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Volumn 59, Issue , 2015, Pages 121-141

Heat shock proteins and their role in human diseases

Author keywords

Cancer; Diabetes; Ethanol toxicity; HSP families; Ischemia reperfusion; Neurodegeneration

Indexed keywords

ALCOHOL; CELL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEASOME;

EID: 84952906625     PISSN: 1588385X     EISSN: 15884082     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (14)

References (220)
  • 1
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development and lifespan
    • Akerfelt M, Morimoto RI, Sistonen L (2010) Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11:545-555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 2
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: cause or consequence?
    • Jul
    • Andersen JK (2004) Oxidative stress in neurodegeneration: cause or consequence? Nat Med Jul;10 Suppl:S18-25.
    • (2004) Nat Med , vol.10 , pp. S18-25
    • Andersen, J.K.1
  • 4
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid ß-protein [AbP-(1-40)] in bilayer membranes
    • Arispe N, Pollard HB, Rojas E (1993) Giant multilevel cation channels formed by Alzheimer disease amyloid ß-protein [AbP-(1-40)] in bilayer membranes. Proc Natl Acad Sci USA 90:10573-10577.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 5
    • 14044250859 scopus 로고    scopus 로고
    • Hsp27 consolidates intracellular redoxhomeostasis by upholding glutathionein its reduced formand by decreasing iron intracellular levels
    • Arrigo AP, Virot S, Chaufour S, Firdaus W, Kretz-Remy C, Diaz-Latoud C (2005) Hsp27 consolidates intracellular redoxhomeostasis by upholding glutathionein its reduced formand by decreasing iron intracellular levels. Antioxid Redox Signal 7:414-422.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 414-422
    • Arrigo, A.P.1    Virot, S.2    Chaufour, S.3    Firdaus, W.4    Kretz-Remy, C.5    Diaz-Latoud, C.6
  • 8
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM (2002) Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295:865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 10
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 19:4535-4545.
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 11
    • 28244493434 scopus 로고    scopus 로고
    • The hyperfluidization of mammalian cell membranes acts as a signal to initiate the heat shock protein response
    • Balogh G, Horváth I, Nagy E, Hoyk Z, Benko S, Bensaude O, Vígh L (2005) The hyperfluidization of mammalian cell membranes acts as a signal to initiate the heat shock protein response. FEBS J 272:6077-6086.
    • (2005) FEBS J , vol.272 , pp. 6077-6086
    • Balogh, G.1    Horváth, I.2    Nagy, E.3    Hoyk, Z.4    Benko, S.5    Bensaude, O.6    Vígh, L.7
  • 13
    • 33749989045 scopus 로고    scopus 로고
    • Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophiclateral sclerosis
    • Batulan Z, Taylor DM, Aarons RJ, Minotti S, Doroudchi MM, Nalbantoglu J, Durham HD (2006) Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophiclateral sclerosis. Neurobiol Dis 24:213-225.
    • (2006) Neurobiol Dis , vol.24 , pp. 213-225
    • Batulan, Z.1    Taylor, D.M.2    Aarons, R.J.3    Minotti, S.4    Doroudchi, M.M.5    Nalbantoglu, J.6    Durham, H.D.7
  • 15
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J, Craig EA (1994) Heat-shock proteins as molecular chaperones. Eur J Biochem 219:11-23.
    • (1994) Eur J Biochem , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 17
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid-ß protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D (1994) Hydrogen peroxide mediates amyloid-ß protein toxicity. Cell 77:817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 18
    • 0026694490 scopus 로고
    • αB-crystallin in cardiac tissue. Association with actin and desmin filaments
    • Bennardini F, Wrzosek A, Chiesi M (1992) αB-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ Res 71:288-294.
    • (1992) Circ Res , vol.71 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 19
    • 77957278382 scopus 로고    scopus 로고
    • Regulation of the members of the mammalian heat shock factor family
    • Björk JK, Sistonen L (2010) Regulation of the members of the mammalian heat shock factor family. FEBS J 277:4126-4139.
    • (2010) FEBS J , vol.277 , pp. 4126-4139
    • Björk, J.K.1    Sistonen, L.2
  • 20
    • 0032990851 scopus 로고    scopus 로고
    • Heat shock proteins delivered with a virus vector can protect cardiac cells against apoptosis as well as against thermal or ischaemic stress
    • Brar BS, Stephanou A, Wagstaff MJD, Coffin RS, Marber MS, Engelmann G, Latchman DS (1999) Heat shock proteins delivered with a virus vector can protect cardiac cells against apoptosis as well as against thermal or ischaemic stress. J Mol Cell Cardiol 31:135-146.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 135-146
    • Brar, B.S.1    Stephanou, A.2    Wagstaff, M.J.D.3    Coffin, R.S.4    Marber, M.S.5    Engelmann, G.6    Latchman, D.S.7
  • 21
    • 84874157611 scopus 로고    scopus 로고
    • The protective and therapeutic function of small heat shock proteins in neurological diseases
    • Brownell SE, Becker RA, Steinman L (2012) The protective and therapeutic function of small heat shock proteins in neurological diseases. Front Immunol 3:74. doi: 10.3389/fimmu.2012.00074.eCollection 2012.
    • (2012) Front Immunol , vol.3 , pp. 74
    • Brownell, S.E.1    Becker, R.A.2    Steinman, L.3
  • 22
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening W, Roy J, Giasson B, Figlewicz DA, Mushynski WE, Durham HD (1999) Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J Neurochem 72(2):693-699.
    • (1999) J Neurochem , vol.72 , Issue.2 , pp. 693-699
    • Bruening, W.1    Roy, J.2    Giasson, B.3    Figlewicz, D.A.4    Mushynski, W.E.5    Durham, H.D.6
  • 24
    • 0029968421 scopus 로고    scopus 로고
    • Stress proteins and SH-groups in oxidant-induced cell damage after acute ethanol administration in rat
    • Calabrese V, Renis M, Calderone A, Russo A, Barcellona ML, Rizza V (1996) Stress proteins and SH-groups in oxidant-induced cell damage after acute ethanol administration in rat. Free Radic Biol Med 20:391-398.
    • (1996) Free Radic Biol Med , vol.20 , pp. 391-398
    • Calabrese, V.1    Renis, M.2    Calderone, A.3    Russo, A.4    Barcellona, M.L.5    Rizza, V.6
  • 25
  • 26
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y, Koppenhafer SL, Bonini NM, Paulson HL (1999) Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 19:10338-10347.
    • (1999) J Neurosci , vol.19 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 27
    • 28644443855 scopus 로고    scopus 로고
    • The HSP90 family of genes in the human genome: insights into their divergence and evolution
    • Chen B, Piel WH, Gui L, Bruford E, Monteiro A (2005) The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86:627-637.
    • (2005) Genomics , vol.86 , pp. 627-637
    • Chen, B.1    Piel, W.H.2    Gui, L.3    Bruford, E.4    Monteiro, A.5
  • 28
    • 0025167955 scopus 로고
    • Cardiac alphacrystallin. III. Involvement during heart ischemia
    • Chiesi M, Longoni S, Limbruno U (1990) Cardiac alphacrystallin. III. Involvement during heart ischemia. Mol Cell Biochem 97:129-136.
    • (1990) Mol Cell Biochem , vol.97 , pp. 129-136
    • Chiesi, M.1    Longoni, S.2    Limbruno, U.3
  • 29
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J, Levey AI, Weintraub ST, Rees HD, Gearing M, Chin LS, Li L (2004) Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J Biol Chem 279:13256-13264.
    • (2004) J Biol Chem , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 31
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
    • Ciocca DR, Calderwood SK (2005) Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10:86-103.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 33
    • 0030453530 scopus 로고    scopus 로고
    • Differential protection of primary rat cardiocytes by transfection of specific heat stress proteins
    • Cumming DVE, Heads RJ, Watson A, Latchman DS, Yellon DM (1996) Differential protection of primary rat cardiocytes by transfection of specific heat stress proteins. J Mol Cell Cardiol 28:2343-2349.
