메뉴 건너뛰기




Volumn 83, Issue 2, 1998, Pages 117-132

Stress (heat shock) proteins molecular chaperones in cardiovascular biology and disease

Author keywords

Aging; Gene expression; Ischemia; Molecular chaperone; Stress protein; Transcription factor; Vascular biology

Indexed keywords

CHAPERONE; CONTRACTILE PROTEIN; HEAT SHOCK PROTEIN; ION CHANNEL; MUTANT PROTEIN;

EID: 0032572603     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.83.2.117     Document Type: Review
Times cited : (814)

References (252)
  • 1
    • 0018846666 scopus 로고
    • Inhibition of protein degradation in the energy-poor heart
    • Rannels DE, Chua B, Kao R, Morgan HE. Inhibition of protein degradation in the energy-poor heart. Adv Myocardiol. 1980;1:535-546.
    • (1980) Adv Myocardiol , vol.1 , pp. 535-546
    • Rannels, D.E.1    Chua, B.2    Kao, R.3    Morgan, H.E.4
  • 2
    • 0026544468 scopus 로고
    • Alterations in myofibrillar function and protein profiles after complete global ischemia in rat hearts
    • Westfall MV, Solaro RJ. Alterations in myofibrillar function and protein profiles after complete global ischemia in rat hearts. Circ Res. 1992;70: 302-313.
    • (1992) Circ Res , vol.70 , pp. 302-313
    • Westfall, M.V.1    Solaro, R.J.2
  • 3
    • 0025095698 scopus 로고
    • Degradation of sarcoplasmic reticulum calcium-pumping ATPase in ischemic-reperfused myocardium: Role of calcium-activated neutral protease
    • Yoshida Y, Shiga T, Imai S. Degradation of sarcoplasmic reticulum calcium-pumping ATPase in ischemic-reperfused myocardium: role of calcium-activated neutral protease. Basic Res Cardiol. 1990;85: 495-507.
    • (1990) Basic Res Cardiol , vol.85 , pp. 495-507
    • Yoshida, Y.1    Shiga, T.2    Imai, S.3
  • 4
    • 0000104030 scopus 로고    scopus 로고
    • Role of troponin I proteolysis in the pathogenesis of stunned myocardium
    • Gao WD, Atar D, Liu Y, Perez NG, Murphy AM, Marban E. Role of troponin I proteolysis in the pathogenesis of stunned myocardium. Circ Res. 1997;80:393-399.
    • (1997) Circ Res , vol.80 , pp. 393-399
    • Gao, W.D.1    Atar, D.2    Liu, Y.3    Perez, N.G.4    Murphy, A.M.5    Marban, E.6
  • 5
    • 0025164036 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: An alpha/beta cardiac myosin heavy chain hybrid gene
    • Tanigawa G, Jarcho JA, Kass S, Solomon SD, Vosberg HP, Seidman JG, Seidman CE. A molecular basis for familial hypertrophic cardiomyopathy: an alpha/beta cardiac myosin heavy chain hybrid gene. Cell. 1990;62:991-998.
    • (1990) Cell , vol.62 , pp. 991-998
    • Tanigawa, G.1    Jarcho, J.A.2    Kass, S.3    Solomon, S.D.4    Vosberg, H.P.5    Seidman, J.G.6    Seidman, C.E.7
  • 6
    • 0025040392 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: A beta cardiac myosin heavy chain gene missense mutation
    • Geisterfer-Lowrance AA, Kass S, Tanigawa G, Vosberg HP, McKenna W, Seidman CE, Seidman JG. A molecular basis for familial hypertrophic cardiomyopathy: a beta cardiac myosin heavy chain gene missense mutation. Cell. 1990;62:999-1006.
    • (1990) Cell , vol.62 , pp. 999-1006
    • Geisterfer-Lowrance, A.A.1    Kass, S.2    Tanigawa, G.3    Vosberg, H.P.4    McKenna, W.5    Seidman, C.E.6    Seidman, J.G.7
  • 7
    • 0030046902 scopus 로고    scopus 로고
    • Contractile protein mutations and heart disease
    • Vikstrom KL, Leinwand LA. Contractile protein mutations and heart disease. Curr Opin Cell Biol. 1996;8:97-105.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 97-105
    • Vikstrom, K.L.1    Leinwand, L.A.2
  • 9
    • 0030071326 scopus 로고    scopus 로고
    • The long QT syndrome: A review of recent molecular genetic and physiologic discoveries
    • Baltimore.
    • Keating MT. The long QT syndrome: a review of recent molecular genetic and physiologic discoveries. Medicine (Baltimore). 1996; 75:1-5.
    • (1996) Medicine , vol.75 , pp. 1-5
    • Keating, M.T.1
  • 11
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J. Protein folding in the cell. Nature. 1992;355: 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 12
    • 0024314918 scopus 로고
    • Molecular chaperones: Proteins essential for the biogenesis of some macromolecular structures
    • Ellis RJ, Hemmingsen SM. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem Sci. 1989;14:339-342.
    • (1989) Trends Biochem Sci. , vol.14 , pp. 339-342
    • Ellis, R.J.1    Hemmingsen, S.M.2
  • 13
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F. Molecular chaperones in cellular protein folding. Nature. 1996; 381:571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.1
  • 14
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock and glucose-regulated proteins
    • Pelham HR. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell. 1986;46:959-961.
    • (1986) Cell , vol.46 , pp. 959-961
    • Pelham, H.R.1
  • 15
    • 0025777354 scopus 로고
    • Heat shock, stress proteins, chaperones, and proteotoxicity
    • Hightower LE. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell. 1991;66:191-197.
    • (1991) Cell , vol.66 , pp. 191-197
    • Hightower, L.E.1
  • 17
    • 0028932259 scopus 로고
    • Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury
    • Marber MS, Mestril R, Chi SH, Sayen MR, Yellon DM, Dillmann WH. Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury. J Clin Invest. 1995;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    Yellon, D.M.5    Dillmann, W.H.6
  • 19
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • Thomas PJ, Qu BH, Pedersen PL. Defective protein folding as a basis of human disease. Trends Biochem Sci. 1995;20:456-459.
    • (1995) Trends Biochem Sci. , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.H.2    Pedersen, P.L.3
  • 20
    • 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
    • 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;272:25421-25424.
    • (1997) J Biol Chem. , vol.272 , pp. 25421-25424
    • Strickland, E.1    Qu, B.H.2    Millen, L.3    Thomas, P.J.4
  • 21
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F. Discovery of the heat shock response. Cell Stress Chaperones. 1996;1:97-98.
    • (1996) Cell Stress Chaperones. , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 22
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissieres A, Mitchell HK, Tracy UM. Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol. 1974;84:389-398.
    • (1974) J Mol Biol. , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 23
    • 0030889612 scopus 로고    scopus 로고
    • Molecular chaperones and the heat shock response at Cold Spring Harbor
    • Hightower LE, Hendershot LM. Molecular chaperones and the heat shock response at Cold Spring Harbor. Cell Stress Chaperones. 1997; 2:1-11.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 1-11
    • Hightower, L.E.1    Hendershot, L.M.2
  • 25
    • 0027420158 scopus 로고
    • How cells respond to stress
    • Welch WJ. How cells respond to stress. Sci Am. 1993;268:56-64.
    • (1993) Sci Am , vol.268 , pp. 56-64
    • Welch, W.J.1
  • 26
    • 0026034137 scopus 로고
    • Response of mammalian cells to metabolic stress: Changes in cell physiology and structure/function of stress proteins
    • Welch WJ, Kang HS, Beckmann RP, Mizzen LA. Response of mammalian cells to metabolic stress: changes in cell physiology and structure/function of stress proteins. Curr Top Microbiol Immunol. 1991;167: 31-55.
    • (1991) Curr Top Microbiol Immunol , vol.167 , pp. 31-55
    • Welch, W.J.1    Kang, H.S.2    Beckmann, R.P.3    Mizzen, L.A.4
  • 27
    • 0026736772 scopus 로고
    • The thermoresistant state: Protection from initial damage or better repair?
    • Laszlo A. The thermoresistant state: protection from initial damage or better repair? Exp Cell Res. 1992;202:519-531.
    • (1992) Exp Cell Res , vol.202 , pp. 519-531
    • Laszlo, A.1
  • 28
    • 0021741946 scopus 로고
    • Role of glycolytic products in damage to ischemic myocardium: Dissociation of adenosine triphosphate levels and recovery of function of reperfused ischemic hearts
    • Neely JR, Grotyohann LW. Role of glycolytic products in damage to ischemic myocardium: dissociation of adenosine triphosphate levels and recovery of function of reperfused ischemic hearts. Circ Res. 1984;55: 816-824.
    • (1984) Circ Res , vol.55 , pp. 816-824
    • Neely, J.R.1    Grotyohann, L.W.2
  • 29
    • 0025122903 scopus 로고
    • Acquired thermotolerance following heat shock protein synthesis prevents impairment of mitochondrial ATPase activity at elevated temperatures in Saccharomyces cerevisiae
    • Patriarca EJ, Maresca B. Acquired thermotolerance following heat shock protein synthesis prevents impairment of mitochondrial ATPase activity at elevated temperatures in Saccharomyces cerevisiae. Exp Cell Res. 1990;190:57-64.
    • (1990) Exp Cell Res , vol.190 , pp. 57-64
    • Patriarca, E.J.1    Maresca, B.2
  • 30
    • 0026823769 scopus 로고
    • Mitochondrial activity and heat-shock response during morphogenesis in the pathogenic fungus Histoplasma capsulatum
    • Patriarca EJ, Kobayashi GS, Maresca B. Mitochondrial activity and heat-shock response during morphogenesis in the pathogenic fungus Histoplasma capsulatum. Biochem Cell Biol. 1992;70:207-214.
    • (1992) Biochem Cell Biol , vol.70 , pp. 207-214
    • Patriarca, E.J.1    Kobayashi, G.S.2    Maresca, B.3
  • 31
    • 0022374761 scopus 로고
    • Mechanism of inhibition of polypeptide chain initiation in heat-shocked Ehrlich cells involves reduction of eukaryotic initiation factor 4F activity
    • Panniers R, Stewart EB, Merrick WC, Henshaw EC. Mechanism of inhibition of polypeptide chain initiation in heat-shocked Ehrlich cells involves reduction of eukaryotic initiation factor 4F activity. J Biol Chem. 1985;260:9648-9653.
