메뉴 건너뛰기




Volumn 122, Issue 17, 2010, Pages 1740-1751

Hold me tight: Role of the heat shock protein family of chaperones in cardiac disease

Author keywords

[No Author keywords available]

Indexed keywords

ARIMOCLOMOL; BINDING PROTEIN; CELASTROL; CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 72; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; IMMUNOPHILIN; MEVINOLIN; PROTEIN BCL 2; PROTEIN DNAJ; SIMVASTATIN; TEPRENONE; TRANSCRIPTION FACTOR;

EID: 78149244970     PISSN: 00097322     EISSN: 15244539     Source Type: Journal    
DOI: 10.1161/CIRCULATIONAHA.110.942250     Document Type: Review
Times cited : (91)

References (145)
  • 3
    • 53549091842 scopus 로고    scopus 로고
    • The heart of autophagy: Deconstructing cardiac proteotoxicity
    • Rothermel BA, Hill JA. The heart of autophagy: Deconstructing cardiac proteotoxicity. Autophagy. 2008;4:932-935.
    • (2008) Autophagy , vol.4 , pp. 932-935
    • Rothermel, B.A.1    Hill, J.A.2
  • 4
    • 58149396003 scopus 로고    scopus 로고
    • Autophagy in load-induced heart disease
    • Rothermel BA, Hill JA. Autophagy in load-induced heart disease. Circ Res. 2008;103:1363-1369.
    • (2008) Circ. Res. , vol.103 , pp. 1363-1369
    • Rothermel, B.A.1    Hill, J.A.2
  • 5
    • 44449104300 scopus 로고    scopus 로고
    • Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure
    • Pattison JS, Sanbe A, Maloyan A, Osinska H, Klevitsky R, Robbins J. Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure. Circulation. 2008;117:2743-2751.
    • (2008) Circulation , vol.117 , pp. 2743-2751
    • Pattison, J.S.1    Sanbe, A.2    Maloyan, A.3    Osinska, H.4    Klevitsky, R.5    Robbins, J.6
  • 6
    • 70449640181 scopus 로고    scopus 로고
    • Quality control against misfolded proteins in the cytosol: A network for cell survival
    • Kubota H. Quality control against misfolded proteins in the cytosol: a network for cell survival. J Biochem. 2009;146:609-616.
    • (2009) J. Biochem. , vol.146 , pp. 609-616
    • Kubota, H.1
  • 7
    • 74249089970 scopus 로고    scopus 로고
    • Regulation of heat shock protein 60 and 72 expression in the failing heart
    • Wang Y, Chen L, Hagiwara N, Knowlton AA. Regulation of heat shock protein 60 and 72 expression in the failing heart. J Mol Cell Cardiol. 2010;48:360-366.
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 360-366
    • Wang, Y.1    Chen, L.2    Hagiwara, N.3    Knowlton, A.A.4
  • 9
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem. 2006;75:271-294.
    • (2006) Annu Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 11
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood). 2003;228:111-133.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 12
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • Daugaard M, Rohde M, Jaattela M. The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions. FEBS Lett. 2007;581:3702-3710.
    • (2007) FEBS Lett. , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 13
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci. 2005;62:670-684.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 14
    • 77950600645 scopus 로고    scopus 로고
    • Mechanisms of the Hsp70 chaperone system
    • Young JC. Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol. 2010;88:291-300.
    • (2010) Biochem. Cell. Biol. , vol.88 , pp. 291-300
    • Young, J.C.1
  • 16
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: Localized functions of cytosolic chaperones
    • Young JC, Barral JM, Ulrich Hartl F. More than folding: localized functions of cytosolic chaperones. Trends Biochem Sci. 2003;28:541-547.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Hartl, F.U.3
  • 17
    • 0036049583 scopus 로고    scopus 로고
    • Function and regulation of cytosolic molecular chaperone CCT
    • Kubota H. Function and regulation of cytosolic molecular chaperone CCT. Vitam Horm. 2002;65:313-331.
    • (2002) Vitam Horm , vol.65 , pp. 313-331
    • Kubota, H.1
  • 18
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • Spiess C, Meyer AS, Reissmann S, Frydman J. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol. 2004;14:598-604.
    • (2004) Trends Cell. Biol. , vol.14 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 19
    • 58149506229 scopus 로고    scopus 로고
    • Crystallin proteins and amyloid fibrils
    • Ecroyd H, Carver JA. Crystallin proteins and amyloid fibrils. Cell Mol Life Sci. 2009;66:62-81.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 62-81
    • Ecroyd, H.1    Carver, J.A.2
  • 23
    • 37249005420 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 is required for proper heart tube formation
    • Brown DD, Christine KS, Showell C, Conlon FL. Small heat shock protein Hsp27 is required for proper heart tube formation. Genesis. 2007;45:667-678.
    • (2007) Genesis , vol.45 , pp. 667-678
    • Brown, D.D.1    Christine, K.S.2    Showell, C.3    Conlon, F.L.4
  • 24
    • 0026694490 scopus 로고
    • Alpha B-crystallin in cardiac tissue: Association with actin and desmin filaments
    • Bennardini F, Wrzosek A, Chiesi M. Alpha B-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
  • 25
    • 0030724879 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with intermediate filaments in response to stress
    • Djabali K, de Nechaud B, Landon F, Portier MM. AlphaB-crystallin interacts with intermediate filaments in response to stress. J Cell Sci. 1997;110(pt 21):2759-2769.