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 2343-2349
    • Cumming, D.V.E.1    Heads, R.J.2    Watson, A.3    Latchman, D.S.4    Yellon, D.M.5
  • 34
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT, Zoghbi HY (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 19:148-154.
    • (1998) Nat Genet , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 36
    • 0023746618 scopus 로고
    • Heatshock response is associated with enhanced postischemic ventricular recovery
    • Currie RW, Karmazyn M, Kloc M, Mailer K (1988) Heatshock response is associated with enhanced postischemic ventricular recovery. Circ Res 63:543-549.
    • (1988) Circ Res , vol.63 , pp. 543-549
    • Currie, R.W.1    Karmazyn, M.2    Kloc, M.3    Mailer, K.4
  • 37
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review
    • Csermely P, Schnaider T, Soti C, Prohászka Z, Nardai G (1998) The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 79:129-168.
    • (1998) Pharmacol Ther , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohászka, Z.4    Nardai, G.5
  • 40
    • 0027312173 scopus 로고
    • Molecular adaptation of cellular defences following preconditioning of the heart by repeated ischemia
    • Das DK, Engelman RM, Kimura Y (1993) Molecular adaptation of cellular defences following preconditioning of the heart by repeated ischemia. Cardiovasc Res 27:578-584.
    • (1993) Cardiovasc Res , vol.27 , pp. 578-584
    • Das, D.K.1    Engelman, R.M.2    Kimura, Y.3
  • 41
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the α-crystallin-small heat-shock protein superfamily
    • de Jong WW, Caspers GJ, Leunissen JAM (1998) Genealogy of the α-crystallin-small heat-shock protein superfamily. Int J Biol Macromol 22:151-162.
    • (1998) Int J Biol Macromol , vol.22 , pp. 151-162
    • de Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.M.3
  • 43
    • 0026570622 scopus 로고
    • Heat shock protein induction in rat hearts. A role for improved myocardial salvage after ischemia and reperfusion?
    • Donnelly TJ, Sievers RE, Vissern FLJ, Welch WJ, Wolfe CL (1992) Heat shock protein induction in rat hearts. A role for improved myocardial salvage after ischemia and reperfusion? Circulation 85:769-778.
    • (1992) Circulation , vol.85 , pp. 769-778
    • Donnelly, T.J.1    Sievers, R.E.2    Vissern, F.L.J.3    Welch, W.J.4    Wolfe, C.L.5
  • 44
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 25:2519-2528.
    • (2006) EMBO J , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 45
    • 0032573597 scopus 로고    scopus 로고
    • Aggregates from mutant and wildtype α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of ß-sheet and amyloid-like filaments
    • El-Agnaf OM, Jakes R, Curran MD, Middleton D, Ingenito R, Bianchi E, Pessi A, Neill D, Wallace A (1998) Aggregates from mutant and wildtype α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of ß-sheet and amyloid-like filaments. FEBS Lett 440:71-75.
    • (1998) FEBS Lett , vol.440 , pp. 71-75
    • El-Agnaf, O.M.1    Jakes, R.2    Curran, M.D.3    Middleton, D.4    Ingenito, R.5    Bianchi, E.6    Pessi, A.7    Neill, D.8    Wallace, A.9
  • 46
    • 0025382818 scopus 로고
    • The molecular chaperone concept
    • Ellis RJ (1990) The molecular chaperone concept. Semin Cell Biol 1:1-9.
    • (1990) Semin Cell Biol , vol.1 , pp. 1-9
    • Ellis, R.J.1
  • 47
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: a review of programmed cell death
    • Elmore S (2007) Apoptosis: a review of programmed cell death. Toxicol Pathol 35:495-516.
    • (2007) Toxicol Pathol , vol.35 , pp. 495-516
    • Elmore, S.1
  • 49
    • 0031688235 scopus 로고    scopus 로고
    • Chronic ethanol consumption: from neuroadaptation to neurodegeneration
    • Fadda F, Rossetti ZL (1998) Chronic ethanol consumption: from neuroadaptation to neurodegeneration. Prog Neurobiol 56:385-431.
    • (1998) Prog Neurobiol , vol.56 , pp. 385-431
    • Fadda, F.1    Rossetti, Z.L.2
  • 50
    • 0029838557 scopus 로고    scopus 로고
    • Apoptosis-mediated neurotoxicity induced by ß-amyloid and PrP fragments
    • Forloni G, Bugiani O, Tagliavini F, Salmona M (1996) Apoptosis-mediated neurotoxicity induced by ß-amyloid and PrP fragments. Mol Chem Neuropathol 28:163-171.
    • (1996) Mol Chem Neuropathol , vol.28 , pp. 163-171
    • Forloni, G.1    Bugiani, O.2    Tagliavini, F.3    Salmona, M.4
  • 51
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman BC, Morimoto RI (1996) The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J 15:2969-2979.
    • (1996) EMBO J , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 52
    • 0037417220 scopus 로고    scopus 로고
    • Apoptosis and caspases in neurodegenerative diseases
    • Friedlander RM (2003) Apoptosis and caspases in neurodegenerative diseases. N Engl J Med 348:1365-1375.
    • (2003) N Engl J Med , vol.348 , pp. 1365-1375
    • Friedlander, R.M.1
  • 53
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor1-activating compounds suppress polyglutamine-nduced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N, Nagai Y, Popiel HA, Okamoto Y, Yamaguchi M, Toda T (2008) Heat shock transcription factor1-activating compounds suppress polyglutamine-nduced neurodegeneration through induction of multiple molecular chaperones. J Biol Chem 283:26188-26197.
    • (2008) J Biol Chem , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5    Toda, T.6
  • 55
    • 0032582562 scopus 로고    scopus 로고
    • Role of Hsp70 in regulation of stress-kinase JNK: implications in apoptosis and aging
    • Gabai VL, Meriin AB, Yaglom JA, Volloch VZ, Sherman MY (1998) Role of Hsp70 in regulation of stress-kinase JNK: implications in apoptosis and aging. FEBS Lett 438:1-4.
    • (1998) FEBS Lett , vol.438 , pp. 1-4
    • Gabai, V.L.1    Meriin, A.B.2    Yaglom, J.A.3    Volloch, V.Z.4    Sherman, M.Y.5
  • 60
    • 0022498112 scopus 로고
    • Effect of alcohol on cellular membranes
    • Goldstein DB (1986) Effect of alcohol on cellular membranes. Ann Emerg Med 15:1013-1018.
    • (1986) Ann Emerg Med , vol.15 , pp. 1013-1018
    • Goldstein, D.B.1
  • 61
    • 12944328888 scopus 로고    scopus 로고
    • Comparison of the small heat shock proteins αB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle
    • Golenhofen N, Perng MD, Quinlan RA, Drenckhahn D (2004) Comparison of the small heat shock proteins αB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem Cell Biol 122:415-425.
    • (2004) Histochem Cell Biol , vol.122 , pp. 415-425
    • Golenhofen, N.1    Perng, M.D.2    Quinlan, R.A.3    Drenckhahn, D.4
  • 62
    • 33750806555 scopus 로고    scopus 로고
    • Ischemia-induced phosphorylation and translocation of stress protein αB-crystallin to Z lines of myocardium
    • Golenhofen N, Ness W, Koob R, Htun P, Schaper W, Drenckhahn D (1998) Ischemia-induced phosphorylation and translocation of stress protein αB-crystallin to Z lines of myocardium. Am J Physiol 274(5 Pt 2):H1457-64.
    • (1998) Am J Physiol , vol.274 , Issue.5 , pp. H1457-64
    • Golenhofen, N.1    Ness, W.2    Koob, R.3    Htun, P.4    Schaper, W.5    Drenckhahn, D.6
  • 63
    • 29044442697 scopus 로고    scopus 로고
    • Ischemia-induced increase of stiffness of αB-crystallin/HSPB2-deficient myocardium
    • Golenhofen N, Redel A, Wawrousek EF, Drenckhahn D (2006) Ischemia-induced increase of stiffness of αB-crystallin/HSPB2-deficient myocardium. Pflugers Arch 451:518-525.
