1989; 2:187-95; PMID:2765096; http://dx.doi.org/10.1016/0896-8411(89)90154-6
    • (1989) J Autoimmun , vol.2 , pp. 187-195
    • Norton, P.M.1    Isenberg, D.A.2    Latchman, D.S.3
  • 167
    • 0025123503 scopus 로고
    • Pathogenic anti-DNA autoantibody-inducing T helper cell lines from patients with active lupus nephritis: Isolation of CD4-8- T helper cell lines that express the gamma delta T-cell antigen receptor
    • PMID:2144899
    • Rajagopalan S, Zordan T, Tsokos GC, Datta SK. Pathogenic anti-DNA autoantibody-inducing T helper cell lines from patients with active lupus nephritis: isolation of CD4-8- T helper cell lines that express the gamma delta T-cell antigen receptor. Proc Natl Acad Sci U S A 1990; 87:7020-4; PMID:2144899; http://dx.doi.org/10.1073/pnas.87.18.7020
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7020-7024
    • Rajagopalan, S.1    Zordan, T.2    Tsokos, G.C.3    Datta, S.K.4
  • 168
    • 0031647680 scopus 로고    scopus 로고
    • The regulation of heat shock proteins and their role in systemic lupus erythematosus
    • PMID:9872476
    • Stephanou A, Latchman DS, Isenberg DA. The regulation of heat shock proteins and their role in systemic lupus erythematosus. Semin Arthritis Rheum 1998; 28:155-62; PMID:9872476; http://dx.doi.org/10.1016/S0049-0172(98)80032-2
    • (1998) Semin Arthritis Rheum , vol.28 , pp. 155-162
    • Stephanou, A.1    Latchman, D.S.2    Isenberg, D.A.3
  • 169
    • 0027729231 scopus 로고
    • Elevated levels of the 70 kD heat shock protein in patients with systemic lupus erythematosus are not dependent on enhanced transcription of the hsp70 gene
    • PMID:8305922
    • Twomey BM, Amin V, Isenberg DA, Latchman DS. Elevated levels of the 70 kD heat shock protein in patients with systemic lupus erythematosus are not dependent on enhanced transcription of the hsp70 gene. Lupus 1993; 2:297-301; PMID:8305922; http://dx.doi.org/10.1177/096120339300200504
    • (1993) Lupus , vol.2 , pp. 297-301
    • Twomey, B.M.1    Amin, V.2    Isenberg, D.A.3    Latchman, D.S.4
  • 170
    • 0028334825 scopus 로고
    • The tissue specific elevation in synthesis of the 90 kDa heat shock protein precedes the onset of disease in lupus prone MRL/lpr mice
    • PMID:8182630
    • Faulds GB, Isenberg DA, Latchman DS. The tissue specific elevation in synthesis of the 90 kDa heat shock protein precedes the onset of disease in lupus prone MRL/lpr mice. J Rheumatol 1994; 21:234-8; PMID:8182630
    • (1994) J Rheumatol , vol.21 , pp. 234-238
    • Faulds, G.B.1    Isenberg, D.A.2    Latchman, D.S.3
  • 171
    • 0036512171 scopus 로고    scopus 로고
    • Roles of heat-shock proteins in innate and adaptive immunity
    • PMID:11913069
    • Srivastava P. Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol 2002; 2:185-94; PMID:11913069; http://dx.doi.org/10. 1038/nri749
    • (2002) Nat Rev Immunol , vol.2 , pp. 185-194
    • Srivastava, P.1
  • 172
    • 0024422312 scopus 로고
    • T cells against a bacterial heat shock protein recognize stressed macrophages
    • PMID:2788923
    • Koga T, Wand-Württenberger A, DeBruyn J, Munk ME, Schoel B, Kaufmann SH. T cells against a bacterial heat shock protein recognize stressed macrophages. Science 1989; 245:1112-5; PMID:2788923; http://dx.doi.org/10.1126/ science.2788923
    • (1989) Science , vol.245 , pp. 1112-1115
    • Koga, T.1    Wand-Württenberger, A.2    DeBruyn, J.3    Munk, M.E.4    Schoel, B.5    Kaufmann, S.H.6
  • 173
    • 0025777274 scopus 로고
    • Synovial fluid-derived Yersinia-reactive T cells responding to human 65-kDa heat-shock protein and heat-stressed antigen-presenting cells
    • PMID:1909642
    • Hermann E, Lohse AW, Van der Zee R, Van Eden W, Mayet WJ, Probst P, Poralla T, Meyer zum Büschenfelde KH, Fleischer B. Synovial fluid-derived Yersinia-reactive T cells responding to human 65-kDa heat-shock protein and heat-stressed antigen-presenting cells. Eur J Immunol 1991; 21:2139-43; PMID:1909642; http://dx.doi.org/10.1002/eji.1830210923
    • (1991) Eur J Immunol , vol.21 , pp. 2139-2143
    • Hermann, E.1    Lohse, A.W.2    Van Der Zee, R.3    Van Eden, W.4    Mayet, W.J.5    Probst, P.6    Poralla, T.7    Meyer Zum Büschenfelde, K.H.8    Fleischer, B.9
  • 174
    • 0025914004 scopus 로고
    • Identification of self peptides bound to purified HLA-B27