    • (1985) J Biol Chem , vol.260 , pp. 9648-9653
    • Panniers, R.1    Stewart, E.B.2    Merrick, W.C.3    Henshaw, E.C.4
  • 32
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis
    • Scorsone KA, Panniers R, Rowlands AG, Henshaw EC. Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis. J Biol Chem. 1987;262:14538-14543.
    • (1987) J Biol Chem , vol.262 , pp. 14538-14543
    • Scorsone, K.A.1    Panniers, R.2    Rowlands, A.G.3    Henshaw, E.C.4
  • 33
    • 0025936233 scopus 로고
    • Inactivation of mRNA cap-binding protein complex in Drosophila melanogaster embryos under heat shock
    • Zapata JM, Maroto FG, Sierra JM. Inactivation of mRNA cap-binding protein complex in Drosophila melanogaster embryos under heat shock. J Biol Chem. 1991;266:16007-16014.
    • (1991) J Biol Chem , vol.266 , pp. 16007-16014
    • Zapata, J.M.1    Maroto, F.G.2    Sierra, J.M.3
  • 34
    • 0023511826 scopus 로고
    • Posttranscriptional regulation of hsp70 expression in human cells: Effects of heat shock, inhibition of protein synthesis, and adenovirus infection on translation and mRNA stability
    • Theodorakis NG, Morimoto RI. Posttranscriptional regulation of hsp70 expression in human cells: effects of heat shock, inhibition of protein synthesis, and adenovirus infection on translation and mRNA stability. Mol Cell Biol. 1987;7:4357-4368.
    • (1987) Mol Cell Biol , vol.7 , pp. 4357-4368
    • Theodorakis, N.G.1    Morimoto, R.I.2
  • 35
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein
    • Arrigo AP, Suhan JP, Welch WJ. Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein. Mol Cell Biol. 1988;8:5059-5071.
    • (1988) Mol Cell Biol , vol.8 , pp. 5059-5071
    • Arrigo, A.P.1    Suhan, J.P.2    Welch, W.J.3
  • 36
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-induced apoptosis
    • McMillan DR, Xiao X, Shao L, Graves K, Benjamin IB. Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-induced apoptosis. J Biol Chem. 1998;273: 7523-7528.
    • (1998) J Biol Chem , vol.273 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.2    Shao, L.3    Graves, K.4    Benjamin, I.B.5
  • 37
    • 0024456475 scopus 로고
    • The role of mRNA and protein stability in gene expression
    • Hargrove JL, Schmidt FH. The role of mRNA and protein stability in gene expression. FASEB J. 1989;3:2360-2370.
    • (1989) FASEB J , vol.3 , pp. 2360-2370
    • Hargrove, J.L.1    Schmidt, F.H.2
  • 38
    • 0026011111 scopus 로고
    • Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae
    • Yost HJ, Lindquist S. Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae. Mol Cell Biol. 1991;11:1062-1068.
    • (1991) Mol Cell Biol , vol.11 , pp. 1062-1068
    • Yost, H.J.1    Lindquist, S.2
  • 39
    • 0028231927 scopus 로고
    • Preferential deadenylation of Hsp70 mRNA plays a key role in regulating Hsp70 expression in Drosophila melanogaster
    • Dellavalle RP, Petersen R, Lindquist S. Preferential deadenylation of Hsp70 mRNA plays a key role in regulating Hsp70 expression in Drosophila melanogaster. Mol Cell Biol. 1994;14:3646-3659.
    • (1994) Mol Cell Biol , vol.14 , pp. 3646-3659
    • Dellavalle, R.P.1    Petersen, R.2    Lindquist, S.3
  • 40
    • 0023746618 scopus 로고
    • Heat-shock response is associated with enhanced postischemic ventricular recovery
    • Currie RW, Karmazyn M, Kloc M, Mailer K. Heat-shock response is associated with enhanced postischemic ventricular recovery. Circ Res. 1988;63:543-549.
    • (1988) Circ Res. , vol.63 , pp. 543-549
    • Currie, R.W.1    Karmazyn, M.2    Kloc, M.3    Mailer, K.4
  • 41
    • 0027163384 scopus 로고
    • Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction
    • Marber MS, Latchman DS, Walker JM, Yellon DM. Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction. Circulation. 1993;88: 1264-1272.
    • (1993) Circulation , vol.88 , pp. 1264-1272
    • Marber, M.S.1    Latchman, D.S.2    Walker, J.M.3    Yellon, D.M.4
  • 42
    • 0001824746 scopus 로고
    • Progress and perspectives on the biology of heat shock proteins and molecular chaperones
    • Morimoto RI, Tissieres A, Georgopoulos C, eds. Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Morimoto RI, Tissieres A, Georgopoulos C. Progress and perspectives on the biology of heat shock proteins and molecular chaperones. In: Morimoto RI, Tissieres A, Georgopoulos C, eds. The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor, NY: Cold Spring Harbor Press: 1994.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones
    • Morimoto, R.I.1    Tissieres, A.2    Georgopoulos, C.3
  • 43
    • 0027522356 scopus 로고
    • Cells in stress: Transcriptional activation of heat shock genes
    • Morimoto RI. Cells in stress: transcriptional activation of heat shock genes. Science. 1993;259:1409-1410.
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 44
    • 0029564954 scopus 로고
    • Heat shock transcription factors: Structure and regulation
    • Wu C. Heat shock transcription factors: structure and regulation. Ann Rev Cell Dev Biol. 1995;11:441-469.
    • (1995) Ann Rev Cell Dev Biol , vol.11 , pp. 441-469
    • Wu, C.1
  • 45
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger PK, Pelham HR. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell. 1988;54:855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.2
  • 46
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • Jedlicka P, Mortin MA, Wu C. Multiple functions of Drosophila heat shock transcription factor in vivo. EMBO J. 1997;16:2452-2462.
    • (1997) EMBO J. , vol.16 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 47
    • 0029121347 scopus 로고
    • The DNA-binding properties of two heat shock factors, HSF1 and HSF3, are induced in the avian erythroblast cell line HD6
    • Nakai A, Kawazoe Y, Tanabe M, Nagata K, Morimoto RI. The DNA-binding properties of two heat shock factors, HSF1 and HSF3, are induced in the avian erythroblast cell line HD6. Mol Cell Biol. 1995; 15:5268-5278.
    • (1995) Mol Cell Biol , vol.15 , pp. 5268-5278
    • Nakai, A.1    Kawazoe, Y.2    Tanabe, M.3    Nagata, K.4    Morimoto, R.I.5
  • 48
    • 0025686194 scopus 로고
    • Three tomato genes code for heat stress transcription factors with a region of remarkable homology to the DNA-binding domain of the yeast HSF
    • published erratum appears in EMBO J. 1991;10:1026
    • Scharf KD, Rose S, Zott W, Schoffl F, Nover L, Schoff F. Three tomato genes code for heat stress transcription factors with a region of remarkable homology to the DNA-binding domain of the yeast HSF [published erratum appears in EMBO J. 1991;10:1026]. EMBOJ. 1990; 9:4495-4501.
    • (1990) EMBOJ , vol.9 , pp. 4495-4501
    • Scharf, K.D.1    Rose, S.2    Zott, W.3    Schoffl, F.4    Nover, L.5    Schoff, F.6
  • 49
    • 0025989349 scopus 로고
    • Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability
    • Sarge KD, Zimarino V, Holm K, Wu C, Morimoto RI. Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability. Genes Dev. 1991;5:1902-1911.
    • (1991) Genes Dev. , vol.5 , pp. 1902-1911
    • Sarge, K.D.1    Zimarino, V.2    Holm, K.3    Wu, C.4    Morimoto, R.I.5
  • 52
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor 1 activity at control temperature by phosphorylation
    • Knauf U, Newton EM, Kyriakis J, Kingston RE. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 1996;10:2782-2793.
    • (1996) Genes Dev. , vol.10 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 53
    • 0030882907 scopus 로고    scopus 로고
    • Analysis of the phosphorylation of human heat shock transcription factor-1 by MAP kinase family members
    • Kim J, Nueda A, Meng YH, Dynan WS, Mivechi NF. Analysis of the phosphorylation of human heat shock transcription factor-1 by MAP kinase family members. J Cell Biochem. 1997;67:43-54.
    • (1997) J Cell Biochem. , vol.67 , pp. 43-54
    • Kim, J.1    Nueda, A.2    Meng, Y.H.3    Dynan, W.S.4    Mivechi, N.F.5
  • 54
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya K, Myers MP, Murphy SP, Morimoto RI. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. 1992;6:1153-1164.
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 55
    • 0028025643 scopus 로고
    • Interaction between heat shock factor 70 and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo
    • Rabindran S, Wisniewski J, Li L, Li G, Wu C. Interaction between heat shock factor 70 and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo. Mol Cell Biol. 1994;14:6552-6560.
    • (1994) Mol Cell Biol. , vol.14 , pp. 6552-6560
    • Rabindran, S.1    Wisniewski, J.2    Li, L.3    Li, G.4    Wu, C.5
  • 56
    • 0027220589 scopus 로고
    • Protein traffic on the heat shock promoter: Parking, stalling, and trucking along
    • Lis J, Wu C. Protein traffic on the heat shock promoter: parking, stalling, and trucking along. Cell. 1993;74:1-4.
    • (1993) Cell , vol.74 , pp. 1-4
    • Lis, J.1    Wu, C.2
  • 57
    • 0024999067 scopus 로고
    • Activation of the heat shock transcription factor by hypoxia in mammalian cells
    • Benjamin IJ, Kroger B, Williams RS. Activation of the heat shock transcription factor by hypoxia in mammalian cells. Proc Natl Acad Sci USA. 1990;87:6263-6267.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6263-6267
    • Benjamin, I.J.1    Kroger, B.2    Williams, R.S.3
  • 58
    • 0026653034 scopus 로고
    • Induction of stress proteins in cultured myogenic cells: Molecular signals for the activation of heat shock transcription factor during ischemia
    • Benjamin IJ, Horie S, Greenberg ML, Alpem RJ, Williams RS. Induction of stress proteins in cultured myogenic cells: molecular signals for the activation of heat shock transcription factor during ischemia. J Clin Invest. 1992;89:1685-1689.
    • (1992) J Clin Invest. , vol.89 , pp. 1685-1689
    • Benjamin, I.J.1    Horie, S.2    Greenberg, M.L.3    Alpem, R.J.4    Williams, R.S.5
  • 59
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan J, Goldberg AL, Voellmy R. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science. 1986;232:522-524.
