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Volumn 38, Issue 3, 2005, Pages 433-444

Small heat shock proteins: A new classification scheme in mammals

Author keywords

Cardioprotection; Chaperone; Crystallin; Ischemia; Myocardium

Indexed keywords

ALPHA B CRYSTALLIN; ALPHA CRYSTALLIN; CHAPERONE; CRYSTALLIN; HEAT SHOCK ASSOCIATED PROTEIN B 2; HEAT SHOCK ASSOCIATED PROTEIN B 3; HEAT SHOCK ASSOCIATED PROTEIN B 7; HEAT SHOCK ASSOCIATED PROTEIN B 8; HEAT SHOCK ASSOCIATED PROTEIN B 9; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 25; HEAT SHOCK PROTEIN 27; HEAT SHOCK TRANSCRIPTION FACTOR 1; OSTEOCLAST DIFFERENTIATION FACTOR; UNCLASSIFIED DRUG;

EID: 14744291911     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2004.12.014     Document Type: Review
Times cited : (186)

References (138)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by a temperature shock and DNP in Drosophila
    • F.M. Ritossa A new puffing pattern induced by a temperature shock and DNP in Drosophila Experientia 18 1962 571 573
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.M.1
  • 2
    • 0018382014 scopus 로고
    • The induction of gene activity in drosophilia by heat shock
    • M. Ashburner, and J.J. Bonner The induction of gene activity in drosophilia by heat shock Cell 17 1979 241 254
    • (1979) Cell , vol.17 , pp. 241-254
    • Ashburner, M.1    Bonner, J.J.2
  • 3
    • 0036809333 scopus 로고    scopus 로고
    • SHsps and their role in the chaperone network
    • M. Haslbeck sHsps and their role in the chaperone network Cell. Mol. Life Sci. 59 2002 1649 1657
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1649-1657
    • Haslbeck, M.1
  • 4
    • 0034855811 scopus 로고    scopus 로고
    • Chaperone-like activity of alpha-crystallin and other small heat shock proteins
    • E. Ganea Chaperone-like activity of alpha-crystallin and other small heat shock proteins Curr. Protein Pept. Sci. 2 2001 205 225
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 205-225
    • Ganea, E.1
  • 5
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • N. Mounier, and A.P. Arrigo Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperones 7 2002 167 176
    • (2002) Cell Stress Chaperones , vol.7 , pp. 167-176
    • Mounier, N.1    Arrigo, A.P.2
  • 6
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • F. Narberhaus Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network Microbiol. Mol. Biol. Rev. 66 2002 64 93
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 7
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
    • R. Van Montfort, C. Slingsby, and E. Vierling Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones Adv. Protein Chem. 59 2001 105 156
    • (2001) Adv. Protein Chem. , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 8
    • 0034862016 scopus 로고    scopus 로고
    • Heat shock proteins and cardiac protection
    • D.S. Latchman Heat shock proteins and cardiac protection Cardiovasc. Res. 51 2001 637 646
    • (2001) Cardiovasc. Res. , vol.51 , pp. 637-646
    • Latchman, D.S.1
  • 9
    • 0002527685 scopus 로고
    • Untersuchung der Proteinsubstanzen in den lichtbrechenden Medien des Auges
    • C.T. Mörner Untersuchung der Proteinsubstanzen in den lichtbrechenden Medien des Auges Hoppe Seylers Z. Physiol. Chem. 18 1894 61 106
    • (1894) Hoppe Seylers Z. Physiol. Chem. , vol.18 , pp. 61-106
    • Mörner, C.T.1
  • 10
    • 0013799419 scopus 로고
    • Structural studies of alpha-crystallin
    • S.G. Waley Structural studies of alpha-crystallin Biochem. J. 96 1965 722 728
    • (1965) Biochem. J. , vol.96 , pp. 722-728
    • Waley, S.G.1
  • 11
    • 0014081136 scopus 로고
    • The structural proteins of the ocular lens
    • S. Lerman The structural proteins of the ocular lens Surv. Ophthalmol. 12 1967 112 129
    • (1967) Surv. Ophthalmol. , vol.12 , pp. 112-129
    • Lerman, S.1
  • 13
    • 0020357212 scopus 로고
    • Classification of rat lens crystallins and identification of proteins encoded by rat lens mRNA
    • F. Ramaekers, H. Dodemont, P. Vorstenbosch, and H. Bloemendal Classification of rat lens crystallins and identification of proteins encoded by rat lens mRNA Eur. J. Biochem. 128 1982 503 508
    • (1982) Eur. J. Biochem. , vol.128 , pp. 503-508
    • Ramaekers, F.1    Dodemont, H.2    Vorstenbosch, P.3    Bloemendal, H.4
  • 14
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • T.D. Ingolia, and E.A. Craig Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin Proc. Natl. Acad. Sci. USA 79 1982 2360 2360
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2360-2360
    • Ingolia, T.D.1    Craig, E.A.2
  • 15
    • 0025340370 scopus 로고
    • Molecular biology: Recent studies on enzyme/crystallins and alpha-crystallin gene expression
    • J. Piatigorsky Molecular biology: recent studies on enzyme/crystallins and alpha-crystallin gene expression Exp. Eye Res. 50 1990 725 728
    • (1990) Exp. Eye Res. , vol.50 , pp. 725-728
    • Piatigorsky, J.1
  • 16
    • 0037270166 scopus 로고    scopus 로고
    • Crystallin genes: Specialization by changes in gene regulation may precede gene duplication
    • J. Piatigorsky Crystallin genes: specialization by changes in gene regulation may precede gene duplication J. Struct. Funct. Genomics 3 2003 131 137
    • (2003) J. Struct. Funct. Genomics , vol.3 , pp. 131-137
    • Piatigorsky, J.1
  • 17
    • 0024095133 scopus 로고
    • Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: A single-copy gene product with two distinct functions
    • W. Hendriks, J.W. Mulders, M.A. Bibby, C. Slingsby, H. Bloemendal, and W.W. de Jong Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions Proc. Natl. Acad. Sci. USA 85 1988 7114 7118
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7114-7118
    • Hendriks, W.1    Mulders, J.W.2    Bibby, M.A.3    Slingsby, C.4    Bloemendal, H.5    De Jong, W.W.6