    • PMID:1922338
    • Jardetzky TS, Lane WS, Robinson RA, Madden DR, Wiley DC. Identification of self peptides bound to purified HLA-B27. Nature 1991; 353:326-9; PMID:1922338; http://dx.doi.org/10.1038/353326a0
    • (1991) Nature , vol.353 , pp. 326-329
    • Jardetzky, T.S.1    Lane, W.S.2    Robinson, R.A.3    Madden, D.R.4    Wiley, D.C.5
  • 175
    • 0033566936 scopus 로고    scopus 로고
    • The HSC73 molecular chaperone: Involvement in MHC class II antigen presentation
    • PMID:10438929
    • Panjwani N, Akbari O, Garcia S, Brazil M, Stockinger B. The HSC73 molecular chaperone: involvement in MHC class II antigen presentation. J Immunol 1999; 163:1936-42; PMID:10438929
    • (1999) J Immunol , vol.163 , pp. 1936-1942
    • Panjwani, N.1    Akbari, O.2    Garcia, S.3    Brazil, M.4    Stockinger, B.5
  • 176
    • 0029879122 scopus 로고    scopus 로고
    • HLA-DR4 and HLA-DR10 motifs that carry susceptibility to rheumatoid arthritis bind 70-kD heat shock proteins
    • PMID:8612229
    • Auger I, Escola JM, Gorvel JP, Roudier J. HLA-DR4 and HLA-DR10 motifs that carry susceptibility to rheumatoid arthritis bind 70-kD heat shock proteins. Nat Med 1996; 2:306-10; PMID:8612229; http://dx.doi.org/10.1038/ nm0396-306
    • (1996) Nat Med , vol.2 , pp. 306-310
    • Auger, I.1    Escola, J.M.2    Gorvel, J.P.3    Roudier, J.4
  • 177
    • 0026490037 scopus 로고
    • Circulating antibodies to heat-shock protein 60 in Crohn's disease and ulcerative colitis
    • PMID:1424286
    • Stevens TR, Winrow VR, Blake DR, Rampton DS. Circulating antibodies to heat-shock protein 60 in Crohn's disease and ulcerative colitis. Clin Exp Immunol 1992; 90:271-4; PMID:1424286; http://dx.doi.org/10.1111/j.1365-2249. 1992.tb07941.x
    • (1992) Clin Exp Immunol , vol.90 , pp. 271-274
    • Stevens, T.R.1    Winrow, V.R.2    Blake, D.R.3    Rampton, D.S.4
  • 178
    • 0029998824 scopus 로고    scopus 로고
    • Incidence of anti Hsp 90 and 70 antibodies in children with SLE, juvenile dermatomyositis and juvenile chronic arthritis
    • PMID:8697668
    • Conroy SE, Tucker L, Latchman DS, Isenberg DA. Incidence of anti Hsp 90 and 70 antibodies in children with SLE, juvenile dermatomyositis and juvenile chronic arthritis. Clin Exp Rheumatol 1996; 14:99-104; PMID:8697668
    • (1996) Clin Exp Rheumatol , vol.14 , pp. 99-104
    • Conroy, S.E.1    Tucker, L.2    Latchman, D.S.3    Isenberg, D.A.4
  • 179
    • 0036239674 scopus 로고    scopus 로고
    • Antibodies to 70 kD and 90 kD heat shock proteins are associated with graft-versus-host disease in peripheral blood stem cell transplant recipients
    • PMID:11966775
    • Goral J, Shenoy S, Mohanakumar T, Clancy J Jr. Antibodies to 70 kD and 90 kD heat shock proteins are associated with graft-versus-host disease in peripheral blood stem cell transplant recipients. Clin Exp Immunol 2002; 127:553-9; PMID:11966775; http://dx.doi.org/10.1046/j.1365-2249.2002.01770.x
    • (2002) Clin Exp Immunol , vol.127 , pp. 553-559
    • Goral, J.1    Shenoy, S.2    Mohanakumar, T.3    Clancy Jr., J.4
  • 180
    • 0032928895 scopus 로고    scopus 로고
    • Anti-heat shock protein 70 kDa and 90 kDa antibodies in serum of patients with rheumatoid arthritis
    • PMID:10225814
    • Hayem G, De Bandt M, Palazzo E, Roux S, Combe B, Eliaou JF, Sany J, Kahn MF, Meyer O. Anti-heat shock protein 70 kDa and 90 kDa antibodies in serum of patients with rheumatoid arthritis. Ann Rheum Dis 1999; 58:291-6; PMID:10225814; http://dx.doi.org/10.1136/ard.58.5.291
    • (1999) Ann Rheum Dis , vol.58 , pp. 291-296
    • Hayem, G.1    De Bandt, M.2    Palazzo, E.3    Roux, S.4    Combe, B.5    Eliaou, J.F.6    Sany, J.7    Kahn, M.F.8    Meyer, O.9
  • 181
    • 0023723489 scopus 로고
    • Autoantibodies to the constitutive 73-kD member of the hsp70 family of heat shock proteins in systemic lupus erythematosus
    • PMID:3171482
    • Minota S, Cameron B, Welch WJ, Winfield JB. Autoantibodies to the constitutive 73-kD member of the hsp70 family of heat shock proteins in systemic lupus erythematosus. J Exp Med 1988; 168:1475-80; PMID:3171482; http://dx.doi.org/10.1084/jem.168.4.1475
    • (1988) J Exp Med , vol.168 , pp. 1475-1480
    • Minota, S.1    Cameron, B.2    Welch, W.J.3    Winfield, J.B.4
  • 182
    • 0024504006 scopus 로고