    • (1986) Science , vol.232 , pp. 522-524
    • Ananthan, J.1    Goldberg, A.L.2    Voellmy, R.3
  • 61
    • 0030961030 scopus 로고    scopus 로고
    • Nitric oxide induces heat-shock protein 70 expression in vascular smooth muscle cells via activation of heat shock factor 1
    • Xu Q, Hu Y, Kleindienst R, Wick G. Nitric oxide induces heat-shock protein 70 expression in vascular smooth muscle cells via activation of heat shock factor 1. J Clin Invest. 1997;100:1089-1097.
    • (1997) J Clin Invest. , vol.100 , pp. 1089-1097
    • Xu, Q.1    Hu, Y.2    Kleindienst, R.3    Wick, G.4
  • 62
    • 0023863121 scopus 로고
    • Germline transformation used to define key features of heat-shock response elements
    • Xiao H, Lis JT. Germline transformation used to define key features of heat-shock response elements. Science. 1988;239:1139-1142.
    • (1988) Science , vol.239 , pp. 1139-1142
    • Xiao, H.1    Lis, J.T.2
  • 63
    • 0023694311 scopus 로고
    • Key features of heat shock regulatory elements
    • Amin J, Ananthan J, Voellmy R. Key features of heat shock regulatory elements. Mol Cell Biol. 1988;8:3761-3769.
    • (1988) Mol Cell Biol. , vol.8 , pp. 3761-3769
    • Amin, J.1    Ananthan, J.2    Voellmy, R.3
  • 65
    • 0023687765 scopus 로고
    • Ischemia induces changes in the level of mRNAs coding for stress protein 71 and creatine kinase M
    • Mehta HB, Popovich BK, Dillmann WH. Ischemia induces changes in the level of mRNAs coding for stress protein 71 and creatine kinase M. Circ Res. 1988;63:512-517.
    • (1988) Circ Res. , vol.63 , pp. 512-517
    • Mehta, H.B.1    Popovich, B.K.2    Dillmann, W.H.3
  • 66
    • 0026090476 scopus 로고
    • Rapid expression of heat shock protein in the rabbit after brief cardiac ischemia
    • Knowlton AA, Brecher P, Apstein CS. Rapid expression of heat shock protein in the rabbit after brief cardiac ischemia. J Clin Invest. 1991; 87:139-147.
    • (1991) J Clin Invest. , vol.87 , pp. 139-147
    • Knowlton, A.A.1    Brecher, P.2    Apstein, C.S.3
  • 68
    • 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 FL, Welch WJ, Wolfe CL. Heat shock protein induction in rat hearts: a role for improved myocardial salvage after ischemia and reperfusion? Circulation. 1992;85:769-778.
    • (1992) Circulation , vol.85 , pp. 769-778
    • Donnelly, T.J.1    Sievers, R.E.2    Vissern, F.L.3    Welch, W.J.4    Wolfe, C.L.5
  • 69
    • 0027463072 scopus 로고
    • Heat-shock response and limitation of tissue necrosis during occlusion/reperfusion in rabbit hearts
    • Currie RW, Tanguay RM, Kingma JG Jr. Heat-shock response and limitation of tissue necrosis during occlusion/reperfusion in rabbit hearts [see comments]. Circulation. 1993;87:963-971.
    • (1993) Circulation , vol.87 , pp. 963-971
    • Currie, R.W.1    Tanguay, R.M.2    Kingma J.G., Jr.3
  • 70
    • 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 CL. 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. 1994;89:355-360.
    • (1994) Circulation , vol.89 , pp. 355-360
    • Hutter, M.M.1    Sievers, R.E.2    Barbosa, V.3    Wolfe, C.L.4
  • 71
    • 0027203476 scopus 로고
    • Human heat shock protein 70 (hsp70) protects murine cells from injury during metabolic stress
    • Williams RS, Thomas JA, Fina M, German Z, Benjamin IJ. Human heat shock protein 70 (hsp70) protects murine cells from injury during metabolic stress. J Clin Invest. 1993;92:503-508.
    • (1993) J Clin Invest. , vol.92 , pp. 503-508
    • Williams, R.S.1    Thomas, J.A.2    Fina, M.3    German, Z.4    Benjamin, I.J.5
  • 72
    • 0028293462 scopus 로고
    • Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury
    • Mestril R, Chi SH, Sayen MR, O'Reilly K, Dillmann WH. Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury. J Clin Invest. 1994; 93:759-767.
    • (1994) J Clin Invest. , vol.93 , pp. 759-767
    • Mestril, R.1    Chi, S.H.2    Sayen, M.R.3    O'Reilly, K.4    Dillmann, W.H.5
  • 73
    • 0029794271 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo
    • Hutter JJ, Mestril R, Tam EK, Sievers RE, Dillmann WH, Wolfe CL. Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo. Circulation. 1996;94:1408-1411.
    • (1996) Circulation , vol.94 , pp. 1408-1411
    • Hutter, J.J.1    Mestril, R.2    Tam, E.K.3    Sievers, R.E.4    Dillmann, W.H.5    Wolfe, C.L.6
  • 74
    • 0031469110 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against ischemic injury in cardiac myocytes
    • Martin JL, Mestril R, Hilal-Dandan R, Brunton LL, Dillmann WH. Small heat shock proteins and protection against ischemic injury in cardiac myocytes. Circulation. 1997;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    Dillmann, W.H.5
  • 75
    • 0002664005 scopus 로고
    • Interactions of vertebrate hsc70 and hsp70 with unfolded proteins and peptides
    • Morimoto RI, Tissieres A, Georgopoulos C, eds. Cold Spring Harbor, NY: Cold Spring Harbor Press
    • Hightower LE, Sadis SE, Takenaka IM. Interactions of vertebrate hsc70 and hsp70 with unfolded proteins and peptides. In: Morimoto RI, Tissieres A, Georgopoulos C, eds. The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor, NY: Cold Spring Harbor Press; 1994.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones
    • Hightower, L.E.1    Sadis, S.E.2    Takenaka, I.M.3
  • 76
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis J. Proteins as molecular chaperones. Nature. 1987;328:378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 77
    • 0029051966 scopus 로고
    • Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
    • Freeman BC, Myers MP, Schumacher R, Morimoto RI. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 1995;14:2281-2292.
    • (1995) EMBO J. , vol.14 , pp. 2281-2292
    • Freeman, B.C.1    Myers, M.P.2    Schumacher, R.3    Morimoto, R.I.4
  • 78
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang HL, Terlecky SR, Plant CP, Dice JF. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science. 1989;246:382-385.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 79
    • 0026652914 scopus 로고
    • Timing of coronary recanalization: Paradigms, paradoxes, and pertinence
    • Tiefenbrunn AJ, Sobel BE. Timing of coronary recanalization: paradigms, paradoxes, and pertinence. Circulation. 1992;85:2311-2315.
    • (1992) Circulation , vol.85 , pp. 2311-2315
    • Tiefenbrunn, A.J.1    Sobel, B.E.2
  • 83
    • 0017694599 scopus 로고
    • Reperfusion of the ischemic myocardium
    • Hearse DJ. Reperfusion of the ischemic myocardium. J Mol Cell Cardiol. 1977;9:605-616.
    • (1977) J Mol Cell Cardiol , vol.9 , pp. 605-616
    • Hearse, D.J.1
  • 84
    • 0029039854 scopus 로고
    • Simultaneous overexpression of copper- And zinc-containing superoxide dismutase and catalase retards age-related oxidative damage and increases metabolic potential in Drosophila melanogaster
    • Sohal RS, Agarwal A, Agarwal S, Orr WC. Simultaneous overexpression of copper- and zinc-containing superoxide dismutase and catalase retards age-related oxidative damage and increases metabolic potential in Drosophila melanogaster. J Biol Chem. 1995;270: 15671-15674.
    • (1995) J Biol Chem , vol.270 , pp. 15671-15674
    • Sohal, R.S.1    Agarwal, A.2    Agarwal, S.3    Orr, W.C.4
  • 86
    • 0030934087 scopus 로고    scopus 로고
    • DNA fragmentation and prolonged expression of c-fos, c-jun, and hsp70 in kainic acid-induced neuronal cell death in transgenic mice overexpressing human CuZn-superoxide dismutase
    • Kondo T, Sharp FR, Honkaniemi J, Mikawa S, Epstein CJ, Chan PH. DNA fragmentation and prolonged expression of c-fos, c-jun, and hsp70 in kainic acid-induced neuronal cell death in transgenic mice overexpressing human CuZn-superoxide dismutase. J Cereb Blood Flow Metab. 1997;17:241-256.
    • (1997) J Cereb Blood Flow Metab , vol.17 , pp. 241-256
    • Kondo, T.1    Sharp, F.R.2    Honkaniemi, J.3    Mikawa, S.4    Epstein, C.J.5    Chan, P.H.6
  • 87
    • 0020414455 scopus 로고
    • The stunned myocardium: Prolonged, post-ischemic ventricular dysfunction
    • Braunwald E, Kloner RA. The stunned myocardium: prolonged, post-ischemic ventricular dysfunction. Circulation. 1982;66:1146-1149.
    • (1982) Circulation , vol.66 , pp. 1146-1149
    • Braunwald, E.1    Kloner, R.A.2
  • 88
    • 0025760521 scopus 로고
    • Oxygen-derived free radicals and myocardial reperfusion injury: An overview
    • Bolli R. Oxygen-derived free radicals and myocardial reperfusion injury: an overview. Cardiovasc Drugs Ther. 1991;2:249-268.
    • (1991) Cardiovasc Drugs Ther , vol.2 , pp. 249-268
    • Bolli, R.1
  • 89
    • 0026541776 scopus 로고
    • Myocardial "stunning" in man
    • Bolli R. Myocardial "stunning" in man. Circulation. 1992;86: 1671-1691.
    • (1992) Circulation , vol.86 , pp. 1671-1691
    • Bolli, R.1
  • 90
    • 0026092493 scopus 로고
    • Myocardial stunning and hibernation: The physiology behind the colloquialisms
    • Marban E. Myocardial stunning and hibernation: the physiology behind the colloquialisms. Circulation. 1991;83:681-688.
    • (1991) Circulation , vol.83 , pp. 681-688
    • Marban, E.1
  • 91
    • 0027254168 scopus 로고
    • Superoxide dismutase plus catalase therapy delays neither cell death nor the loss of the TTC reaction in experimental myocardial infarction in dogs
    • Tanaka M, Richard VJ, Murry CE, Jennings RB, Reimer KA. Superoxide dismutase plus catalase therapy delays neither cell death nor the loss of the TTC reaction in experimental myocardial infarction in dogs. J Mol Cell Cardiol. 1993;25:367-378.
