메뉴 건너뛰기




Volumn 9, Issue 1, 2005, Pages 51-58

HSP60, Bax, apoptosis and the heart

Author keywords

Apoptosis; Bak; Bax; Bcl 2; Bcl XL; Cytocrome c; HSP60

Indexed keywords

BAX PROTEIN, HUMAN; CASPASE; CHAPERONIN; CYTOCHROME C; CYTOCHROME C''; PROTEIN BAX; PROTEIN BCL 2;

EID: 17144421593     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2005.tb00336.x     Document Type: Review
Times cited : (166)

References (63)
  • 1
    • 0024988094 scopus 로고
    • The E. coli dnaK gene product, the HSP70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner
    • Skowyra D., Georgopoulos C., Zylicz M., The E. coli dnaK gene product, the HSP70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner, Cell, 62: 939-944, 1990
    • (1990) Cell , vol.62 , pp. 939-944
    • Skowyra, D.1    Georgopoulos, C.2    Zylicz, M.3
  • 2
    • 0026090476 scopus 로고
    • Rapid expression of heat shock protein in the rabbit after brief cardiac ischemia
    • Knowlton A. A., Brecher P., Apstein C. S., Rapid expression of heat shock protein in the rabbit after brief cardiac ischemia, J. Clin. Invest., 87: 139-147, 1991
    • (1991) J. Clin. Invest. , vol.87 , pp. 139-147
    • Knowlton, A.A.1    Brecher, P.2    Apstein, C.S.3
  • 3
    • 0030893652 scopus 로고    scopus 로고
    • Blocking the endogenous increase in HSP72 increases susceptibility to hypoxia and reoxygenation in isolated adult feline cardiocytes
    • Nakano M., Mann D. L., Knowlton A. A., Blocking the endogenous increase in HSP72 increases susceptibility to hypoxia and reoxygenation in isolated adult feline cardiocytes, Circulation, 95: 1523-1531, 1997
    • (1997) Circulation , vol.95 , pp. 1523-1531
    • Nakano, M.1    Mann, D.L.2    Knowlton, A.A.3
  • 4
    • 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
    • Marbe M. S., Mestril R., Chi S. H., Sayen M. R., Yellon D. M., Dillmann W. H., 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., 95: 1854-1860, 1995
    • (1995) J. Clin. Invest. , vol.95 , pp. 1854-1860
    • Marbe, M.S.1    Mestril, R.2    Chi, S.H.3    Sayen, M.R.4    Yellon, D.M.5    Dillmann, W.H.6
  • 6
    • 0027163384 scopus 로고
    • Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction
    • Marber M. S., Latchman D. S., Walker J. M., Yellon D. M., Cardiac stress protein elevation 24 hours after brief ischemia or heat stress is associated with resistance to myocardial infarction, Circulation, 88: 1264-1272, 1993
    • (1993) Circulation , vol.88 , pp. 1264-1272
    • Marber, M.S.1    Latchman, D.S.2    Walker, J.M.3    Yellon, D.M.4
  • 7
    • 0021259444 scopus 로고
    • Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells
    • Welch W. J., Feramisco J. R., Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells, J. Biol. Chem., 259: 4501-4513, 1984
    • (1984) J. Biol. Chem. , vol.259 , pp. 4501-4513
    • Welch, W.J.1    Feramisco, J.R.2
  • 8
    • 0028816976 scopus 로고
    • Late preconditioning against myocardial stunning: An endogenous protective mechanism that confers resistance to postischemic dysfunction 24 h after brief ischemia in conscious pigs
    • Sun J. Z., Tang X. L., Knowlton A. A., Park S. W., Qiu Y., Bolli R., Late preconditioning against myocardial stunning: An endogenous protective mechanism that confers resistance to postischemic dysfunction 24 h after brief ischemia in conscious pigs, J. Clin. Invest., 95: 388-403, 1995
    • (1995) J. Clin. Invest. , vol.95 , pp. 388-403
    • Sun, J.Z.1    Tang, X.L.2    Knowlton, A.A.3    Park, S.W.4    Qiu, Y.5    Bolli, R.6
  • 9
    • 0033106368 scopus 로고    scopus 로고
    • Mutation of amino acids 246-251 alters nuclear accumulation of human heat shock protein (HSP) 72 with stress, but does not reduce viability
    • Knowlton A. A., Mutation of amino acids 246-251 alters nuclear accumulation of human heat shock protein (HSP) 72 with stress, but does not reduce viability, J. Mol. Cell. Cardiol., 31: 523-532, 1999
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 523-532
    • Knowlton, A.A.1
  • 10
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (HSP60) in mammalian cells
    • Soltys B. J., Gupta, R. S., Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (HSP60) in mammalian cells, Ex. Cell Res., 222: 16-27, 1996
    • (1996) Ex. Cell Res. , vol.222 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 11