    • Isolation of CD4- CD8- mycobacteria-reactive T lymphocyte clones from rheumatoid arthritis synovial fluid
    • PMID:2524009
    • Holoshitz J, Koning F, Coligan JE, De Bruyn J, Strober S. Isolation of CD4- CD8- mycobacteria-reactive T lymphocyte clones from rheumatoid arthritis synovial fluid. Nature 1989; 339:226-9; PMID:2524009; http://dx.doi.org/10.1038/ 339226a0
    • (1989) Nature , vol.339 , pp. 226-229
    • Holoshitz, J.1    Koning, F.2    Coligan, J.E.3    De Bruyn, J.4    Strober, S.5
  • 183
    • 0024369788 scopus 로고
    • Activation of gamma delta T cells in the primary immune response to Mycobacterium tuberculosis
    • PMID:2524098
    • Janis EM, Kaufmann SH, Schwartz RH, Pardoll DM. Activation of gamma delta T cells in the primary immune response to Mycobacterium tuberculosis. Science 1989; 244:713-6; PMID:2524098; http://dx.doi.org/10.1126/science.2524098
    • (1989) Science , vol.244 , pp. 713-716
    • Janis, E.M.1    Kaufmann, S.H.2    Schwartz, R.H.3    Pardoll, D.M.4
  • 184
    • 0024380520 scopus 로고
    • Stimulation of a major subset of lymphocytes expressing T cell receptor gamma delta by an antigen derived from Mycobacterium tuberculosis
    • PMID:2524273
    • O'Brien RL, Happ MP, Dallas A, Palmer E, Kubo R, Born WK. Stimulation of a major subset of lymphocytes expressing T cell receptor gamma delta by an antigen derived from Mycobacterium tuberculosis. Cell 1989; 57:667-74; PMID:2524273; http://dx.doi.org/10.1016/0092-8674(89)90135-9
    • (1989) Cell , vol.57 , pp. 667-674
    • O'Brien, R.L.1    Happ, M.P.2    Dallas, A.3    Palmer, E.4    Kubo, R.5    Born, W.K.6
  • 185
  • 186
    • 0027385461 scopus 로고
    • 70 kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity
    • PMID:8228242
    • Tamura Y, Tsuboi N, Sato N, Kikuchi K. 70 kDa heat shock cognate protein is a transformation-associated antigen and a possible target for the host's anti-tumor immunity. J Immunol 1993; 151:5516-24; PMID:8228242
    • (1993) J Immunol , vol.151 , pp. 5516-5524
    • Tamura, Y.1    Tsuboi, N.2    Sato, N.3    Kikuchi, K.4
  • 187
    • 0038246341 scopus 로고    scopus 로고
    • T-cell receptor variable gamma chain gene expression in the interaction between rat gammadelta-type T cells and heat-shock protein 70-like molecule
    • PMID:12825896
    • Ichinohe T, Ichimiya S, Kishi A, Tamura Y, Kondo N, Ueda G, Torigoe T, Yamaguchi A, Hiratsuka H, Hirai I, et al. T-cell receptor variable gamma chain gene expression in the interaction between rat gammadelta-type T cells and heat-shock protein 70-like molecule. Microbiol Immunol 2003; 47:351-7; PMID:12825896
    • (2003) Microbiol Immunol , vol.47 , pp. 351-357
    • Ichinohe, T.1    Ichimiya, S.2    Kishi, A.3    Tamura, Y.4    Kondo, N.5    Ueda, G.6    Torigoe, T.7    Yamaguchi, A.8    Hiratsuka, H.9    Hirai, I.10
  • 188
    • 33845965024 scopus 로고    scopus 로고
    • Cytokines direct the regulation of Bim mRNA stability by heat-shock cognate protein 70
    • PMID:17218274
    • Matsui H, Asou H, Inaba T. Cytokines direct the regulation of Bim mRNA stability by heat-shock cognate protein 70. Mol Cell 2007; 25:99-112; PMID:17218274; http://dx.doi.org/10.1016/j.molcel.2006.12.007
    • (2007) Mol Cell , vol.25 , pp. 99-112
    • Matsui, H.1    Asou, H.2    Inaba, T.3
  • 189
    • 0033607506 scopus 로고    scopus 로고
    • Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity
    • PMID:10576740
    • Bouillet P, Metcalf D, Huang DC, Tarlinton DM, Kay TW, Köntgen F, Adams JM, Strasser A. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 1999; 286:1735-8; PMID:10576740; http://dx.doi.org/10.1126/science.286. 5445.1735
    • (1999) Science , vol.286 , pp. 1735-1738
    • Bouillet, P.1    Metcalf, D.2    Huang, D.C.3    Tarlinton, D.M.4    Kay, T.W.5    Köntgen, F.6    Adams, J.M.7    Strasser, A.8
  • 190
    • 67149133632 scopus 로고    scopus 로고
    • Heat shock proteins and immune system
    • PMID:19276179
    • Tsan MF, Gao B. Heat shock proteins and immune system. J Leukoc Biol 2009; 85:905-10; PMID:19276179; http://dx.doi.org/10.1189/jlb.0109005
    • (2009) J Leukoc Biol , vol.85 , pp. 905-910
    • Tsan, M.F.1    Gao, B.2
  • 193
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: A unique way to enter the lysosome world
    • PMID:22748206