    • (1997) J. Cell. Sci. , vol.110 , Issue.21 PART , pp. 2759-2769
    • Djabali, K.1    De Nechaud, B.2    Landon, F.3    Portier, M.M.4
  • 27
    • 0036951869 scopus 로고    scopus 로고
    • Desmin filaments and cardiac disease: Establishing causality
    • Wang X, Osinska H, Gerdes AM, Robbins J. Desmin filaments and cardiac disease: establishing causality. J Card Fail. 2002;8:S287-292.
    • (2002) J. Card. Fail , vol.8
    • Wang, X.1    Osinska, H.2    Gerdes, A.M.3    Robbins, J.4
  • 28
    • 0028960169 scopus 로고
    • Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells
    • Gupta RS. Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells. Mol Microbiol. 1995;15:1-11.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1-11
    • Gupta, R.S.1
  • 29
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells
    • Soltys BJ, Gupta RS. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp Cell Res. 1996;222:16-27.
    • (1996) Exp. Cell. Res. , vol.222 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 30
    • 40649106751 scopus 로고    scopus 로고
    • Heat-shock protein 60 and cardiovascular disease: A paradoxical role
    • Knowlton AA, Srivatsa U. Heat-shock protein 60 and cardiovascular disease: a paradoxical role. Future Cardiol. 2008;4:151-161.
    • (2008) Future Cardiol. , vol.4 , pp. 151-161
    • Knowlton, A.A.1    Srivatsa, U.2
  • 31
    • 0037129860 scopus 로고    scopus 로고
    • Cytosolic heat shock protein 60, apoptosis, and myocardial injury
    • Kirchhoff SR, Gupta S, Knowlton AA. Cytosolic heat shock protein 60, apoptosis, and myocardial injury. Circulation. 2002;105:2899-2904.
    • (2002) Circulation , vol.105 , pp. 2899-2904
    • Kirchhoff, S.R.1    Gupta, S.2    Knowlton, A.A.3
  • 32
    • 0042330503 scopus 로고    scopus 로고
    • Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells
    • Shan YX, Liu TJ, Su HF, Samsamshariat A, Mestril R, Wang PH. Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells. J Mol Cell Cardiol. 2003;35:1135-1143.
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 1135-1143
    • Shan, Y.X.1    Liu, T.J.2    Su, H.F.3    Samsamshariat, A.4    Mestril, R.5    Wang, P.H.6
  • 33
    • 0028342786 scopus 로고
    • Amino acid specificity of the Escherichia coli chaperone GroEL (heat shock protein 60)
    • Richarme G, Kohiyama M. Amino acid specificity of the Escherichia coli chaperone GroEL (heat shock protein 60). J Biol Chem. 1994;269:7095-7098.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7095-7098
    • Richarme, G.1    Kohiyama, M.2
  • 35
    • 0035980016 scopus 로고    scopus 로고
    • Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor
    • Gassler CS, Wiederkehr T, Brehmer D, Bukau B, Mayer MP. Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J Biol Chem. 2001;276:32538-32544.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32538-32544
    • Gassler, C.S.1    Wiederkehr, T.2    Brehmer, D.3    Bukau, B.4    Mayer, M.P.5
  • 36
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Hohfeld J, Patterson C. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J Biol Chem. 2001;276:42938-42944.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 37
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand J, Alberti S, Patterson C, Hohfeld J. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr Biol. 2001;11:1569-1577.
    • (2001) Curr. Biol. , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 41
    • 84934443868 scopus 로고    scopus 로고
    • Heat shock factor 1 as a coordinator of stress and developmental pathways
    • Anckar J, Sistonen L. Heat shock factor 1 as a coordinator of stress and developmental pathways. Adv Exp Med Biol. 2007;594:78-88.
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 78-88
    • Anckar, J.1    Sistonen, L.2
  • 42
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y, Mosser DD, Morimoto RI. Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 1998;12:654-666.
    • (1998) Genes Dev. , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 43
    • 77649162855 scopus 로고    scopus 로고
    • Sent to destroy: The ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease
    • Willis MS, Townley-Tilson WH, Kang EY, Homeister JW, Patterson C. Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease. Circ Res. 2010;106:463-478.
    • (2010) Circ. Res. , vol.106 , pp. 463-478
    • Willis, M.S.1    Townley-Tilson, W.H.2    Kang, E.Y.3    Homeister, J.W.4    Patterson, C.5
  • 44
    • 34147149523 scopus 로고    scopus 로고
    • Heat shock factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1
    • Ostling P, Bjork JK, Roos-Mattjus P, Mezger V, Sistonen L. Heat shock factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1. J Biol Chem. 2007;282:7077-7086.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7077-7086
    • Ostling, P.1    Bjork, J.K.2    Roos-Mattjus, P.3    Mezger, V.4    Sistonen, L.5
  • 47
    • 53149144349 scopus 로고    scopus 로고
    • Expression and localization of Hsps in the heart and blood vessel of heat-stressed broilers
    • Yu J, Bao E, Yan J, Lei L. Expression and localization of Hsps in the heart and blood vessel of heat-stressed broilers. Cell Stress Chaperones. 2008;13:327-335.