    • (2006) Pflugers Arch , vol.451 , pp. 518-525
    • Golenhofen, N.1    Redel, A.2    Wawrousek, E.F.3    Drenckhahn, D.4
  • 65
    • 62749130586 scopus 로고    scopus 로고
    • Heat treatment improves glucose tolerance and prevents skeletal muscle insulin resistance in rats fed a high-fat diet
    • Gupte AA, Bomhoff GL, Swerdlow RH, Geiger PC (2009) Heat treatment improves glucose tolerance and prevents skeletal muscle insulin resistance in rats fed a high-fat diet. Diabetes 58:567-578.
    • (2009) Diabetes , vol.58 , pp. 567-578
    • Gupte, A.A.1    Bomhoff, G.L.2    Swerdlow, R.H.3    Geiger, P.C.4
  • 66
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid ß-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid ß-peptide. Nat Rev Mol Cell Biol 8:101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 68
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes SA, Dice JF (1996) Roles of molecular chaperones in protein degradation. J Cell Biol 132:255-258.
    • (1996) J Cell Biol , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 71
    • 0020067552 scopus 로고
    • Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery
    • Hickey ED, Weber LA (1982) Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery. Biochemistry 21:1513-1521.
    • (1982) Biochemistry , vol.21 , pp. 1513-1521
    • Hickey, E.D.1    Weber, L.A.2
  • 72
    • 10044254417 scopus 로고    scopus 로고
    • Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model
    • Hollander JM, Martin JL, Belke DD, Scott BT, Swanson E, Krishnamoorthy V, Dillmann WH (2004) Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model. Circulation 110:3544-3552.
    • (2004) Circulation , vol.110 , pp. 3544-3552
    • Hollander, J.M.1    Martin, J.L.2    Belke, D.D.3    Scott, B.T.4    Swanson, E.5    Krishnamoorthy, V.6    Dillmann, W.H.7
  • 73
    • 0029089158 scopus 로고
    • The effect of ethanol on HSP70 in cultured rat glial cells and in brain areas of rat pups exposed to ethanol in utero
    • Holownia A, Ledig M, Copin JC, Tholey G (1995) The effect of ethanol on HSP70 in cultured rat glial cells and in brain areas of rat pups exposed to ethanol in utero. Neurochem Res 20:875-878.
    • (1995) Neurochem Res , vol.20 , pp. 875-878
    • Holownia, A.1    Ledig, M.2    Copin, J.C.3    Tholey, G.4
  • 74
    • 0033575998 scopus 로고    scopus 로고
    • Hot-tub therapy for type 2 diabetes mellitus
    • Hooper PL (1999) Hot-tub therapy for type 2 diabetes mellitus. N Engl J Med 341:924-925.
    • (1999) N Engl J Med , vol.341 , pp. 924-925
    • Hooper, P.L.1
  • 75
    • 84904107498 scopus 로고    scopus 로고
    • The importance of the cellular stress response in the pathogenesis and treatment of type 2 diabetes
    • Hooper PL, Balogh G, Rivas E, Kavanagh K, Vigh L (2014) The importance of the cellular stress response in the pathogenesis and treatment of type 2 diabetes. Cell Stress Chaperones 19:447-464.
    • (2014) Cell Stress Chaperones , vol.19 , pp. 447-464
    • Hooper, P.L.1    Balogh, G.2    Rivas, E.3    Kavanagh, K.4    Vigh, L.5
  • 76
    • 84868146609 scopus 로고    scopus 로고
    • Loss of stress response as a consequence of viral infection: implications for disease and therapy
    • Hooper PL, Hightower LE, Hooper PL (2012) Loss of stress response as a consequence of viral infection: implications for disease and therapy. Cell Stress Chaperones 17:647-655.
    • (2012) Cell Stress Chaperones , vol.17 , pp. 647-655
    • Hooper, P.L.1    Hightower, L.E.2    Hooper, P.L.3
  • 78
  • 83
    • 0028032068 scopus 로고
    • Heat shock protein induction in rat hearts. A direct correlation between the amount of heat shock protein induced and the degree of myocardial protection
    • Hutter MM, Sievers RE, Barbosa V, Wolfe C (1994) Heat shock protein induction in rat hearts. A direct correlation between the amount of heat shock protein induced and the degree of myocardial protection. Circulation 89:353-360.
    • (1994) Circulation , vol.89 , pp. 353-360
    • Hutter, M.M.1    Sievers, R.E.2    Barbosa, V.3    Wolfe, C.4
  • 84
    • 0034946508 scopus 로고    scopus 로고
    • A non-toxic heat shock protein 70 inducer, geranylgeranylacetone, suppresses apoptosis of cultured rat hepatocytes caused by hydrogen peroxide and ethanol
    • Ikeyama S, Kusumoto K, Miyake H, Rokutan K, Tashiro S (2001) A non-toxic heat shock protein 70 inducer, geranylgeranylacetone, suppresses apoptosis of cultured rat hepatocytes caused by hydrogen peroxide and ethanol. J Hepatol 35:53-61.
    • (2001) J Hepatol , vol.35 , pp. 53-61
    • Ikeyama, S.1    Kusumoto, K.2    Miyake, H.3    Rokutan, K.4    Tashiro, S.5
  • 86
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jaattela M,Wissing D, Kokholm K, Kallunki T, Egeblad M (1998) Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J 17:6124-6134.
    • (1998) EMBO J , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 87
    • 0023701108 scopus 로고
    • Constitutive binding of yeast heat shock factor to DNA in vivo
    • Jakobsen BK, Pelham HRB (1988) Constitutive binding of yeast heat shock factor to DNA in vivo. Mol Cell Biol 8:5040-5042.
    • (1988) Mol Cell Biol , vol.8 , pp. 5040-5042
    • Jakobsen, B.K.1    Pelham, H.R.B.2
  • 88
    • 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
    • Jana NR, Tanaka M, Wang Gh, Nukina N (2000) 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 9:2009-2018.
    • (2000) Hum Mol Genet , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 89
    • 84897939278 scopus 로고    scopus 로고
    • Barcoding heat shock proteins to human diseases:looking beyond the heat shock response
    • Kakkar V, Meister-Broekema M, Minoia M, Carra S, Kampinga HH (2014) Barcoding heat shock proteins to human diseases:looking beyond the heat shock response. Dis Model Mech 7:421-434.
    • (2014) Dis Model Mech , vol.7 , pp. 421-434
    • Kakkar, V.1    Meister-Broekema, M.2    Minoia, M.3    Carra, S.4    Kampinga, H.H.5
  • 92
    • 34047179973 scopus 로고    scopus 로고
    • Ubiquitinated-protein aggregates form in pancreatic beta-cells during diabetes-induced oxidative stress and are regulated by autophagy
    • Kaniuk NA, Kiraly M, Bates H, Vranic M, Volchuk A, Brumell JH (2007) Ubiquitinated-protein aggregates form in pancreatic beta-cells during diabetes-induced oxidative stress and are regulated by autophagy. Diabetes 56:930-939.
    • (2007) Diabetes , vol.56 , pp. 930-939
    • Kaniuk, N.A.1    Kiraly, M.2    Bates, H.3    Vranic, M.4    Volchuk, A.5    Brumell, J.H.6
  • 94
    • 77955665257 scopus 로고    scopus 로고
    • Why proteins without an α-crystallin domain should not be included in the human small heat shock protein family HSPB
    • Kappe G, Boelens WC, de Jong WW (2010) Why proteins without an α-crystallin domain should not be included in the human small heat shock protein family HSPB. Cell Stress Chaperones 15:457-461.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 457-461
    • Kappe, G.1    Boelens, W.C.2    de Jong, W.W.3
  • 95
    • 84894493712 scopus 로고    scopus 로고
    • Heat shock prevents insulin resistance-induced vascular complications by augmenting angiotensin-(1-7) signaling
    • Karpe PA, Tikoo K (2014) Heat shock prevents insulin resistance-induced vascular complications by augmenting angiotensin-(1-7) signaling. Diabetes 63:1124-1139.