  • 18
    • 0030580048 scopus 로고    scopus 로고
    • The mechanism of recruitment of the lactate dehydrogenase-B/epsilon- crystallin gene by the duck lens
    • G.A. Brunekreef, H.J. Kraft, J.G. Schoenmakers, and N.H. Lubsen The mechanism of recruitment of the lactate dehydrogenase-B/epsilon-crystallin gene by the duck lens J. Mol. Biol. 262 1996 629 639
    • (1996) J. Mol. Biol. , vol.262 , pp. 629-639
    • Brunekreef, G.A.1    Kraft, H.J.2    Schoenmakers, J.G.3    Lubsen, N.H.4
  • 19
    • 0024580908 scopus 로고
    • Expression of the murine alpha B-crystallin gene is not restricted to the lens
    • R.A. Dubin, E.F. Wawrousek, and J. Piatigorsky Expression of the murine alpha B-crystallin gene is not restricted to the lens Mol. Cell. Biol. 9 1989 1083 1091
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1083-1091
    • Dubin, R.A.1    Wawrousek, E.F.2    Piatigorsky, J.3
  • 20
    • 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
    • R.I. Morimoto Regulation of the heat shock transcriptional response: cross-talk between a family of heat shock factors, molecular chaperones, and negative regulators Genes Dev. 12 1998 3788 3796
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 21
    • 0036160052 scopus 로고    scopus 로고
    • Heat shock factor 1 and heat shock proteins: Critical partners in protection against acute cell injury
    • E.S. Christians, L.J. Yan, and I.J. Benjamin Heat shock factor 1 and heat shock proteins: critical partners in protection against acute cell injury Crit. Care Med. 30 2002 S43 S50
    • (2002) Crit. Care Med. , vol.30
    • Christians, E.S.1    Yan, L.J.2    Benjamin, I.J.3
  • 22
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis
    • D.R. McMillan, X. Xiao, L. Shao, K. Graves, and I.J. Benjamin Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis J. Biol. Chem. 273 1998 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.J.5
  • 23
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • X. Xiao, X. Zuo, A.A. Davis, D.R. McMillan, B.B. Curry, and J.A. Richardson HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice EMBO J. 18 1999 5943 5952
    • (1999) EMBO J. , vol.18 , pp. 5943-5952
    • Xiao, X.1    Zuo, X.2    Davis, A.A.3    McMillan, D.R.4    Curry, B.B.5    Richardson, J.A.6
  • 24
    • 0036790590 scopus 로고    scopus 로고
    • Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage
    • L.J. Yan, E.S. Christians, L. Liu, X. Xiao, R.S. Sohal, and I.J. Benjamin Mouse heat shock transcription factor 1 deficiency alters cardiac redox homeostasis and increases mitochondrial oxidative damage EMBO J. 21 2002 5164 5172
    • (2002) EMBO J. , vol.21 , pp. 5164-5172
    • Yan, L.J.1    Christians, E.S.2    Liu, L.3    Xiao, X.4    Sohal, R.S.5    Benjamin, I.J.6
  • 25
    • 0031868230 scopus 로고    scopus 로고
    • Correlation between glutathione oxidation and trimerization of heat shock factor 1, an early step in stress induction of the Hsp response
    • J. Zou, W.F. Salminen, S.M. Roberts, and R. Voellmy Correlation between glutathione oxidation and trimerization of heat shock factor 1, an early step in stress induction of the Hsp response Cell Stress Chaperones 3 1998 130 141
    • (1998) Cell Stress Chaperones , vol.3 , pp. 130-141
    • Zou, J.1    Salminen, W.F.2    Roberts, S.M.3    Voellmy, R.4
  • 26
    • 0033231351 scopus 로고    scopus 로고
    • Gene expression and the thiol redox state
    • A.P. Arrigo Gene expression and the thiol redox state Free Radic. Biol. Med. 27 1999 936 944
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 936-944
    • Arrigo, A.P.1
  • 27
    • 0032112367 scopus 로고    scopus 로고
    • Direct sensing of heat and oxidation by Drosophila heat shock transcription factor
    • M. Zhong, A. Orosz, and C. Wu Direct sensing of heat and oxidation by Drosophila heat shock transcription factor Mol. Cell 2 1998 101 108
    • (1998) Mol. Cell , vol.2 , pp. 101-108
    • Zhong, M.1    Orosz, A.2    Wu, C.3
  • 28
    • 0035968256 scopus 로고    scopus 로고
    • Resolution, detection, and characterization of redox conformers of human HSF1
    • D.J. Manalo, and A.Y. Liu Resolution, detection, and characterization of redox conformers of human HSF1 J. Biol. Chem. 276 2001 23554 25561
    • (2001) J. Biol. Chem. , vol.276 , pp. 23554-25561
    • Manalo, D.J.1    Liu, A.Y.2
  • 29
    • 0036710399 scopus 로고    scopus 로고
    • Importance of individuality in oxidative stress and aging
    • E.R. Stadtman Importance of individuality in oxidative stress and aging Free Radic. Biol. Med. 33 2002 597 604
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 597-604
    • Stadtman, E.R.1
  • 30
    • 0037442768 scopus 로고    scopus 로고
    • Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress
    • S.G. Ahn, and D.J. Thiele Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress Genes Dev. 17 2003 516 528
    • (2003) Genes Dev. , vol.17 , pp. 516-528
    • Ahn, S.G.1    Thiele, D.J.2
  • 31
    • 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
    • R. Gopal-Srivastava, and J. Piatigorsky 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. 13 1993 7144 7152
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7144-7152
    • Gopal-Srivastava, R.1    Piatigorsky, J.2
  • 33
    • 0029661431 scopus 로고    scopus 로고
    • Differential expression of B-crystallin and Hsp27 in skeletal muscle during continuous contractile activity. Relationship to myogenic regulatory factors
    • P.D. Neufer, and I.J. Benjamin Differential expression of B-crystallin and Hsp27 in skeletal muscle during continuous contractile activity. Relationship to myogenic regulatory factors J. Biol. Chem. 271 1996 24089 24095
    • (1996) J. Biol. Chem. , vol.271 , pp. 24089-24095
    • Neufer, P.D.1    Benjamin, I.J.2
  • 34
    • 0028972717 scopus 로고