    • (2008) Cell. Stress Chaperones , vol.13 , pp. 327-335
    • Yu, J.1    Bao, E.2    Yan, J.3    Lei, L.4
  • 49
    • 58149345103 scopus 로고    scopus 로고
    • A new (heat) shocking player in cardiac hypertrophy
    • Vondriska TM, Wang Y. A new (heat) shocking player in cardiac hypertrophy. Circ Res. 2008;103:1194-1196.
    • (2008) Circ. Res. , vol.103 , pp. 1194-1196
    • Vondriska, T.M.1    Wang, Y.2
  • 50
    • 33645293437 scopus 로고    scopus 로고
    • CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
    • Qian SB, McDonough H, Boellmann F, Cyr DM, Patterson C. CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature. 2006;440:551-555.
    • (2006) Nature , vol.440 , pp. 551-555
    • Qian, S.B.1    McDonough, H.2    Boellmann, F.3    Cyr, D.M.4    Patterson, C.5
  • 51
    • 59449097421 scopus 로고    scopus 로고
    • Build it up-tear it down: Protein quality control in the cardiac sarcomere
    • Willis MS, Schisler JC, Portbury AL, Patterson C. Build it up-tear it down: protein quality control in the cardiac sarcomere. Cardiovasc Res. 2009;81:439-448.
    • (2009) Cardiovasc. Res. , vol.81 , pp. 439-448
    • Willis, M.S.1    Schisler, J.C.2    Portbury, A.L.3    Patterson, C.4
  • 52
    • 68849104798 scopus 로고    scopus 로고
    • Tragedy in a heartbeat: Malfunctioning desmin causes skeletal and cardiac muscle disease
    • Goldfarb LG, Dalakas MC. Tragedy in a heartbeat: malfunctioning desmin causes skeletal and cardiac muscle disease. J Clin Invest. 2009;119:1806-1813.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1806-1813
    • Goldfarb, L.G.1    Dalakas, M.C.2
  • 53
    • 0037709152 scopus 로고    scopus 로고
    • The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin
    • Tessier DJ, Komalavilas P, Panitch A, Joshi L, Brophy CM. The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin. J Surg Res. 2003;111:152-157.
    • (2003) J. Surg. Res. , vol.111 , pp. 152-157
    • Tessier, D.J.1    Komalavilas, P.2    Panitch, A.3    Joshi, L.4    Brophy, C.M.5
  • 54
    • 33846523468 scopus 로고    scopus 로고
    • Interaction of mammalian Hsp22 with lipid membranes
    • Chowdary TK, Raman B, Ramakrishna T, Rao ChM. Interaction of mammalian Hsp22 with lipid membranes. Biochem J. 2007;401:437-445.
    • (2007) Biochem. J. , vol.401 , pp. 437-445
    • Chowdary, T.K.1    Raman, B.2    Ramakrishna, T.3    ChM, R.4
  • 61
    • 0043092396 scopus 로고    scopus 로고
    • Myocardial heat shock protein changes in the failing heart following coronary artery ligation
    • Tanonaka K, Toga W, Yoshida H, Takeo S. Myocardial heat shock protein changes in the failing heart following coronary artery ligation. Heart Lung Circ. 2003;12:60-65.
    • (2003) Heart Lung Circ. , vol.12 , pp. 60-65
    • Tanonaka, K.1    Toga, W.2    Yoshida, H.3    Takeo, S.4
  • 62
    • 33846100051 scopus 로고    scopus 로고
    • Changes in Hsp60 level of the failing heart following acute myocardial infarction and the effect of long-term treatment with trandolapril
    • Toga W, Tanonaka K, Takeo S. Changes in Hsp60 level of the failing heart following acute myocardial infarction and the effect of long-term treatment with trandolapril. Biol Pharm Bull. 2007;30:105-110.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 105-110
    • Toga, W.1    Tanonaka, K.2    Takeo, S.3
  • 65
    • 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
  • 66
    • 66349123063 scopus 로고    scopus 로고
    • MicroRNA-320 is involved in the regulation of cardiac ischemia/reperfusion injury by targeting heat-shock protein 20
    • Ren XP, Wu J, Wang X, Sartor MA, Qian J, Jones K, Nicolaou P, Pritchard TJ, Fan GC. MicroRNA-320 is involved in the regulation of cardiac ischemia/reperfusion injury by targeting heat-shock protein 20. Circulation. 2009;119:2357-2366.
    • (2009) Circulation , vol.119 , pp. 2357-2366
    • Ren, X.P.1    Wu, J.2    Wang, X.3    Sartor, M.A.4    Qian, J.5    Jones, K.6    Nicolaou, P.7    Pritchard, T.J.8    Fan, G.C.9
  • 69
    • 35348854946 scopus 로고    scopus 로고
    • HSF2 binds to the Hsp90, Hsp27, and c-Fos promoters constitutively and modulates their expression
    • Wilkerson DC, Skaggs HS, Sarge KD. HSF2 binds to the Hsp90, Hsp27, and c-Fos promoters constitutively and modulates their expression. Cell Stress Chaperones. 2007;12:283-290.