    • Kaushik S, Cuervo AM. Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol 2012; 22:407-17; PMID:22748206; http://dx.doi.org/10.1016/j.tcb.2012.05.006
    • (2012) Trends Cell Biol , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 194
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • PMID:11559757
    • Agarraberes FA, Dice JF. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 2001; 114:2491-9; PMID:11559757
    • (2001) J Cell Sci , vol.114 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 195
    • 0034282931 scopus 로고    scopus 로고
    • Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state
    • PMID:10862611
    • Salvador N, Aguado C, Horst M, Knecht E. Import of a cytosolic protein into lysosomes by chaperone-mediated autophagy depends on its folding state. J Biol Chem 2000; 275:27447-56; PMID:10862611
    • (2000) J Biol Chem , vol.275 , pp. 27447-27456
    • Salvador, N.1    Aguado, C.2    Horst, M.3    Knecht, E.4
  • 196
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • PMID:9151685
    • Agarraberes FA, Terlecky SR, Dice JF. An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 1997; 137:825-34; PMID:9151685; http://dx.doi.org/10.1083/jcb.137.4.825
    • (1997) J Cell Biol , vol.137 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 197
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • PMID:9038169
    • Cuervo AM, Dice JF, Knecht E. A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J Biol Chem 1997; 272:5606-15; PMID:9038169; http://dx.doi.org/10.1074/jbc.272.9. 5606
    • (1997) J Biol Chem , vol.272 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 198
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • PMID:7491910
    • Cuervo AM, Knecht E, Terlecky SR, Dice JF. Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am J Physiol 1995; 269:C1200-8; PMID:7491910
    • (1995) Am J Physiol , vol.269
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 199
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidative stress
    • PMID:15331765
    • Kiffin R, Christian C, Knecht E, Cuervo AM. Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell 2004; 15:4829-40; PMID:15331765; http://dx.doi.org/10.1091/mbc.E04-06-0477
    • (2004) Mol Biol Cell , vol.15 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 200
    • 33645829816 scopus 로고    scopus 로고
    • Consequences of the selective blockage of chaperone-mediated autophagy
    • PMID:16585521
    • Massey AC, Kaushik S, Sovak G, Kiffin R, Cuervo AM. Consequences of the selective blockage of chaperone-mediated autophagy. Proc Natl Acad Sci U S A 2006; 103:5805-10; PMID:16585521; http://dx.doi.org/10.1073/pnas.0507436103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5805-5810
    • Massey, A.C.1    Kaushik, S.2    Sovak, G.3    Kiffin, R.4    Cuervo, A.M.5
  • 201
    • 48249091611 scopus 로고    scopus 로고
    • Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy
    • PMID:18337468
    • Kaushik S, Massey AC, Mizushima N, Cuervo AM. Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol Biol Cell 2008; 19:2179-92; PMID:18337468; http://dx.doi.org/10.1091/mbc.E07-11-1155
    • (2008) Mol Biol Cell , vol.19 , pp. 2179-2192
    • Kaushik, S.1    Massey, A.C.2    Mizushima, N.3    Cuervo, A.M.4
  • 202
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • PMID:18644871
    • Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM. The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 2008; 28:5747-63; PMID:18644871; http://dx.doi.org/10.1128/MCB.02070-07
    • (2008) Mol Cell Biol , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 203
    • 84859161154 scopus 로고    scopus 로고
    • Microautophagy: Lesser-known self-eating
    • PMID:22080117
    • Li WW, Li J, Bao JK. Microautophagy: lesser-known self-eating. Cell Mol Life Sci 2012; 69:1125-36; PMID:22080117; http://dx.doi.org/10.1007/s00018-011- 0865-5
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1125-1136
    • Li, W.W.1    Li, J.2    Bao, J.K.3
  • 205
    • 80053438277 scopus 로고    scopus 로고
    • Molecular machinery of macroautophagy and its deregulation in diseases
    • PMID:21787863
    • Wong AS, Cheung ZH, Ip NY. Molecular machinery of macroautophagy and its deregulation in diseases. Biochim Biophys Acta 2011; 1812:1490-7; PMID:21787863; http://dx.doi.org/10.1016/j.bbadis.2011.07.005