    • (2014) Diabetes , vol.63 , pp. 1124-1139
    • Karpe, P.A.1    Tikoo, K.2
  • 96
    • 0031735836 scopus 로고    scopus 로고
    • In acute myeloid leukaemia, coexpression of at least two proteins, including P-glycoprotein, the multidrug resistance-related protein, bcl-2, mutant p53, and heat shock protein 27, is predictive of the response to induction chemotherapy
    • Kasimir-Bauer S, Ottinger H, Meusers P, Beelen DW, Brittinger G, Seeber S, Scheulen ME (1998) In acute myeloid leukaemia, coexpression of at least two proteins, including P-glycoprotein, the multidrug resistance-related protein, bcl-2, mutant p53, and heat shock protein 27, is predictive of the response to induction chemotherapy. Exp Hematol 26:1111-1117.
    • (1998) Exp Hematol , vol.26 , pp. 1111-1117
    • Kasimir-Bauer, S.1    Ottinger, H.2    Meusers, P.3    Beelen, D.W.4    Brittinger, G.5    Seeber, S.6    Scheulen, M.E.7
  • 98
    • 66149106728 scopus 로고    scopus 로고
    • Tissue-specific regulation and expression of heat shock proteins in type 2 diabetic monkeys
    • Kavanagh K, Zhang L, Wagner JD (2009) Tissue-specific regulation and expression of heat shock proteins in type 2 diabetic monkeys. Cell Stress Chaperones 14:291-299.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 291-299
    • Kavanagh, K.1    Zhang, L.2    Wagner, J.D.3
  • 99
    • 84897366749 scopus 로고    scopus 로고
    • Age sensitivity of behavioral tests and brain substrates of normal aging in mice
    • Kennard JA, Woodruff-Pak DS (2011) Age sensitivity of behavioral tests and brain substrates of normal aging in mice. Front Aging Neurosci 3:9.
    • (2011) Front Aging Neurosci , vol.3 , pp. 9
    • Kennard, J.A.1    Woodruff-Pak, D.S.2
  • 100
    • 80052827401 scopus 로고    scopus 로고
    • Inflammation in the early stages of neurodegenerative pathology
    • Khandelwal PJ, Herman AM, Moussa CE (2011) Inflammation in the early stages of neurodegenerative pathology. J Neuroimmunol 238:1-11.
    • (2011) J Neuroimmunol , vol.238 , pp. 1-11
    • Khandelwal, P.J.1    Herman, A.M.2    Moussa, C.E.3
  • 101
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D, KalmarB, Dic k JR, Riddoch-Contreras J, Burnstock G, Greensmith L (2004) Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med 10:402-405.
    • (2004) Nat Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dic k, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 106
    • 36749055907 scopus 로고    scopus 로고
    • Effect of glycation on α-crystallin structure and chaperone-like function
    • Kumar PA, Kumar MS, Reddy GB (2007) Effect of glycation on α-crystallin structure and chaperone-like function. Biochem J 408:251-258.
    • (2007) Biochem J , vol.408 , pp. 251-258
    • Kumar, P.A.1    Kumar, M.S.2    Reddy, G.B.3
  • 108
    • 0036227062 scopus 로고    scopus 로고
    • Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance
    • Kurucz I, Morva A, Vaag A, Eriksson KF, Huang X, Groop L, Koranyi L (2002) Decreased expression of heat shock protein 72 in skeletal muscle of patients with type 2 diabetes correlates with insulin resistance. Diabetes 51:1102-1109.
    • (2002) Diabetes , vol.51 , pp. 1102-1109
    • Kurucz, I.1    Morva, A.2    Vaag, A.3    Eriksson, K.F.4    Huang, X.5    Groop, L.6    Koranyi, L.7
  • 109
    • 0028981717 scopus 로고
    • The Alzheimer's Aß peptide induces neurodegeneration and apoptotic cell death in transgenic mice
    • LaFerla FM, Tinkle BT, Bieberich CJ, Haudenschild CC, Jay G (1995) The Alzheimer's Aß peptide induces neurodegeneration and apoptotic cell death in transgenic mice. Nat Genet 9:21-30.
    • (1995) Nat Genet , vol.9 , pp. 21-30
    • LaFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 111
    • 0034862016 scopus 로고    scopus 로고
    • Heat shock proteins and cardiac protection
    • Latchman DS (2001) Heat shock proteins and cardiac protection. Cardiovasc Res 51:637-646.
    • (2001) Cardiovasc Res , vol.51 , pp. 637-646
    • Latchman, D.S.1
  • 113
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee AS (2005) The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 35:373-381.
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 114
    • 0035118930 scopus 로고    scopus 로고
    • Effect of overexpression of wild-type and mutant Cu/Zn-superoxide dismutases on oxidative damage and antioxidant defences: relevance to Down's syndrome and familial amyotrophic lateral sclerosis
    • Lee M, Hyun D, Jenner P, Halliwell B (2001) Effect of overexpression of wild-type and mutant Cu/Zn-superoxide dismutases on oxidative damage and antioxidant defences: relevance to Down's syndrome and familial amyotrophic lateral sclerosis. J Neurochem 76:957-965.
    • (2001) J Neurochem , vol.76 , pp. 957-965
    • Lee, M.1    Hyun, D.2    Jenner, P.3    Halliwell, B.4
  • 115
    • 0032833144 scopus 로고    scopus 로고
    • Low cell motility induced by hsp27 overexpression decreases osteolytic bone metastases of human breast cancer cells in vivo
    • Lemieux P, Harvey J, Guise T, Dallas M, Oesterreich S, Yin Jj, Selander K, Fuqua S (1999) Low cell motility induced by hsp27 overexpression decreases osteolytic bone metastases of human breast cancer cells in vivo. J Bone Miner Res 14:1570-1575.
    • (1999) J Bone Miner Res , vol.14 , pp. 1570-1575
    • Lemieux, P.1    Harvey, J.2    Guise, T.3    Dallas, M.4    Oesterreich, S.5    Yin, J.J.6    Selander, K.7    Fuqua, S.8
  • 116
    • 0025363926 scopus 로고
    • The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA
    • Leung TK, Rajendran MY, Monfries C, Hall C, Lim L (1990) The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA. Biochem J 267:125-132.
    • (1990) Biochem J , vol.267 , pp. 125-132
    • Leung, T.K.1    Rajendran, M.Y.2    Monfries, C.3    Hall, C.4    Lim, L.5
  • 117
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts
    • Li CG Werb Z (1982) Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts. Proc Natl Acad Sci USA 79:3218-3222.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3218-3222
    • Li Werb Z, C.G.1
  • 118
    • 33745090846 scopus 로고    scopus 로고
    • Identification of breast cancer metastasis-associated proteins in an isogenic tumor metastasis model using two-dimensional gel electrophoresis and liquid chromatography-ion trap-mass spectrometry
    • Li DQ, Wang L, Fei F, Hou YF, Luo JM, Wei-Chen, Zeng R, Wu J, Lu JS, Di GH, Ou ZL, Xia QC, Shen ZZ, Shao ZM (2006) Identification of breast cancer metastasis-associated proteins in an isogenic tumor metastasis model using two-dimensional gel electrophoresis and liquid chromatography-ion trap-mass spectrometry. Proteomics 6:3352-3368.
    • (2006) Proteomics , vol.6 , pp. 3352-3368
    • Li, D.Q.1    Wang, L.2    Fei, F.3    Hou, Y.F.4    Luo, J.M.5    Wei-Chen6    Zeng, R.7    Wu, J.8    Lu, J.S.9    Di, G.H.10    Ou, Z.L.11    Xia, Q.C.12    Shen, Z.Z.13    Shao, Z.M.14
  • 119
    • 0026705546 scopus 로고
    • Distribution of the 72-kd heat-shock protein as a function of transient focal cerebral ischemia in rats
    • Li Y, Chopp M, Garcia JH, Yoshida Y, Zhang ZG, Levine SR (1992) Distribution of the 72-kd heat-shock protein as a function of transient focal cerebral ischemia in rats. Stroke 23:1292-1298.