    • Regulation of the murine alpha B-crystallin/small heat shock protein gene in cardiac muscle
    • R. Gopal-Srivastava, J.I. Haynes 2nd, and J. Piatigorsky Regulation of the murine alpha B-crystallin/small heat shock protein gene in cardiac muscle Mol. Cell. Biol. 15 1995 7081 7090
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7081-7090
    • Gopal-Srivastava, R.1    Haynes II, J.I.2    Piatigorsky, J.3
  • 35
    • 0030700472 scopus 로고    scopus 로고
    • Identification and characterization of the gene encoding a new member of the alpha-crystallin/small hsp family, closely linked to the alphaB-crystallin gene in a head-to-head manner
    • A. Iwaki, T. Nagano, M. Nakagawa, T. Iwaki, and Y. Fukumaki Identification and characterization of the gene encoding a new member of the alpha-crystallin/small hsp family, closely linked to the alphaB-crystallin gene in a head-to-head manner Genomics 45 1997 386 394
    • (1997) Genomics , vol.45 , pp. 386-394
    • Iwaki, A.1    Nagano, T.2    Nakagawa, M.3    Iwaki, T.4    Fukumaki, Y.5
  • 36
    • 0032498791 scopus 로고    scopus 로고
    • MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase
    • A. Suzuki, Y. Sugiyama, Y. Hayashi, N. Nyu-i, M. Yoshida, and I. Nonaka MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase J. Cell Biol. 140 1998 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
  • 38
    • 0037147248 scopus 로고    scopus 로고
    • Orientation-dependent influence of an intergenic enhancer on the promoter activity of the divergently transcribed mouse Shsp/alpha B-crystallin and Mkbp/HspB2 genes
    • S.K. Swamynathan, and J. Piatigorsky Orientation-dependent influence of an intergenic enhancer on the promoter activity of the divergently transcribed mouse Shsp/alpha B-crystallin and Mkbp/HspB2 genes J. Biol. Chem. 277 2002 49700 49706
    • (2002) J. Biol. Chem. , vol.277 , pp. 49700-49706
    • Swamynathan, S.K.1    Piatigorsky, J.2
  • 39
    • 0020067552 scopus 로고
    • Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery
    • E.D. Hickey, and L.A. Weber Modulation of heat-shock polypeptide synthesis in HeLa cells during hyperthermia and recovery Biochemistry 21 1982 1513 1521
    • (1982) Biochemistry , vol.21 , pp. 1513-1521
    • Hickey, E.D.1    Weber, L.A.2
  • 40
    • 0036371814 scopus 로고    scopus 로고
    • Drosophila small heat shock proteins: Cell and organelle-specific chaperones?
    • S. Michaud, G. Morrow, J. Marchand, and R.M. Tanguay Drosophila small heat shock proteins: cell and organelle-specific chaperones? Prog. Mol. Subcell. Biol. 28 2002 79 101
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 79-101
    • Michaud, S.1    Morrow, G.2    Marchand, J.3    Tanguay, R.M.4
  • 41
    • 3442885854 scopus 로고    scopus 로고
    • Small heat shock proteins from extremophiles: A review
    • P. Laksanalamai, and F.T. Robb Small heat shock proteins from extremophiles: a review Extremophiles 8 2004 1 11
    • (2004) Extremophiles , vol.8 , pp. 1-11
    • Laksanalamai, P.1    Robb, F.T.2
  • 42
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • J. Horwitz Alpha-crystallin Exp. Eye Res. 76 2003 145 153
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 43
    • 0026336971 scopus 로고
    • Stress proteins and cardiovascular disease
    • R.S. Williams, and I.J. Benjamin Stress proteins and cardiovascular disease Mol. Biol. Med. 8 1991 197 206
    • (1991) Mol. Biol. Med. , vol.8 , pp. 197-206
    • Williams, R.S.1    Benjamin, I.J.2
  • 44
    • 0032572603 scopus 로고    scopus 로고
    • Stress (heat shock) proteins: Molecular chaperones in cardiovascular biology and disease
    • I.J. Benjamin, and D.R. McMillan Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease Circ. Res. 83 1998 117 132
    • (1998) Circ. Res. , vol.83 , pp. 117-132
    • Benjamin, I.J.1    McMillan, D.R.2
  • 45
    • 0031469110 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against ischemic injury in cardiac myocytes
    • J.L. Martin, R. Mestril, R. Hilal-Dandan, L.L. Brunton, and W.H. Dillmann Small heat shock proteins and protection against ischemic injury in cardiac myocytes Circulation 96 1997 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
  • 46
    • 0038482397 scopus 로고    scopus 로고
    • Stress proteins and myocardial protection
    • M. Locke E.G. Noble CRC Press Boca Raton, FL
    • J.W. Starnes Stress proteins and myocardial protection M. Locke E.G. Noble Exercise and stress response: the role of stress proteins 2002 CRC Press Boca Raton, FL 97 121
    • (2002) Exercise and Stress Response: The Role of Stress Proteins , pp. 97-121
    • Starnes, J.W.1
  • 47
    • 0037495846 scopus 로고    scopus 로고
    • Age, cell signalling and cardioprotection
    • R.P. Taylor, and J.W. Starnes Age, cell signalling and cardioprotection Acta Physiol. Scand. 178 2003 107 116
    • (2003) Acta Physiol. Scand. , vol.178 , pp. 107-116
    • Taylor, R.P.1    Starnes, J.W.2
  • 48
    • 0029620869 scopus 로고
    • Heat shock proteins in myocardial stress
    • W.H. Dillmann, and R. Mestril Heat shock proteins in myocardial stress Z. Kardiol. 84 Suppl 4 1995 87 90
    • (1995) Z. Kardiol. , vol.84 , Issue.4 SUPPL. , pp. 87-90
    • Dillmann, W.H.1    Mestril, R.2
  • 49
    • 0032931496 scopus 로고    scopus 로고
    • Heat shock proteins and protection against ischemic injury
    • W.H. Dillmann Heat shock proteins and protection against ischemic injury Infect. Dis. Obstet. Gynecol. 7 1999 55 57
    • (1999) Infect. Dis. Obstet. Gynecol. , vol.7 , pp. 55-57
    • Dillmann, W.H.1
  • 50
    • 0032812783 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against injury
    • W.H. Dillmann Small heat shock proteins and protection against injury Ann. N. Y. Acad. Sci. 874 1999 66 68
    • (1999) Ann. N. Y. Acad. Sci. , vol.874 , pp. 66-68
    • Dillmann, W.H.1
  • 51
    • 0028916211 scopus 로고