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 1490-1497
    • Wong, A.S.1    Cheung, Z.H.2    Ip, N.Y.3
  • 209
    • 65449117176 scopus 로고    scopus 로고
    • Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
    • PMID:19229298
    • Gamerdinger M, Hajieva P, Kaya AM, Wolfrum U, Hartl FU, Behl C. Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. EMBO J 2009; 28:889-901; PMID:19229298; http://dx.doi.org/10.1038/ emboj.2009.29
    • (2009) EMBO J , vol.28 , pp. 889-901
    • Gamerdinger, M.1    Hajieva, P.2    Kaya, A.M.3    Wolfrum, U.4    Hartl, F.U.5    Behl, C.6
  • 210
    • 84865618692 scopus 로고    scopus 로고
    • Inhibition of HSP70: A challenging anti-cancer strategy
    • PMID:22750096
    • Goloudina AR, Demidov ON, Garrido C. Inhibition of HSP70: a challenging anti-cancer strategy. Cancer Lett 2012; 325:117-24; PMID:22750096; http://dx.doi.org/10.1016/j.canlet.2012.06.003
    • (2012) Cancer Lett , vol.325 , pp. 117-124
    • Goloudina, A.R.1    Demidov, O.N.2    Garrido, C.3
  • 211
    • 0022364247 scopus 로고
    • Synthesis and antitumor activity of spergualin analogues. I. Chemical modification of 7-guanidino-3-hydroxyacyl moiety
    • Tokyo PMID:4030502
    • Umeda Y, Moriguchi M, Kuroda H, Nakamura T, Iinuma H, Takeuchi T, Umezawa H. Synthesis and antitumor activity of spergualin analogues. I. Chemical modification of 7-guanidino-3-hydroxyacyl moiety. J Antibiot (Tokyo) 1985; 38:886-98; PMID:4030502; http://dx.doi.org/10.7164/antibiotics.38.886
    • (1985) J Antibiot , vol.38 , pp. 886-898
    • Umeda, Y.1    Moriguchi, M.2    Kuroda, H.3    Nakamura, T.4    Iinuma, H.5    Takeuchi, T.6    Umezawa, H.7
  • 212
    • 0026526303 scopus 로고
    • Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins
    • PMID:1411548
    • Nadler SG, Tepper MA, Schacter B, Mazzucco CE. Interaction of the immunosuppressant deoxyspergualin with a member of the Hsp70 family of heat shock proteins. Science 1992; 258:484-6; PMID:1411548; http://dx.doi.org/10. 1126/science.1411548
    • (1992) Science , vol.258 , pp. 484-486
    • Nadler, S.G.1    Tepper, M.A.2    Schacter, B.3    Mazzucco, C.E.4
  • 213
    • 0028230782 scopus 로고
    • Quantitation of the interaction of the immunosuppressant deoxyspergualin and analogs with Hsc70 and Hsp90
    • PMID:8117717
    • Nadeau K, Nadler SG, Saulnier M, Tepper MA, Walsh CT. Quantitation of the interaction of the immunosuppressant deoxyspergualin and analogs with Hsc70 and Hsp90. Biochemistry 1994; 33:2561-7; PMID:8117717; http://dx.doi.org/10.1021/ bi00175a027
    • (1994) Biochemistry , vol.33 , pp. 2561-2567
    • Nadeau, K.1    Nadler, S.G.2    Saulnier, M.3    Tepper, M.A.4    Walsh, C.T.5
  • 215
    • 0033561687 scopus 로고    scopus 로고
    • Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin: Modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactions
    • PMID:10086320
    • Brodsky JL. Selectivity of the molecular chaperone-specific immunosuppressive agent 15-deoxyspergualin: modulation of Hsc70 ATPase activity without compromising DnaJ chaperone interactions. Biochem Pharmacol 1999; 57:877-80; PMID:10086320; http://dx.doi.org/10.1016/S0006-2952(98)00376-1
    • (1999) Biochem Pharmacol , vol.57 , pp. 877-880
    • Brodsky, J.L.1
  • 216
    • 0028029788 scopus 로고
    • Immunosuppressant deoxyspergualin inhibits antigen processing in monocytes
    • PMID:7930603
    • Hoeger PH, Tepper MA, Faith A, Higgins JA, Lamb JR, Geha RS. Immunosuppressant deoxyspergualin inhibits antigen processing in monocytes. J Immunol 1994; 153:3908-16; PMID:7930603
    • (1994) J Immunol , vol.153 , pp. 3908-3916
    • Hoeger, P.H.1    Tepper, M.A.2    Faith, A.3    Higgins, J.A.4    Lamb, J.R.5    Geha, R.S.6
  • 218
    • 64049089075 scopus 로고    scopus 로고
    • Polyamine compound deoxyspergualin inhibits heat shock protein-induced activation of immature dendritic cells
    • PMID:18686015
    • Sugawara A, Torigoe T, Tamura Y, Kamiguchi K, Nemoto K, Oguro H, Sato N. Polyamine compound deoxyspergualin inhibits heat shock protein-induced activation of immature dendritic cells. Cell Stress Chaperones 2009; 14:133-9; PMID:18686015; http://dx.doi.org/10.1007/s12192-008-0064-y
    • (2009) Cell Stress Chaperones , vol.14 , pp. 133-139