    • (1992) Stroke , vol.23 , pp. 1292-1298
    • Li, Y.1    Chopp, M.2    Garcia, J.H.3    Yoshida, Y.4    Zhang, Z.G.5    Levine, S.R.6
  • 120
    • 0036512501 scopus 로고    scopus 로고
    • An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response
    • Li Z, Dai J, Zheng H, Liu B, Caudill M (2002) An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response. Front Biosci 7:d731-51.
    • (2002) Front Biosci , vol.7 , pp. d731-d751
    • Li, Z.1    Dai, J.2    Zheng, H.3    Liu, B.4    Caudill, M.5
  • 124
    • 0029978319 scopus 로고    scopus 로고
    • The potential role of HSP70 as an indicator of response to radiation and hyperthermia treatments for recurrent breast cancer
    • Liu FF, Miller N, Levin W, et al. 1996. The potential role of HSP70 as an indicator of response to radiation and hyperthermia treatments for recurrent breast cancer. Int J Hypertherm 12:197-208.
    • (1996) Int J Hypertherm , vol.12 , pp. 197-208
    • Liu, F.F.1    Miller, N.2    Levin, W.3
  • 125
    • 0033578875 scopus 로고    scopus 로고
    • The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone
    • Liu XD, Morano KA, Thiele DJ (1999) The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. J Biol Chem 274:26654-26660.
    • (1999) J Biol Chem , vol.274 , pp. 26654-26660
    • Liu, X.D.1    Morano, K.A.2    Thiele, D.J.3
  • 128
    • 0036319568 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia
    • Lu A, Ran R, Parmentier-Batteur S, Nee A, Sharp FR (2002) Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia. J Neurochem 81:355-364.
    • (2002) J Neurochem , vol.81 , pp. 355-364
    • Lu, A.1    Ran, R.2    Parmentier-Batteur, S.3    Nee, A.4    Sharp, F.R.5
  • 129
    • 84893106531 scopus 로고    scopus 로고
    • Heat shock protein 70 is necessary to improve mitochondrial bioenergetics and reverse diabetic sensory neuropathy following KU-32 therapy
    • Ma J, Farmer KL, Pan P, Urban MJ, Zhao H, Blagg BS, Dobrowsky RT (2014) Heat shock protein 70 is necessary to improve mitochondrial bioenergetics and reverse diabetic sensory neuropathy following KU-32 therapy. J Pharmacol Exp Ther 348(2):281-292.
    • (2014) J Pharmacol Exp Ther , vol.348 , Issue.2 , pp. 281-292
    • Ma, J.1    Farmer, K.L.2    Pan, P.3    Urban, M.J.4    Zhao, H.5    Blagg, B.S.6    Dobrowsky, R.T.7
  • 130
    • 55549115036 scopus 로고    scopus 로고
    • Alcohol exposure regulates heat shock transcription factor binding and heat shock proteins 70 and 90 in monocytes and macrophages: implication for TNF-α regulation
    • Mandrekar P, Catalano D, Jeliazkova V, Kodys K (2008) Alcohol exposure regulates heat shock transcription factor binding and heat shock proteins 70 and 90 in monocytes and macrophages: implication for TNF-α regulation. J Leukoc Biol 84:1335-1345.
    • (2008) J Leukoc Biol , vol.84 , pp. 1335-1345
    • Mandrekar, P.1    Catalano, D.2    Jeliazkova, V.3    Kodys, K.4
  • 131
    • 0027163384 scopus 로고
    • Cardiac stress protein elevation 24 hours after brief ischaemia or heat stress isassociated with resistance to myocardial infarction
    • Marber MS, Latchman DS, Walker JM, Yellon DM (1993) Cardiac stress protein elevation 24 hours after brief ischaemia or heat stress isassociated with resistance to myocardial infarction. Circ Res 88:1264-1272.
    • (1993) Circ Res , vol.88 , pp. 1264-1272
    • Marber, M.S.1    Latchman, D.S.2    Walker, J.M.3    Yellon, D.M.4
  • 132
    • 0028932259 scopus 로고
    • Overexpression of the rat inducible 70 kDa heat shock protein in a transgenic mouse increases the resistance of the heart to ischemic injury
    • Marber MS, Mestril R, Chi SH, Sayen MR (1995) Overexpression of the rat inducible 70 kDa heat shock protein in a transgenic mouse increases the resistance of the heart to ischemic injury. J Clin Invest 95:1446-1456.
    • (1995) J Clin Invest , vol.95 , pp. 1446-1456
    • Marber, M.S.1    Mestril, R.2    Chi, S.H.3    Sayen, M.R.4
  • 133
    • 0031469110 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against ischaemic injury in cardiac myocytes
    • Martin JL, Mestril R, Hilal-Dandan R, Brunton LL, Dilmann WH (1997) Small heat shock proteins and protection against ischaemic injury in cardiac myocytes. Circulation 96:4343-4348.
    • (1997) Circulation , vol.96 , pp. 4343-4348
    • Martin, J.L.1    Mestril, R.2    Hilal-Dandan, R.3    Brunton, L.L.4    Dilmann, W.H.5
  • 134
    • 0030925506 scopus 로고    scopus 로고
    • Effect of oxidative stress on membrane structure: small-angle X-ray diffraction analysis
    • Mason RP, Walter MF, Mason PE (1997) Effect of oxidative stress on membrane structure: small-angle X-ray diffraction analysis. Free Radic Biol Med 23:419-425.
    • (1997) Free Radic Biol Med , vol.23 , pp. 419-425
    • Mason, R.P.1    Walter, M.F.2    Mason, P.E.3
  • 135
    • 0031841818 scopus 로고    scopus 로고
    • Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway
    • Mathew A, Mathur SK, Morimoto RI (1998) Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway. Mol Cell Biol 18:5091-5098.
    • (1998) Mol Cell Biol , vol.18 , pp. 5091-5098
    • Mathew, A.1    Mathur, S.K.2    Morimoto, R.I.3
  • 136
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson MP (2000) Apoptosis in neurodegenerative disorders. Nat Rev Mol Cell Biol 1:120-129.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 138
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human ß-crystallin expression-mediated increase in glutathione is essential for the protective activity of these protein against TNFα-induced cell death
    • Mehlen P, C Kretz-Remy, X Préville, A P Arrigo (1996). Human hsp27, Drosophila hsp27 and human ß-crystallin expression-mediated increase in glutathione is essential for the protective activity of these protein against TNFα-induced cell death. EMBO J 15:2695-2706.
    • (1996) EMBO J , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Kretz-Remy, C.2    Préville, X.3    Arrigo, A.P.4
  • 139
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata Y, Yahara I (1992) The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J Biol Chem 267:7042-7047.
    • (1992) J Biol Chem , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 140
    • 0033027343 scopus 로고    scopus 로고
    • Suppression of ethanol-induced apoptotic DNA fragmentation by geranylgeranylacetone in cultured guinea pig gastric mucosal cells
    • Mizushima T, Tsutsumi S, Rokutan K, Tsuchiya T (1999) Suppression of ethanol-induced apoptotic DNA fragmentation by geranylgeranylacetone in cultured guinea pig gastric mucosal cells. Dig Dis Sci 44:510-514.
    • (1999) Dig Dis Sci , vol.44 , pp. 510-514
    • Mizushima, T.1    Tsutsumi, S.2    Rokutan, K.3    Tsuchiya, T.4
  • 141
    • 0034125918 scopus 로고    scopus 로고
    • Poly-L-glutamine forms cation channels: Relevance to the pathogenesis of the polyglutamine diseases
    • Monoi H, Futaki S, Kugimiya S, Minakata H, Yoshihara K (2000) Poly-L-glutamine forms cation channels: Relevance to the pathogenesis of the polyglutamine diseases. Biophys J 78:2892-2899.
