메뉴 건너뛰기




Volumn 97, Issue 3, 2003, Pages 223-261

Regulation of cardiac myocyte cell death

Author keywords

Apoptosis; Bcl 2; Cardiac myocytes; Caspases; Death receptors; Mitochondria

Indexed keywords

CALPAIN; CASPASE; CATHEPSIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BCL 2; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN P53; PROTEINASE;

EID: 0037357698     PISSN: 01637258     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0163-7258(02)00339-X     Document Type: Review
Times cited : (108)

References (367)
  • 1
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation
    • Acehan D., Jiang X., Morgan D.G., Heuser J.E., Wang X., Akey C.W. Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation. Mol Cell. 9:2002;423-432.
    • (2002) Mol Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 4
    • 0035146929 scopus 로고    scopus 로고
    • Life-or-death decisions by the Bcl-2 protein family
    • Adams J.A., Cory S. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem Sci. 26:2001;61-66.
    • (2001) Trends Biochem Sci , vol.26 , pp. 61-66
    • Adams, J.A.1    Cory, S.2
  • 5
    • 0034623814 scopus 로고    scopus 로고
    • Cardiomyocyte apoptosis induced by Gαq signaling is mediated by permeability transition pore formation and activation of the mitochondrial death pathway
    • Adams J.W., Pagel A.L., Means C.K., Oksenberg D., Armstrong R.C., Brown J.H. Cardiomyocyte apoptosis induced by Gαq signaling is mediated by permeability transition pore formation and activation of the mitochondrial death pathway. Circ Res. 87:2000;1180-1187.
    • (2000) Circ Res , vol.87 , pp. 1180-1187
    • Adams, J.W.1    Pagel, A.L.2    Means, C.K.3    Oksenberg, D.4    Armstrong, R.C.5    Brown, J.H.6
  • 6
    • 0035369143 scopus 로고    scopus 로고
    • The mitochondrial apoptosome: A killer unleashed by cytochrome seas
    • Adrain C., Martin S.J. The mitochondrial apoptosome: a killer unleashed by cytochrome seas. Trends Biochem Sci. 26:2001;390-397.
    • (2001) Trends Biochem Sci , vol.26 , pp. 390-397
    • Adrain, C.1    Martin, S.J.2
  • 7
    • 0030886770 scopus 로고    scopus 로고
    • Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats
    • Aikawa R., Komura I., Yamazaki T., Zou Y., Kudoh S., Tanaka M., Shiojima I., Hiroi Y., Yazaki Y. Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats. J Clin Invest. 100:1997;1813-1821.
    • (1997) J Clin Invest , vol.100 , pp. 1813-1821
    • Aikawa, R.1    Komura, I.2    Yamazaki, T.3    Zou, Y.4    Kudoh, S.5    Tanaka, M.6    Shiojima, I.7    Hiroi, Y.8    Yazaki, Y.9
  • 8
    • 0035933436 scopus 로고    scopus 로고
    • Mitochondrial ATP-sensitive potassium channels inhibit apoptosis induced by oxidative stress in cardiac cells
    • Akao M., Ohler A., O'Rourke B., Marban E. Mitochondrial ATP-sensitive potassium channels inhibit apoptosis induced by oxidative stress in cardiac cells. Circ Res. 88:2001;1267-1275.
    • (2001) Circ Res , vol.88 , pp. 1267-1275
    • Akao, M.1    Ohler, A.2    O'Rourke, B.3    Marban, E.4
  • 11
    • 0035213530 scopus 로고    scopus 로고
    • Bax and other pro-apoptotic Bcl-2 family "killer-proteins" and their victim, the mitochondrion
    • Antonsson B. Bax and other pro-apoptotic Bcl-2 family "killer-proteins" and their victim, the mitochondrion. Cell Tissue Res. 306:2001;347-361.
    • (2001) Cell Tissue Res , vol.306 , pp. 347-361
    • Antonsson, B.1
  • 12
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B., Montessuit S., Lauper S., Eskes R., Martinou J.C. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem J. 345:2000;271-278.
    • (2000) Biochem J , vol.345 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 13
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B., Montessuit S., Sanchez B., Martinou J.C. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J Biol Chem. 276:2001;11615-11623.
    • (2001) J Biol Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 15
    • 0037155837 scopus 로고    scopus 로고
    • Direct activation of mitochondrial apoptosis machinery by c-Jun N-terminal kinase in adult cardiac myocytes
    • Aoki H., Kang P.M., Hampe J., Yoshimura K., Noma T., Matsuzaki M., Izumo S. Direct activation of mitochondrial apoptosis machinery by c-Jun N-terminal kinase in adult cardiac myocytes. J Biol Chem. 277:2002;10244-10250.
    • (2002) J Biol Chem , vol.277 , pp. 10244-10250
    • Aoki, H.1    Kang, P.M.2    Hampe, J.3    Yoshimura, K.4    Noma, T.5    Matsuzaki, M.6    Izumo, S.7
  • 19
    • 0033998888 scopus 로고    scopus 로고
    • Inhibition of the cardiac p38-MAPK pathway by SB203580 delays ischemic death
    • Barabcik M., Htun P., Strohm C., Kilian S., Schaper W. Inhibition of the cardiac p38-MAPK pathway by SB203580 delays ischemic death. J Cardiovasc Pharmacol. 35:2000;474-483.
    • (2000) J Cardiovasc Pharmacol , vol.35 , pp. 474-483
    • Barabcik, M.1    Htun, P.2    Strohm, C.3    Kilian, S.4    Schaper, W.5
  • 20
    • 0034875172 scopus 로고    scopus 로고
    • Involvement of protein kinase C-δ in DNA damage-induced apoptosis
    • Basu A., Woolard M.D., Johnson C.L. Involvement of protein kinase C-δ in DNA damage-induced apoptosis. Cell Death Differ. 8:2001;899-908.
    • (2001) Cell Death Differ , vol.8 , pp. 899-908
    • Basu, A.1    Woolard, M.D.2    Johnson, C.L.3
  • 21
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • Baud V., Karin M. Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol. 11:2001;372-377.
    • (2001) Trends Cell Biol , vol.11 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 23
    • 0034708504 scopus 로고    scopus 로고
    • Expression and functional analysis of Apaf-1 isoforms. Extra WD-40 repeat is required for cytochrome c binding and regulated activation of procaspase-9
    • Benedict M.A., Hu Y., Inohara N., Nunez G. Expression and functional analysis of Apaf-1 isoforms. Extra WD-40 repeat is required for cytochrome c binding and regulated activation of procaspase-9. J Biol Chem. 275:2000;8461-8468.
    • (2000) J Biol Chem , vol.275 , pp. 8461-8468
    • Benedict, M.A.1    Hu, Y.2    Inohara, N.3    Nunez, G.4
  • 24
  • 25
    • 0034957413 scopus 로고    scopus 로고
    • Effect of NF-κB inhibition on TNF-α-induced apoptosis and downstream pathways in cardiomyocytes
    • Bergmann M.W., Loser P., Dietz R., Von Harsdorf R. Effect of NF-κB inhibition on TNF-α-induced apoptosis and downstream pathways in cardiomyocytes. J Mol Cell Cardiol. 33:2001;1223-1232.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1223-1232
    • Bergmann, M.W.1    Loser, P.2    Dietz, R.3    Von Harsdorf, R.4
  • 26
    • 0030819138 scopus 로고    scopus 로고
    • Myocyte apoptosis during acute myocardial infarction in the mouse localizes to hypoxic regions but occurs independently of p53
    • Bialik S., Geenen D.L., Sasson I.E., Cheng R., Horner J.W., Evans S.M., Lord E.M., Koch C.J., Kitsis R.N. Myocyte apoptosis during acute myocardial infarction in the mouse localizes to hypoxic regions but occurs independently of p53. J Clin Invest. 100:1997;1363-1372.
    • (1997) J Clin Invest , vol.100 , pp. 1363-1372
    • Bialik, S.1    Geenen, D.L.2    Sasson, I.E.3    Cheng, R.4    Horner, J.W.5    Evans, S.M.6    Lord, E.M.7    Koch, C.J.8    Kitsis, R.N.9
  • 27
    • 0033520463 scopus 로고    scopus 로고
    • The mitochondrial apoptotic pathway is activated by serum and glucose deprivation in cardiac myocytes
    • Bialik S., Cryns V.L., Drincic A., Miyata S., Wollowick A.L., Srinivasan A., Kitsis R.N. The mitochondrial apoptotic pathway is activated by serum and glucose deprivation in cardiac myocytes. Circ Res. 85:1999;403-414.
    • (1999) Circ Res , vol.85 , pp. 403-414
    • Bialik, S.1    Cryns, V.L.2    Drincic, A.3    Miyata, S.4    Wollowick, A.L.5    Srinivasan, A.6    Kitsis, R.N.7
  • 28
    • 0034988898 scopus 로고    scopus 로고
    • Unwinding the loop of Bcl-2 phosphorylation
    • Blagosklonny M.V. Unwinding the loop of Bcl-2 phosphorylation. Leukemia. 15:2001;869-874.