    • (1993) J Mol Cell Cardiol , vol.25 , pp. 367-378
    • Tanaka, M.1    Richard, V.J.2    Murry, C.E.3    Jennings, R.B.4    Reimer, K.A.5
  • 92
    • 0028196994 scopus 로고
    • Myocardial reperfusion injury: Role of oxygen radicals and potential therapy with antioxidants
    • Jeroudi MO, Hartley CJ, Bolli R. Myocardial reperfusion injury: role of oxygen radicals and potential therapy with antioxidants. Am J Cardiol. 1994;73:2B-7B.
    • (1994) Am J Cardiol , vol.73
    • Jeroudi, M.O.1    Hartley, C.J.2    Bolli, R.3
  • 93
    • 0002801207 scopus 로고
    • Free radicals in autoxidation and in aging
    • Armstrong D, Sohal RS, Cutler RG, Slater TF, eds. New York, NY: Raven Press Publishers
    • Pryor WA. Free radicals in autoxidation and in aging. In: Armstrong D, Sohal RS, Cutler RG, Slater TF, eds. Free Radicals in Molecular Biology, Aging, and Disease. New York, NY: Raven Press Publishers; 1984:13-41.
    • (1984) Free Radicals in Molecular Biology, Aging, and Disease , pp. 13-41
    • Pryor, W.A.1
  • 94
    • 0025145831 scopus 로고
    • Acquisition and decay of heat-shock-enhanced postischemic ventricular recovery
    • Karmazyn M, Mailer K, Currie RW. Acquisition and decay of heat-shock-enhanced postischemic ventricular recovery. Am J Physiol. 1990; 259:H424-H431.
    • (1990) Am J Physiol. , vol.259
    • Karmazyn, M.1    Mailer, K.2    Currie, R.W.3
  • 97
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann R, Mizzen L, Welch W. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science. 1990;248:850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.1    Mizzen, L.2    Welch, W.3
  • 98
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn G, Pohl J, Flocco M, Rothman J. Peptide-binding specificity of the molecular chaperone BiP. Nature. 1991;353:726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.1    Pohl, J.2    Flocco, M.3    Rothman, J.4
  • 100
    • 0025753142 scopus 로고
    • Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein
    • Flaherty KM, McKay DB, Kabsch W, Holmes KC. Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc Natl Acad Sci U S A. 1991; 88:5041-5045.
    • (1991) Proc Natl Acad Sci U S A. , vol.88 , pp. 5041-5045
    • Flaherty, K.M.1    McKay, D.B.2    Kabsch, W.3    Holmes, K.C.4
  • 101
    • 0026645957 scopus 로고
    • The consequences of expressing hsp70 in Drosophila cells at normal temperatures
    • Feder JH, Rossi JM, Solomon J, Solomon N, Lindquist S. The consequences of expressing hsp70 in Drosophila cells at normal temperatures. Genes Dev. 1992;6:1402-1413.
    • (1992) Genes Dev , vol.6 , pp. 1402-1413
    • Feder, J.H.1    Rossi, J.M.2    Solomon, J.3    Solomon, N.4    Lindquist, S.5
  • 102
    • 0031016469 scopus 로고    scopus 로고
    • Functional specificity among Hsp70 molecular chaperones
    • James P, Pfund C, Craig EA. Functional specificity among Hsp70 molecular chaperones. Science. 1997;275:387-389.
    • (1997) Science , vol.275 , pp. 387-389
    • James, P.1    Pfund, C.2    Craig, E.A.3
  • 103
    • 0021708673 scopus 로고
    • Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies
    • Lai B, Chin N, Stanek A, Keh W, Lanks K. Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies. Mol Cell Biol. 1984;4:2802-2810.
    • (1984) Mol Cell Biol , vol.4 , pp. 2802-2810
    • Lai, B.1    Chin, N.2    Stanek, A.3    Keh, W.4    Lanks, K.5
  • 104
    • 0024970241 scopus 로고
    • The Mr approximately 90,000 heat shock protein: An important modulator of ligand and DNA-binding properties of the glucocorticoid receptor
    • Denis M, Gustafsson J. The Mr approximately 90,000 heat shock protein: an important modulator of ligand and DNA-binding properties of the glucocorticoid receptor. Cancer Res. 1989;49:2275s-2281s.
    • (1989) Cancer Res , vol.49
    • Denis, M.1    Gustafsson, J.2
  • 105
    • 0030039916 scopus 로고    scopus 로고
    • The 90 kDA heat-shock protein (hsp90) modulates the binding of the oestrogen receptor to its cognate DNA
    • Sabbah M, Radanyi C, Redeuilh G, Balieu E. The 90 kDA heat-shock protein (hsp90) modulates the binding of the oestrogen receptor to its cognate DNA. Biochem J. 1996;314:205-213.
    • (1996) Biochem J , vol.314 , pp. 205-213
    • Sabbah, M.1    Radanyi, C.2    Redeuilh, G.3    Balieu, E.4
  • 106
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt W. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J Biol Chem. 1993;268:21455-21458.
    • (1993) J Biol Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.1
  • 107
    • 0024421221 scopus 로고
    • hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich KA, Farrelly FW, Finkelstein DB, Taulien J, Lindquist S. hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol. 1989;9: 3919-3930.
    • (1989) Mol Cell Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 108
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • Cruse I, Maines MD. Evidence suggesting that the two forms of heme oxygenase are products of different genes. J Biol Chem. 1988;263: 3348-3353.
    • (1988) J Biol Chem , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 109
    • 0026012324 scopus 로고
    • Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: Heme oxygenase 2 is not a heat shock protein
    • Ewing JF, Maines MD. Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: heme oxygenase 2 is not a heat shock protein. Proc Natl Acad Sci U S A. 1991;88:5364-5368.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5364-5368
    • Ewing, J.F.1    Maines, M.D.2
  • 110
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey WK Jr, Huang TJ, Maines MD. Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur J Biochem. 1997;247:725-732.
    • (1997) Eur J Biochem , vol.247 , pp. 725-732
    • McCoubrey W.K., Jr.1    Huang, T.J.2    Maines, M.D.3
  • 111
    • 0023154641 scopus 로고
    • Identification of heme oxygenase and cytochrome P-450 in the rabbit heart
    • Abraham NG, Pinto A, Levere RD, Mullane K. Identification of heme oxygenase and cytochrome P-450 in the rabbit heart. J Mol Cell Cardiol. 1987;19:73-81.
    • (1987) J Mol Cell Cardiol , vol.19 , pp. 73-81
    • Abraham, N.G.1    Pinto, A.2    Levere, R.D.3    Mullane, K.4
  • 112
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines MD. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J. 1988;2:2557-2568.
    • (1988) FASEB J , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 113
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler JS, Singel DJ, Loscalzo J. Biochemistry of nitric oxide and its redox-activated forms. Science. 1992;258:1898-1902.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 114
    • 0028945134 scopus 로고
    • Vascular smooth muscle cell heme oxygenases generate guanylyl cyclase-stimulatory carbon monoxide
    • Christodoulides N, Durante W, Kroll MH, Schafer AI. Vascular smooth muscle cell heme oxygenases generate guanylyl cyclase-stimulatory carbon monoxide. Circulation. 1995;91:2306-2309.
    • (1995) Circulation , vol.91 , pp. 2306-2309
    • Christodoulides, N.1    Durante, W.2    Kroll, M.H.3    Schafer, A.I.4
  • 115
    • 0030856625 scopus 로고    scopus 로고
    • Hemodynamic forces induce the expression of heme oxygenase in cultured vascular smooth muscle cells
    • Wagner CT, Durante W, Christodoulides N, Heliums JD, Schafer AI. Hemodynamic forces induce the expression of heme oxygenase in cultured vascular smooth muscle cells. J Clin Invest. 1997;100:589-596.
    • (1997) J Clin Invest , vol.100 , pp. 589-596
    • Wagner, C.T.1    Durante, W.2    Christodoulides, N.3    Heliums, J.D.4    Schafer, A.I.5
  • 116
    • 0030961521 scopus 로고    scopus 로고
    • Nitric oxide induces heme oxygenase-1 gene expression and carbon monoxide production in vascular smooth muscle cells
    • Durante W, Kroll MH, Christodoulides N, Peyton KJ, Schafer AI. Nitric oxide induces heme oxygenase-1 gene expression and carbon monoxide production in vascular smooth muscle cells. Circ Res. 1997;80:557-564.
    • (1997) Circ Res , vol.80 , pp. 557-564
    • Durante, W.1    Kroll, M.H.2    Christodoulides, N.3    Peyton, K.J.4    Schafer, A.I.5
  • 117
    • 0031026658 scopus 로고    scopus 로고
    • Heme oxygenase-1 is regulated by angio-tensin II in rat vascular smooth muscle cells
    • Ishizaka N, Griendling KK. Heme oxygenase-1 is regulated by angio-tensin II in rat vascular smooth muscle cells. Hypertension. 1997;29: 790-795.
    • (1997) Hypertension , vol.29 , pp. 790-795
    • Ishizaka, N.1    Griendling, K.K.2
  • 119
    • 0023665016 scopus 로고
    • Transcriptional control of rat heme oxygenase by heat shock
    • Shibahara S, Muller RM, Taguchi H. Transcriptional control of rat heme oxygenase by heat shock. J Biol Chem. 1987;262:12889-12892.
    • (1987) J Biol Chem , vol.262 , pp. 12889-12892
    • Shibahara, S.1    Muller, R.M.2    Taguchi, H.3
  • 120
    • 0023654799 scopus 로고
    • Nucleotide sequence and organization of the rat heme oxygenase gene
    • Muller RM, Taguchi H, Shibahara S. Nucleotide sequence and organization of the rat heme oxygenase gene. J Biol Chem. 1987;262: 6795-6802.
    • (1987) J Biol Chem. , vol.262 , pp. 6795-6802
    • Muller, R.M.1    Taguchi, H.2    Shibahara, S.3
  • 121
    • 0031041377 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia
    • Lee PJ, Jiang BH, Chin BY, Iyer NV, Alam J, Semenza GL, Choi AM. Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia. J Biol Chem. 1997;272: 5375-5381.
    • (1997) J Biol Chem , vol.272 , pp. 5375-5381
    • Lee, P.J.1    Jiang, B.H.2    Chin, B.Y.3    Iyer, N.V.4    Alam, J.5    Semenza, G.L.6    Choi, A.M.7
  • 122
    • 0030963616 scopus 로고    scopus 로고
    • The hypoxic response: Huffing and HIFing
    • Guillemin K, Krasnow MA. The hypoxic response: huffing and HIFing. Cell. 1997;89:9-12.