    • Heat shock proteins and protection against myocardial ischemia
    • R. Mestril, and W.H. Dillmann Heat shock proteins and protection against myocardial ischemia J. Mol. Cell. Cardiol. 27 1995 45 52
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 45-52
    • Mestril, R.1    Dillmann, W.H.2
  • 52
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • U. Jakob, M. Gaestel, K. Engel, and J. Buchner Small heat shock proteins are molecular chaperones J. Biol. Chem. 268 1993 1517 1520
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 53
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • J. Horwitz Alpha-crystallin can function as a molecular chaperone Proc. Natl. Acad. Sci. USA 89 1992 10449 10453
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 55
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • P. Vicart, A. Caron, P. Guicheney, Z. Li, M.C. Prevost, and A. Faure A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy Nat. Genet. 20 1998 92 95
    • (1998) Nat. Genet. , vol.20 , pp. 92-95
    • Vicart, P.1    Caron, A.2    Guicheney, P.3    Li, Z.4    Prevost, M.C.5    Faure, A.6
  • 56
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant
    • A.T. Chavez Zobel, A. Loranger, N. Marceau, J.R. Theriault, H. Lambert, and J. Landry Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant Hum. Mol. Genet. 12 2003 1609 1620
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1609-1620
    • Chavez Zobel, A.T.1    Loranger, A.2    Marceau, N.3    Theriault, J.R.4    Lambert, H.5    Landry, J.6
  • 57
    • 0242637569 scopus 로고    scopus 로고
    • AlphaB-crystallin modulates protein aggregation of abnormal desmin
    • X. Wang, R. Klevitsky, W. Huang, J. Glasford, F. Li, and J. Robbins AlphaB-crystallin modulates protein aggregation of abnormal desmin Circ. Res. 93 2003 998 1005
    • (2003) Circ. Res. , vol.93 , pp. 998-1005
    • Wang, X.1    Klevitsky, R.2    Huang, W.3    Glasford, J.4    Li, F.5    Robbins, J.6
  • 58
    • 0038652123 scopus 로고    scopus 로고
    • Heart-specific genes revealed by expressed sequence tag (EST) sampling
    • K. Megy, S. Audic, and J.M. Claverie Heart-specific genes revealed by expressed sequence tag (EST) sampling Genome Biol. 3 2002 research0074.1- research.11
    • (2002) Genome Biol. , vol.3
    • Megy, K.1    Audic, S.2    Claverie, J.M.3
  • 59
    • 0033579508 scopus 로고    scopus 로고
    • Identification and characterization of cvHsp. A novel human small stress protein selectively expressed in cardiovascular and insulin-sensitive tissues
    • S. Krief, J.F. Faivre, P. Robert, B. Le Douarin, N. Brument-Larignon, and I. Lefrere Identification and characterization of cvHsp. A novel human small stress protein selectively expressed in cardiovascular and insulin-sensitive tissues J. Biol. Chem. 274 1999 36592 36600
    • (1999) J. Biol. Chem. , vol.274 , pp. 36592-36600
    • Krief, S.1    Faivre, J.F.2    Robert, P.3    Le Douarin, B.4    Brument-Larignon, N.5    Lefrere, I.6
  • 60
    • 0026947554 scopus 로고
    • Large scale cDNA sequencing for analysis of quantitative and qualitative aspects of gene expression
    • K. Okubo, N. Hori, R. Matoba, T. Niiyama, A. Fukushima, and Y. Kojima Large scale cDNA sequencing for analysis of quantitative and qualitative aspects of gene expression Nat. Genet. 2 1992 173 179
    • (1992) Nat. Genet. , vol.2 , pp. 173-179
    • Okubo, K.1    Hori, N.2    Matoba, R.3    Niiyama, T.4    Fukushima, A.5    Kojima, Y.6
  • 62
    • 0242407366 scopus 로고    scopus 로고
    • Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig
    • P. Verschuure, C. Tatard, W.C. Boelens, J.F. Grongnet, and J.C. David Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig Eur. J. Cell Biol. 82 2003 523 530
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 523-530
    • Verschuure, P.1    Tatard, C.2    Boelens, W.C.3    Grongnet, J.F.4    David, J.C.5
  • 63
    • 0038638997 scopus 로고    scopus 로고
    • Dual perinatal and developmental expression of the small heat shock proteins alphaB-crystallin and Hsp27 in different tissues of the developing piglet
    • P. Tallot, J.F. Grongnet, and J.C. David Dual perinatal and developmental expression of the small heat shock proteins alphaB-crystallin and Hsp27 in different tissues of the developing piglet Biol. Neonate 83 2003 281 288
    • (2003) Biol. Neonate , vol.83 , pp. 281-288
    • Tallot, P.1    Grongnet, J.F.2    David, J.C.3
  • 64
    • 0033984092 scopus 로고    scopus 로고
    • Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation
    • Y. Sugiyama, A. Suzuki, M. Kishikawa, R. Akutsu, T. Hirose, and M.M. Waye Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation J. Biol. Chem. 275 2000 1095 1104
    • (2000) J. Biol. Chem. , vol.275 , pp. 1095-1104
    • Sugiyama, Y.1    Suzuki, A.2    Kishikawa, M.3    Akutsu, R.4    Hirose, T.5    Waye, M.M.6
  • 65
    • 0030575918 scopus 로고    scopus 로고
    • Isolation and characterization of a human heart cDNA encoding a new member of the small heat shock protein family - HSPL27
    • W.Y. Lam, S.K. Wing Tsui, P.T. Law, S.C. Luk, K.P. Fung, and C.Y. Lee Isolation and characterization of a human heart cDNA encoding a new member of the small heat shock protein family - HSPL27 Biochim. Biophys. Acta 1314 1996 120 124
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 120-124
    • Lam, W.Y.1    Wing Tsui, S.K.2    Law, P.T.3    Luk, S.C.4    Fung, K.P.5    Lee, C.Y.6
  • 66
    • 0032506095 scopus 로고    scopus 로고
    • HspB3, the most deviating of the six known human small heat shock proteins
    • W.C. Boelens, M.A. Van Boekel, and W.W. De Jong HspB3, the most deviating of the six known human small heat shock proteins Biochim. Biophys. Acta 1388 1998 513 516
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 513-516
    • Boelens, W.C.1    Van Boekel, M.A.2    De Jong, W.W.3
  • 69