    • Sugawara, A.1    Torigoe, T.2    Tamura, Y.3    Kamiguchi, K.4    Nemoto, K.5    Oguro, H.6    Sato, N.7
  • 219
    • 0026537928 scopus 로고
    • Treatment of renal transplant rejection with 15-deoxyspergualin - A dose-finding study in man
    • PMID:1539294
    • Ohlman S, Gannedahl G, Tydén G, Tufveson G, Groth CG. Treatment of renal transplant rejection with 15-deoxyspergualin - a dose-finding study in man. Transplant Proc 1992; 24:318-20; PMID:1539294
    • (1992) Transplant Proc , vol.24 , pp. 318-320
    • Ohlman, S.1    Gannedahl, G.2    Tydén, G.3    Tufveson, G.4    Groth, C.G.5
  • 220
    • 0027528909 scopus 로고
    • 15-Deoxyspergualin "rescue therapy" for methylprednisolone- resistant rejection of renal transplants as compared with anti-T cell monoclonal antibody (OKT3)
    • PMID:8456469
    • Okubo M, Tamura K, Kamata K, Tsukamoto Y, Nakayama Y, Osakabe T, Sato K, Go M, Kumano K, Endo T. 15-Deoxyspergualin "rescue therapy" for methylprednisolone-resistant rejection of renal transplants as compared with anti-T cell monoclonal antibody (OKT3). Transplantation 1993; 55:505-8; PMID:8456469; http://dx.doi.org/10.1097/00007890-199303000-00010
    • (1993) Transplantation , vol.55 , pp. 505-508
    • Okubo, M.1    Tamura, K.2    Kamata, K.3    Tsukamoto, Y.4    Nakayama, Y.5    Osakabe, T.6    Sato, K.7    Go, M.8    Kumano, K.9    Endo, T.10
  • 221
    • 0028085299 scopus 로고
    • Pharmacokinetics of 15-deoxyspergualin studied in renal transplant patients receiving the drug during graft rejection
    • PMID:8117404
    • Ohlman S, Zilg H, Schindel F, Lindholm A. Pharmacokinetics of 15-deoxyspergualin studied in renal transplant patients receiving the drug during graft rejection. Transpl Int 1994; 7:5-10; PMID:8117404; http://dx.doi.org/10.1111/j.1432-2277.1994.tb01270.x
    • (1994) Transpl Int , vol.7 , pp. 5-10
    • Ohlman, S.1    Zilg, H.2    Schindel, F.3    Lindholm, A.4
  • 223
    • 10944263745 scopus 로고    scopus 로고
    • Small molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity
    • PMID:15448148
    • Fewell SW, Smith CM, Lyon MA, Dumitrescu TP, Wipf P, Day BW, Brodsky JL. Small molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity. J Biol Chem 2004; 279:51131-40; PMID:15448148; http://dx.doi.org/10. 1074/jbc.M404857200
    • (2004) J Biol Chem , vol.279 , pp. 51131-51140
    • Fewell, S.W.1    Smith, C.M.2    Lyon, M.A.3    Dumitrescu, T.P.4    Wipf, P.5    Day, B.W.6    Brodsky, J.L.7
  • 224
    • 37549046818 scopus 로고    scopus 로고
    • Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase
    • PMID:18060774
    • Wisén S, Androsavich J, Evans CG, Chang L, Gestwicki JE. Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase. Bioorg Med Chem Lett 2008; 18:60-5; PMID:18060774; http://dx.doi.org/10.1016/j.bmcl.2007.11.027
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 60-65
    • Wisén, S.1    Androsavich, J.2    Evans, C.G.3    Chang, L.4    Gestwicki, J.E.5
  • 225
    • 36148989163 scopus 로고    scopus 로고
    • High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK
    • PMID:17904512
    • Chang L, Bertelsen EB, Wisén S, Larsen EM, Zuiderweg ER, Gestwicki JE. High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. Anal Biochem 2008; 372:167-76; PMID:17904512; http://dx.doi.org/10.1016/j.ab.2007.08.020
    • (2008) Anal Biochem , vol.372 , pp. 167-176
    • Chang, L.1    Bertelsen, E.B.2    Wisén, S.3    Larsen, E.M.4    Zuiderweg, E.R.5    Gestwicki, J.E.6
  • 226
    • 39149117364 scopus 로고    scopus 로고
    • Identification of small molecules that modify the protein folding activity of heat shock protein 70
    • PMID:18191466
    • Wisén S, Gestwicki JE. Identification of small molecules that modify the protein folding activity of heat shock protein 70. Anal Biochem 2008; 374:371-7; PMID:18191466; http://dx.doi.org/10.1016/j.ab.2007.12.009
    • (2008) Anal Biochem , vol.374 , pp. 371-377
    • Wisén, S.1    Gestwicki, J.E.2
  • 227
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro
    • PMID:16973602
    • Evans CG, Wisén S, Gestwicki JE. Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro. J Biol Chem 2006; 281:33182-91; PMID:16973602; http://dx.doi.org/10.1074/jbc.M606192200
    • (2006) J Biol Chem , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisén, S.2    Gestwicki, J.E.3
  • 230