    • (2000) Biophys J , vol.78 , pp. 2892-2899
    • Monoi, H.1    Futaki, S.2    Kugimiya, S.3    Minakata, H.4    Yoshihara, K.5
  • 142
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: cross talk between a family of heat shock-factors, molecular chaperones, and negative regulators
    • Morimoto RI (1998) Regulation of the heat shock transcriptional response: cross talk between a family of heat shock-factors, molecular chaperones, and negative regulators. Genes Dev 12:3788-3796.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 143
    • 0037047429 scopus 로고    scopus 로고
    • Dynamic remodeling of transcription complexes by molecular chaperones
    • Morimoto RI (2002) Dynamic remodeling of transcription complexes by molecular chaperones. Cell 110:281-284.
    • (2002) Cell , vol.110 , pp. 281-284
    • Morimoto, R.I.1
  • 144
    • 0026592050 scopus 로고
    • Transcriptional regulation of heat shock genes. A paradigm for inducible genomic responses
    • Morimoto RI, Sarge KD, Abravaya K (1992) Transcriptional regulation of heat shock genes. A paradigm for inducible genomic responses. J Biol Chem 267:21987-21990.
    • (1992) J Biol Chem , vol.267 , pp. 21987-21990
    • Morimoto, R.I.1    Sarge, K.D.2    Abravaya, K.3
  • 145
  • 146
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6:11-22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 147
    • 0030224714 scopus 로고    scopus 로고
    • Cell surface expression of heat shock proteins and the immune response
    • Multhoff G, Hightower LE (1996) Cell surface expression of heat shock proteins and the immune response. Cell Stress Chaperones 1:167-176.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 167-176
    • Multhoff, G.1    Hightower, L.E.2
  • 148
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata S, Minami Y, Minami M, Chiba T, Tanaka K (2001) CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep 2:1133-1138.
    • (2001) EMBO Rep , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 149
  • 151
    • 4544360560 scopus 로고    scopus 로고
    • Protection of liver cells from ethanol cytotoxicity by curcumin in liver slice culture in vitro
    • Naik RS, Mujumdar AM, Ghaskadbi S (2004) Protection of liver cells from ethanol cytotoxicity by curcumin in liver slice culture in vitro. J Ethnopharmacol 95:31-37.
    • (2004) J Ethnopharmacol , vol.95 , pp. 31-37
    • Naik, R.S.1    Mujumdar, A.M.2    Ghaskadbi, S.3
  • 152
    • 33846945050 scopus 로고    scopus 로고
    • The small heat shock proteins and their clients
    • Nakamoto H, Vígh L (2007) The small heat shock proteins and their clients. Cell Mol Life Sci 64:294-306.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 294-306
    • Nakamoto, H.1    Vígh, L.2
  • 153
    • 0029805267 scopus 로고    scopus 로고
    • Reperfusion causes significant activation of heat shock transcription factor-1 in ischemic rat heart
    • Nishizawa J, Nakai A, Higashi T, Tanabe M, Nomoto S, Matsuda K, Ban T, Nagata K (1996) Reperfusion causes significant activation of heat shock transcription factor-1 in ischemic rat heart. Circulation 94:2185-2192.
    • (1996) Circulation , vol.94 , pp. 2185-2192
    • Nishizawa, J.1    Nakai, A.2    Higashi, T.3    Tanabe, M.4    Nomoto, S.5    Matsuda, K.6    Ban, T.7    Nagata, K.8
  • 154
    • 0025284285 scopus 로고
    • Ethanol-induced lipid peroxidation and oxidative stress in extrahepatic tissues
    • Nordmann R, Riviere C, Rouach H (1990) Ethanol-induced lipid peroxidation and oxidative stress in extrahepatic tissues. Alcohol Alcohol 25:231-237.
    • (1990) Alcohol Alcohol , vol.25 , pp. 231-237
    • Nordmann, R.1    Riviere, C.2    Rouach, H.3
  • 155
    • 0001133526 scopus 로고    scopus 로고
    • Hsp110 protects heatdenatured proteins and confers cellular thermoresistance
    • Oh HJ, Chen X, Subjeck JR (1997) Hsp110 protects heatdenatured proteins and confers cellular thermoresistance. J Biol Chem 272: 31636-31640.
    • (1997) J Biol Chem , vol.272 , pp. 31636-31640
    • Oh, H.J.1    Chen, X.2    Subjeck, J.R.3
  • 156
    • 20444452142 scopus 로고    scopus 로고
    • Effects of insulin resistance on geranylgeranylacetoneinduced expression of heat shock protein 72 and cardioprotection in high-fat diet rats
    • Ooie T, Kajimoto M, Takahashi N, Shinohara T, Taniguchi Y, Kouno H, Wakisaka O, Yoshimatsu H, Saikawa T (2005) Effects of insulin resistance on geranylgeranylacetoneinduced expression of heat shock protein 72 and cardioprotection in high-fat diet rats. Life Sci 77:869-881.
    • (2005) Life Sci , vol.77 , pp. 869-881
    • Ooie, T.1    Kajimoto, M.2    Takahashi, N.3    Shinohara, T.4    Taniguchi, Y.5    Kouno, H.6    Wakisaka, O.7    Yoshimatsu, H.8    Saikawa, T.9
  • 158
    • 84871400877 scopus 로고    scopus 로고
    • Intraneuronal ß-amyloid and its interactions with proteins and subcellular organelles
    • Penke B, Tóth AM, Földi I, Szucs M, Janáky T (2012) Intraneuronal ß-amyloid and its interactions with proteins and subcellular organelles. Electrophoresis 33:3608-3616.
    • (2012) Electrophoresis , vol.33 , pp. 3608-3616
    • Penke, B.1    Tóth, A.M.2    Földi, I.3    Szucs, M.4    Janáky, T.5
  • 159
    • 0001521232 scopus 로고
    • Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains
    • Perry G, Friedman R, Shaw G, Chau V (1987) Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains. Proc Natl Acad Sci USA 84:3033-3036.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3033-3036
    • Perry, G.1    Friedman, R.2    Shaw, G.3    Chau, V.4
  • 165
    • 33751265748 scopus 로고    scopus 로고
    • The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
    • Qiu XB, Shao YM, Miao S, Wang L (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63:2560-2570.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2560-2570
    • Qiu, X.B.1    Shao, Y.M.2    Miao, S.3    Wang, L.4
  • 167
    • 0035124724 scopus 로고    scopus 로고
    • Transgene overexpression of aB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion
    • Ray PS, Martin JL, Swanson EA, Otani H, Dillmann WH, Das DK (2001) Transgene overexpression of aB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. FASEB J 15:393-402.
    • (2001) FASEB J , vol.15 , pp. 393-402
    • Ray, P.S.1    Martin, J.L.2    Swanson, E.A.3    Otani, H.4    Dillmann, W.H.5    Das, D.K.6
  • 168
    • 80052261937 scopus 로고    scopus 로고
    • Lipid peroxidation and neurodegenerative disease
    • Reed TT (2011) Lipid peroxidation and neurodegenerative disease. Free Radic Biol Med 51:1302-1319.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1302-1319
    • Reed, T.T.1
  • 169
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa F (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 18:571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 171
    • 3142604036 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases
    • Ross CA, Pickart CM (2004) The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol 14:703-711.
    • (2004) Trends Cell Biol , vol.14 , pp. 703-711
    • Ross, C.A.1    Pickart, C.M.2
  • 174
  • 175
    • 84880335788 scopus 로고    scopus 로고
    • Gastroprotective effect of desmosdumotin C isolated from Mitrella kentii against ethanol-induced gastric mucosal hemorrhage in rats: possible involvement of glutathione, heat-shock protein-70, sulfhydryl compounds, nitric oxide, and anti-Helicobacter pylori activity
    • Sidahmed HM, Azizan AH, Mohan S, Abdulla MA, Abdelwahab SI, Taha MM, Hadi AH, Ketuly KA, Hashim NM, Loke MF, Vadivelu J (2013) Gastroprotective effect of desmosdumotin C isolated from Mitrella kentii against ethanol-induced gastric mucosal hemorrhage in rats: possible involvement of glutathione, heat-shock protein-70, sulfhydryl compounds, nitric oxide, and anti-Helicobacter pylori activity. BMC Complement Altern Med 13:183.