    • (2001) Leukemia , vol.15 , pp. 869-874
    • Blagosklonny, M.V.1
  • 29
    • 0035971091 scopus 로고    scopus 로고
    • Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia. A mechanism of "pathological apoptosis"?
    • Blomgren K., Zhu C., Wang X., Karlsson J.-O., Leverin A.-L., Bahr B.A., Mallard C., Hagberg H. Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia. A mechanism of "pathological apoptosis"? J Biol Chem. 276:2001;10191-10198.
    • (2001) J Biol Chem , vol.276 , pp. 10191-10198
    • Blomgren, K.1    Zhu, C.2    Wang, X.3    Karlsson, J.-O.4    Leverin, A.-L.5    Bahr, B.A.6    Mallard, C.7    Hagberg, H.8
  • 30
    • 0035964964 scopus 로고    scopus 로고
    • Release of mitochondrial cytochrome c and activation of cytosolic caspases induced by myocardial ischaemia
    • Borutaite V., Budriumaite A., Morkuniene R., Brown G.C. Release of mitochondrial cytochrome c and activation of cytosolic caspases induced by myocardial ischaemia. Biochim Biophys Acta. 1537:2001;101-109.
    • (2001) Biochim Biophys Acta , vol.1537 , pp. 101-109
    • Borutaite, V.1    Budriumaite, A.2    Morkuniene, R.3    Brown, G.C.4
  • 32
    • 0031778992 scopus 로고    scopus 로고
    • Molecular aspects of myocarditis
    • Bowles N.E., Towbin J.A. Molecular aspects of myocarditis. Curr Opin Cardiol. 13:1998;179-184.
    • (1998) Curr Opin Cardiol , vol.13 , pp. 179-184
    • Bowles, N.E.1    Towbin, J.A.2
  • 33
    • 0035283038 scopus 로고    scopus 로고
    • Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes
    • Bratton S.B., Walker G., Srinivasula S.M., Sun X.M., Butterworth M., Alnemri E.S., Cohen G.M. Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes. EMBO J. 20:2001;998-1009.
    • (2001) EMBO J , vol.20 , pp. 998-1009
    • Bratton, S.B.1    Walker, G.2    Srinivasula, S.M.3    Sun, X.M.4    Butterworth, M.5    Alnemri, E.S.6    Cohen, G.M.7
  • 34
    • 0030803278 scopus 로고    scopus 로고
    • Fas- or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153
    • Brenner B., Koppenhoefer U., Weinstock C., Linderkamp O., Lang F., Gulbins E. Fas- or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153. J Biol Chem. 272:1997;22173-22181.
    • (1997) J Biol Chem , vol.272 , pp. 22173-22181
    • Brenner, B.1    Koppenhoefer, U.2    Weinstock, C.3    Linderkamp, O.4    Lang, F.5    Gulbins, E.6
  • 35
    • 0034644837 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor α mRNA stability by the mitogen-activated protein kinase p38 signalling cascade
    • Brook M., Sully G., Clark A.R., Saklatvala J. Regulation of tumour necrosis factor α mRNA stability by the mitogen-activated protein kinase p38 signalling cascade. FEBS Lett. 483:2000;57-61.
    • (2000) FEBS Lett , vol.483 , pp. 57-61
    • Brook, M.1    Sully, G.2    Clark, A.R.3    Saklatvala, J.4
  • 36
    • 0030134625 scopus 로고    scopus 로고
    • Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway
    • Brown J.L., Stowers L., Baer M., Trejo J., Coughlin S., Chant J. Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway. Curr Biol. 6:1996;598-605.
    • (1996) Curr Biol , vol.6 , pp. 598-605
    • Brown, J.L.1    Stowers, L.2    Baer, M.3    Trejo, J.4    Coughlin, S.5    Chant, J.6
  • 37
    • 0029128217 scopus 로고
    • Cardioprotective effect of insulin-like growth factor I in myocardial ischemia followed by reperfusion
    • Buerke M., Murohara T., Skurk C., Nuss C., Tomaselli K., Lefer A.M. Cardioprotective effect of insulin-like growth factor I in myocardial ischemia followed by reperfusion. Proc Natl Acad Sci USA. 92:1995;8031-8035.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8031-8035
    • Buerke, M.1    Murohara, T.2    Skurk, C.3    Nuss, C.4    Tomaselli, K.5    Lefer, A.M.6
  • 39
    • 0033551070 scopus 로고    scopus 로고
    • New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway
    • Cantley L.C., Neel B.G. New insights into tumor suppression: PTEN suppresses tumor formation by restraining the phosphoinositide 3-kinase/AKT pathway. Proc Natl Acad Sci USA. 96:1999;4240-4245.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4240-4245
    • Cantley, L.C.1    Neel, B.G.2
  • 40
    • 0030755579 scopus 로고    scopus 로고
    • The regulation of anoikis: MEKK1 activation requires cleavage by caspases
    • Cardone M.H., Salveson G.S., Widmann C., Johnson G., Frisch S.M. The regulation of anoikis: MEKK1 activation requires cleavage by caspases. Cell. 90:1997;315-323.
    • (1997) Cell , vol.90 , pp. 315-323
    • Cardone, M.H.1    Salveson, G.S.2    Widmann, C.3    Johnson, G.4    Frisch, S.M.5
  • 42
    • 0035504081 scopus 로고    scopus 로고
    • Transcriptional regulation of bcl-2 by nuclear factor κB and its significance in prostate cancer
    • Catz S.D., Johnson J.L. Transcriptional regulation of bcl-2 by nuclear factor κB and its significance in prostate cancer. Oncogene. 20:2001;7342-7351.
    • (2001) Oncogene , vol.20 , pp. 7342-7351
    • Catz, S.D.1    Johnson, J.L.2
  • 43
    • 0035800882 scopus 로고    scopus 로고
    • Oxidative stress-mediated cardiac cell death is a major determinant of ventricular dysfunction and failure in dog dilated cardiomyopathy
    • Cesselli D., Jakoniuk I., Barlucchi L., Beltrami A.P., Hintze T.H., Nadal-Ginard B., Kajstura J., Leri A., Anversa P. Oxidative stress-mediated cardiac cell death is a major determinant of ventricular dysfunction and failure in dog dilated cardiomyopathy. Circ Res. 89:2001;279-286.
    • (2001) Circ Res , vol.89 , pp. 279-286
    • Cesselli, D.1    Jakoniuk, I.2    Barlucchi, L.3    Beltrami, A.P.4    Hintze, T.H.5    Nadal-Ginard, B.6    Kajstura, J.7    Leri, A.8    Anversa, P.9
  • 47
    • 0034631789 scopus 로고    scopus 로고
    • Role of cAMP-dependent pathway in eosinophil apoptosis and survival
    • Chang H.S., Jeon K.W., Kim Y.H., Chung I.Y., Park C.S. Role of cAMP-dependent pathway in eosinophil apoptosis and survival. Cell Immunol. 203:2000;29-38.
    • (2000) Cell Immunol , vol.203 , pp. 29-38
    • Chang, H.S.1    Jeon, K.W.2    Kim, Y.H.3    Chung, I.Y.4    Park, C.S.5
  • 48
    • 0034970934 scopus 로고    scopus 로고
    • Opposing effects of δ and ε PKC in ethanol-induced cardioprotection
    • Chen C.-H., Mochly-Rosen D. Opposing effects of δ and ε PKC in ethanol-induced cardioprotection. J Mol Cell Cardiol. 33:2001;581-585.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 581-585
    • Chen, C.-H.1    Mochly-Rosen, D.2
  • 50
    • 0035903235 scopus 로고    scopus 로고
    • Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion
    • Chen M., He H., Zhan S., Krajewski S., Reed J.C., Gottlieb R.A. Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion. J Biol Chem. 276:2001;30724-30728.
    • (2001) J Biol Chem , vol.276 , pp. 30724-30728
    • Chen, M.1    He, H.2    Zhan, S.3    Krajewski, S.4    Reed, J.C.5    Gottlieb, R.A.6
  • 51
    • 0008996894 scopus 로고    scopus 로고
    • Overexpression of Bcl-2 attenuates apoptosis and protects against myocardial I/R injury in transgenic mice
    • Chen Z., Chua C.C., Ho Y.S., Hamdy R.C., Chua B.H. Overexpression of Bcl-2 attenuates apoptosis and protects against myocardial I/R injury in transgenic mice. Am J Physiol. 280:2001;H2313-H2320.
    • (2001) Am J Physiol , vol.280
    • Chen, Z.1    Chua, C.C.2    Ho, Y.S.3    Hamdy, R.C.4    Chua, B.H.5
  • 53
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • Chou J.J., Li H., Salvesen G.S., Yuan J., Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell. 96:1999;615-624.