    • (1997) Cell , vol.89 , pp. 9-12
    • Guillemin, K.1    Krasnow, M.A.2
  • 123
    • 0029814162 scopus 로고    scopus 로고
    • Overexpression of heme oxygenase-1 in human pulmonary epithelial cells results in cell growth arrest and increased resistance to hyperoxia
    • Lee PJ, Alam J, Wiegand GW, Choi AM. Overexpression of heme oxygenase-1 in human pulmonary epithelial cells results in cell growth arrest and increased resistance to hyperoxia. Proc Natl Acad Sci U S A. 1996;93:10393-10398.
    • (1996) Proc Natl Acad Sci U S A. , vol.93 , pp. 10393-10398
    • Lee, P.J.1    Alam, J.2    Wiegand, G.W.3    Choi, A.M.4
  • 124
    • 0030065052 scopus 로고    scopus 로고
    • NO-mediated activation of heme oxygenase: Endogenous cytoprotection against oxidative stress to endothelium
    • Motterlini R, Foresti R, Intaglietta M, Winslow RM. NO-mediated activation of heme oxygenase: endogenous cytoprotection against oxidative stress to endothelium. Am J Physiol. 1996;270:H107-H114.
    • (1996) Am J Physiol. , vol.270
    • Motterlini, R.1    Foresti, R.2    Intaglietta, M.3    Winslow, R.M.4
  • 125
    • 0030788030 scopus 로고    scopus 로고
    • The stress response and the lung
    • Wong HR, Wispe JR. The stress response and the lung. Am J Physiol. 1997;273:L1-L9.
    • (1997) Am J Physiol , vol.273
    • Wong, H.R.1    Wispe, J.R.2
  • 126
    • 0025813543 scopus 로고
    • A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein
    • Miron T, Vancompernolle K, Vandekerckhove J, Wilchek M, Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J Cell Biol. 1991;114:255-261.
    • (1991) J Cell Biol , vol.114 , pp. 255-261
    • Miron, T.1    Vancompernolle, K.2    Vandekerckhove, J.3    Wilchek, M.4    Geiger, B.5
  • 128
    • 0026570931 scopus 로고
    • Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II
    • Landry J, Lambert H, Zhou M, Lavoie JN, Mickey E, Weber LA, Anderson CW. Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II. J Biol Chem. 1992;267:794-803.
    • (1992) J Biol Chem , vol.267 , pp. 794-803
    • Landry, J.1    Lambert, H.2    Zhou, M.3    Lavoie, J.N.4    Mickey, E.5    Weber, L.A.6    Anderson, C.W.7
  • 129
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot J, Houle F, Spitz DR, Landry J. HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res. 1996;56:273-279.
    • (1996) Cancer Res , vol.56 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3    Landry, J.4
  • 130
    • 0029744885 scopus 로고    scopus 로고
    • Sounding the alarm: Protein kinase cascades activated by stress and inflammation
    • Kyriakis JM, Avruch J. Sounding the alarm: protein kinase cascades activated by stress and inflammation. J Biol Chem. 1996;271: 24313-24316.
    • (1996) J Biol Chem , vol.271 , pp. 24313-24316
    • Kyriakis, J.M.1    Avruch, J.2
  • 131
    • 0030036727 scopus 로고    scopus 로고
    • Stimulation of the stress-activated mitogen-activated protein kinase subfamilies in perfused heart: P38/RK mitogen-activated protein kinases and c-Jun N-terminal kinases are activated by ischemia/reperfusion
    • Bogoyevitch MA, Gillespie-Brown J, Ketterman AJ, Fuller SJ, Ben-Levy R, Ashworth A, Marshall CJ, Sugden PH. Stimulation of the stress-activated mitogen-activated protein kinase subfamilies in perfused heart: p38/RK mitogen-activated protein kinases and c-Jun N-terminal kinases are activated by ischemia/reperfusion. Circ Res. 1996;79:162-173.
    • (1996) Circ Res , vol.79 , pp. 162-173
    • Bogoyevitch, M.A.1    Gillespie-Brown, J.2    Ketterman, A.J.3    Fuller, S.J.4    Ben-Levy, R.5    Ashworth, A.6    Marshall, C.J.7    Sugden, P.H.8
  • 132
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of heat shock proteins
    • Rouse J, Cohen P, Trigon S, Morange M. Alonso-Llamarazes A, Zamanillo D, Hunt T, Nebreda AR. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of heat shock proteins. Cell. 1994;78:1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamarazes, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 133
    • 0030734010 scopus 로고    scopus 로고
    • p38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells
    • Rousseau S, Houle F, Landry J, Huot J. p38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells. Oncogene. 1997;15:2169-2177.
    • (1997) Oncogene , vol.15 , pp. 2169-2177
    • Rousseau, S.1    Houle, F.2    Landry, J.3    Huot, J.4
  • 134
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J, Houle F, Marceau F, Landry J. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. Circ Res. 1997;80:383-392.
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 136
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc Natl Acad Sci U S A. 1982;79:2360-2364.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 138
    • 0027472047 scopus 로고
    • Evolution of the alpha-crystaUin/small heat-shock protein family
    • de long WW, Leunissen JA, Voorter CE. Evolution of the alpha-crystaUin/small heat-shock protein family. Mol Biol Evol. 1993;10:103-126.
    • (1993) Mol Biol Evol , vol.10 , pp. 103-126
    • De Long, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 139
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem. 1993;268:1517-1520.
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 140
    • 0025877859 scopus 로고
    • Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system
    • Kato K, Shinohara H, Kurobe N, Inaguma Y, Shimizu K, Ohshima K. Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system. Biochim Biophys Acta. 1991;1074:201-208.
    • (1991) Biochim Biophys Acta , vol.1074 , pp. 201-208
    • Kato, K.1    Shinohara, H.2    Kurobe, N.3    Inaguma, Y.4    Shimizu, K.5    Ohshima, K.6
  • 141
    • 0027982174 scopus 로고
    • Alpha-B crystallin in the normal human myocardium and cardiac conducting system
    • Leach IH, Tsang ML, Church RJ, Lowe J. Alpha-B crystallin in the normal human myocardium and cardiac conducting system. J Pathol. 1994;173:255-260.
    • (1994) J Pathol , vol.173 , pp. 255-260
    • Leach, I.H.1    Tsang, M.L.2    Church, R.J.3    Lowe, J.4
  • 142
    • 0026694490 scopus 로고
    • αB-Crystallin in cardiac tissue: Association with actin and desmin filaments
    • Bennardini F, Wrzosek A, Chiesi M. αB-Crystallin in cardiac tissue: association with actin and desmin filaments. Circ Res. 1992;71:288-294.
    • (1992) Circ Res , vol.71 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 144
    • 0025699482 scopus 로고
    • Cardiac alpha-crystallin, I: Isolation and identification
    • corrected and republished with original paging, article originally printed in Mol Cell Biochem. 1990;97:113-20
    • Longoni S, James P, Chiesi M. Cardiac alpha-crystallin, I: isolation and identification [corrected and republished with original paging, article originally printed in Mol Cell Biochem. 1990;97:113-20]. Mol Cell Biochem. 1990;99:113-120.
    • (1990) Mol Cell Biochem , vol.99 , pp. 113-120
    • Longoni, S.1    James, P.2    Chiesi, M.3
  • 145
    • 0029781314 scopus 로고    scopus 로고
    • Spatial and temporal activity of the alpha B-crystallin/small heat shock protein gene promoter in transgenic mice
    • Haynes JI II, Duncan MK, Piatigorsky J. Spatial and temporal activity of the alpha B-crystallin/small heat shock protein gene promoter in transgenic mice. Dev Dyn. 1996;207:75-88.
    • (1996) Dev Dyn , vol.207 , pp. 75-88
    • Haynes J.I. II1    Duncan, M.K.2    Piatigorsky, J.3
  • 146
    • 0027330980 scopus 로고
    • The murine alpha B-crystallin/small heat shock protein enhancer: Identification of alpha BE-1, alpha BE-2, alpha BE-3. and MRF control elements
    • Gopal-Srivastava R, Piatigorsky J. The murine alpha B-crystallin/small heat shock protein enhancer: identification of alpha BE-1, alpha BE-2, alpha BE-3. and MRF control elements. Mol Cell Biol. 1993;13: 7144-7152.
    • (1993) Mol Cell Biol , vol.13 , pp. 7144-7152
    • Gopal-Srivastava, R.1    Piatigorsky, J.2
  • 147
    • 0027327918 scopus 로고
    • Regulation of muscle transcription by the MyoD family: The heart of the matter
    • Olson EN. Regulation of muscle transcription by the MyoD family: the heart of the matter. Circ Res. 1993;72:1-6.
    • (1993) Circ Res , vol.72 , pp. 1-6
    • Olson, E.N.1
  • 148
    • 0029661431 scopus 로고    scopus 로고
    • Differential expression of alpha B-crystallin and hsp27 in skeletal muscle during continuous contractile activity: Relationship to myogenic regulatory factors
    • Neufer PD, Benjamin IJ. Differential expression of alpha B-crystallin and hsp27 in skeletal muscle during continuous contractile activity: relationship to myogenic regulatory factors. J Biol Chem. 1996;271: 24089-24095.
    • (1996) J Biol Chem , vol.271 , pp. 24089-24095
    • Neufer, P.D.1    Benjamin, I.J.2
  • 149
    • 0031454881 scopus 로고    scopus 로고
    • Hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells
    • Mehlen P, Mehlen A, Godet J. Arrigo AP. Hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells. J Biol Chem. 1997;272:31657-31665.
    • (1997) J Biol Chem , vol.272 , pp. 31657-31665
    • Mehlen, P.1    Mehlen, A.2    Godet, J.3    Arrigo, A.P.4
  • 150
    • 0031031926 scopus 로고    scopus 로고
    • Temporospatial expression of the small HSP/alpha B-crystallin in cardiac and skeletal muscle during mouse development
    • Benjamin IJ, Shelton J, Carry DJ, Richardson JA. Temporospatial expression of the small HSP/alpha B-crystallin in cardiac and skeletal muscle during mouse development. Dev Dyn. 1997;208:75-84.
    • (1997) Dev Dyn , vol.208 , pp. 75-84
    • Benjamin, I.J.1    Shelton, J.2    Carry, D.J.3    Richardson, J.A.4
  • 151
    • 0028972717 scopus 로고
    • Regulation of the murine aB-crystallin/small heat shock protein gene in cardiac muscle
    • Gopal-Srivastava R, Hapnes JI II, Piatigorsky J. Regulation of the murine aB-crystallin/small heat shock protein gene in cardiac muscle. Mol Cell Biol. 1995;15:7081-7090.