    • 50349096803 scopus 로고    scopus 로고
    • Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis
    • PMID:18772114
    • Powers MV, Clarke PA, Workman P. Dual targeting of HSC70 and HSP72 inhibits HSP90 function and induces tumor-specific apoptosis. Cancer Cell 2008; 14:250-62; PMID:18772114; http://dx.doi.org/10.1016/j.ccr.2008.08.002
    • (2008) Cancer Cell , vol.14 , pp. 250-262
    • Powers, M.V.1    Clarke, P.A.2    Workman, P.3
  • 234
    • 70349768075 scopus 로고    scopus 로고
    • A small molecule inhibitor of inducible heat shock protein 70
    • PMID:19818706
    • Leu JI, Pimkina J, Frank A, Murphy ME, George DL. A small molecule inhibitor of inducible heat shock protein 70. Mol Cell 2009; 36:15-27; PMID:19818706; http://dx.doi.org/10.1016/j.molcel.2009.09.023
    • (2009) Mol Cell , vol.36 , pp. 15-27
    • Leu, J.I.1    Pimkina, J.2    Frank, A.3    Murphy, M.E.4    George, D.L.5
  • 235
    • 79960694363 scopus 로고    scopus 로고
    • HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells
    • PMID:21636681
    • Leu JI, Pimkina J, Pandey P, Murphy ME, George DL. HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells. Mol Cancer Res 2011; 9:936-47; PMID:21636681; http://dx.doi.org/10.1158/1541-7786.MCR-11-0019
    • (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
  • 236
    • 0030064081 scopus 로고    scopus 로고
    • MKT-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation
    • PMID:8564968
    • Koya K, Li Y, Wang H, Ukai T, Tatsuta N, Kawakami M, Shishido, Chen LB. MKT-077, a novel rhodacyanine dye in clinical trials, exhibits anticarcinoma activity in preclinical studies based on selective mitochondrial accumulation. Cancer Res 1996; 56:538-43; PMID:8564968
    • (1996) Cancer Res , vol.56 , pp. 538-543
    • Koya, K.1    Li, Y.2    Wang, H.3    Ukai, T.4    Tatsuta, N.5    Kawakami, M.6    Shishido7    Chen, L.B.8
  • 238
    • 0034671731 scopus 로고    scopus 로고
    • Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function
    • PMID:11156371
    • Wadhwa R, Sugihara T, Yoshida A, Nomura H, Reddel RR, Simpson R, Maruta H, Kaul SC. Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function. Cancer Res 2000; 60:6818-21; PMID:11156371
    • (2000) Cancer Res , vol.60 , pp. 6818-6821
    • Wadhwa, R.1    Sugihara, T.2    Yoshida, A.3    Nomura, H.4    Reddel, R.R.5    Simpson, R.6    Maruta, H.7    Kaul, S.C.8
  • 239
    • 79960927001 scopus 로고    scopus 로고
    • Allosteric drugs: The interaction of antitumor compound MKT-077 with human Hsp70 chaperones
    • PMID:21708173
    • Rousaki A, Miyata Y, Jinwal UK, Dickey CA, Gestwicki JE, Zuiderweg ER. Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones. J Mol Biol 2011; 411:614-32; PMID:21708173; http://dx.doi.org/10. 1016/j.jmb.2011.06.003
    • (2011) J Mol Biol , vol.411 , pp. 614-632
    • Rousaki, A.1    Miyata, Y.2    Jinwal, U.K.3    Dickey, C.A.4    Gestwicki, J.E.5    Zuiderweg, E.R.6
  • 241
    • 84882250523 scopus 로고    scopus 로고
    • Allosteric heat shock protein 70 inhibitors rapidly rescue synaptic plasticity deficits by reducing aberrant tau
    • PMID:23607970
    • Abisambra J, Jinwal UK, Miyata Y, Rogers J, Blair L, Li X, Seguin SP, Wang L, Jin Y, Bacon J, et al. Allosteric heat shock protein 70 inhibitors rapidly rescue synaptic plasticity deficits by reducing aberrant tau. Biol Psychiatry 2013; 74:367-74; PMID:23607970; http://dx.doi.org/10.1016/j.biopsych. 2013.02.027
    • (2013) Biol Psychiatry , vol.74 , pp. 367-374
    • Abisambra, J.1    Jinwal, U.K.2    Miyata, Y.3    Rogers, J.4    Blair, L.5    Li, X.6    Seguin, S.P.7    Wang, L.8    Jin, Y.9    Bacon, J.10
  • 242
    • 84879767467 scopus 로고    scopus 로고
    • Synthesis and Initial Evaluation of YM-08, a Blood-Brain Barrier Permeable Derivative of the Heat Shock Protein 70 (Hsp70) Inhibitor MKT-077, Which Reduces Tau Levels
    • Miyata Y, Li X, Lee HF, Jinwal UK, Srinivasan SR, Seguin SP, et al. Synthesis and Initial Evaluation of YM-08, a Blood-Brain Barrier Permeable Derivative of the Heat Shock Protein 70 (Hsp70) Inhibitor MKT-077, Which Reduces Tau Levels. ACS Chem Neurosci 2013
    • (2013) ACS Chem Neurosci
    • Miyata, Y.1    Li, X.2    Lee, H.F.3    Jinwal, U.K.4    Srinivasan, S.R.5    Seguin, S.P.6
  • 243
    • 79951837256 scopus 로고    scopus 로고