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 54
    • 0035937797 scopus 로고    scopus 로고
    • A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis
    • Chu Z.-L., Pio F., Xie Z., Welsh K., Krajewska M., Krajewski S., Godzik A., Reed J.C. A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis. J Biol Chem. 276:2001;9239-9245.
    • (2001) J Biol Chem , vol.276 , pp. 9239-9245
    • Chu, Z.-L.1    Pio, F.2    Xie, Z.3    Welsh, K.4    Krajewska, M.5    Krajewski, S.6    Godzik, A.7    Reed, J.C.8
  • 55
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases
    • Chua B.T., Guo K., Li P. Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J Biol Chem. 275:2000;5131-5135.
    • (2000) J Biol Chem , vol.275 , pp. 5131-5135
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 56
    • 0034775233 scopus 로고    scopus 로고
    • Death by protein kinase C inhibitor: A stressful event
    • Clerk A. Death by protein kinase C inhibitor: a stressful event. J Mol Cell Cardiol. 33:2001;1773-1776.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1773-1776
    • Clerk, A.1
  • 57
    • 0032571270 scopus 로고    scopus 로고
    • Stimulation of "stress-regulated" mitogen-activated protein kinases (SAPKs/JNKs and p38-MAPKs) in perfused rat hearts by oxidative and other stresses
    • Clerk A., Fuller S.J., Michael A., Sugden P.H. Stimulation of "stress-regulated" mitogen-activated protein kinases (SAPKs/JNKs and p38-MAPKs) in perfused rat hearts by oxidative and other stresses. J Biol Chem. 273:1998;7228-7234.
    • (1998) J Biol Chem , vol.273 , pp. 7228-7234
    • Clerk, A.1    Fuller, S.J.2    Michael, A.3    Sugden, P.H.4
  • 58
    • 0032143920 scopus 로고    scopus 로고
    • Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes
    • Clerk A., Michael A., Sugden P.H. Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes. Biochem J. 333:1998;581-589.
    • (1998) Biochem J , vol.333 , pp. 581-589
    • Clerk, A.1    Michael, A.2    Sugden, P.H.3
  • 59
    • 0032578406 scopus 로고    scopus 로고
    • Norepinephrine stimulates apoptosis in adult ventricular myocytes by activation of the β-adrenergic pathway
    • Communal C., Singh K., Pimental D.R., Colucci W.S. Norepinephrine stimulates apoptosis in adult ventricular myocytes by activation of the β-adrenergic pathway. Circulation. 98:1998;1329-1334.
    • (1998) Circulation , vol.98 , pp. 1329-1334
    • Communal, C.1    Singh, K.2    Pimental, D.R.3    Colucci, W.S.4
  • 60
    • 0032729995 scopus 로고    scopus 로고
    • 2-adrenergic receptors on cardiac myocyte apoptosis: Role of a pertussis toxin-sensitive G protein
    • 2-adrenergic receptors on cardiac myocyte apoptosis: role of a pertussis toxin-sensitive G protein. Circulation. 100:1999;2210-2212.
    • (1999) Circulation , vol.100 , pp. 2210-2212
    • Communal, C.1    Singh, K.2    Sawyer, D.B.3    Colucci, W.S.4
  • 63
    • 0033774569 scopus 로고    scopus 로고
    • Failure of Bcl-2 family members to interact with Apaf-1 in normal and apoptotic cells
    • Conus S., Rosse T., Borner C. Failure of Bcl-2 family members to interact with Apaf-1 in normal and apoptotic cells. Cell Death Differ. 7:2000;947-954.
    • (2000) Cell Death Differ , vol.7 , pp. 947-954
    • Conus, S.1    Rosse, T.2    Borner, C.3
  • 64
    • 0032745819 scopus 로고    scopus 로고
    • Regulation of Bcl-2 family proteins during development and in response to oxidative stress in cardiac myocytes: Association with changes in mitochondrial membrane potential
    • Cook S.A., Sugden P.H., Clerk A. Regulation of Bcl-2 family proteins during development and in response to oxidative stress in cardiac myocytes: association with changes in mitochondrial membrane potential. Circ Res. 85:1999;940-949.
    • (1999) Circ Res , vol.85 , pp. 940-949
    • Cook, S.A.1    Sugden, P.H.2    Clerk, A.3
  • 65
    • 0032485854 scopus 로고    scopus 로고
    • Multiple conformations of physiological membrane-bound cytochrome c
    • Cortese J.D., Voglino A.L., Hackenbrock C.R. Multiple conformations of physiological membrane-bound cytochrome c. Biochemistry. 37:1998;6402-6409.
    • (1998) Biochemistry , vol.37 , pp. 6402-6409
    • Cortese, J.D.1    Voglino, A.L.2    Hackenbrock, C.R.3
  • 66
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J. 341:1999;233-249.
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 67
    • 0030701527 scopus 로고    scopus 로고
    • Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy
    • Cryns V.L., Byun Y., Rana A., Mellor H., Lustig K.D., Ghanem L., Parker P.J., Kirschner M.W., Yuan J. Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy. J Biol Chem. 272:1997;29449-29453.
    • (1997) J Biol Chem , vol.272 , pp. 29449-29453
    • Cryns, V.L.1    Byun, Y.2    Rana, A.3    Mellor, H.4    Lustig, K.D.5    Ghanem, L.6    Parker, P.J.7    Kirschner, M.W.8    Yuan, J.9
  • 68
    • 0023654014 scopus 로고
    • Purification and characterization of the potent endonuclease in extracts of bovine heart mitochondria
    • Cummings O.W., King T.C., Holden J.A., Low R.L. Purification and characterization of the potent endonuclease in extracts of bovine heart mitochondria. J Biol Chem. 262:1987;2005-2015.
    • (1987) J Biol Chem , vol.262 , pp. 2005-2015
    • Cummings, O.W.1    King, T.C.2    Holden, J.A.3    Low, R.L.4
  • 69
    • 0030795091 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of protein kinase C θ in induction of apoptosis
    • Datta R., Kojima H., Yoshida K., Kufe D. Caspase-3-mediated cleavage of protein kinase C θ in induction of apoptosis. J Biol Chem. 272:1997;20317-20320.
    • (1997) J Biol Chem , vol.272 , pp. 20317-20320
    • Datta, R.1    Kojima, H.2    Yoshida, K.3    Kufe, D.4
  • 70
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • Datta S.R., Katsov A., Hu L., Petros A., Fesik A., Yaffe M.B., Greenberg M.E. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol Cell. 6:2000;41-51.
    • (2000) Mol Cell , vol.6 , pp. 41-51
    • Datta, S.R.1    Katsov, A.2    Hu, L.3    Petros, A.4    Fesik, A.5    Yaffe, M.B.6    Greenberg, M.E.7
  • 71
    • 0034617449 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): A ubiquitous mitochondrial oxidoreductase involved in apoptosis
    • Daugas E., Nochy D., Ravagnan L., Loeffler M., Susin S.A., Zamzami N., Kroemer G. Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis. FEBS Lett. 476:2000;118-123.
    • (2000) FEBS Lett , vol.476 , pp. 118-123
    • Daugas, E.1    Nochy, D.2    Ravagnan, L.3    Loeffler, M.4    Susin, S.A.5    Zamzami, N.6    Kroemer, G.7
  • 72
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J. 351:2000;95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 73
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis R.J. Signal transduction by the JNK group of MAP kinases. Cell. 103:2000;239-252.
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 74
    • 0036144679 scopus 로고    scopus 로고
    • Caspase activation and disruption of mitochondrial membrane potential during UV radiation-induced apoptosis of human keratinocytes requires activation of protein kinase C
    • Denning M.F., Wang Y., Tobudin S., Alkan S., Nickoloff B.J., Qin J.Z. Caspase activation and disruption of mitochondrial membrane potential during UV radiation-induced apoptosis of human keratinocytes requires activation of protein kinase C. Cell Death Differ. 9:2002;40-52.
    • (2002) Cell Death Differ , vol.9 , pp. 40-52
    • Denning, M.F.1    Wang, Y.2    Tobudin, S.3    Alkan, S.4    Nickoloff, B.J.5    Qin, J.Z.6
  • 76
    • 0033215040 scopus 로고    scopus 로고
    • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    • Deveraux Q.L., Leo E., Stennicker H.R., Welsh K., Salvesen G.S., Reed J.C. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J. 18:1999;5242-5251.
    • (1999) EMBO J , vol.18 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicker, H.R.3    Welsh, K.4    Salvesen, G.S.5    Reed, J.C.6
  • 77
    • 0033982992 scopus 로고    scopus 로고
    • Calcineurin-mediated hypertrophy protects cardiomyocytes from apoptosis in vitro and in vivo: An apoptosis-independent model of dilated heart failure
    • De Windt L.J., Lim H.W., Taigen T., Wencker D., Condorelli G., Dorn G.W. II, Kitsis R.N., Molkentin J.D. Calcineurin-mediated hypertrophy protects cardiomyocytes from apoptosis in vitro and in vivo: an apoptosis-independent model of dilated heart failure. Circ Res. 86:2000;255-263.