    • (2007) Cell. Stress Chaperones , vol.12 , pp. 283-290
    • Wilkerson, D.C.1    Skaggs, H.S.2    Sarge, K.D.3
  • 70
    • 0031558784 scopus 로고    scopus 로고
    • The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62
    • Yoshima T, Yura T, Yanagi H. The trimerization domain of human heat shock factor 2 is able to interact with nucleoporin p62. Biochem Biophys Res Commun. 1997;240:228-233.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 228-233
    • Yoshima, T.1    Yura, T.2    Yanagi, H.3
  • 71
    • 0036065951 scopus 로고    scopus 로고
    • Increased preload directly induces the activation of heat shock transcription factor 1 in the left ventricular overloaded heart
    • Nishizawa J, Nakai A, Komeda M, Ban T, Nagata K. Increased preload directly induces the activation of heat shock transcription factor 1 in the left ventricular overloaded heart. Cardiovasc Res. 2002;55:341-348.
    • (2002) Cardiovasc. Res. , vol.55 , pp. 341-348
    • Nishizawa, J.1    Nakai, A.2    Komeda, M.3    Ban, T.4    Nagata, K.5
  • 72
    • 0033596678 scopus 로고    scopus 로고
    • Reactive oxygen species play an important role in the activation of heat shock factor 1 in ischemic-reperfused heart
    • Nishizawa J, Nakai A, Matsuda K, Komeda M, Ban T, Nagata K. Reactive oxygen species play an important role in the activation of heat shock factor 1 in ischemic-reperfused heart. Circulation. 1999;99:934-941.
    • (1999) Circulation , vol.99 , pp. 934-941
    • Nishizawa, J.1    Nakai, A.2    Matsuda, K.3    Komeda, M.4    Ban, T.5    Nagata, K.6
  • 73
    • 0035021650 scopus 로고    scopus 로고
    • Activation of the heat shock response: Relationship to energy metabolites: A (31) P NMR study in rat hearts
    • Chang J, Knowlton AA, Xu F, Wasser JS. Activation of the heat shock response: relationship to energy metabolites: a (31) P NMR study in rat hearts. Am J Physiol Heart Circ Physiol. 2001;280:H426-H433.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.280
    • Chang, J.1    Knowlton, A.A.2    Xu, F.3    Wasser, J.S.4
  • 74
    • 0027425585 scopus 로고
    • Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
    • Hendrick JP, Langer T, Davis TA, Hartl FU, Wiedmann M. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc Natl Acad Sci U S A. 1993;90:10216-10220.
    • (1993) Proc. Natl. Acad. Sci. U S A , vol.90 , pp. 10216-10220
    • Hendrick, J.P.1    Langer, T.2    Davis, T.A.3    Hartl, F.U.4    Wiedmann, M.5
  • 75
  • 77
    • 33846254999 scopus 로고    scopus 로고
    • RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O (2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha
    • Liu YV, Baek JH, Zhang H, Diez R, Cole RN, Semenza GL. RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O (2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha. Mol Cell. 2007;25:207-217.
    • (2007) Mol. Cell. , vol.25 , pp. 207-217
    • Liu, Y.V.1    Baek, J.H.2    Zhang, H.3    Diez, R.4    Cole, R.N.5    Semenza, G.L.6
  • 78
    • 36049043184 scopus 로고    scopus 로고
    • Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38
    • Bai X, Ma D, Liu A, Shen X, Wang QJ, Liu Y, Jiang Y. Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38. Science. 2007;318:977-980.
    • (2007) Science , vol.318 , pp. 977-980
    • Bai, X.1    Ma, D.2    Liu, A.3    Shen, X.4    Wang, Q.J.5    Liu, Y.6    Jiang, Y.7
  • 80
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
    • Hansen WJ, Cowan NJ, Welch WJ. Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J Cell Biol. 1999;145:265-277.
    • (1999) J. Cell. Biol. , vol.145 , pp. 265-277
    • Hansen, W.J.1    Cowan, N.J.2    Welch, W.J.3
  • 82
    • 0037401171 scopus 로고    scopus 로고
    • Characterization of pDJA1, a cardiac-specific chaperone found by genomic profiling of the post-ischemic swine heart
    • Depre C, Wang L, Tomlinson JE, Gaussin V, Abdellatif M, Topper JN, Vatner SF. Characterization of pDJA1, a cardiac-specific chaperone found by genomic profiling of the post-ischemic swine heart. Cardiovasc Res. 2003;58:126-135.
    • (2003) Cardiovasc. Res. , vol.58 , pp. 126-135
    • Depre, C.1    Wang, L.2    Tomlinson, J.E.3    Gaussin, V.4    Abdellatif, M.5    Topper, J.N.6    Vatner, S.F.7
  • 83
    • 2442658924 scopus 로고    scopus 로고
    • BAG-1 proteins protect cardiac myocytes from simulated ischemia/reperfusion-induced apoptosis via an alternate mechanism of cell survival independent of the proteasome
    • Townsend PA, Cutress RI, Carroll CJ, Lawrence KM, Scarabelli TM, Packham G, Stephanou A, Latchman DS. BAG-1 proteins protect cardiac myocytes from simulated ischemia/reperfusion-induced apoptosis via an alternate mechanism of cell survival independent of the proteasome. J Biol Chem. 2004;279:20723-20728.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20723-20728
    • Townsend, P.A.1    Cutress, R.I.2    Carroll, C.J.3    Lawrence, K.M.4    Scarabelli, T.M.5    Packham, G.6    Stephanou, A.7    Latchman, D.S.8
  • 85
    • 19344370546 scopus 로고    scopus 로고
    • CHIP, a cochaperone/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice
    • Zhang C, Xu Z, He XR, Michael LH, Patterson C. CHIP, a cochaperone/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice. Am J Physiol Heart Circ Physiol. 2005;288:H2836-H2842.