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C., Apoptosis in the pathogenesis and treatment of disease, Science, 267: 1456-1462, 1995
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.1
  • 13
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M. O., The biochemistry of apoptosis, Nature, 407: 770-776, 2000
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 14
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing machineries of death
    • Newmeyer D., Ferguson-Miller S., Mitochondria: Releasing power for life and unleashing machineries of death, Cell, 112: 481-490, 2003
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.1    Ferguson-Miller, S.2
  • 15
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D. R., Kroemer G., The pathophysiology of mitochondrial cell death, Science, 305: 626-629, 2004
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 16
    • 0036313059 scopus 로고    scopus 로고
    • Calcium-induced Cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane
    • Brustovetsky N., Brustovetsky T., Jemmerson R., Dubinsky, J. M., Calcium-induced Cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane, Journal of Neurochemistry, 80: 207-218, 2002
    • (2002) Journal of Neurochemistry , vol.80 , pp. 207-218
    • Brustovetsky, N.1    Brustovetsky, T.2    Jemmerson, R.3    Dubinsky, J.M.4
  • 17
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N. A., Lazebnik Y., Caspases: Enemies Within, Science, 281: 1312-1316, 1998
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 18
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial N. N., Korsmeyer S. J., Cell Death: Critical Control Points, Cell, 116: 205-219, 2004
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 19
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L., O'Roarke K., Desnoyers S., Zeng Z., Beidler D., Poirier G., Salvesen G., Dixit V., Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase, Cell, 81: 801-809, 1995
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.2    O'Roarke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.6    Poirier, G.7    Salvesen, G.8    Dixit, V.9
  • 21
    • 0029890823 scopus 로고    scopus 로고
    • Apopain/CPP32 cleaves proteins that are essential for cellular repair: A fundamental principle of apoptotic death
    • Casciola-Rosen L., Nicholson D. W., Chong T., Rowan K. R., Thornberry N. A., Miller D. K., Rosen A., Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death, J.Exp.Med., 183: 1957-1964, 1996
    • (1996) J. Exp. Med. , vol.183 , pp. 1957-1964
    • Casciola-Rosen, L.1    Nicholson, D.W.2    Chong, T.3    Rowan, K.R.4    Thornberry, N.A.5    Miller, D.K.6    Rosen, A.7
  • 22
    • 0027999537 scopus 로고
    • Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of cell death
    • Casciola-Rosen L. A., Miller D. K., Anhalt G. J., Rosen A., Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of cell death, J. Biol. Chem., 269: 30757-30760, 1994
    • (1994) J. Biol. Chem. , vol.269 , pp. 30757-30760
    • Casciola-Rosen, L.A.1    Miller, D.K.2    Anhalt, G.J.3    Rosen, A.4
  • 24
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a hertodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X., Zou H., Slaughter C., Wang X., DFF, a hertodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis, Cell, 89: 175-184, 1997
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 27
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • Madesh M., Hajnoczky G., VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release, J. Cell Biol., 155: 1003-1016, 2001
    • (2001) J. Cell Biol. , vol.155 , pp. 1003-1016
    • Madesh, M.1    Hajnoczky, G.2
  • 28
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., Reed, J. C., Mitochondrial control of cell death, Nature Med., 6: 513-519, 2000
    • (2000) Nature Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 30
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for bcl-2 regulation of apoptosis
    • Kluck R. M., Bossy-Wetzel E., Green D. R., Newmeyer D. D., The release of cytochrome c from mitochondria: A primary site for bcl-2 regulation of apoptosis, Science, 275: 1132-1136, 1997
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 31
    • 0034786019 scopus 로고    scopus 로고