    • (2000) Circ Res , vol.86 , pp. 255-263
    • De Windt, L.J.1    Lim, H.W.2    Taigen, T.3    Wencker, D.4    Condorelli, G.5    Dorn G.W. II6    Kitsis, R.N.7    Molkentin, J.D.8
  • 78
    • 0034683031 scopus 로고    scopus 로고
    • Status of myocardial antioxidants in ischemia-reperfusion injury
    • Dhalla N.S., Elmoselhi A.B., Hata T., Makino N. Status of myocardial antioxidants in ischemia-reperfusion injury. Cardiovasc Res. 47:2000;446-456.
    • (2000) Cardiovasc Res , vol.47 , pp. 446-456
    • Dhalla, N.S.1    Elmoselhi, A.B.2    Hata, T.3    Makino, N.4
  • 80
    • 0037086678 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinase promotes survival of cardiac myocytes after oxidative stress
    • Dougherty C.J., Kubasiak L.A., Prentice H., Andreka P., Bishopric N.H., Webster K.A. Activation of c-Jun N-terminal kinase promotes survival of cardiac myocytes after oxidative stress. Biochem J. 362:2002;561-571.
    • (2002) Biochem J , vol.362 , pp. 561-571
    • Dougherty, C.J.1    Kubasiak, L.A.2    Prentice, H.3    Andreka, P.4    Bishopric, N.H.5    Webster, K.A.6
  • 82
    • 0034671217 scopus 로고    scopus 로고
    • Identification of a caspase-2 isoform that behaves as an endogenous inhibitor of the caspase cascade
    • Droin N., Beauchemin M., Solary E., Bertrand R. Identification of a caspase-2 isoform that behaves as an endogenous inhibitor of the caspase cascade. Cancer Res. 60:2000;7039-7047.
    • (2000) Cancer Res , vol.60 , pp. 7039-7047
    • Droin, N.1    Beauchemin, M.2    Solary, E.3    Bertrand, R.4
  • 83
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 102:2000;33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 86
    • 0033539994 scopus 로고    scopus 로고
    • ARC inhibits cytochrome c release from mitochondria and protects against hypoxia-induced apoptosis in heart-derived H9c2 cells
    • Ekhterae D., Lin Z., Lundberg M.S., Crow M.T., Brosius F.C., Nunez G. ARC inhibits cytochrome c release from mitochondria and protects against hypoxia-induced apoptosis in heart-derived H9c2 cells. Circ Res. 85:1999;70-77.
    • (1999) Circ Res , vol.85 , pp. 70-77
    • Ekhterae, D.1    Lin, Z.2    Lundberg, M.S.3    Crow, M.T.4    Brosius, F.C.5    Nunez, G.6
  • 87
    • 0033837033 scopus 로고    scopus 로고
    • Unresolved issues regarding the role of apoptosis in the pathogenesis of ischemic injury and heart failure
    • Elsä A., Suzuki K., Schaper J. Unresolved issues regarding the role of apoptosis in the pathogenesis of ischemic injury and heart failure. J Mol Cell Cardiol. 32:2000;711-724.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 711-724
    • Elsä, A.1    Suzuki, K.2    Schaper, J.3
  • 89
    • 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. 20:2000;929-935.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.-C.4
  • 90
    • 0033581927 scopus 로고    scopus 로고
    • Regulation of BAD phosphorylation by the Ras/mitogen-activated protein kinase pathway
    • Fang X., Yu S., Eder A., Mao M., Bast R.C. Jr., Boyd D., Mills G.B. Regulation of BAD phosphorylation by the Ras/mitogen-activated protein kinase pathway. Oncogene. 18:1999;6635-6640.
    • (1999) Oncogene , vol.18 , pp. 6635-6640
    • Fang, X.1    Yu, S.2    Eder, A.3    Mao, M.4    Bast R.C., Jr.5    Boyd, D.6    Mills, G.B.7
  • 92
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K.F., Kroemer G. Organelle-specific initiation of cell death pathways. Nat Cell Biol. 3:2001;E255-E263.
    • (2001) Nat Cell Biol , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 96
    • 0035671710 scopus 로고    scopus 로고
    • Cardiomyocyte apoptotic cell death in arterial hypertension: Mechanisms and potential management
    • Fortuno M.A., Ravassa S., Fortuno A., Zalba G., Diez J. Cardiomyocyte apoptotic cell death in arterial hypertension: mechanisms and potential management. Hypertension. 38:2001;1406-1412.
    • (2001) Hypertension , vol.38 , pp. 1406-1412
    • Fortuno, M.A.1    Ravassa, S.2    Fortuno, A.3    Zalba, G.4    Diez, J.5
  • 97
    • 0040175067 scopus 로고    scopus 로고
    • Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction
    • Frodin M., Gammeltoft S. Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction. Mol Cell Endocrinol. 151:1999;65-77.
    • (1999) Mol Cell Endocrinol , vol.151 , pp. 65-77
    • Frodin, M.1    Gammeltoft, S.2
  • 98
    • 0033574277 scopus 로고    scopus 로고
    • Cleavage of ζPKC but not λ/ιPKC by caspase-3 during UV-induced apoptosis
    • Frutos S., Moscat J., Diaz-Meco M.T. Cleavage of ζPKC but not λ/ιPKC by caspase-3 during UV-induced apoptosis. J Biol Chem. 274:1999;10765-10770.
    • (1999) J Biol Chem , vol.274 , pp. 10765-10770
    • Frutos, S.1    Moscat, J.2    Diaz-Meco, M.T.3
  • 99
    • 0034651983 scopus 로고    scopus 로고
    • Akt promotes survival of myocytes in vitro and protects against ischemia-reperfusion injury in mouse heart
    • Fujio Y., Nguyen T., Wencker D., Kitsis R.N., Walsh K. Akt promotes survival of myocytes in vitro and protects against ischemia-reperfusion injury in mouse heart. Circulation. 101:2000;660-667.
    • (2000) Circulation , vol.101 , pp. 660-667
    • Fujio, Y.1    Nguyen, T.2    Wencker, D.3    Kitsis, R.N.4    Walsh, K.5
  • 102
    • 0033837293 scopus 로고    scopus 로고
    • ATP in the heart - What happens, and what does not happen
    • ATP in the heart - what happens, and what does not happen. Basic Res Cardiol. 95:2000;275-279.
    • (2000) Basic Res Cardiol , vol.95 , pp. 275-279
    • Garlid, K.D.1
  • 103
    • 0033080402 scopus 로고    scopus 로고
    • Transcriptional regulation of the p21(WAF1/CIP1) gene
    • Gartel A.L., Tyner A.L. Transcriptional regulation of the p21(WAF1/CIP1) gene. Exp Cell Res. 246:1999;280-289.
    • (1999) Exp Cell Res , vol.246 , pp. 280-289
    • Gartel, A.L.1    Tyner, A.L.2
  • 104
    • 12644268232 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase C δ by an ICE/CED 3-like protease induces characteristics of apoptosis
    • Ghayur T. Proteolytic activation of protein kinase C δ by an ICE/CED 3-like protease induces characteristics of apoptosis. J Exp Med. 184:1996;2399-2404.
    • (1996) J Exp Med , vol.184 , pp. 2399-2404
    • Ghayur, T.1
  • 105
    • 0034879150 scopus 로고    scopus 로고
    • Transcriptional regulation of the BCL-X gene by NF-κB is an element of hypoxic responses in the rat brain
    • Glasgow J.N., Qiu J., Rassin D., Grafe M., Wood T., Perez-Pol J.R. Transcriptional regulation of the BCL-X gene by NF-κB is an element of hypoxic responses in the rat brain. Neurochem Res. 26:2001;359-647.
    • (2001) Neurochem Res , vol.26 , pp. 359-647
    • Glasgow, J.N.1    Qiu, J.2    Rassin, D.3    Grafe, M.4    Wood, T.5    Perez-Pol, J.R.6
  • 106
    • 0028170778 scopus 로고
    • Bcl-xL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria
    • Gonzalez-Garcia M., Perez-Ballestero R., Ding L., Duan L., Boise L.H., Thompson C.B., Nunez G. Bcl-xL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria. Development. 120:1994;3033-3042.
    • (1994) Development , vol.120 , pp. 3033-3042
    • Gonzalez-Garcia, M.1    Perez-Ballestero, R.2    Ding, L.3    Duan, L.4    Boise, L.H.5    Thompson, C.B.6    Nunez, G.7
  • 108
    • 0029885316 scopus 로고    scopus 로고
    • Preconditioning in rabbit cardiomyocytes: Role of pH, vacuolar proton ATPase, and apoptosis
    • Gottlieb R.A., Gruol D.L., Zhu J.Y., Engler R.L. Preconditioning in rabbit cardiomyocytes: role of pH, vacuolar proton ATPase, and apoptosis. J Clin Invest. 97:1996;2391-2398.