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.288
    • Zhang, C.1    Xu, Z.2    He, X.R.3    Michael, L.H.4    Patterson, C.5
  • 87
    • 0037162697 scopus 로고    scopus 로고
    • Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy
    • Zhang CL, McKinsey TA, Chang S, Antos CL, Hill JA, Olson EN. Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy. Cell. 2002;110:479-488.
    • (2002) Cell. , vol.110 , pp. 479-488
    • Zhang, C.L.1    McKinsey, T.A.2    Chang, S.3    Antos, C.L.4    Hill, J.A.5    Olson, E.N.6
  • 88
    • 0142186685 scopus 로고    scopus 로고
    • HATs off to Hop: Recruitment of a class I histone deacetylase incriminates a novel transcriptional pathway that opposes cardiac hypertrophy
    • Hamamori Y, Schneider MD. HATs off to Hop: recruitment of a class I histone deacetylase incriminates a novel transcriptional pathway that opposes cardiac hypertrophy. J Clin Invest. 2003;112:824-826.
    • (2003) J. Clin. Invest. , vol.112 , pp. 824-826
    • Hamamori, Y.1    Schneider, M.D.2
  • 89
    • 34247272428 scopus 로고    scopus 로고
    • Therapeutic potential of H11 kinase for the ischemic heart
    • Danan IJ, Rashed ER, Depre C. Therapeutic potential of H11 kinase for the ischemic heart. Cardiovasc Drug Rev. 2007;25:14-29.
    • (2007) Cardiovasc. Drug Rev. , vol.25 , pp. 14-29
    • Danan, I.J.1    Rashed, E.R.2    Depre, C.3
  • 91
    • 43049123435 scopus 로고    scopus 로고
    • Role of heat shock transcriptional factor 1 and heat shock proteins in cardiac hypertrophy
    • Toko H, Minamino T, Komuro I. Role of heat shock transcriptional factor 1 and heat shock proteins in cardiac hypertrophy. Trends Cardiovasc Med. 2008;18:88-93.
    • (2008) Trends Cardiovasc. Med. , vol.18 , pp. 88-93
    • Toko, H.1    Minamino, T.2    Komuro, I.3
  • 93
    • 0031907281 scopus 로고    scopus 로고
    • Pathological versus physiological left ventricular hypertrophy: A review
    • Richey PA, Brown SP. Pathological versus physiological left ventricular hypertrophy: a review. J Sports Sci. 1998;16:129-141.
    • (1998) J. Sports Sci. , vol.16 , pp. 129-141
    • Richey, P.A.1    Brown, S.P.2
  • 95
    • 33846966331 scopus 로고    scopus 로고
    • Differences between pathological and physiological cardiac hypertrophy: Novel therapeutic strategies to treat heart failure
    • McMullen JR, Jennings GL. Differences between pathological and physiological cardiac hypertrophy: novel therapeutic strategies to treat heart failure. Clin Exp Pharmacol Physiol. 2007;34:255-262.
    • (2007) Clin. Exp. Pharmacol. Physiol. , vol.34 , pp. 255-262
    • McMullen, J.R.1    Jennings, G.L.2
  • 97
    • 2542498855 scopus 로고    scopus 로고
    • Autoimmune and inflammatory mechanisms in atherosclerosis
    • Wick G, Knoflach M, Xu Q. Autoimmune and inflammatory mechanisms in atherosclerosis. Annu Rev Immunol. 2004;22:361-403.
    • (2004) Annu Rev. Immunol. , vol.22 , pp. 361-403
    • Wick, G.1    Knoflach, M.2    Xu, Q.3
  • 98
    • 74049129476 scopus 로고    scopus 로고
    • Integrating the cell stress response: A new view of molecular chaperones as immunological and physiological homeostatic regulators
    • Henderson B. Integrating the cell stress response: a new view of molecular chaperones as immunological and physiological homeostatic regulators. Cell Biochem Funct. 28:1-14.
    • Cell. Biochem. Funct , vol.28 , pp. 1-14
    • Henderson, B.1
  • 99
    • 0032896726 scopus 로고    scopus 로고
    • Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals
    • Pockley AG, Bulmer J, Hanks BM, Wright BH. Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individuals. Cell Stress Chaperones. 1999;4:29-35.
    • (1999) Cell. Stress Chaperones , vol.4 , pp. 29-35
    • Pockley, A.G.1    Bulmer, J.2    Hanks, B.M.3    Wright, B.H.4
  • 100
    • 0030893652 scopus 로고    scopus 로고
    • Blocking the endogenous increase in HSP 72 increases susceptibility to hypoxia and reoxygenation in isolated adult feline cardiocytes
    • Nakano M, Mann DL, Knowlton AA. Blocking the endogenous increase in HSP 72 increases susceptibility to hypoxia and reoxygenation in isolated adult feline cardiocytes. Circulation. 1997;95:1523-1531.