    • (2013) BMC Complement Altern Med , vol.13 , pp. 183
    • Sidahmed, H.M.1    Azizan, A.H.2    Mohan, S.3    Abdulla, M.A.4    Abdelwahab, S.I.5    Taha, M.M.6    Hadi, A.H.7    Ketuly, K.A.8    Hashim, N.M.9    Loke, M.F.10    Vadivelu, J.11
  • 176
    • 0032454360 scopus 로고    scopus 로고
    • Molecular chaperones in the etiology and therapy of cancer
    • Soti C, Csermely P (1998) Molecular chaperones in the etiology and therapy of cancer. Pathol Oncol Res 4:316-321.
    • (1998) Pathol Oncol Res , vol.4 , pp. 316-321
    • Soti, C.1    Csermely, P.2
  • 177
    • 0036883535 scopus 로고    scopus 로고
    • Chaperones and aging: role in neurodegeneration and in other civilizational diseases
    • Soti C, Csermely P (2002) Chaperones and aging: role in neurodegeneration and in other civilizational diseases. Neurochem Int 41:383-389.
    • (2002) Neurochem Int , vol.41 , pp. 383-389
    • Soti, C.1    Csermely, P.2
  • 179
    • 1542718628 scopus 로고    scopus 로고
    • Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy: a comprehensive review
    • Sreedhar AS, Csermely P (2004) Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy: a comprehensive review. Pharmacol Ther 101:227-257.
    • (2004) Pharmacol Ther , vol.101 , pp. 227-257
    • Sreedhar, A.S.1    Csermely, P.2
  • 180
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava PK, Udono H, Blachere NE, Li Z (1994) Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 39:93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 181
    • 0032030809 scopus 로고    scopus 로고
    • Constitutive and inducible hsp70s are involved in oxidative resistance evoked by heat shock or ethanol
    • Su CY, Chong KY, Owen OE, Dillmann WH, Chang C, Lai CC (1998) Constitutive and inducible hsp70s are involved in oxidative resistance evoked by heat shock or ethanol. J Mol Cell Cardiol 30:587-598.
    • (1998) J Mol Cell Cardiol , vol.30 , pp. 587-598
    • Su, C.Y.1    Chong, K.Y.2    Owen, O.E.3    Dillmann, W.H.4    Chang, C.5    Lai, C.C.6
  • 182
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • SunY, MacRae TH (2005) The small heat shock proteins and their role in human disease. FEBS J 272:2613-2627.
    • (2005) FEBS J , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 183
    • 0032103481 scopus 로고    scopus 로고
    • Overexpressed heat shock protein 70 attenuates hypoxic injury in coronary endothelial cells
    • Suzuki K, Sawa Y, Kaneda Y, Ichikawa H, Shirakura R, Matsuda H (1998) Overexpressed heat shock protein 70 attenuates hypoxic injury in coronary endothelial cells. J Mol Cell Cardiol 30:1129-1136.
    • (1998) J Mol Cell Cardiol , vol.30 , pp. 1129-1136
    • Suzuki, K.1    Sawa, Y.2    Kaneda, Y.3    Ichikawa, H.4    Shirakura, R.5    Matsuda, H.6
  • 184
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama S, Reed JC, Homma S (2003) Heat-shock proteins as regulators of apoptosis. Oncogene 22:9041-9047.
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 185
    • 0030820099 scopus 로고    scopus 로고
    • Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations
    • Tamura Y, Peng P, Liu K, Daou M, Srivastava PK (1997) Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science 278:117-120.
    • (1997) Science , vol.278 , pp. 117-120
    • Tamura, Y.1    Peng, P.2    Liu, K.3    Daou, M.4    Srivastava, P.K.5
  • 186
    • 0030920718 scopus 로고    scopus 로고
    • Different thresholds in the responses of two heat shock transcription factors, HSF1 and HSF3
    • Tanabe M, Nakai A, Kawazoe Y, Nagata K (1997) Different thresholds in the responses of two heat shock transcription factors, HSF1 and HSF3. J Biol Chem 272:15389-15395.
    • (1997) J Biol Chem , vol.272 , pp. 15389-15395
    • Tanabe, M.1    Nakai, A.2    Kawazoe, Y.3    Nagata, K.4
  • 187
    • 0033600816 scopus 로고    scopus 로고
    • The mammalian HSF4 gene generates both an activator and a repressor of heat shock genes by alternative splicing
    • Tanabe M, Sasai N, Nagata K, Liu XD, Liu PC, Thiele DJ, Nakai A (1999) The mammalian HSF4 gene generates both an activator and a repressor of heat shock genes by alternative splicing. J Biol Chem 274:27845-27856.
    • (1999) J Biol Chem , vol.274 , pp. 27845-27856
    • Tanabe, M.1    Sasai, N.2    Nagata, K.3    Liu, X.D.4    Liu, P.C.5    Thiele, D.J.6    Nakai, A.7
  • 188
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissieres A, Mitchell HK, Tracy UM (1974) Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs. J Mol Biol 84:389-398.
    • (1974) J Mol Biol , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 189
    • 78149464449 scopus 로고    scopus 로고
    • Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration
    • Toth ME, Gonda S, Vígh L, Santha M (2010) Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration. Cell Stress Chaperones 15:807-817.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 807-817
    • Toth, M.E.1    Gonda, S.2    Vígh, L.3    Santha, M.4
  • 192
    • 0031692853 scopus 로고    scopus 로고
    • Heat shock protein 72 expression in osteosarcomas correlated with good response to neoadjuvant chemotherapy
    • Trieb K, Lechleitner T, Lang S, Windhager R, Kotz R, Dirnhofer S (1998) Heat shock protein 72 expression in osteosarcomas correlated with good response to neoadjuvant chemotherapy. Human Pathol 29:1050-1055.
    • (1998) Human Pathol , vol.29 , pp. 1050-1055
    • Trieb, K.1    Lechleitner, T.2    Lang, S.3    Windhager, R.4    Kotz, R.5    Dirnhofer, S.6
  • 193
    • 79954992107 scopus 로고    scopus 로고
    • Hsp70 and its molecular role in nervous system diseases
    • Turturici G, Sconzo G, Geraci F (2011) Hsp70 and its molecular role in nervous system diseases. Biochem Res Int 2011:618127.
    • (2011) Biochem Res Int , vol.2011 , pp. 618127
    • Turturici, G.1    Sconzo, G.2    Geraci, F.3
  • 194
    • 0031708908 scopus 로고    scopus 로고
    • Heat shock expression and drug resistance in breast cancer patients treated with induction chemotherapy
    • Vargas-Roig LM, Gago FE, Tello O, Aznar JC, Ciocca DR (1998) Heat shock expression and drug resistance in breast cancer patients treated with induction chemotherapy. Int J Cancer (Pred Oncol) 79:468-475.
    • (1998) Int J Cancer (Pred Oncol) , vol.79 , pp. 468-475
    • Vargas-Roig, L.M.1    Gago, F.E.2    Tello, O.3    Aznar, J.C.4    Ciocca, D.R.5
  • 195
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane:binding sites and implications for Alzheimer's disease
    • Verdier Y, Zarándi M, Penke B (2004) Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane:binding sites and implications for Alzheimer's disease. J Pept Sci 10:229-248.
    • (2004) J Pept Sci , vol.10 , pp. 229-248
    • Verdier, Y.1    Zarándi, M.2    Penke, B.3
  • 196
    • 84865170479 scopus 로고    scopus 로고
    • Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target
    • Vidyasagar A, Wilson NA, Djamali A (2012) Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target. Fibrogen Tissue Repair 5:7.