    • (1995) Mol Cell Biol , vol.15 , pp. 7081-7090
    • Gopal-Srivastava, R.1    Hapnes J.I. II2    Piatigorsky, J.3
  • 153
    • 0029549692 scopus 로고
    • A subclass of bHLH proteins required for cardiac morphogenesis
    • Srivastava D, Cserjesi P, Olson EN. A subclass of bHLH proteins required for cardiac morphogenesis. Science. 1995;270:1995-1999.
    • (1995) Science , vol.270 , pp. 1995-1999
    • Srivastava, D.1    Cserjesi, P.2    Olson, E.N.3
  • 154
    • 0028365670 scopus 로고
    • Purification and characterization of a 20-kDa protein that is highly homologous to alpha B-crystallin
    • Kato K, Goto S, Inaguma Y, Hasegawa K, Morishita K, Asano T. Purification and characterization of a 20-kDa protein that is highly homologous to alpha B-crystallin. J Biol Chem. 1994;269:15302-15309.
    • (1994) J Biol Chem , vol.269 , pp. 15302-15309
    • Kato, K.1    Goto, S.2    Inaguma, Y.3    Hasegawa, K.4    Morishita, K.5    Asano, T.6
  • 155
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain."
    • Caspars GJ, Leunissen JA, de Jong WW. The expanding small heat-shock protein family, and structure predictions of the conserved "alpha-crystallin domain." J Mol Evol. 1995;40:238-248.
    • (1995) J Mol Evol , vol.40 , pp. 238-248
    • Caspars, G.J.1    Leunissen, J.A.2    De Jong, W.W.3
  • 156
    • 0030966372 scopus 로고    scopus 로고
    • Cyclic nucleotide-dependent vasorelaxation is associated with the phosphorylation of a small heat shock-related protein
    • Beall AC, Kato K, Goldenring JR, Rasmussen H, Brophy CM. Cyclic nucleotide-dependent vasorelaxation is associated with the phosphorylation of a small heat shock-related protein. J Biol Chem. 1997;272:11283-11287.
    • (1997) J Biol Chem , vol.272 , pp. 11283-11287
    • Beall, A.C.1    Kato, K.2    Goldenring, J.R.3    Rasmussen, H.4    Brophy, C.M.5
  • 157
    • 0032498791 scopus 로고    scopus 로고
    • MKBP. A novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase
    • Suzuki A, Sugiyama Y, Hayashi Y. Nyu-i N, Yoshida M, Nonaka I, Ishiura S, Arahata K, Ohno S. MKBP. a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase. J Cell Biol. 1998;140:1113-1124.
    • (1998) J Cell Biol , vol.140 , pp. 1113-1124
    • Suzuki, A.1    Sugiyama, Y.2    Hayashi, Y.3    Nyu-i, N.4    Yoshida, M.5    Nonaka, I.6    Ishiura, S.7    Arahata, K.8    Ohno, S.9
  • 158
    • 0029079045 scopus 로고
    • Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein
    • Lee-Yoon D, Easton D, Murawski M, Burd R, Subjeck JR. Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein. J Biol Chem. 1995;270: 15725-15733.
    • (1995) J Biol Chem , vol.270 , pp. 15725-15733
    • Lee-Yoon, D.1    Easton, D.2    Murawski, M.3    Burd, R.4    Subjeck, J.R.5
  • 159
    • 0029564092 scopus 로고
    • Cloning and expression of murine high molecular mass heat shock proteins, HSP105
    • Yasuda K, Nakai A, Hatayama T,-Nagata K. Cloning and expression of murine high molecular mass heat shock proteins, HSP105. J Biol Chem. 1995;270:29718-29723.
    • (1995) J Biol Chem , vol.270 , pp. 29718-29723
    • Yasuda, K.1    Nakai, A.2    Hatayama, T.3    Nagata, K.4
  • 160
    • 0031017476 scopus 로고    scopus 로고
    • A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures
    • Kaneko Y, Nishiyama H, Nonoguchi K, Higashitsuji H, Kishishita M, Fujita J. A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures. J Biol Chem. 1997;272:2640-2645.
    • (1997) J Biol Chem , vol.272 , pp. 2640-2645
    • Kaneko, Y.1    Nishiyama, H.2    Nonoguchi, K.3    Higashitsuji, H.4    Kishishita, M.5    Fujita, J.6
  • 161
    • 17544366510 scopus 로고    scopus 로고
    • Osmotic stress protein 94 (Osp94): A new member of the Hsp110/SSE gene subfamily
    • Kojima R, Randall J, Brenner B, Gullans S. Osmotic stress protein 94 (Osp94): a new member of the Hsp110/SSE gene subfamily. J Biol Chem. 1996;271:12327-12332.
    • (1996) J Biol Chem , vol.271 , pp. 12327-12332
    • Kojima, R.1    Randall, J.2    Brenner, B.3    Gullans, S.4
  • 162
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, Kowal AS, Singer MA, Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature. 1994;372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 165
    • 0027077442 scopus 로고
    • Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
    • Frydman J, Nimmesgern E, Erdjument-Bromage H, Wall JS, Tempst P, Haiti FU. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 1992;11:4767-4778.
    • (1992) EMBO J , vol.11 , pp. 4767-4778
    • Frydman, J.1    Nimmesgern, E.2    Erdjument-Bromage, H.3    Wall, J.S.4    Tempst, P.5    Haiti, F.U.6
  • 166
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Hohfeld J, Minami Y, Hartl F. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell. 1995;83:589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Hohfeld, J.1    Minami, Y.2    Hartl, F.3
  • 167
    • 0029114263 scopus 로고
    • Mitochondrial biogenesis during pressure overload induced cardiac hypertrophy in adult rats
    • Nishio ML, Ornatsky OI, Craig EE, Hood DA. Mitochondrial biogenesis during pressure overload induced cardiac hypertrophy in adult rats. Can J Physiol Pharmacol. 1995;73:630-637.
    • (1995) Can J Physiol Pharmacol , vol.73 , pp. 630-637
    • Nishio, M.L.1    Ornatsky, O.I.2    Craig, E.E.3    Hood, D.A.4
  • 168
    • 0028342438 scopus 로고
    • Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse
    • Sohal RS, Ku H-H, Agarwal S, Forster MJ, Lal H. Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse. Mech Ageing Dev. 1994;74:121-133.
    • (1994) Mech Ageing Dev , vol.74 , pp. 121-133
    • Sohal, R.S.1    Ku, H.-H.2    Agarwal, S.3    Forster, M.J.4    Lal, H.5
  • 169
    • 0002003685 scopus 로고
    • Expression and function of stress proteins in the ischemic heart
    • Morimoto RI, Tissieres A, Georgopoulos S. eds. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Benjamin IJ, Williams RS. Expression and function of stress proteins in the ischemic heart. In: Morimoto RI, Tissieres A, Georgopoulos S. eds. The Biology of Heal Shock Proteins and Molecular Chaperones. 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press: 1994:533-552.
    • (1994) The Biology of Heal Shock Proteins and Molecular Chaperones. 2nd Ed. , pp. 533-552
    • Benjamin, I.J.1    Williams, R.S.2
  • 170
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner RD, Sitia R. Protein degradation in the endoplasmic reticulum. Cell. 1990;62:611-614.
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 171
    • 0030481624 scopus 로고    scopus 로고
    • Congenital hypothyroid goiter with deficient thyroglobulin: Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones
    • Medeiros-Neto G, Kim PS, Yoo SE, Vono J, Targovnik HM, Camargo R, Hossain SA, Arvan P. Congenital hypothyroid goiter with deficient thyroglobulin: identification of an endoplasmic reticulum storage disease with induction of molecular chaperones. J Clin Invest. 1996;98:2838-2844.
    • (1996) J Clin Invest , vol.98 , pp. 2838-2844
    • Medeiros-Neto, G.1    Kim, P.S.2    Yoo, S.E.3    Vono, J.4    Targovnik, H.M.5    Camargo, R.6    Hossain, S.A.7    Arvan, P.8
  • 172
    • 0027136174 scopus 로고
    • The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin
    • Lin HY, Masso-Welch P, Di YP, Cai JW, Shen JW, Subjeck JR. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol Biol Cell. 1993;4:1109-1119.
    • (1993) Mol Biol Cell , vol.4 , pp. 1109-1119
    • Lin, H.Y.1    Masso-Welch, P.2    Di, Y.P.3    Cai, J.W.4    Shen, J.W.5    Subjeck, J.R.6
  • 173
    • 0029741720 scopus 로고    scopus 로고
    • Regional distribution of HSP70 proteins after myocardial infraction
    • Kilgore JL, Musch TI, Ross CR. Regional distribution of HSP70 proteins after myocardial infraction. Basic Res Cardiol. 1996;91:283-288.
    • (1996) Basic Res Cardiol , vol.91 , pp. 283-288
    • Kilgore, J.L.1    Musch, T.I.2    Ross, C.R.3
  • 174
    • 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. Reperfusion causes significant activation of heat shock transcription factor 1 in ischemic rat heart. Circulation. 1996;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
  • 175
    • 0026772964 scopus 로고
    • Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
    • Nakai A, Satoh M, Hirayoshi K, Nagata K. Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum. J Cell Biol. 1992;117:903-914.
    • (1992) J Cell Biol , vol.117 , pp. 903-914
    • Nakai, A.1    Satoh, M.2    Hirayoshi, K.3    Nagata, K.4
  • 176
    • 0029968576 scopus 로고    scopus 로고
    • Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen
    • Satoh M, Hirayoshi K, Yokota S, Hosokawa N, Nagata K. Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen. J Cell Biol. 1996;133:469-483.
    • (1996) J Cell Biol , vol.133 , pp. 469-483
    • Satoh, M.1    Hirayoshi, K.2    Yokota, S.3    Hosokawa, N.4    Nagata, K.5
  • 177
    • 33646286416 scopus 로고    scopus 로고
    • Hsp47: A collagen-specific molecular chaperone
    • Nagata K. Hsp47: a collagen-specific molecular chaperone. Trends Biochem Sci. 1996;21:22-26.
    • (1996) Trends Biochem Sci , vol.21 , pp. 22-26
    • Nagata, K.1
  • 182
    • 0028816976 scopus 로고
    • Late preconditioning against myocardial stunning: An endogenous
    • Sun JZ, Tang XL, Knowlton AA, Park SW, Qiu Y, Bolli R. Late preconditioning against myocardial stunning: an endogenous protective mechanism that confers resistance to postischemic dysfunction 24 h after brief ischemia in conscious pigs. J Clin Invest. 1995;95:388-403.