    • (1997) Circulation , vol.95 , pp. 1523-1531
    • Nakano, M.1    Mann, D.L.2    Knowlton, A.A.3
  • 101
    • 0035852728 scopus 로고    scopus 로고
    • Gene transfer of heat-shock protein 70 reduces infarct size in vivo after ischemia/reperfusion in the rabbit heart
    • Okubo S, Wildner O, Shah MR, Chelliah JC, Hess ML, Kukreja RC. Gene transfer of heat-shock protein 70 reduces infarct size in vivo after ischemia/reperfusion in the rabbit heart. Circulation. 2001;103:877-881.
    • (2001) Circulation , vol.103 , pp. 877-881
    • Okubo, S.1    Wildner, O.2    Shah, M.R.3    Chelliah, J.C.4    Hess, M.L.5    Kukreja, R.C.6
  • 102
    • 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
  • 105
    • 0032519663 scopus 로고    scopus 로고
    • Protection against myocardial dysfunction after a brief ischemic period in transgenic mice expressing inducible heat shock protein 70
    • Trost SU, Omens JH, Karlon WJ, Meyer M, Mestril R, Covell JW, Dillmann WH. Protection against myocardial dysfunction after a brief ischemic period in transgenic mice expressing inducible heat shock protein 70. J Clin Invest. 1998;101:855-862.
    • (1998) J. Clin. Invest. , vol.101 , pp. 855-862
    • Trost, S.U.1    Omens, J.H.2    Karlon, W.J.3    Meyer, M.4    Mestril, R.5    Covell, J.W.6    Dillmann, W.H.7
  • 106
    • 1042268059 scopus 로고    scopus 로고
    • Phosphoproteome analysis of cardiomyocytes subjected to beta-adrenergic stimulation: Identification and characterization of a cardiac heat shock protein p20
    • Chu G, Egnaczyk GF, Zhao W, Jo SH, Fan GC, Maggio JE, Xiao RP, Kranias EG. Phosphoproteome analysis of cardiomyocytes subjected to beta-adrenergic stimulation: identification and characterization of a cardiac heat shock protein p20. Circ Res. 2004;94:184-193.
    • (2004) Circ. Res. , vol.94 , pp. 184-193
    • Chu, G.1    Egnaczyk, G.F.2    Zhao, W.3    Jo, S.H.4    Fan, G.C.5    Maggio, J.E.6    Xiao, R.P.7    Kranias, E.G.8
  • 107
    • 2942689980 scopus 로고    scopus 로고
    • Small heat-shock protein Hsp20 phosphorylation inhibits beta-agonist-induced cardiac apoptosis
    • Fan GC, Chu G, Mitton B, Song Q, Yuan Q, Kranias EG. Small heat-shock protein Hsp20 phosphorylation inhibits beta-agonist-induced cardiac apoptosis. Circ Res. 2004;94:1474-1482.
    • (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
  • 108
  • 109
    • 73349134699 scopus 로고    scopus 로고
    • Blockade of Hsp20 phosphorylation exacerbates cardiac ischemia/reperfusion injury by suppressed autophagy and increased cell death
    • Qian J, Ren X, Wang X, Zhang P, Jones WK, Molkentin JD, Fan GC, Kranias EG. Blockade of Hsp20 phosphorylation exacerbates cardiac ischemia/reperfusion injury by suppressed autophagy and increased cell death. Circ Res. 2009;105:1223-1231.
    • (2009) Circ. Res. , vol.105 , pp. 1223-1231
    • Qian, J.1    Ren, X.2    Wang, X.3    Zhang, P.4    Jones, W.K.5    Molkentin, J.D.6    Fan, G.C.7    Kranias, E.G.8
  • 110
    • 58149343451 scopus 로고    scopus 로고
    • Heat shock protein 20 interacting with phosphorylated Akt reduces doxorubicin-triggered oxidative stress and cardiotoxicity
    • Fan GC, Zhou X, Wang X, Song G, Qian J, Nicolaou P, Chen G, Ren X, Kranias EG. Heat shock protein 20 interacting with phosphorylated Akt reduces doxorubicin-triggered oxidative stress and cardiotoxicity. Circ Res. 2008;103:1270-1279.
    • (2008) Circ. Res. , vol.103 , pp. 1270-1279
    • Fan, G.C.1    Zhou, X.2    Wang, X.3    Song, G.4    Qian, J.5    Nicolaou, P.6    Chen, G.7    Ren, X.8    Kranias, E.G.9
  • 111
    • 65249153121 scopus 로고    scopus 로고
    • Activation of the bone morphogenetic protein receptor by H11kinase/Hsp22 promotes cardiac cell growth and survival
    • Sui X, Li D, Qiu H, Gaussin V, Depre C. Activation of the bone morphogenetic protein receptor by H11kinase/Hsp22 promotes cardiac cell growth and survival. Circ Res. 2009;104:887-895.