    • Bcl-2, Bcl-xl sequester BH3 domain-only molecules preventing Bax- and Bak-mediated mitochondrial apoptosis
    • Cheng E. H. Y., Wei M. C., Weiler S., Flavell R. A., Mak T. W., Lindsten T., Korsmeyer S. J., Bcl-2, Bcl-xl sequester BH3 domain-only molecules preventing Bax-and Bak-mediated mitochondrial apoptosis, Mol. Cell., 8: 705-711, 2001
    • (2001) Mol. Cell. , vol.8 , pp. 705-711
    • Cheng, E.H.Y.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 32
    • 0031845008 scopus 로고    scopus 로고
    • Apoptosis induced by microinjection of cytochrome c is caspase-dependent and is inhibited by Bcl-2
    • Brustugun O., Fladmark K., Doskeland S., Orrenius S., Zhivotovsky B., Apoptosis induced by microinjection of cytochrome c is caspase-dependent and is inhibited by Bcl-2, Cell Death Diff., 5: 660-668, 1998
    • (1998) Cell Death Diff. , vol.5 , pp. 660-668
    • Brustugun, O.1    Fladmark, K.2    Doskeland, S.3    Orrenius, S.4    Zhivotovsky, B.5
  • 33
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c
    • Rosse T., Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c, Nature, 391: 496-499, 1998
    • (1998) Nature , vol.391 , pp. 496-499
    • Rosse, T.1
  • 34
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G., The proto-oncogene Bcl-2 and its role in regulating apoptosis, Nature Med., 3: 614-620, 1997
    • (1997) Nature Med. , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 38
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A., Smith C. L., Hsu Y. T., Youle R. J., Conformation of the Bax C-terminus regulates subcellular location and cell death, EMBO, 18: 2230-2241, 1999
    • (1999) EMBO , vol.18 , pp. 2230-2241
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 39
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of bax into the outer mitochondrial membrane
    • Eskes R., Desagher S., Antonsson B., Martinou J. C., Bid induces the oligomerization and insertion of bax into the outer mitochondrial membrane, Mol. Cell. Biol., 20: 929-935, 2000
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 40
    • 0034605121 scopus 로고    scopus 로고
    • Preservation of mitochondrial structure and function after bid- or bax-mediated cytochrome c release
    • von Ahnsen O., Renkin C., Perkins G., Kluck R., Bossy-Wetzel E., Newmeyer D. D., Preservation of mitochondrial structure and function after bid- or bax-mediated cytochrome c release, J. Cell Biol., 150: 1027-1036, 2001
    • (2001) J. Cell Biol. , vol.150 , pp. 1027-1036
    • Von Ahnsen, O.1    Renkin, C.2    Perkins, G.3    Kluck, R.4    Bossy-Wetzel, E.5    Newmeyer, D.D.6
  • 43
    • 0030041936 scopus 로고    scopus 로고
    • Heat shock proteins increase resistance to apoptosis
    • Samali A., Cotter T. G., Heat shock proteins increase resistance to apoptosis, Ex.l Cell Res., 223: 163-170, 1996
    • (1996) Ex. Cell Res. , vol.223 , pp. 163-170
    • Samali, A.1    Cotter, T.G.2
  • 44
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis
    • Mehlen P., Schulze-Osthoff K., Arrigo A. P., Small stress proteins as novel regulators of apoptosis, J. Biol. Chem., 271: 16510-16514, 1996
    • (1996) J. Biol. Chem. , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 45
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C., Morimoto R. I., Role of the heat shock response and molecular chaperones in oncogenesis and cell death, J. Nat. Can. Inst., 92: 1564-1572, 2000
    • (2000) J. Nat. Can. Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 50
    • 0032989818 scopus 로고    scopus 로고
    • Prior heat stress inhibits apoptosis in adenosine triphosphate-depleted renal tubular cells
    • Wang Y., Knowlton A. A., Christensen T. G., Shih T., and Borkan S. C., Prior heat stress inhibits apoptosis in adenosine triphosphate-depleted renal tubular cells, Kidney International, 55: 2224-2235, 1999
    • (1999) Kidney International , vol.55 , pp. 2224-2235
    • Wang, Y.1    Knowlton, A.A.2    Christensen, T.G.3    Shih, T.4    Borkan, S.C.5
  • 51
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • Kamradt M. C., Chen F., Cryns V. L., The Small Heat Shock Protein alpha B-Crystallin Negatively Regulates Cytochrome c- and Caspase-8-dependent Activation of Caspase-3 by Inhibiting Its Autoproteolytic Maturation, J. Biol. Chem., 276: 16059-16063, 2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 52