    • 0037359564 scopus 로고    scopus 로고
    • The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins
    • J.M. Fontaine, J.S. Rest, M.J. Welsh, and R. Benndorf The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins Cell Stress Chaperones 8 2003 62 69
    • (2003) Cell Stress Chaperones , vol.8 , pp. 62-69
    • Fontaine, J.M.1    Rest, J.S.2    Welsh, M.J.3    Benndorf, R.4
  • 70
    • 0034682806 scopus 로고    scopus 로고
    • A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells
    • C.C. Smith, Y.X. Yu, M. Kulka, and L. Aurelian A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells J. Biol. Chem. 275 2000 25690 25699
    • (2000) J. Biol. Chem. , vol.275 , pp. 25690-25699
    • Smith, C.C.1    Yu, Y.X.2    Kulka, M.3    Aurelian, L.4
  • 72
    • 0035667159 scopus 로고    scopus 로고
    • ATP causes small heat shock proteins to release denatured protein
    • K. Wang, and A. Spector ATP causes small heat shock proteins to release denatured protein Eur. J. Biochem. 268 2001 6335 6345
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6335-6345
    • Wang, K.1    Spector, A.2
  • 73
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • M. Ehrnsperger, S. Graber, M. Gaestel, and J. Buchner Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation EMBO J. 16 1997 221 229
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 74
    • 0033970942 scopus 로고    scopus 로고
    • Characterization of native interaction of hsp110 with hsp25 and hsc70
    • X.Y. Wang, X. Chen, H.J. Oh, E. Repasky, L. Kazim, and J. Subjeck Characterization of native interaction of hsp110 with hsp25 and hsc70 FEBS Lett. 465 2000 98 102
    • (2000) FEBS Lett. , vol.465 , pp. 98-102
    • Wang, X.Y.1    Chen, X.2    Oh, H.J.3    Repasky, E.4    Kazim, L.5    Subjeck, J.6
  • 76
    • 0035063182 scopus 로고    scopus 로고
    • Transcriptional control at regulatory checkpoints by histone deacetylases: Molecular connections between cancer and chromatin
    • P.A. Wade Transcriptional control at regulatory checkpoints by histone deacetylases: molecular connections between cancer and chromatin Hum. Mol. Genet. 10 2001 693 698
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 693-698
    • Wade, P.A.1
  • 77
    • 0031017669 scopus 로고    scopus 로고
    • Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin
    • J.P. Brady, D. Garland, Y. Duglas-Tabor, W.G. Robison Jr., A. Groome, and E.F. Wawrousek Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin Proc. Natl. Acad. Sci. USA 94 1997 884 889
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 884-889
    • Brady, J.P.1    Garland, D.2    Duglas-Tabor, Y.3    Robison Jr., W.G.4    Groome, A.5    Wawrousek, E.F.6
  • 79
    • 0025877859 scopus 로고
    • Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system
    • K. Kato, H. Shinohara, N. Kurobe, Y. Inaguma, K. Shimizu, and K. Ohshima Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system Biochim. Biophys. Acta 1074 1991 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
  • 80
    • 0031031926 scopus 로고    scopus 로고
    • Temporospatial expression of the small HSP/alpha B-crystallin in cardiac and skeletal muscle during mouse development
    • I.J. Benjamin, J. Shelton, D.J. Garry, and J.A. Richardson Temporospatial expression of the small HSP/alpha B-crystallin in cardiac and skeletal muscle during mouse development Dev. Dyn. 208 1997 75 84
    • (1997) Dev. Dyn. , vol.208 , pp. 75-84
    • Benjamin, I.J.1    Shelton, J.2    Garry, D.J.3    Richardson, J.A.4
  • 81
    • 0028365670 scopus 로고
    • Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin
    • K. Kato, S. Goto, Y. Inaguma, K. Hasegawa, R. Morishita, and T. Asano Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin J. Biol. Chem. 269 1994 15302 15309
    • (1994) J. Biol. Chem. , vol.269 , pp. 15302-15309
    • Kato, K.1    Goto, S.2    Inaguma, Y.3    Hasegawa, K.4    Morishita, R.5    Asano, T.6
  • 83
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
    • N.B. Gusev, N.V. Bogatcheva, and S.B. Marston Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins Biochemistry (Mosc.) 67 2002 511 519
    • (2002) Biochemistry (Mosc.) , vol.67 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 84
    • 0033545355 scopus 로고    scopus 로고
    • Molecular chaperones: Small heat shock proteins in the limelight
    • I.P. Van den, D.G. Norman, and R.A. Quinlan Molecular chaperones: small heat shock proteins in the limelight Curr. Biol. 9 1999 R103 R1035
    • (1999) Curr. Biol. , vol.9
    • Van Den, I.P.1    Norman, D.G.2    Quinlan, R.A.3
  • 86
    • 0031912961 scopus 로고    scopus 로고
    • Van den IPR, Snoeckx LH, de Jong WW. Alpha B-crystallin and hsp25 in neonatal cardiac cells - Differences in cellular localization under stress conditions
    • F.A. Van de Klundert, and M.L. Gijsen van den IPR, Snoeckx LH, de Jong WW. Alpha B-crystallin and hsp25 in neonatal cardiac cells - differences in cellular localization under stress conditions Eur. J. Cell Biol. 75 1998 38 45
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 38-45
    • Van De Klundert, F.A.1    Gijsen, M.L.2
  • 87
    • 0142090565 scopus 로고    scopus 로고
    • Brief episode of ischemia activates protective genetic program in rat heart: A gene chip study
    • B.Z. Simkhovich, P. Marjoram, C. Poizat, L. Kedes, and R.A. Kloner Brief episode of ischemia activates protective genetic program in rat heart: a gene chip study Cardiovasc. Res. 59 2003 450 459
    • (2003) Cardiovasc. Res. , vol.59 , pp. 450-459
    • Simkhovich, B.Z.1    Marjoram, P.2    Poizat, C.3    Kedes, L.4    Kloner, R.A.5
  • 88
    • 0030862335 scopus 로고    scopus 로고
    • Abundance and location of the small heat shock proteins HSP25 and alphaB-crystallin in rat and human heart