    • (2009) Circ. Res. , vol.104 , pp. 887-895
    • Sui, X.1    Li, D.2    Qiu, H.3    Gaussin, V.4    Depre, C.5
  • 112
    • 0036085215 scopus 로고    scopus 로고
    • Increased expression of HSP27 protects canine myocytes from simulated ischemia-reperfusion injury
    • Vander Heide RS. Increased expression of HSP27 protects canine myocytes from simulated ischemia-reperfusion injury. Am J Physiol Heart Circ Physiol. 2002;282:H935-H941.
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282
    • Heide, R.S.V.1
  • 113
    • 0035124724 scopus 로고    scopus 로고
    • Transgene overexpression of alphaB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion
    • Ray PS, Martin JL, Swanson EA, Otani H, Dillmann WH, Das DK. Transgene overexpression of alphaB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. FASEB J. 2001;15:393-402.
    • (2001) FASEB J. , vol.15 , pp. 393-402
    • Ray, P.S.1    Martin, J.L.2    Swanson, E.A.3    Otani, H.4    Dillmann, W.H.5    Das, D.K.6
  • 116
    • 24944455101 scopus 로고    scopus 로고
    • Silencing heat shock factor 1 by small interfering RNA abrogates heat shock-induced cardioprotection against ischemia-reperfusion injury in mice
    • Yin C, Xi L, Wang X, Eapen M, Kukreja RC. Silencing heat shock factor 1 by small interfering RNA abrogates heat shock-induced cardioprotection against ischemia-reperfusion injury in mice. J Mol Cell Cardiol. 2005;39:681-689.
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 681-689
    • Yin, C.1    Xi, L.2    Wang, X.3    Eapen, M.4    Kukreja, R.C.5
  • 117
    • 74049097964 scopus 로고    scopus 로고
    • Cardioprotection by CaMKII-deltaB is mediated by phosphorylation of heat shock factor 1 and subsequent expression of inducible heat shock protein 70
    • Peng W, Zhang Y, Zheng M, Cheng H, Zhu W, Cao CM, Xiao RP. Cardioprotection by CaMKII-deltaB is mediated by phosphorylation of heat shock factor 1 and subsequent expression of inducible heat shock protein 70. Circ Res. 2010;106:102-110.
    • (2010) Circ. Res. , vol.106 , pp. 102-110
    • Peng, W.1    Zhang, Y.2    Zheng, M.3    Cheng, H.4    Zhu, W.5    Cao, C.M.6    Xiao, R.P.7
  • 118
    • 35648993510 scopus 로고    scopus 로고
    • To be, or not to be: Molecular chaperones in protein degradation
    • Arndt V, Rogon C, Hohfeld J. To be, or not to be: molecular chaperones in protein degradation. Cell Mol Life Sci. 2007;64:2525-2541.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2525-2541
    • Arndt, V.1    Rogon, C.2    Hohfeld, J.3
  • 121
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • Jana NR, Dikshit P, Goswami A, Kotliarova S, Murata S, Tanaka K, Nukina N. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J Biol Chem. 2005;280:11635-11640.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 126
  • 127
    • 33748528911 scopus 로고    scopus 로고
    • Into the heart: The emerging role of the ubiquitin-proteasome system
    • Willis MS, Patterson C. Into the heart: the emerging role of the ubiquitin-proteasome system. J Mol Cell Cardiol. 2006;41:567-579.
    • (2006) J. Mol. Cell. Cardiol. , vol.41 , pp. 567-579
    • Willis, M.S.1    Patterson, C.2
  • 128
    • 38049174964 scopus 로고    scopus 로고
    • Appetite for destruction: E3 ubiquitin-ligase protection in cardiac disease
    • Willis MS, Schisler JC, Patterson C. Appetite for destruction: E3 ubiquitin-ligase protection in cardiac disease. Future Cardiol. 2008;4:65-75.
    • (2008) Future Cardiol. , vol.4 , pp. 65-75
    • Willis, M.S.1    Schisler, J.C.2    Patterson, C.3
  • 129
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening W, Roy J, Giasson B, Figlewicz DA, Mushynski WE, Durham HD. Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J Neurochem. 1999;72:693-699.
    • (1999) J. Neurochem. , vol.72 , pp. 693-699
    • Bruening, W.1    Roy, J.2    Giasson, B.3    Figlewicz, D.A.4    Mushynski, W.E.5    Durham, H.D.6
  • 130
    • 0035834026 scopus 로고    scopus 로고
    • Single oral dose of geranylgeranylacetone induces heat-shock protein 72 and renders protection against ischemia/reperfusion injury in rat heart
    • Ooie T, Takahashi N, Saikawa T, Nawata T, Arikawa M, Yamanaka K, Hara M, Shimada T, Sakata T. Single oral dose of geranylgeranylacetone induces heat-shock protein 72 and renders protection against ischemia/reperfusion injury in rat heart. Circulation. 2001;104:1837-1843.
    • (2001) Circulation , vol.104 , pp. 1837-1843
    • Ooie, T.1    Takahashi, N.2    Saikawa, T.3    Nawata, T.4    Arikawa, M.5    Yamanaka, K.6    Hara, M.7    Shimada, T.8    Sakata, T.9
  • 131
    • 0033801478 scopus 로고    scopus 로고
    • Effects of geranyl-geranyl-acetone administration before heat shock preconditioning for conferring tolerance against ischemiareperfusion injury in rat livers
    • Yamagami K, Yamamoto Y, Ishikawa Y, Yonezawa K, Toyokuni S, Yamaoka Y. Effects of geranyl-geranyl-acetone administration before heat shock preconditioning for conferring tolerance against ischemiareperfusion injury in rat livers. J Lab Clin Med. 2000;135:465-475.