    • (1996) J Clin Invest , vol.97 , pp. 2391-2398
    • Gottlieb, R.A.1    Gruol, D.L.2    Zhu, J.Y.3    Engler, R.L.4
  • 109
    • 0035937420 scopus 로고    scopus 로고
    • Cell death inhibition: Keeping caspases in check
    • Goyal L. Cell death inhibition: keeping caspases in check. Cell. 104:2001;805-808.
    • (2001) Cell , vol.104 , pp. 805-808
    • Goyal, L.1
  • 110
    • 0034616946 scopus 로고    scopus 로고
    • Apoptotic pathways: Paper wraps stone blunts scissors
    • Green D.R. Apoptotic pathways: paper wraps stone blunts scissors. Cell. 102:2001;1-4.
    • (2001) Cell , vol.102 , pp. 1-4
    • Green, D.R.1
  • 111
    • 0035891057 scopus 로고    scopus 로고
    • Cellular amage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak
    • Griffiths G.J., Corfe B.M., Savory P., Leech S., Esposti M.D., Hickman J.A., Dive C. Cellular amage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak. Oncogene. 20:2001;7668-7676.
    • (2001) Oncogene , vol.20 , pp. 7668-7676
    • Griffiths, G.J.1    Corfe, B.M.2    Savory, P.3    Leech, S.4    Esposti, M.D.5    Hickman, J.A.6    Dive, C.7
  • 113
    • 0034806590 scopus 로고    scopus 로고
    • CREB DNA binding activity is inhibited by glycogen synthase kinase-3β and facilitated by lithium
    • Grimes C.A., Jope R.S. CREB DNA binding activity is inhibited by glycogen synthase kinase-3β and facilitated by lithium. J Neurochem. 78:2001;1219-1232.
    • (2001) J Neurochem , vol.78 , pp. 1219-1232
    • Grimes, C.A.1    Jope, R.S.2
  • 115
    • 0033841726 scopus 로고    scopus 로고
    • ATP channels in cardioprotection
    • ATP channels in cardioprotection. Basic Res Cardiol. 95:2000;280-284.
    • (2000) Basic Res Cardiol , vol.95 , pp. 280-284
    • Gross, G.J.1
  • 116
    • 0034522342 scopus 로고    scopus 로고
    • Caspases: Key players in programmed cell death
    • Grütter M.G. Caspases: key players in programmed cell death. Curr Opin Cell Biol. 10:2000;649-655.
    • (2000) Curr Opin Cell Biol , vol.10 , pp. 649-655
    • Grütter, M.G.1
  • 118
    • 10244219861 scopus 로고    scopus 로고
    • Fas-induced apoptosis is mediated by activation of a Ras and Rac protein-regulated signaling pathway
    • Gulbins E., Coggeshall K.M., Brenner B., Schlottmann K., Linderkamp O., Lang F. Fas-induced apoptosis is mediated by activation of a Ras and Rac protein-regulated signaling pathway. J Biol Chem. 271:1996;26389-26394.
    • (1996) J Biol Chem , vol.271 , pp. 26389-26394
    • Gulbins, E.1    Coggeshall, K.M.2    Brenner, B.3    Schlottmann, K.4    Linderkamp, O.5    Lang, F.6
  • 120
    • 0035834279 scopus 로고    scopus 로고
    • Molecular steps of death receptor and mitochondrial pathways of apoptosis
    • Gupta S. Molecular steps of death receptor and mitochondrial pathways of apoptosis. Life Sci. 69:2001;2957-2964.
    • (2001) Life Sci , vol.69 , pp. 2957-2964
    • Gupta, S.1
  • 121
    • 0035859956 scopus 로고    scopus 로고
    • P70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD
    • Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J. p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD. Proc Natl Acad Sci USA. 98:2001;9666-9670.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9666-9670
    • Harada, H.1    Andersen, J.S.2    Mann, M.3    Terada, N.4    Korsmeyer, S.J.5
  • 123
    • 0032478614 scopus 로고    scopus 로고
    • Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist
    • Hegde R., Srinivasula S.M., Ahmad M., Fernandes-Alnemri R., Alnemri E.S. Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist. J Biol Chem. 273:1998;7783-7786.
    • (1998) J Biol Chem , vol.273 , pp. 7783-7786
    • Hegde, R.1    Srinivasula, S.M.2    Ahmad, M.3    Fernandes-Alnemri, R.4    Alnemri, E.S.5
  • 125
    • 0035834817 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase C-ε and δ in neonatal rat ventricular myocytes
    • Heidkamp M.C., Bayer A.L., Martin J.L., Samarel A.M. Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase C-ε and δ in neonatal rat ventricular myocytes. Circ Res. 89:2001;882-890.
    • (2001) Circ Res , vol.89 , pp. 882-890
    • Heidkamp, M.C.1    Bayer, A.L.2    Martin, J.L.3    Samarel, A.M.4
  • 126
    • 0034749317 scopus 로고    scopus 로고
    • Apoptosis of ventricular and atrial myocytes from pacing-induced canine heart failure
    • Heinke M.Y., Yao M., Chang D., Einstein R., Dos Remedios C.G. Apoptosis of ventricular and atrial myocytes from pacing-induced canine heart failure. Cardiovasc Res. 49:2001;127-134.
    • (2001) Cardiovasc Res , vol.49 , pp. 127-134
    • Heinke, M.Y.1    Yao, M.2    Chang, D.3    Einstein, R.4    Dos Remedios, C.G.5
  • 127
    • 0033675205 scopus 로고    scopus 로고
    • Low catecholamine concentrations protect adult rat ventricular myocytes against apoptosis through cAMP-dependent extracellular signal-regulated kinase activation
    • Henaff M., Hatem S.N., Mercadier J.J. Low catecholamine concentrations protect adult rat ventricular myocytes against apoptosis through cAMP-dependent extracellular signal-regulated kinase activation. Mol Pharmacol. 58:2000;1546-1553.
    • (2000) Mol Pharmacol , vol.58 , pp. 1546-1553
    • Henaff, M.1    Hatem, S.N.2    Mercadier, J.J.3
  • 129
    • 0032536519 scopus 로고    scopus 로고
    • Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis
    • Hirata H., Takahashi A., Kohayashi S., Yonehara S., Sawai H., Okazaki T., Yamamoto K., Sasada M. Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. J Exp Med. 187:1998;587-600.
    • (1998) J Exp Med , vol.187 , pp. 587-600
    • Hirata, H.1    Takahashi, A.2    Kohayashi, S.3    Yonehara, S.4    Sawai, H.5    Okazaki, T.6    Yamamoto, K.7    Sasada, M.8
  • 130
    • 0033575142 scopus 로고    scopus 로고
    • 2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis
    • 2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis. J Biol Chem. 274:1999;20415-20420.
    • (1999) J Biol Chem , vol.274 , pp. 20415-20420
    • Hirotani, M.1    Zhang, Y.2    Fujita, N.3    Naito, M.4    Tsuruo, T.5
  • 132
    • 0032870898 scopus 로고    scopus 로고
    • Caspase inhibition reduces myocyte cell death induced by myocardial ischemia and reperfusion in vivo
    • Holly T.A., Drincic A., Byun Y., Nakamura S., Harris K., Klocke F.J., Cryns V.L. Caspase inhibition reduces myocyte cell death induced by myocardial ischemia and reperfusion in vivo. J Mol Cell Cardiol. 31:1999;1709-1715.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 1709-1715
    • Holly, T.A.1    Drincic, A.2    Byun, Y.3    Nakamura, S.4    Harris, K.5    Klocke, F.J.6    Cryns, V.L.7
  • 133
    • 0035951395 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 protects H9c2 cardiac myoblasts from oxidative stress-induced apoptosis via phosphatidylinositol 3-kinase and extracellular signal-regulated kinase pathways
    • Hong F., Kwon S.J., Jhun B.S., Kim S.S., Ha J., Kim S.J., Sohn N.W., Kang C., Kang I. Insulin-like growth factor-1 protects H9c2 cardiac myoblasts from oxidative stress-induced apoptosis via phosphatidylinositol 3-kinase and extracellular signal-regulated kinase pathways. Life Sci. 68:2001;1095-1105.
    • (2001) Life Sci , vol.68 , pp. 1095-1105
    • Hong, F.1    Kwon, S.J.2    Jhun, B.S.3    Kim, S.S.4    Ha, J.5    Kim, S.J.6    Sohn, N.W.7    Kang, C.8    Kang, I.9
  • 134
    • 0035872242 scopus 로고    scopus 로고
    • Selective degradation of the PKC-ε isoform during cell death in AKR-2B fibroblasts
    • Hoppe J., Hoppe V., Schafer R. Selective degradation of the PKC-ε isoform during cell death in AKR-2B fibroblasts. Exp Cell Res. 266:2001;64-73.
    • (2001) Exp Cell Res , vol.266 , pp. 64-73
    • Hoppe, J.1    Hoppe, V.2    Schafer, R.3
  • 135
    • 0034674259 scopus 로고    scopus 로고
    • Dominant expression of a novel splice variant of caspase-8 in human peripheral blood lymphocytes
    • Horiuchi T., Himeji D., Tsukamoto H., Harashima S., Hayashi K. Dominant expression of a novel splice variant of caspase-8 in human peripheral blood lymphocytes. Biochem Biophys Res Commun. 272:2000;877-881.