    • G. Lutsch, R. Vetter, U. Offhauss, M. Wieske, H.J. Grone, and R. Klemenz Abundance and location of the small heat shock proteins HSP25 and alphaB-crystallin in rat and human heart Circulation 96 1997 3466 3476
    • (1997) Circulation , vol.96 , pp. 3466-3476
    • Lutsch, G.1    Vetter, R.2    Offhauss, U.3    Wieske, M.4    Grone, H.J.5    Klemenz, R.6
  • 92
    • 0036359596 scopus 로고    scopus 로고
    • Expression and phosphorylation of mammalian small heat shock proteins
    • K. Kato, H. Ito, and Y. Inaguma Expression and phosphorylation of mammalian small heat shock proteins Prog. Mol. Subcell. Biol. 28 2002 129 150
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 129-150
    • Kato, K.1    Ito, H.2    Inaguma, Y.3
  • 93
    • 0036966031 scopus 로고    scopus 로고
    • Free-radical production triggered by hyperthermia contributes to heat stress-induced cardioprotection in isolated rat hearts
    • C. Arnaud, M. Joyeux, C. Garrel, D. Godin-Ribuot, P. Demenge, and C. Ribuot Free-radical production triggered by hyperthermia contributes to heat stress-induced cardioprotection in isolated rat hearts Br. J. Pharmacol. 135 2002 1776 1782
    • (2002) Br. J. Pharmacol. , vol.135 , pp. 1776-1782
    • Arnaud, C.1    Joyeux, M.2    Garrel, C.3    Godin-Ribuot, D.4    Demenge, P.5    Ribuot, C.6
  • 94
    • 0029004307 scopus 로고
    • Induction of the synthesis of hsp27 and alpha B crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist
    • Y. Inaguma, K. Hasegawa, S. Goto, H. Ito, and K. Kato Induction of the synthesis of hsp27 and alpha B crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist J. Biochem. (Tokyo) 117 1995 1238 1243
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 1238-1243
    • Inaguma, Y.1    Hasegawa, K.2    Goto, S.3    Ito, H.4    Kato, K.5
  • 95
    • 0026342759 scopus 로고
    • Identification of the phosphorylation sites of the murine small heat shock protein hsp25
    • M. Gaestel, W. Schroder, R. Benndorf, C. Lippmann, K. Buchner, and F. Hucho Identification of the phosphorylation sites of the murine small heat shock protein hsp25 J. Biol. Chem. 266 1991 14721 14724
    • (1991) J. Biol. Chem. , vol.266 , pp. 14721-14724
    • Gaestel, M.1    Schroder, W.2    Benndorf, R.3    Lippmann, C.4    Buchner, K.5    Hucho, F.6
  • 96
    • 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
    • J. Landry, H. Lambert, M. Zhou, J.N. Lavoie, E. Hickey, and L.A. Weber Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II J. Biol. Chem. 267 1992 794 803
    • (1992) J. Biol. Chem. , vol.267 , pp. 794-803
    • Landry, J.1    Lambert, H.2    Zhou, M.3    Lavoie, J.N.4    Hickey, E.5    Weber, L.A.6
  • 97
    • 0035072677 scopus 로고    scopus 로고
    • Protein kinase inhibitors can suppress stress-induced dissociation of Hsp27
    • K. Kato, H. Ito, I. Iwamoto, K. Lida, and Y. Inaguma Protein kinase inhibitors can suppress stress-induced dissociation of Hsp27 Cell Stress Chaperones 6 2001 16 20
    • (2001) Cell Stress Chaperones , vol.6 , pp. 16-20
    • Kato, K.1    Ito, H.2    Iwamoto, I.3    Lida, K.4    Inaguma, Y.5
  • 98
    • 0037179756 scopus 로고    scopus 로고
    • Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival
    • S.C. Benn, D. Perrelet, A.C. Kato, J. Scholz, I. Decosterd, and R.J. Mannion Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival Neuron 36 2002 45 56
    • (2002) Neuron , vol.36 , pp. 45-56
    • Benn, S.C.1    Perrelet, D.2    Kato, A.C.3    Scholz, J.4    Decosterd, I.5    Mannion, R.J.6
  • 99
    • 0034607120 scopus 로고    scopus 로고
    • Translocation of HSP27 to sarcomere induced by ischemic preconditioning in isolated rat hearts
    • K. Sakamoto, T. Urushidani, and T. Nagao Translocation of HSP27 to sarcomere induced by ischemic preconditioning in isolated rat hearts Biochem. Biophys. Res. Commun. 269 2000 137 142
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 137-142
    • Sakamoto, K.1    Urushidani, T.2    Nagao, T.3
  • 100
    • 0033841185 scopus 로고    scopus 로고
    • Ischemic preconditioning: A potential role for constitutive low molecular weight stress protein translocation and phosphorylation?
    • P. Eaton, W.I. Awad, J.I. Miller, D.J. Hearse, and M.J. Shattock Ischemic preconditioning: a potential role for constitutive low molecular weight stress protein translocation and phosphorylation? J. Mol. Cell. Cardiol. 32 2000 961 971
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 961-971
    • Eaton, P.1    Awad, W.I.2    Miller, J.I.3    Hearse, D.J.4    Shattock, M.J.5
  • 101
    • 0036359558 scopus 로고    scopus 로고
    • Small stress proteins: Modulation of intracellular redox state and protection against oxidative stress
    • A.P. Arrigo, C. Paul, C. Ducasse, O. Sauvageot, and C. Kretz-Remy Small stress proteins: modulation of intracellular redox state and protection against oxidative stress Prog. Mol. Subcell. Biol. 28 2002 171 184
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 171-184
    • Arrigo, A.P.1    Paul, C.2    Ducasse, C.3    Sauvageot, O.4    Kretz-Remy, C.5
  • 102
    • 0024520027 scopus 로고
    • Enzyme/crystallins: Gene sharing as an evolutionary strategy
    • J. Piatigorsky, and G.J. Wistow Enzyme/crystallins: gene sharing as an evolutionary strategy Cell 57 1989 197 199
    • (1989) Cell , vol.57 , pp. 197-199
    • Piatigorsky, J.1    Wistow, G.J.2
  • 103
    • 0020046326 scopus 로고
    • Drosophila gene related to the major heat shock-induced gene is transcribed at normal temperatures and not induced by heat shock
    • T.D. Ingolia, and E.A. Craig Drosophila gene related to the major heat shock-induced gene is transcribed at normal temperatures and not induced by heat shock Proc. Natl. Acad. Sci. USA 79 1982 525 529
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 525-529
    • Ingolia, T.D.1    Craig, E.A.2
  • 104
    • 0032879383 scopus 로고    scopus 로고