    • (2012) Fibrogen Tissue Repair , vol.5 , pp. 7
    • Vidyasagar, A.1    Wilson, N.A.2    Djamali, A.3
  • 198
    • 34547190663 scopus 로고    scopus 로고
    • Can the stress protein response be controlled by 'membrane-lipid therapy'?
    • Vígh L, Horváth I, Maresca B, Harwood JL (2007a) Can the stress protein response be controlled by 'membrane-lipid therapy'? Trends Biochem Sci 32:357-363.
    • (2007) Trends Biochem Sci , vol.32 , pp. 357-363
    • Vígh, L.1    Horváth, I.2    Maresca, B.3    Harwood, J.L.4
  • 200
    • 0031786750 scopus 로고    scopus 로고
    • Does the membrane's physical state control the expression of heat shock and other genes?
    • Vígh L, Maresca B, Harwood JL (1998) Does the membrane's physical state control the expression of heat shock and other genes? Trends Biochem Sci 23:369-374.
    • (1998) Trends Biochem Sci , vol.23 , pp. 369-374
    • Vígh, L.1    Maresca, B.2    Harwood, J.L.3
  • 202
    • 0033638733 scopus 로고    scopus 로고
    • Cellular predictive factors for the drug response of lung cancer
    • Volm M, Rittgen W (2000) Cellular predictive factors for the drug response of lung cancer. Anticancer Res 20:3449-3458.
    • (2000) Anticancer Res , vol.20 , pp. 3449-3458
    • Volm, M.1    Rittgen, W.2
  • 203
    • 34548126863 scopus 로고    scopus 로고
    • Ethanol preconditioning protects against ischemia/reperfusion-induced brain damage: role of NADPH oxidase-derived ROS
    • Wang Q, Sun AY, Simonyi A, Kalogeris TJ, Miller DK, Sun GY, Korthuis RJ (2007) Ethanol preconditioning protects against ischemia/reperfusion-induced brain damage: role of NADPH oxidase-derived ROS. Free Radic Biol Med 43:1048-1060.
    • (2007) Free Radic Biol Med , vol.43 , pp. 1048-1060
    • Wang, Q.1    Sun, A.Y.2    Simonyi, A.3    Kalogeris, T.J.4    Miller, D.K.5    Sun, G.Y.6    Korthuis, R.J.7
  • 204
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, Bonini NM (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 23:425-428.
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 205
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • Welch WJ, Feramisco JR (1984) Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J Biol Chem 259:4501-4513.
    • (1984) J Biol Chem , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 206
    • 36248968668 scopus 로고    scopus 로고
    • Heat shock proteins and amateur chaperones in amyloid-Beta accumulation and clearance in Alzheimer's disease
    • Wilhelmus MM, de Waal RM, Verbeek MM (2007) Heat shock proteins and amateur chaperones in amyloid-Beta accumulation and clearance in Alzheimer's disease. Mol Neurobiol 35:203-216.
    • (2007) Mol Neurobiol , vol.35 , pp. 203-216
    • Wilhelmus, M.M.1    de Waal, R.M.2    Verbeek, M.M.3
  • 207
    • 33646857038 scopus 로고    scopus 로고
    • Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta proteintoxicity
    • Wilhelmus MM, Boelens WC, Otte-Höller I, Kamps B, de Waal RM, Verbeek MM (2006b) Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta proteintoxicity. Brain Res 1089:67-78.
    • (2006) Brain Res , vol.1089 , pp. 67-78
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Höller, I.3    Kamps, B.4    de Waal, R.M.5    Verbeek, M.M.6
  • 209
    • 16544383147 scopus 로고    scopus 로고
    • Alcohol, oxidative stress, and free radical damage
    • Wu D, Cederbaum AI (2003) Alcohol, oxidative stress, and free radical damage. Alcohol Res Health 27:277-284.
    • (2003) Alcohol Res Health , vol.27 , pp. 277-284
    • Wu, D.1    Cederbaum, A.I.2
  • 210
    • 84876874138 scopus 로고    scopus 로고
    • The role of heat shock proteins during neurodegeneration in Alzheimer's, Parkinson's and Huntington's disease
    • In Richter-Landesberg C, ed., TX: Landes-Bioscience
    • Wyttenbach A, Arrigo AP (2009) The role of heat shock proteins during neurodegeneration in Alzheimer's, Parkinson's and Huntington's disease. In Richter-Landesberg C, ed., Heat Shock Proteins in Neural Cells. TX: Landes-Bioscience, 81-99.
    • (2009) Heat Shock Proteins in Neural Cells , pp. 81-99
    • Wyttenbach, A.1    Arrigo, A.P.2
  • 211
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach A, Sauvageot O, Carmichael J, Diaz-Latoud C, Arrigo AP, Rubinsztein DC (2002) Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 11:1137-1151.
    • (2002) Hum Mol Genet , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 212
    • 0029849363 scopus 로고    scopus 로고
    • Expression and roles of heat shock proteins in human breast cancer
    • Yano M, Naito Z, Tanaka S, Asano G (1996) Expression and roles of heat shock proteins in human breast cancer. Jpn J Cancer Res 87:908-915.
    • (1996) Jpn J Cancer Res , vol.87 , pp. 908-915
    • Yano, M.1    Naito, Z.2    Tanaka, S.3    Asano, G.4
  • 214
    • 39849097515 scopus 로고    scopus 로고
    • Ginseng, the root of Panax ginseng C.A. Meyer, protects ethanol-induced gastric damages in rat through the induction of cytoprotective heat-shock protein 27
    • Yeo M, Kim DK, Cho SW, Hong HD (2008) Ginseng, the root of Panax ginseng C.A. Meyer, protects ethanol-induced gastric damages in rat through the induction of cytoprotective heat-shock protein 27. Dig Dis Sci 53:606-613.
    • (2008) Dig Dis Sci , vol.53 , pp. 606-613
    • Yeo, M.1    Kim, D.K.2    Cho, S.W.3    Hong, H.D.4
  • 215
    • 0035943343 scopus 로고    scopus 로고
    • Cholesterol, a modulator of membrane-associated Aß-fibrillogenesis and neurotoxicity
    • Yip CM, Elton EA, Darabie AA, Morrison MR, McLaurin J (2001) Cholesterol, a modulator of membrane-associated Aß-fibrillogenesis and neurotoxicity. J Mol Biol 311:723-734.
    • (2001) J Mol Biol , vol.311 , pp. 723-734
    • Yip, C.M.1    Elton, E.A.2    Darabie, A.A.3    Morrison, M.R.4    McLaurin, J.5
  • 217
    • 37549004821 scopus 로고    scopus 로고
    • Antiinflammatory effects of the 70 kDa heat shock protein in experimental stroke
    • Zheng Z, Kim JY, Ma H, Lee JE, Yenari MA (2008) Antiinflammatory effects of the 70 kDa heat shock protein in experimental stroke. J Cereb Blood Flow Metab 28:53-63.
    • (2008) J Cereb Blood Flow Metab , vol.28 , pp. 53-63
    • Zheng, Z.1    Kim, J.Y.2    Ma, H.3    Lee, J.E.4    Yenari, M.A.5
  • 218
    • 0035408265 scopus 로고    scopus 로고
    • Ethanol-induced apoptosis in mouse liver: Fas- and cytochrome c-mediated caspase-3 activation pathway
    • Zhou Z, Sun X, Kang YJ (2001) Ethanol-induced apoptosis in mouse liver: Fas- and cytochrome c-mediated caspase-3 activation pathway. Am J Pathol 159:329-338.
    • (2001) Am J Pathol , vol.159 , pp. 329-338
    • Zhou, Z.1    Sun, X.2    Kang, Y.J.3
  • 220
    • 1642356755 scopus 로고    scopus 로고
    • HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells
    • Zourlidou A, Payne Smith MD, Latchman DS (2004) HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells. J Neurochem 88:1439-1448.
    • (2004) J Neurochem , vol.88 , pp. 1439-1448
    • Zourlidou, A.1    Payne Smith, M.D.2    Latchman, D.S.3


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