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 877-881
    • Horiuchi, T.1    Himeji, D.2    Tsukamoto, H.3    Harashima, S.4    Hayashi, K.5
  • 136
    • 0035065271 scopus 로고    scopus 로고
    • Inhibition of c-Jun N-terminal kinase 1, but not c-Jun N-terminal kinase 2, suppresses apoptosis induced by ischemia/reoxygenation in rat cardiac myocytes
    • Hreniuk D., Garay M., Gaarde W., Monia B.P., McKay R.A., Ioffi C.L. Inhibition of c-Jun N-terminal kinase 1, but not c-Jun N-terminal kinase 2, suppresses apoptosis induced by ischemia/reoxygenation in rat cardiac myocytes. Mol Pharmacol. 59:2001;867-874.
    • (2001) Mol Pharmacol , vol.59 , pp. 867-874
    • Hreniuk, D.1    Garay, M.2    Gaarde, W.3    Monia, B.P.4    McKay, R.A.5    Ioffi, C.L.6
  • 138
    • 0034720786 scopus 로고    scopus 로고
    • Prolonged survival of heart allografts from p53-deficient mice
    • Hu Y., Zou Y., Hala M., Deitrich H., Wick G., Xu Q. Prolonged survival of heart allografts from p53-deficient mice. Transplantation. 69:2000;2634-2640.
    • (2000) Transplantation , vol.69 , pp. 2634-2640
    • Hu, Y.1    Zou, Y.2    Hala, M.3    Deitrich, H.4    Wick, G.5    Xu, Q.6
  • 139
    • 0030465072 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
    • Huang B., Eberstadt M., Olejniczak E.T., Meadows R.P., Fesid S.W. NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain. Nature. 384:1996;638-641.
    • (1996) Nature , vol.384 , pp. 638-641
    • Huang, B.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Fesid, S.W.5
  • 140
    • 0033635733 scopus 로고    scopus 로고
    • BH3-only proteins - Essential initiators of apoptotic cell death
    • Huang D.C.S., Strasser A. BH3-only proteins - essential initiators of apoptotic cell death. Cell. 103:2000;839-842.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.S.1    Strasser, A.2
  • 141
    • 0032481346 scopus 로고    scopus 로고
    • The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4
    • Huang D.C.S., Adams J.M., Cory S. The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. EMBO J. 17:1998;1029-1039.
    • (1998) EMBO J , vol.17 , pp. 1029-1039
    • Huang, D.C.S.1    Adams, J.M.2    Cory, S.3
  • 142
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • Huang Y., Wang K.K.W. The calpain family and human disease. Trends Mol Med. 7:2001;355-362.
    • (2001) Trends Mol Med , vol.7 , pp. 355-362
    • Huang, Y.1    Wang, K.K.W.2
  • 143
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain
    • Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., Wu H. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell. 104:2001;781-790.
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4    Myszka, D.G.5    Wu, H.6
  • 144
    • 0032546783 scopus 로고    scopus 로고
    • ERICE, a novel FLICE-activatable caspase
    • Humke E.W., Ni J., Dixit V.M. ERICE, a novel FLICE-activatable caspase. J Biol Chem. 273:1998;15702-15707.
    • (1998) J Biol Chem , vol.273 , pp. 15702-15707
    • Humke, E.W.1    Ni, J.2    Dixit, V.M.3
  • 147
    • 0033593596 scopus 로고    scopus 로고
    • Modulation of cytokine-induced cardiac myocyte apoptosis by nitric oxide, Bad, and Bcl-x
    • Ing D.J., Zang J., Dzau V.J., Webster K.A., Bishopric N.H. Modulation of cytokine-induced cardiac myocyte apoptosis by nitric oxide, Bad, and Bcl-x. Circ Res. 84:1999;21-33.
    • (1999) Circ Res , vol.84 , pp. 21-33
    • Ing, D.J.1    Zang, J.2    Dzau, V.J.3    Webster, K.A.4    Bishopric, N.H.5
  • 148
    • 0032546795 scopus 로고    scopus 로고
    • Caspase-3 is required for α-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis
    • Janicke R.U., Ng P., Sprengart M.L., Porter A.G. Caspase-3 is required for α-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J Biol Chem. 273:1998;15540-15545.
    • (1998) J Biol Chem , vol.273 , pp. 15540-15545
    • Janicke, R.U.1    Ng, P.2    Sprengart, M.L.3    Porter, A.G.4
  • 149
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • Janicke R.U., Sprengart M.L., Wati M.R., Porter A.G. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J Biol Chem. 273:1998;9357-9360.
    • (1998) J Biol Chem , vol.273 , pp. 9357-9360
    • Janicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 150
    • 0033522889 scopus 로고    scopus 로고
    • The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD
    • Jeong E.-J., Bang S., Lee T.H., Park Y.I., Sim W.-S., Kim K.-S. The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. J Biol Chem. 274:1999;16337-16342.
    • (1999) J Biol Chem , vol.274 , pp. 16337-16342
    • Jeong, E.-J.1    Bang, S.2    Lee, T.H.3    Park, Y.I.4    Sim, W.-S.5    Kim, K.-S.6
  • 152
    • 0034613302 scopus 로고    scopus 로고
    • Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1
    • Jiang X., Wang X. Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1. J Biol Chem. 275:2000;31199-31203.
    • (2000) J Biol Chem , vol.275 , pp. 31199-31203
    • Jiang, X.1    Wang, X.2
  • 153
    • 0034967218 scopus 로고    scopus 로고
    • Bax κ, a novel Bax splice variant from ischemic rat brain lacking an ART domain, promotes neuronal cell death
    • Jin K.L., Graham S.H., Mao X.O., He X., Nagayama T., Simon R.P., Greenberg D.A. Bax κ, a novel Bax splice variant from ischemic rat brain lacking an ART domain, promotes neuronal cell death. J Neurochem. 77:2001;1508-1519.
    • (2001) J Neurochem , vol.77 , pp. 1508-1519
    • Jin, K.L.1    Graham, S.H.2    Mao, X.O.3    He, X.4    Nagayama, T.5    Simon, R.P.6    Greenberg, D.A.7
  • 154
    • 0033841763 scopus 로고    scopus 로고
    • Insulin administered at reoxygenation exerts a cardioprotective effect in myocytes by a possible anti-apoptotic mechanism
    • Jonassen A.K., Brar B.K., Mjos O.D., Sack M.N., Latchman D.S., Yellon D.M. Insulin administered at reoxygenation exerts a cardioprotective effect in myocytes by a possible anti-apoptotic mechanism. J Mol Cell Cardiol. 32:2000;757-764.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 757-764
    • Jonassen, A.K.1    Brar, B.K.2    Mjos, O.D.3    Sack, M.N.4    Latchman, D.S.5    Yellon, D.M.6
  • 157
    • 0034625535 scopus 로고    scopus 로고
    • Apoptosis and heart failure: A critical review of the literature
    • Kang P.M., Izumo S. Apoptosis and heart failure: a critical review of the literature. Circ Res. 86:2000;1107-1113.
    • (2000) Circ Res , vol.86 , pp. 1107-1113
    • Kang, P.M.1    Izumo, S.2
  • 158
    • 0034698118 scopus 로고    scopus 로고
    • Morphological and molecular characterization of adult cardiomyocyte apoptosis during hypoxia and reoxygenation
    • Kang P.M., Haunstetter A., Aoki H., Usheva A., Izumo S. Morphological and molecular characterization of adult cardiomyocyte apoptosis during hypoxia and reoxygenation. Circ Res. 87:2000;118-125.
    • (2000) Circ Res , vol.87 , pp. 118-125
    • Kang, P.M.1    Haunstetter, A.2    Aoki, H.3    Usheva, A.4    Izumo, S.5
  • 159
    • 0035377522 scopus 로고    scopus 로고
    • Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension
    • Kataoka T., Holler N., Micheau O., Martinou F., Tinel A., Hofmann K., Tschopp J. Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension. J Biol Chem. 276:2001;19548-19554.
    • (2001) J Biol Chem , vol.276 , pp. 19548-19554
    • Kataoka, T.1    Holler, N.2    Micheau, O.3    Martinou, F.4    Tinel, A.5    Hofmann, K.6    Tschopp, J.7
  • 160
    • 0035190026 scopus 로고    scopus 로고
    • Cellular function of phosphoinositide 3-kinases: Implications for development, homeostasis, and cancer
    • Katso R., Okkenhaug K., Ahmadi K., White S., Timms J., Waterfield M.D. Cellular function of phosphoinositide 3-kinases: implications for development, homeostasis, and cancer. Annu Rev Cell Dev Biol. 17:2001;615-675.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 615-675
    • Katso, R.1    Okkenhaug, K.2    Ahmadi, K.3    White, S.4    Timms, J.5    Waterfield, M.D.6
  • 161
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: The role of the BH3 domain in apoptosis
    • Kelekar A., Thompson C.B. Bcl-2-family proteins: the role of the BH3 domain in apoptosis. Trends Cell Biol. 8:1998;324-330.