    • (1995) J Clin Invest , vol.95 , pp. 388-403
    • Sun, J.Z.1    Tang, X.L.2    Knowlton, A.A.3    Park, S.W.4    Qiu, Y.5    Bolli, R.6
  • 183
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • Murry CE, Jennings RB, Reimer KA. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation. 1986; 74:1124-1136.
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 185
    • 0028242791 scopus 로고
    • Cellular mechanisms in ischemic preconditioning: The role of adenosine and protein kinase C
    • Downey JM, Cohen MV, Ytrehus K, Liu Y. Cellular mechanisms in ischemic preconditioning: the role of adenosine and protein kinase C. Ann N Y Acad Sci. 1994;723:82-98.
    • (1994) Ann N Y Acad Sci , vol.723 , pp. 82-98
    • Downey, J.M.1    Cohen, M.V.2    Ytrehus, K.3    Liu, Y.4
  • 186
    • 0028867873 scopus 로고
    • Differential stress protein mRNA expression during early ischaemic preconditioning in the rabbit heart and its relationship to adenosine receptor function
    • Heads RJ, Latchman DS, Yellon DM. Differential stress protein mRNA expression during early ischaemic preconditioning in the rabbit heart and its relationship to adenosine receptor function. J Mol Cell Cardiol. 1995;27:2133-2148.
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 2133-2148
    • Heads, R.J.1    Latchman, D.S.2    Yellon, D.M.3
  • 187
    • 85047675697 scopus 로고
    • Ischaemia and myocyte cytoskeleton: Review and speculation
    • Ganote C, Armstrong S. Ischaemia and myocyte cytoskeleton: review and speculation. Cardiovasc Res. 1993;27:1387-1403.
    • (1993) Cardiovasc Res , vol.27 , pp. 1387-1403
    • Ganote, C.1    Armstrong, S.2
  • 188
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang P, MacRae TH. Molecular chaperones and the cytoskeleton. J Cell Sci. 1997;110:1431-1440.
    • (1997) J Cell Sci , vol.110 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 191
    • 0029822231 scopus 로고    scopus 로고
    • Time course of late preconditioning against myocardial stunning in conscious pigs
    • Tang X-L, Qiu Y, Park S-W, Sun J-Z, Kalya A, Bolli R. Time course of late preconditioning against myocardial stunning in conscious pigs. Circ Res. 1996;79:424-434.
    • (1996) Circ Res , vol.79 , pp. 424-434
    • Tang, X.-L.1    Qiu, Y.2    Park, S.-W.3    Sun, J.-Z.4    Kalya, A.5    Bolli, R.6
  • 194
    • 0030669442 scopus 로고    scopus 로고
    • ATP-sensitive potassium channel mediates delayed ischemic protection by heat stress in rabbit heart
    • Hoag JB, Qian YZ, Nayeem MA, D'Angelo M, Kukreja RC. ATP-sensitive potassium channel mediates delayed ischemic protection by heat stress in rabbit heart. Am J Physiol. 1997;273:H2458-H2464.
    • (1997) Am J Physiol , vol.273
    • Hoag, J.B.1    Qian, Y.Z.2    Nayeem, M.A.3    D'Angelo, M.4    Kukreja, R.C.5
  • 195
    • 0029818659 scopus 로고    scopus 로고
    • Role of protein kinase C in ischemic preconditioning: Player or spectator ?
    • Brooks G, Hearse DJ. Role of protein kinase C in ischemic preconditioning: player or spectator [editorial]? Circ Res. 1996;79:627-630.
    • (1996) Circ Res , vol.79 , pp. 627-630
    • Brooks, G.1    Hearse, D.J.2
  • 197
    • 0031563771 scopus 로고    scopus 로고
    • Modulation of heat-shock protein 70 (HSP70) gene expression by sodium butyrate in U-937 promonocytic cells: Relationships with differentiation and apoptosis
    • Garcia-Bermejo L, Vilaboa N, Perez C, Galan A, De Blas E, Aller P. Modulation of heat-shock protein 70 (HSP70) gene expression by sodium butyrate in U-937 promonocytic cells: relationships with differentiation and apoptosis. Exp Cell Res. 1997;236:268-274.
    • (1997) Exp Cell Res , vol.236 , pp. 268-274
    • Garcia-Bermejo, L.1    Vilaboa, N.2    Perez, C.3    Galan, A.4    De Blas, E.5    Aller, P.6
  • 198
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • Mosser D, Caron A, Bourget L, Denis-Larose C, Massie B. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol Cell Biol. 1997;17:5317-5327.
    • (1997) Mol Cell Biol , vol.17 , pp. 5317-5327
    • Mosser, D.1    Caron, A.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 199
    • 0026688162 scopus 로고
    • Apoptotic cell death induced by c-myc is inhibited by bcl-2
    • Bissonnette RP, Echeverri F, Mahboubi A, Green DR. Apoptotic cell death induced by c-myc is inhibited by bcl-2. Nature. 1992;359:552-554.
    • (1992) Nature , vol.359 , pp. 552-554
    • Bissonnette, R.P.1    Echeverri, F.2    Mahboubi, A.3    Green, D.R.4
  • 200
    • 0029886404 scopus 로고    scopus 로고
    • Apoptosis in heat-induced cell killing: The protective role of hsp-70 and the sensitization effect of the c-myc gene
    • Li WX, Chen CH, Ling CC, Li GC. Apoptosis in heat-induced cell killing: the protective role of hsp-70 and the sensitization effect of the c-myc gene. Radiat Res. 1996;145:324-330.
    • (1996) Radiat Res , vol.145 , pp. 324-330
    • Li, W.X.1    Chen, C.H.2    Ling, C.C.3    Li, G.C.4
  • 201
    • 0029060160 scopus 로고
    • Bcl-2 and thermotolerance cooperate in cell survival
    • Strasser A, Anderson RL. Bcl-2 and thermotolerance cooperate in cell survival. Cell Growth Differ. 1995;6:799-805.
    • (1995) Cell Growth Differ , vol.6 , pp. 799-805
    • Strasser, A.1    Anderson, R.L.2
  • 204
    • 0029947822 scopus 로고    scopus 로고
    • Mitochondria are selective targets for the protective effects of heat shock against oxidative injury: Dual regulation of heat-shock transcription factor (HSF) activation and DNA-binding activity by H2O2: role of thioredoxin
    • Polla BS, Kantengwa S, Francois D, Salvioli S, Franceschi C, Marsac C, Cossarizza A. Jacquier-Sarlin MR. Polla BS. Mitochondria are selective targets for the protective effects of heat shock against oxidative injury: dual regulation of heat-shock transcription factor (HSF) activation and DNA-binding activity by H2O2: role of thioredoxin. Proc Natl Acad Sci U S A. 1996;93:6458-6463.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6458-6463
    • Polla, B.S.1    Kantengwa, S.2    Francois, D.3    Salvioli, S.4    Franceschi, C.5    Marsac, C.6    Cossarizza, A.7    Jacquier-Sarlin, M.R.8    Polla, B.S.9
  • 205
    • 0029885118 scopus 로고    scopus 로고
    • Relation of oxidative stress and glutathione synthesis to CD95(Fas/APO-1)-mediated apoptosis of adult T cell leukemia cells
    • Kohno T, Yamada Y, Hata T, Mori H, Yamamura M, Tomonaga M, Urata Y, Goto S, Kondo T. Relation of oxidative stress and glutathione synthesis to CD95(Fas/APO-1)-mediated apoptosis of adult T cell leukemia cells. J Immunol. 1996;156:4722-4728.
    • (1996) J Immunol , vol.156 , pp. 4722-4728
    • Kohno, T.1    Yamada, Y.2    Hata, T.3    Mori, H.4    Yamamura, M.5    Tomonaga, M.6    Urata, Y.7    Goto, S.8    Kondo, T.9
  • 206
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis: Heat shock protein 27 blocks Fas/APO-1- And staurosporine-induced cell death
    • Mehlen P, Schulze-Osthoff K, Arrigo AP. Small stress proteins as novel regulators of apoptosis: heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J Biol Chem. 1996;271:16510-16514.
    • (1996) J Biol Chem , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 207
    • 0025324129 scopus 로고
    • Stress-induced proteins in aortic smooth muscle cells and aorta of hypertensive rats
    • Kohane DS, Sarzani R, Schwanz JH, Chobanian AV. Brecher P. Stress-induced proteins in aortic smooth muscle cells and aorta of hypertensive rats. Am J Physiol. 1990;258:H1699-H1705.
    • (1990) Am J Physiol , vol.258
    • Kohane, D.S.1    Sarzani, R.2    Schwanz, J.H.3    Chobanian, A.V.4    Brecher, P.5
  • 208
    • 0029097150 scopus 로고
    • Acute hypertension induces heat-shock protein 70 gene expression in rat aorta
    • Xu Q, Li DG, Holbrook NJ, Udelsman R. Acute hypertension induces heat-shock protein 70 gene expression in rat aorta. Circulation. 1995; 92:1223-1229.
    • (1995) Circulation , vol.92 , pp. 1223-1229
    • Xu, Q.1    Li, D.G.2    Holbrook, N.J.3    Udelsman, R.4
  • 209
    • 0029160854 scopus 로고
    • Components of the protein synthesis and folding machinery are induced in vascular smooth muscle cells by hypertrophic and hyperplastic agents: Identification by comparative protein phenotyping and microsequencing
    • Patton WF, Erdjument-Bromage H, Marks AR, Tempst P. Taubman MB. Components of the protein synthesis and folding machinery are induced in vascular smooth muscle cells by hypertrophic and hyperplastic agents: identification by comparative protein phenotyping and microsequencing. J Biol Chem. 1995;270:21404-21410.
    • (1995) J Biol Chem , vol.270 , pp. 21404-21410
    • Patton, W.F.1    Erdjument-Bromage, H.2    Marks, A.R.3    Tempst, P.4    Taubman, M.B.5
  • 210
    • 0030322758 scopus 로고    scopus 로고
    • Diminished heat shock response in the aged myocardium
    • Locke M, Tanguay RM. Diminished heat shock response in the aged myocardium. Cell Stress Chaperones. 1996;1:251-260.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 251-260
    • Locke, M.1    Tanguay, R.M.2
  • 211
    • 0003162860 scopus 로고    scopus 로고
    • Role of mitochondria and oxidative stress in the aging process
    • Beal MF, Howell N. Bodis-Wollner I, eds. New York, NY: Wiley-Liss Inc
    • Sohal RS. Role of mitochondria and oxidative stress in the aging process. In: Beal MF, Howell N. Bodis-Wollner I, eds. Mitochondria and Free Radicals in Neurogeneralive Diseases. New York, NY: Wiley-Liss Inc; 1997.