    • The small heat shock proteins Hsp20 and alphaB-crystallin in cultured cardiac myocytes: Differences in cellular localization and solubilization after heat stress
    • F.A. Van de Klundert, and W.W. de Jong The small heat shock proteins Hsp20 and alphaB-crystallin in cultured cardiac myocytes: differences in cellular localization and solubilization after heat stress Eur. J. Cell Biol. 78 1999 567 572
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 567-572
    • Van De Klundert, F.A.1    De Jong, W.W.2
  • 105
    • 0028883722 scopus 로고
    • Sequence analysis of frog alpha B-crystallin cDNA: Sequence homology and evolutionary comparison of alpha A, alpha B and heat shock proteins
    • S.F. Lu, F.M. Pan, and S.H. Chiou Sequence analysis of frog alpha B-crystallin cDNA: sequence homology and evolutionary comparison of alpha A, alpha B and heat shock proteins Biochem. Biophys. Res. Commun. 216 1995 881 891
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 881-891
    • Lu, S.F.1    Pan, F.M.2    Chiou, S.H.3
  • 106
    • 0033927557 scopus 로고    scopus 로고
    • Structure and function of small heat shock/alpha-crystallin proteins: Established concepts and emerging ideas
    • T.H. MacRae Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas Cell. Mol. Life Sci. 57 2000 899 913
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 899-913
    • MacRae, T.H.1
  • 107
    • 0028254544 scopus 로고
    • Expression of the alpha-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues
    • C.M. Sax, and J. Piatigorsky Expression of the alpha-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues Adv. Enzymol. Relat. Areas Mol. Biol. 69 1994 155 201
    • (1994) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.69 , pp. 155-201
    • Sax, C.M.1    Piatigorsky, J.2
  • 108
    • 0024578954 scopus 로고
    • Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues
    • S.P. Bhat, and C.N. Nagineni Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues Biochem. Biophys. Res. Commun. 158 1989 319 325
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 109
    • 0037469234 scopus 로고    scopus 로고
    • Localization, macromolecular associations, and function of the small heat shock-related protein HSP20 in rat heart
    • W. Pipkin, J.A. Johnson, T.L. Creazzo, J. Burch, P. Komalavilas, and C. Brophy Localization, macromolecular associations, and function of the small heat shock-related protein HSP20 in rat heart Circulation 107 2003 469 476
    • (2003) Circulation , vol.107 , pp. 469-476
    • Pipkin, W.1    Johnson, J.A.2    Creazzo, T.L.3    Burch, J.4    Komalavilas, P.5    Brophy, C.6
  • 112
    • 0035124724 scopus 로고    scopus 로고
    • Transgene overexpression of alphaB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion
    • P.S. Ray, J.L. Martin, E.A. Swanson, H. Otani, W.H. Dillmann, and D.K. Das Transgene overexpression of alphaB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion FASEB J. 15 2001 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
  • 114
    • 0034839862 scopus 로고    scopus 로고
    • Desmin-related myopathies in mice and man
    • L. Carlsson, and L.E. Thornell Desmin-related myopathies in mice and man Acta Physiol. Scand. 171 2001 341 348
    • (2001) Acta Physiol. Scand. , vol.171 , pp. 341-348
    • Carlsson, L.1    Thornell, L.E.2
  • 117
    • 2942648296 scopus 로고    scopus 로고
    • Heat induced HSP20 phosphorylation without increased cyclic nucleotide levels in swine carotid media
    • C.M. Rembold, and E. Kaufman Heat induced HSP20 phosphorylation without increased cyclic nucleotide levels in swine carotid media BMC Physiol. 3 2003 3
    • (2003) BMC Physiol. , vol.3 , pp. 3
    • Rembold, C.M.1    Kaufman, E.2
  • 118
    • 2942689980 scopus 로고    scopus 로고
    • Small heat-shock protein Hsp20 phosphorylation inhibits beta-agonist-induced cardiac apoptosis
    • G.C. Fan, G. Chu, B. Mitton, Q. Song, Q. Yuan, and E.G. Kranias Small heat-shock protein Hsp20 phosphorylation inhibits beta-agonist-induced cardiac apoptosis Circ. Res. 94 2004 1474 1482
    • (2004) Circ. Res. , vol.94 , pp. 1474-1482
    • Fan, G.C.1    Chu, G.2    Mitton, B.3    Song, Q.4    Yuan, Q.5    Kranias, E.G.6
  • 119
    • 0036636103 scopus 로고    scopus 로고
    • Stress and vascular disease at the cellular and molecular levels
    • C.M. Brophy Stress and vascular disease at the cellular and molecular levels World J. Surg. 26 2002 779 782
    • (2002) World J. Surg. , vol.26 , pp. 779-782
    • Brophy, C.M.1
  • 120
    • 0035920143 scopus 로고    scopus 로고
    • HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)
    • R. Benndorf, X. Sun, R.R. Gilmont, K.J. Biederman, M.P. Molloy, and C.W. Goodmurphy HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27) J. Biol. Chem. 276 2001 26753 26761
    • (2001) J. Biol. Chem. , vol.276 , pp. 26753-26761
    • Benndorf, R.1    Sun, X.2    Gilmont, R.R.3    Biederman, K.J.4    Molloy, M.P.5    Goodmurphy, C.W.6
  • 121
    • 3242776825 scopus 로고    scopus 로고
    • Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
    • T.K. Chowdary, B. Raman, T. Ramakrishna, and C.M. Rao Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity Biochem. J. 381 2004 379 387
    • (2004) Biochem. J. , vol.381 , pp. 379-387
    • Chowdary, T.K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 122
    • 0037195691 scopus 로고    scopus 로고
    • H11 kinase is a novel mediator of myocardial hypertrophy in vivo
    • C. Depre, M. Hase, V. Gaussin, A. Zajac, L. Wang, and L. Hittinger H11 kinase is a novel mediator of myocardial hypertrophy in vivo Circ. Res. 91 2002 1007 1014
    • (2002) Circ. Res. , vol.91 , pp. 1007-1014
    • Depre, C.1    Hase, M.2    Gaussin, V.3    Zajac, A.4    Wang, L.5    Hittinger, L.6
  • 123
    • 0035344104 scopus 로고    scopus 로고
    • Expression analysis and chromosome location of a novel gene (H11) associated with the growth of human melanoma cells