    • (1998) Trends Cell Biol , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 162
    • 0032525052 scopus 로고    scopus 로고
    • Phosphorylation of FADD/MORT1 and Fas by kinases that associate with the membrane-proximal cytoplasmic domain of Fas
    • Kennedy N.J., Budd R.C. Phosphorylation of FADD/MORT1 and Fas by kinases that associate with the membrane-proximal cytoplasmic domain of Fas. J Immunol. 160:1998;4881-4888.
    • (1998) J Immunol , vol.160 , pp. 4881-4888
    • Kennedy, N.J.1    Budd, R.C.2
  • 163
    • 0034096201 scopus 로고    scopus 로고
    • Protein phosphatases and the regulation of mitogen-activated protein kinase signalling
    • Keyse S.M. Protein phosphatases and the regulation of mitogen-activated protein kinase signalling. Curr Opin Cell Biol. 12:2000;186-192.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 186-192
    • Keyse, S.M.1
  • 165
    • 0030870555 scopus 로고    scopus 로고
    • The bcl-2 gene product prevents programmed cell death of ventricular myocytes
    • Kirshenbaum L.A., de Moissac D. The bcl-2 gene product prevents programmed cell death of ventricular myocytes. Circulation. 96:1997;1580-1585.
    • (1997) Circulation , vol.96 , pp. 1580-1585
    • Kirshenbaum, L.A.1    De Moissac, D.2
  • 166
    • 0035846605 scopus 로고    scopus 로고
    • Consequences of brief ischemia: Stunning preconditioning, and their clinical implications: Part 1
    • Kloner R.A., Jennings R.B. Consequences of brief ischemia: stunning preconditioning, and their clinical implications: part 1. Circulation. 104:2001;2981-2989.
    • (2001) Circulation , vol.104 , pp. 2981-2989
    • Kloner, R.A.1    Jennings, R.B.2
  • 167
    • 0035909985 scopus 로고    scopus 로고
    • Consequences of brief ischemia: Stunning, preconditioning, and their clinical implications: Part 2
    • Kloner R.A., Jennings R.B. Consequences of brief ischemia: stunning, preconditioning, and their clinical implications: part 2. Circulation. 104:2001;3158-3167.
    • (2001) Circulation , vol.104 , pp. 3158-3167
    • Kloner, R.A.1    Jennings, R.B.2
  • 168
    • 0034801418 scopus 로고    scopus 로고
    • Evidence that caspase-13 is not a human but a bovine gene
    • Koenig U., Eckhart L., Tschachler E. Evidence that caspase-13 is not a human but a bovine gene. Biochem Biophys Res Commun. 285:2001;1150-1154.
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 1150-1154
    • Koenig, U.1    Eckhart, L.2    Tschachler, E.3
  • 170
    • 0034521338 scopus 로고    scopus 로고
    • Forkhead transcription factors are targets of signalling by the proto-oncogene PKB (C-AKT)
    • Kops G.J.P.L., Burgering B.M.T. Forkhead transcription factors are targets of signalling by the proto-oncogene PKB (C-AKT). J Anat. 197:2000;571-574.
    • (2000) J Anat , vol.197 , pp. 571-574
    • Kops, G.J.P.L.1    Burgering, B.M.T.2
  • 171
    • 0032727468 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase C δ and ε by caspase-3 in U937 cells during chemotherapeutic agent-induced apoptosis
    • Koriyama H., Kouchi Z., Umeda T., Saido T.C., Momoi T., Ishiura S., Suzuki K. Proteolytic activation of protein kinase C δ and ε by caspase-3 in U937 cells during chemotherapeutic agent-induced apoptosis. Cell Signal. 11:1999;831-838.
    • (1999) Cell Signal , vol.11 , pp. 831-838
    • Koriyama, H.1    Kouchi, Z.2    Umeda, T.3    Saido, T.C.4    Momoi, T.5    Ishiura, S.6    Suzuki, K.7
  • 172
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer S.J., Wei M.C., Saito M., Weiler S., Oh K.J., Schlesinger P.H. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ. 7:2000;1166-1173.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 173
    • 0032574745 scopus 로고    scopus 로고
    • ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases
    • Koseki T., Inohara N., Chen S., Nunez G. ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases. Proc Natl Acad Sci USA. 95:1998;156-160.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 156-160
    • Koseki, T.1    Inohara, N.2    Chen, S.3    Nunez, G.4
  • 174
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S., Tanaka S., Takayama S., Schibler M.J., Fenton W., Reed J.C. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53:1993;4701-4714.
    • (1993) Cancer Res , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 175
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 176
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G., Dallaporta B., Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol. 60:1998;619-642.
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 177
  • 183
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • Kyriakis J.M., Avruch J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol Rev. 81:2001;807-869.
    • (2001) Physiol Rev , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 185
    • 0034845958 scopus 로고    scopus 로고
    • PKB/Akt: A key mediator of cell proliferation, survival and insulin response?
    • Lawlor M.A., Alessi D.R. PKB/Akt: a key mediator of cell proliferation, survival and insulin response? J Cell Sci. 114:2001;2903-2910.
    • (2001) J Cell Sci , vol.114 , pp. 2903-2910
    • Lawlor, M.A.1    Alessi, D.R.2
  • 186
    • 0033305658 scopus 로고    scopus 로고
    • Insulin-like growth factor I improves cardiovascular function and suppresses apoptosis of cardiomyocytes in dilated cardiomyopathy
    • Lee W.L., Chen J.W., Ting C.T., Ishiwata T., Lin S.J., Korc M., Wang P.H. Insulin-like growth factor I improves cardiovascular function and suppresses apoptosis of cardiomyocytes in dilated cardiomyopathy. Endocrinology. 140:1999;4831-4840.
    • (1999) Endocrinology , vol.140 , pp. 4831-4840
    • Lee, W.L.1    Chen, J.W.2    Ting, C.T.3    Ishiwata, T.4    Lin, S.J.5    Korc, M.6    Wang, P.H.7
  • 187
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M., Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol. 2:2001;589-598.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 188
    • 0032190514 scopus 로고    scopus 로고
    • ATP converts necrosis to apoptosis in oxidant-injured endothelial cells
    • Lelli J.L., Becks L.L., Dabrowska M.I., Hinshaw D.B. ATP converts necrosis to apoptosis in oxidant-injured endothelial cells. Free Radic Biol Med. 25:1998;694-702.
    • (1998) Free Radic Biol Med , vol.25 , pp. 694-702
    • Lelli, J.L.1    Becks, L.L.2    Dabrowska, M.I.3    Hinshaw, D.B.4
  • 190
    • 0034925481 scopus 로고    scopus 로고
    • Decreased p38 MAPK activity in end-stage failing human myocardium: P38 MAPK α is the predominant isoform expressed in human heart
    • Lemke L.E., Bloem L.J., Fouts R., Esterman M., Sandusky G., Vlahos C.J. Decreased p38 MAPK activity in end-stage failing human myocardium: p38 MAPK α is the predominant isoform expressed in human heart. J Mol Cell Cardiol. 33:2000;1527-1540.
    • (2000) J Mol Cell Cardiol , vol.33 , pp. 1527-1540
    • Lemke, L.E.1    Bloem, L.J.2    Fouts, R.3    Esterman, M.4    Sandusky, G.5    Vlahos, C.J.6
  • 193
    • 33751276291 scopus 로고    scopus 로고
    • Myocardial ischemia decreases oxidative phosphorylation through cytochrome oxidase in subsarcolemmal mitochondria
    • Lesnefsky E.J., Tandler B., Ye J., Slabe T.J., Turkaly J., Hoppel C.L. Myocardial ischemia decreases oxidative phosphorylation through cytochrome oxidase in subsarcolemmal mitochondria. Am J Physiol. 273:1997;H1544-H1554.
    • (1997) Am J Physiol , vol.273
    • Lesnefsky, E.J.1    Tandler, B.2    Ye, J.3    Slabe, T.J.4    Turkaly, J.5    Hoppel, C.L.6
  • 194
    • 0033553389 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 attenuates the detrimental impact of nonocclusive coronary artery constriction on the heart
    • Li B., Setoguchi M., Dreoli A.M., Leri A., Malhotra A., Kajstura J., Anversa P. Insulin-like growth factor-1 attenuates the detrimental impact of nonocclusive coronary artery constriction on the heart. Circ Res. 84:1999;1007-1019.