    • 0032582562 scopus 로고    scopus 로고
    • Role of HSP70 in regulation of stress-kinase JNK: Implications for apoptosis and aging
    • Gabai V. L., Meriin A. B., Yaglom J. A., Volloch V. Z., Sherman M. Y., Role of HSP70 in regulation of stress-kinase JNK: implications for apoptosis and aging, FEBS Lett., 43: 1-4, 1998
    • (1998) FEBS Lett. , vol.43 , pp. 1-4
    • Gabai, V.L.1    Meriin, A.B.2    Yaglom, J.A.3    Volloch, V.Z.4    Sherman, M.Y.5
  • 53
    • 0032476668 scopus 로고    scopus 로고
    • HSP70 exerts is anti-apoptotic function downstream of caspase-3-like proteases
    • Jäättela M., Wissing D., Kikolm K., Kallunki T., Egeblad M., HSP70 exerts is anti-apoptotic function downstream of caspase-3-like proteases, EMBO, 17: 6124-6134, 1998
    • (1998) EMBO , vol.17 , pp. 6124-6134
    • Jäättela, M.1    Wissing, D.2    Kikolm, K.3    Kallunki, T.4    Egeblad, M.5
  • 54
    • 0030293446 scopus 로고    scopus 로고
    • Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid line U937 following induction with TNF-″ and cycloheximide
    • Galea-Lauri J., Richardson A. J., Latchman D. S., Katz D. R., Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid line U937 following induction with TNF-″ and cycloheximide, J. Immunol., 157: 4109-4118, 1996
    • (1996) J. Immunol. , vol.157 , pp. 4109-4118
    • Galea-Lauri, J.1    Richardson, A.J.2    Latchman, D.S.3    Katz, D.R.4
  • 55
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • Lin K. M., Lin B., Lian I. Y., Mestril R., Scheffler I., Dillmann W. H., Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation, Circulation, 103: 1787-1792, 2001
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.5    Dillmann, W.H.6
  • 56
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of procaspase-3, HSP60 and HSP10 in the mitochondrial fraction of Jurkat cells
    • Samali A., Cai J., Zhivotovsky B., Jones D. P., Orrenius S., Presence of a pre-apoptotic complex of procaspase-3, HSP60 and HSP10 in the mitochondrial fraction of Jurkat cells, EMBO, 18: 2040-2048, 1999
    • (1999) EMBO , vol.18 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 57
    • 0037129860 scopus 로고    scopus 로고
    • Cytosolic HSP60, apoptosis, and myocardial injury
    • Kirchhoff S. R., Gupta S., Knowlton A. A., Cytosolic HSP60, Apoptosis, and Myocardial Injury, Circulation, 105: 2899-2904, 2002
    • (2002) Circulation , vol.105 , pp. 2899-2904
    • Kirchhoff, S.R.1    Gupta, S.2    Knowlton, A.A.3
  • 58
    • 0037137296 scopus 로고    scopus 로고
    • Cytosolic HSP60, hypoxia and apoptosis
    • Gupta S., Knowlton A. A., Cytosolic HSP60, Hypoxia and Apoptosis, Circulation, 106: 2727-2733, 2002
    • (2002) Circulation , vol.106 , pp. 2727-2733
    • Gupta, S.1    Knowlton, A.A.2
  • 59
    • 0033956449 scopus 로고    scopus 로고
    • The putative pore forming domain of Bax regulates mitochondrial localization and interaction with Bcl-Xl
    • Nouraini S., Six E., Matsuyama S., Reed J. C., The putative pore forming domain of Bax regulates mitochondrial localization and interaction with Bcl-Xl, Mol. and Cell. Biol., 20: 1604-1615, 2000
    • (2000) Mol. and Cell. Biol. , vol.20 , pp. 1604-1615
    • Nouraini, S.1    Six, E.2    Matsuyama, S.3    Reed, J.C.4
  • 60
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-Xl during apoptosis
    • Hsu Y. T., Wolter K. G., and Youle R. J., Cytosol-to-membrane redistribution of Bax and Bcl-Xl during apoptosis, PNAS, USA, 94: 3668-3672, 1997
    • (1997) PNAS, USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 61
    • 0032585644 scopus 로고    scopus 로고
    • Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury
    • Saikumar P., Dong Z., Patel Y., Hall K., Hopfer U., Weinberg J. M., Venkatachalam M. A., Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury, Oncogene, 17: 3401-3415, 1998
    • (1998) Oncogene , vol.17 , pp. 3401-3415
    • Saikumar, P.1    Dong, Z.2    Patel, Y.3    Hall, K.4    Hopfer, U.5    Weinberg, J.M.6    Venkatachalam, M.A.7
  • 63
    • 0042330503 scopus 로고    scopus 로고
    • Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells
    • Shan Y. X., Liu T. J., Su H. F., Samsamshariat A., Mestril R., Wang P. H., Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells, J. Mol. Cell. Cardiol., 35: 1135-1143, 2003
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.