    • (1997) Mitochondria and Free Radicals in Neurogeneralive Diseases
    • Sohal, R.S.1
  • 212
    • 0031883160 scopus 로고    scopus 로고
    • α-Tropomyosin knockouts: A blow against transcriptional chauvinism
    • Robbins J. α-Tropomyosin knockouts: a blow against transcriptional chauvinism. Circ Res. 1998;82:134-136.
    • (1998) Circ Res , vol.82 , pp. 134-136
    • Robbins, J.1
  • 216
    • 0028215215 scopus 로고
    • International consensus conference on postmenopausal hormone therapy and the cardiovascular system
    • Lobo RA, Speroff L. International consensus conference on postmenopausal hormone therapy and the cardiovascular system [editorial]. Fertil Steril. 1994;61:592-595.
    • (1994) Fertil Steril , vol.61 , pp. 592-595
    • Lobo, R.A.1    Speroff, L.2
  • 217
    • 0028338796 scopus 로고
    • Supplemental estrogen replacement
    • Marchant DJ. Supplemental estrogen replacement. Cancer. 1994;74: 512-517.
    • (1994) Cancer , vol.74 , pp. 512-517
    • Marchant, D.J.1
  • 218
  • 219
    • 0021354536 scopus 로고
    • Epidemiology of coronary heart disease: The Framingham study
    • Castelli WP. Epidemiology of coronary heart disease: the Framingham study. Am J Med. 1984;76:4-12.
    • (1984) Am J Med , vol.76 , pp. 4-12
    • Castelli, W.P.1
  • 220
    • 0028836338 scopus 로고
    • Risk factors that attenuate the female coronary disease advantage
    • Kannel WB, Wilson PW. Risk factors that attenuate the female coronary disease advantage. Arch Intent Med. 1995;155:57-61.
    • (1995) Arch Intent Med , vol.155 , pp. 57-61
    • Kannel, W.B.1    Wilson, P.W.2
  • 221
    • 0029962414 scopus 로고    scopus 로고
    • The vascular protective effects of estrogen
    • Farhat MY, Lavigne MC, Ramwell PW. The vascular protective effects of estrogen. FASEB J. 1996;10:615-624.
    • (1996) FASEB J , vol.10 , pp. 615-624
    • Farhat, M.Y.1    Lavigne, M.C.2    Ramwell, P.W.3
  • 222
    • 0030229050 scopus 로고    scopus 로고
    • The role of heat shock proteins in protection and pathophysiology of the arterial wall
    • Xu Q, Wick G. The role of heat shock proteins in protection and pathophysiology of the arterial wall. Mol Med Today. 1996;2:372-379.
    • (1996) Mol Med Today , vol.2 , pp. 372-379
    • Xu, Q.1    Wick, G.2
  • 226
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush KT, Goldberg AL, Nigam SK. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J Biol Chem. 1997;272:9086-9092.
    • (1997) J Biol Chem , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 229
    • 0027460056 scopus 로고
    • Heat shock proteins and the ischemic heart: An endogenous protective mechanism
    • Black SC, Lucchesi BR. Heat shock proteins and the ischemic heart: an endogenous protective mechanism [editorial comment]. Circulation. 1993;87:1048-1051.
    • (1993) Circulation , vol.87 , pp. 1048-1051
    • Black, S.C.1    Lucchesi, B.R.2
  • 230
    • 0015350090 scopus 로고
    • Myocardial calcium and magnesium in acute ischemic injury
    • Shen AC, Jennings RB. Myocardial calcium and magnesium in acute ischemic injury. Am J Pathol. 1972;67:417-440.
    • (1972) Am J Pathol , vol.67 , pp. 417-440
    • Shen, A.C.1    Jennings, R.B.2
  • 232
    • 0017101439 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover: Purification from porcine muscle
    • 2+-activated protease possibly involved in myofibrillar protein turnover: purification from porcine muscle. Biochemistry. 1976;15:2150-2158.
    • (1976) Biochemistry , vol.15 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3    Robson, R.M.4    Reville, W.J.5
  • 233
    • 0018873210 scopus 로고
    • 2+-activated protease that partially degrades myofibrils
    • 2+-activated protease that partially degrades myofibrils. J Mol Cell Cardiol. 1980;12:533-551.
    • (1980) J Mol Cell Cardiol , vol.12 , pp. 533-551
    • Dayton, W.R.1    Schollmeyer, J.V.2
  • 234
    • 0022412039 scopus 로고
    • Contracture and the calcium paradox
    • Ganote CE, Nayler WG. Contracture and the calcium paradox. J Mol Cell Cardiol. 1985;17:733-745.
    • (1985) J Mol Cell Cardiol , vol.17 , pp. 733-745
    • Ganote, C.E.1    Nayler, W.G.2
  • 235
    • 0027374184 scopus 로고
    • Reperfusion injury after myocardial infarction: The role of free radicals and the inflammatory response
    • Kilgore KS, Lucchesi BR. Reperfusion injury after myocardial infarction: the role of free radicals and the inflammatory response. Clin Biochem. 1993;26:359-370.
    • (1993) Clin Biochem , vol.26 , pp. 359-370
    • Kilgore, K.S.1    Lucchesi, B.R.2
  • 236
    • 0019333950 scopus 로고
    • Protein synthesis in chloroplasts, IX: Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts
    • Barraclough R, Ellis RJ. Protein synthesis in chloroplasts, IX: assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochim Biophys Acta. 1980;608:19-31.
    • (1980) Biochim Biophys Acta , vol.608 , pp. 19-31
    • Barraclough, R.1    Ellis, R.J.2
  • 237
    • 0027925677 scopus 로고
    • The general concept of molecular chaperones
    • Ellis RJ. The general concept of molecular chaperones. Philos Trans R Soc Lond B Biol Sci. 1993;339:257-261.
    • (1993) Philos Trans r Soc Lond b Biol Sci , vol.339 , pp. 257-261
    • Ellis, R.J.1
  • 238
    • 0029906974 scopus 로고    scopus 로고
    • TNF alpha alters mitochondrial membrane potential in L929 but not in TNF alpha-resistant L929.12 cells: Relationship with the expression of stress proteins, annexin 1 and superoxide dismutase activity
    • Polla BS, Jacquier-Sarlin MR, Kantengwa S, Mariethoz E, Hennet T, Russo-Marie F, Cossarizza A. TNF alpha alters mitochondrial membrane potential in L929 but not in TNF alpha-resistant L929.12 cells: relationship with the expression of stress proteins, annexin 1 and superoxide dismutase activity. Free Radic Res. 1996;25:125-131.
    • (1996) Free Radic Res , vol.25 , pp. 125-131
    • Polla, B.S.1    Jacquier-Sarlin, M.R.2    Kantengwa, S.3    Mariethoz, E.4    Hennet, T.5    Russo-Marie, F.6    Cossarizza, A.7
  • 240
    • 0029000181 scopus 로고
    • Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy
    • Medina R, Wing SS, Goldberg AL. Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochem J. 1995;307:631-637.
    • (1995) Biochem J , vol.307 , pp. 631-637
    • Medina, R.1    Wing, S.S.2    Goldberg, A.L.3
  • 241
    • 0029684296 scopus 로고    scopus 로고
    • Involvement of molecular chaperones in intracellular protein breakdown
    • Sherman MY, Goldberg AL. Involvement of molecular chaperones in intracellular protein breakdown. EXS. 1996;77:57-78.
    • (1996) EXS , vol.77 , pp. 57-78
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 242
    • 0029763452 scopus 로고    scopus 로고
    • Transcriptional repression of the prointerleukin 1beta gene by heat shock factor 1
    • Cahill CM, Waterman WR, Xie Y, Auron PE, Calderwood SK. Transcriptional repression of the prointerleukin 1beta gene by heat shock factor 1. J Biol Chem. 1996;271:24874-24879.
    • (1996) J Biol Chem , vol.271 , pp. 24874-24879
    • Cahill, C.M.1    Waterman, W.R.2    Xie, Y.3    Auron, P.E.4    Calderwood, S.K.5
  • 246
    • 0029962998 scopus 로고    scopus 로고
    • Stable expression of a human HSP70 gene in a rat myogenic cell line confers protection against endotoxin
    • Chi SH, Mestril R. Stable expression of a human HSP70 gene in a rat myogenic cell line confers protection against endotoxin. Am J Physiol. 1996;270:C1017-C1021.
    • (1996) Am J Physiol , vol.270
    • Chi, S.H.1    Mestril, R.2
  • 247
    • 0030455750 scopus 로고    scopus 로고
    • Response of the neonatal rat cardiomyocyte in culture to energy depletion: Effects of cytokines, nitric oxide, and heat shock proteins
    • Wang D, McMillin JB, Bick R, Buja LM. Response of the neonatal rat cardiomyocyte in culture to energy depletion: effects of cytokines, nitric oxide, and heat shock proteins. Lab Invest. 1996;75:809-818.
    • (1996) Lab Invest , vol.75 , pp. 809-818
    • Wang, D.1    McMillin, J.B.2    Bick, R.3    Buja, L.M.4
  • 249
    • 0029964506 scopus 로고    scopus 로고
    • Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein
    • Prapapanich V, Chen S, Nair S, Rimerman R, Smith D. Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein. Mol Endocrinol. 1996;10:420-431.
    • (1996) Mol Endocrinol , vol.10 , pp. 420-431
    • Prapapanich, V.1    Chen, S.2    Nair, S.3    Rimerman, R.4    Smith, D.5
  • 250
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
    • Chen S, Prapapanich V, Rimerman RA. Honoré B, DF Smith. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol Endocrinol. 1996;10:682-693.
    • (1996) Mol Endocrinol , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honoré, B.4    Smith, D.F.5
  • 251
    • 0029927148 scopus 로고    scopus 로고
    • Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of hsp 70
    • Gross M, Hessefort S. Purification and characterization of a 66-kDa protein from rabbit reticulocyte lysate which promotes the recycling of hsp 70. J Biol Chem. 1996;271:16833-16841.
    • (1996) J Biol Chem , vol.271 , pp. 16833-16841
    • Gross, M.1    Hessefort, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.