    • Y.X. Yu, A. Heller, T. Liehr, C.C. Smith, and L. Aurelian Expression analysis and chromosome location of a novel gene (H11) associated with the growth of human melanoma cells Int. J. Oncol. 18 2001 905 911
    • (2001) Int. J. Oncol. , vol.18 , pp. 905-911
    • Yu, Y.X.1    Heller, A.2    Liehr, T.3    Smith, C.C.4    Aurelian, L.5
  • 124
    • 0037188910 scopus 로고    scopus 로고
    • Bidirectional gene organization: A common architectural feature of the human genome
    • N. Adachi, and M.R. Lieber Bidirectional gene organization: a common architectural feature of the human genome Cell 109 2002 807 809
    • (2002) Cell , vol.109 , pp. 807-809
    • Adachi, N.1    Lieber, M.R.2
  • 125
    • 0022775691 scopus 로고
    • Efficient transcription of a Caenorhabditis elegans heat shock gene pair in mouse fibroblasts is dependent on multiple promoter elements which can function bidirectionally
    • R.J. Kay, R.J. Boissy, R.H. Russnak, and E.P. Candido Efficient transcription of a Caenorhabditis elegans heat shock gene pair in mouse fibroblasts is dependent on multiple promoter elements which can function bidirectionally Mol. Cell. Biol. 6 1986 3134 3143
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3134-3143
    • Kay, R.J.1    Boissy, R.J.2    Russnak, R.H.3    Candido, E.P.4
  • 127
    • 0036487279 scopus 로고    scopus 로고
    • Van den IPR, Quinlan RA, de Jong WW, Boelens WC. Translocation of small heat shock proteins to the actin cytoskeleton upon proteasomal inhibition
    • P. Verschuure, and Y. Croes van den IPR, Quinlan RA, de Jong WW, Boelens WC. Translocation of small heat shock proteins to the actin cytoskeleton upon proteasomal inhibition J. Mol. Cell. Cardiol. 34 2002 117 128
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , pp. 117-128
    • Verschuure, P.1    Croes, Y.2
  • 128
    • 85068306850 scopus 로고    scopus 로고
    • Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle
    • N. Golenhofen, M.D. Perng, R.A. Quinlan, and D. Drenckhahn Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle Histochem Cell Biol 2004
    • (2004) Histochem Cell Biol
    • Golenhofen, N.1    Perng, M.D.2    Quinlan, R.A.3    Drenckhahn, D.4
  • 129
    • 0026470980 scopus 로고
    • Alpha A-crystallin is expressed in non-ocular tissues
    • A.N. Srinivasan, C.N. Nagineni, and S.P. Bhat Alpha A-crystallin is expressed in non-ocular tissues J. Biol. Chem. 267 1992 23337 23341
    • (1992) J. Biol. Chem. , vol.267 , pp. 23337-23341
    • Srinivasan, A.N.1    Nagineni, C.N.2    Bhat, S.P.3
  • 130
    • 0026040828 scopus 로고
    • Immunoreactive alpha a crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method
    • K. Kato, H. Shinohara, N. Kurobe, S. Goto, Y. Inaguma, and K. Ohshima Immunoreactive alpha A crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method Biochim. Biophys. Acta 1080 1991 173 180
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 173-180
    • Kato, K.1    Shinohara, H.2    Kurobe, N.3    Goto, S.4    Inaguma, Y.5    Ohshima, K.6
  • 131
    • 0031087167 scopus 로고    scopus 로고
    • Extralenticular expression of the alpha A-crystallin promoter/gamma interferon transgene
    • C.E. Egwuagu, and A.B. Chepelinsky Extralenticular expression of the alpha A-crystallin promoter/gamma interferon transgene Exp. Eye Res. 64 1997 491 495
    • (1997) Exp. Eye Res. , vol.64 , pp. 491-495
    • Egwuagu, C.E.1    Chepelinsky, A.B.2
  • 132
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: Structure, stability, and function
    • R. Jaenicke, and C. Slingsby Lens crystallins and their microbial homologs: structure, stability, and function Crit. Rev. Biochem. Mol. Biol. 36 2001 435 499
    • (2001) Crit. Rev. Biochem. Mol. Biol. , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 133
    • 0025036798 scopus 로고
    • A new rat gene RT7 is specifically expressed during spermatogenesis
    • F.A. Van der Hoorn, H.A. Tarnasky, and S.K. Nordeen A new rat gene RT7 is specifically expressed during spermatogenesis Dev. Biol. 142 1990 147 154
    • (1990) Dev. Biol. , vol.142 , pp. 147-154
    • Van Der Hoorn, F.A.1    Tarnasky, H.A.2    Nordeen, S.K.3
  • 134
    • 0028340931 scopus 로고
    • Testis-specific RT7 protein localizes to the sperm tail and associates with itself
    • N.A. Higgy, T. Pastoor, C. Renz, H.A. Tarnasky, and F.A. Van der Hoorn Testis-specific RT7 protein localizes to the sperm tail and associates with itself Biol. Reprod. 50 1994 1357 1366
    • (1994) Biol. Reprod. , vol.50 , pp. 1357-1366
    • Higgy, N.A.1    Pastoor, T.2    Renz, C.3    Tarnasky, H.A.4    Van Der Hoorn, F.A.5
  • 135
    • 0023656751 scopus 로고
    • Characterization and purification of the small 28,000-Da mammalian heat shock protein
    • A.P. Arrigo, and W.J. Welch Characterization and purification of the small 28,000-Da mammalian heat shock protein J. Biol. Chem. 262 1987 15359 15369
    • (1987) J. Biol. Chem. , vol.262 , pp. 15359-15369
    • Arrigo, A.P.1    Welch, W.J.2
  • 136
    • 0020429331 scopus 로고
    • Molecular and cellular effects of heat-shock and related treatments of mammalian tissue-culture cells
    • G.P. Thomas, W.J. Welch, M.B. Mathews, and J.R. Feramisco Molecular and cellular effects of heat-shock and related treatments of mammalian tissue-culture cells Cold Spring Harb. Symp. Quant. Biol. 46 Pt 2 1982 985 996
    • (1982) Cold Spring Harb. Symp. Quant. Biol. , vol.46 , Issue.2 PART , pp. 985-996
    • Thomas, G.P.1    Welch, W.J.2    Mathews, M.B.3    Feramisco, J.R.4
  • 138
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • R.D. Page TreeView: an application to display phylogenetic trees on personal computers Comput. Appl. Biosci. 12 1996 357 358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1


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