    • Chemical screens against a reconstituted multiprotein complex: Myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism
    • PMID:21338918
    • Chang L, Miyata Y, Ung PM, Bertelsen EB, McQuade TJ, Carlson HA, Zuiderweg ER, Gestwicki JE. Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism. Chem Biol 2011; 18:210-21; PMID:21338918; http://dx.doi.org/10.1016/j.chembiol.2010.12.010
    • (2011) Chem Biol , vol.18 , pp. 210-221
    • Chang, L.1    Miyata, Y.2    Ung, P.M.3    Bertelsen, E.B.4    McQuade, T.J.5    Carlson, H.A.6    Zuiderweg, E.R.7    Gestwicki, J.E.8
  • 244
    • 65449168745 scopus 로고    scopus 로고
    • The spliceosomal phosphopeptide P140 controls the lupus disease by interacting with the HSC70 protein and via a mechanism mediated by gammadelta T cells
    • PMID:19390596
    • Page N, Schall N, Strub JM, Quinternet M, Chaloin O, Décossas M, Cung MT, Van Dorsselaer A, Briand JP, Muller S. The spliceosomal phosphopeptide P140 controls the lupus disease by interacting with the HSC70 protein and via a mechanism mediated by gammadelta T cells. PLoS One 2009; 4:e5273; PMID:19390596; http://dx.doi.org/10.1371/journal.pone.0005273
    • (2009) PLoS One , vol.4
    • Page, N.1    Schall, N.2    Strub, J.M.3    Quinternet, M.4    Chaloin, O.5    Décossas, M.6    Cung, M.T.7    Van Dorsselaer, A.8    Briand, J.P.9    Muller, S.10
  • 245
    • 36849014916 scopus 로고    scopus 로고
    • Importance of spliceosomal RNP1 motif for intermolecular T-B cell spreading and tolerance restoration in lupus
    • PMID:17963484
    • Monneaux F, Parietti V, Briand JP, Muller S. Importance of spliceosomal RNP1 motif for intermolecular T-B cell spreading and tolerance restoration in lupus. Arthritis Res Ther 2007; 9:R111; PMID:17963484; http://dx.doi.org/10. 1186/ar2317
    • (2007) Arthritis Res Ther , vol.9
    • Monneaux, F.1    Parietti, V.2    Briand, J.P.3    Muller, S.4
  • 246
    • 0345701527 scopus 로고    scopus 로고
    • T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MR/lpr mice
    • PMID:12548559
    • Monneaux F, Lozano JM, Patarroyo ME, Briand JP, Muller S. T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MR/lpr mice. Eur J Immunol 2003; 33:287-96; PMID:12548559; http://dx.doi.org/10.1002/immu.200310002
    • (2003) Eur J Immunol , vol.33 , pp. 287-296
    • Monneaux, F.1    Lozano, J.M.2    Patarroyo, M.E.3    Briand, J.P.4    Muller, S.5
  • 247
    • 84865390207 scopus 로고    scopus 로고
    • Peptide-based approaches to treat lupus and other autoimmune diseases
    • PMID:22727561
    • Schall N, Page N, Macri C, Chaloin O, Briand JP, Muller S. Peptide-based approaches to treat lupus and other autoimmune diseases. J Autoimmun 2012; 39:143-53; PMID:22727561; http://dx.doi.org/10.1016/j.jaut.2012.05.016
    • (2012) J Autoimmun , vol.39 , pp. 143-153
    • Schall, N.1    Page, N.2    Macri, C.3    Chaloin, O.4    Briand, J.P.5    Muller, S.6
  • 248
    • 57349101501 scopus 로고    scopus 로고
    • Spliceosomal peptide P140 for immunotherapy of systemic lupus erythematosus: Results of an early phase II clinical trial
    • PMID:19035498
    • Muller S, Monneaux F, Schall N, Rashkov RK, Oparanov BA, Wiesel P, Geiger JM, Zimmer R. Spliceosomal peptide P140 for immunotherapy of systemic lupus erythematosus: results of an early phase II clinical trial. Arthritis Rheum 2008; 58:3873-83; PMID:19035498; http://dx.doi.org/10.1002/art.24027
    • (2008) Arthritis Rheum , vol.58 , pp. 3873-3883
    • Muller, S.1    Monneaux, F.2    Schall, N.3    Rashkov, R.K.4    Oparanov, B.A.5    Wiesel, P.6    Geiger, J.M.7    Zimmer, R.8
  • 249
    • 84885182982 scopus 로고    scopus 로고
    • Lupuzor/P140 peptide in patients with systemic lupus erythematosus: A randomised, double-blind, placebo-controlled phase IIb clinical trial
    • PMID:23172751
    • Zimmer R, Scherbarth HR, Rillo OL, Gomez-Reino JJ, Muller S. Lupuzor/P140 peptide in patients with systemic lupus erythematosus: a randomised, double-blind, placebo-controlled phase IIb clinical trial. Ann Rheum Dis 2013; 72:1830-5; PMID:23172751; http://dx.doi.org/10.1136/annrheumdis-2012-202460
    • (2013) Ann Rheum Dis , vol.72 , pp. 1830-1835
    • Zimmer, R.1    Scherbarth, H.R.2    Rillo, O.L.3    Gomez-Reino, J.J.4    Muller, S.5


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