    • (2000) J. Lab. Clin. Med. , vol.135 , pp. 465-475
    • Yamagami, K.1    Yamamoto, Y.2    Ishikawa, Y.3    Yonezawa, K.4    Toyokuni, S.5    Yamaoka, Y.6
  • 132
    • 77949877628 scopus 로고    scopus 로고
    • Heat shock proteins: Therapeutic drug targets for chronic neurodegeneration?
    • Sajjad MU, Samson B, Wyttenbach A. Heat shock proteins: therapeutic drug targets for chronic neurodegeneration? Curr Pharm Biotechnol. 2010;11:198-215.
    • (2010) Curr. Pharm. Biotechnol. , vol.11 , pp. 198-215
    • Sajjad, M.U.1    Samson, B.2    Wyttenbach, A.3
  • 134
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D, Kalmar B, Dick JR, Riddoch-Contreras J, Burnstock G, Greensmith L. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med. 2004;10:402-405.
    • (2004) Nat. Med. , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 136
    • 33744486642 scopus 로고    scopus 로고
    • Celastrol blocks neuronal cell death and extends life in transgenic mouse model of amyotrophic lateral sclerosis
    • Kiaei M, Kipiani K, Petri S, Chen J, Calingasan NY, Beal MF. Celastrol blocks neuronal cell death and extends life in transgenic mouse model of amyotrophic lateral sclerosis. Neurodegener Dis. 2005;2:246-254.
    • (2005) Neurodegener Dis. , vol.2 , pp. 246-254
    • Kiaei, M.1    Kipiani, K.2    Petri, S.3    Chen, J.4    Calingasan, N.Y.5    Beal, M.F.6
  • 137
    • 0034528569 scopus 로고    scopus 로고
    • Immunomodulation: A new role for statins?
    • Palinski W. Immunomodulation: a new role for statins? Nat Med. 2000;6:1311-1312.
    • (2000) Nat. Med. , vol.6 , pp. 1311-1312
    • Palinski, W.1
  • 138
    • 18444391234 scopus 로고    scopus 로고
    • Statin-induced vascular smooth muscle cell apoptosis: A possible role in the prevention of restenosis?
    • Erl W. Statin-induced vascular smooth muscle cell apoptosis: a possible role in the prevention of restenosis? Curr Drug Targets Cardiovasc Haematol Disord. 2005;5:135-144.
    • (2005) Curr. Drug Targets Cardiovasc. Haematol Disord. , vol.5 , pp. 135-144
    • Erl, W.1
  • 139
    • 0034687606 scopus 로고    scopus 로고
    • Suppression of endothelial nitric oxide production after withdrawal of statin treatment is mediated by negative feedback regulation of rho GTPase gene transcription
    • Laufs U, Endres M, Custodis F, Gertz K, Nickenig G, Liao JK, Bohm M. Suppression of endothelial nitric oxide production after withdrawal of statin treatment is mediated by negative feedback regulation of rho GTPase gene transcription. Circulation. 2000;102:3104-3110.
    • (2000) Circulation , vol.102 , pp. 3104-3110
    • Laufs, U.1    Endres, M.2    Custodis, F.3    Gertz, K.4    Nickenig, G.5    Liao, J.K.6    Bohm, M.7
  • 142
    • 30744458323 scopus 로고    scopus 로고
    • Simvastatin promotes heat shock protein 27 expression and Akt activation in the rat retina and protects axotomized retinal ganglion cells in vivo
    • Kretz A, Schmeer C, Tausch S, Isenmann S. Simvastatin promotes heat shock protein 27 expression and Akt activation in the rat retina and protects axotomized retinal ganglion cells in vivo. Neurobiol Dis. 2006;21:421-430.
    • (2006) Neurobiol. Dis. , vol.21 , pp. 421-430
    • Kretz, A.1    Schmeer, C.2    Tausch, S.3    Isenmann, S.4
  • 143
    • 56149102958 scopus 로고    scopus 로고
    • Statins modulate heat shock protein expression and enhance retinal ganglion cell survival after transient retinal ischemia/reperfusion in vivo
    • Schmeer C, Gamez A, Tausch S, Witte OW, Isenmann S. Statins modulate heat shock protein expression and enhance retinal ganglion cell survival after transient retinal ischemia/reperfusion in vivo. Invest Ophthalmol Vis Sci. 2008;49:4971-4981.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 4971-4981
    • Schmeer, C.1    Gamez, A.2    Tausch, S.3    Witte, O.W.4    Isenmann, S.5
  • 144
    • 0027010408 scopus 로고
    • Case report of dentigerous cyst of lower incisor
    • Ojo MA, Akpata O. Case report of dentigerous cyst of lower incisor. Afr Dent J. 1992;6:34-37.
    • (1992) Afr Dent J. , vol.6 , pp. 34-37
    • Ojo, M.A.1    Akpata, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.