    • (1999) Circ Res , vol.84 , pp. 1007-1019
    • Li, B.1    Setoguchi, M.2    Dreoli, A.M.3    Leri, A.4    Malhotra, A.5    Kajstura, J.6    Anversa, P.7
  • 195
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase-8 mediates the mitochondrial in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of BID by caspase-8 mediates the mitochondrial in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 196
    • 0033233483 scopus 로고    scopus 로고
    • Protein kinase C δ targets mitochondria, alters mitochondrial membrane potential and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector
    • Li L., Lorenzo P.S., Bogi K., Blumberg P.M., Yuspa S.H. Protein kinase C δ targets mitochondria, alters mitochondrial membrane potential and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector. Mol Cell Biol. 19:1999;8547-8558.
    • (1999) Mol Cell Biol , vol.19 , pp. 8547-8558
    • Li, L.1    Lorenzo, P.S.2    Bogi, K.3    Blumberg, P.M.4    Yuspa, S.H.5
  • 197
    • 0030829808 scopus 로고    scopus 로고
    • Overexpression of insulin-like growth factor-1 in mice protects from myocyte death after infarction, attenuating ventricular dilation, wall stress, and cardiac hypertrophy
    • Li Q., Li B., Wang X., Leri A., Jana K.P., Liu Y., Baserga R., Anversa P. Overexpression of insulin-like growth factor-1 in mice protects from myocyte death after infarction, attenuating ventricular dilation, wall stress, and cardiac hypertrophy. J Clin Invest. 100:1997;1991-1999.
    • (1997) J Clin Invest , vol.100 , pp. 1991-1999
    • Li, Q.1    Li, B.2    Wang, X.3    Leri, A.4    Jana, K.P.5    Liu, Y.6    Baserga, R.7    Anversa, P.8
  • 198
    • 0034807142 scopus 로고    scopus 로고
    • Regulation of MAP kinase activity by peptide receptor signalling pathway: Paradigms of multiplicity
    • Liebman C. Regulation of MAP kinase activity by peptide receptor signalling pathway: paradigms of multiplicity. Cell Signal. 13:2001;777-785.
    • (2001) Cell Signal , vol.13 , pp. 777-785
    • Liebman, C.1
  • 199
    • 0027977928 scopus 로고
    • The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane
    • Lithgow T., Van Driel R., Bertram J.F., Strasser A. The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane. Cell Growth Differ. 5:1994;411-417.
    • (1994) Cell Growth Differ , vol.5 , pp. 411-417
    • Lithgow, T.1    Van Driel, R.2    Bertram, J.F.3    Strasser, A.4
  • 202
    • 0034661857 scopus 로고    scopus 로고
    • Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155
    • Lizcano J.M., Morrice N., Cohen P. Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. Biochem J. 349:2000;547-557.
    • (2000) Biochem J , vol.349 , pp. 547-557
    • Lizcano, J.M.1    Morrice, N.2    Cohen, P.3
  • 203
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: Integrating mammalian biology
    • Locksley R.M., Killeen N., Lenardo M.J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell. 104:2001;487-501.
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 205
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 206
    • 0033525760 scopus 로고    scopus 로고
    • An inhibitor of p38 mitogen-activated protein kinase protects neonatal cardiac myocyte from ischemia
    • Mackay K., Mochly-Rosen D. An inhibitor of p38 mitogen-activated protein kinase protects neonatal cardiac myocyte from ischemia. J Biol Chem. 274:1999;6272-6279.
    • (1999) J Biol Chem , vol.274 , pp. 6272-6279
    • Mackay, K.1    Mochly-Rosen, D.2
  • 207
    • 0034958672 scopus 로고    scopus 로고
    • Localization, anchoring, and functions of protein kinase C isozymes in the heart
    • Mackay K., Mochly-Rosen D. Localization, anchoring, and functions of protein kinase C isozymes in the heart. J Mol Cell Cardiol. 33:2001;1301-1307.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1301-1307
    • Mackay, K.1    Mochly-Rosen, D.2
  • 208
    • 0033961280 scopus 로고    scopus 로고
    • Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB
    • Madrir L.V., Wang C.Y., Guttridge D.C., Schottelius A.J., Baldwin A.S., Mayo M.W. Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB. Mol Cell Biol. 20:2000;1626-1638.
    • (2000) Mol Cell Biol , vol.20 , pp. 1626-1638
    • Madrir, L.V.1    Wang, C.Y.2    Guttridge, D.C.3    Schottelius, A.J.4    Baldwin, A.S.5    Mayo, M.W.6
  • 209
    • 0034816062 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor α mRNA stability
    • Mahtani K.R., Brook M., Dean J.L., Sully G., Saklatvala J., Clark A.R. Mitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor α mRNA stability. Mol Cell Biol. 21:2001;6461-6469.
    • (2001) Mol Cell Biol , vol.21 , pp. 6461-6469
    • Mahtani, K.R.1    Brook, M.2    Dean, J.L.3    Sully, G.4    Saklatvala, J.5    Clark, A.R.6
  • 210
    • 0034698182 scopus 로고    scopus 로고
    • Mitochondrial translocation of protein kinase C δ in phorbol ester-induced cytochrome c release and apoptosis
    • Majumder P.K., Pandey P., Sun X., Cheng K., Datta R., Saxena S., Kharbanda S., Kufe D. Mitochondrial translocation of protein kinase C δ in phorbol ester-induced cytochrome c release and apoptosis. J Biol Chem. 275:2000;21793-21796.
    • (2000) J Biol Chem , vol.275 , pp. 21793-21796
    • Majumder, P.K.1    Pandey, P.2    Sun, X.3    Cheng, K.4    Datta, R.5    Saxena, S.6    Kharbanda, S.7    Kufe, D.8
  • 212
    • 0035680903 scopus 로고    scopus 로고
    • The oxidative stress hypothesis of congestive heart failure
    • Mak S., Newton G.E. The oxidative stress hypothesis of congestive heart failure. Chest. 120:2001;2035-2046.
    • (2001) Chest , vol.120 , pp. 2035-2046
    • Mak, S.1    Newton, G.E.2
  • 213
    • 0035955751 scopus 로고    scopus 로고
    • Antiischemic effects of SB203580 are mediated through the inhibition of p38α mitogen-activated protein kinase: Evidence from ectopic expression of an inhibition-resistant kinase
    • Martin J.L., Avkiran M., Quinlan R.A., Cohen P., Marber M.S. Antiischemic effects of SB203580 are mediated through the inhibition of p38α mitogen-activated protein kinase: evidence from ectopic expression of an inhibition-resistant kinase. Circ Res. 89:2001;750-752.
    • (2001) Circ Res , vol.89 , pp. 750-752
    • Martin, J.L.1    Avkiran, M.2    Quinlan, R.A.3    Cohen, P.4    Marber, M.S.5
  • 214
    • 0035976930 scopus 로고    scopus 로고
    • Cyclic AMP regulation of neutrophil apoptosis occurs via a novel protein kinase A-independent signaling pathway
    • Martin M.C., Dransfield I., Haslett C., Rossi A.G. Cyclic AMP regulation of neutrophil apoptosis occurs via a novel protein kinase A-independent signaling pathway. J Biol Chem. 276:2001;45041-45050.
    • (2001) J Biol Chem , vol.276 , pp. 45041-45050
    • Martin, M.C.1    Dransfield, I.2    Haslett, C.3    Rossi, A.G.4
  • 216
    • 0035839635 scopus 로고    scopus 로고
    • PKCδ is required for mitochondrial-dependent apoptosis in salivary epithelial cells
    • Matassa A.A., Carpenter L., Biden T.J., Humphries M.J., Reyland M.E. PKCδ is required for mitochondrial-dependent apoptosis in salivary epithelial cells. J Biol Chem. 276:2001;29719-29728.
    • (2001) J Biol Chem , vol.276 , pp. 29719-29728
    • Matassa, A.A.1    Carpenter, L.2    Biden, T.J.3    Humphries, M.J.4    Reyland, M.E.5
  • 217
    • 0033534088 scopus 로고    scopus 로고
    • Adenoviral gene transfer of activated phosphatidylinositol 3′-kinase and Akt inhibits apoptosis of hypoxic cardiomyocytes in vitro
    • Matsui T., Li L., Del Monte R., Fukui Y., Franke T.F., Hajjar R.J., Rosenzweig A. Adenoviral gene transfer of activated phosphatidylinositol 3′-kinase and Akt inhibits apoptosis of hypoxic cardiomyocytes in vitro. Circulation. 100:1999;2373-2379.
    • (1999) Circulation , vol.100 , pp. 2373-2379
    • Matsui, T.1    Li, L.2    Del Monte, R.3    Fukui, Y.4    Franke, T.F.5    Hajjar, R.J.6    Rosenzweig, A.7
  • 220
    • 0035940387 scopus 로고    scopus 로고
    • In cardiomyocyte hypoxia, insulin-like growth factor-I-induced antiapoptotic signaling requires phosphatidylinositol-3-OH-kinase-dependent and mitogen-activated protein kinase-dependent activation of the transcription factor cAMP response element-binding protein
    • Mehrhof F.B., Muller F.U., Bergmann M.W., Li P., Wang Y., Schmitz W., Dietz R., Von Harsdorf R. In cardiomyocyte hypoxia, insulin-like growth factor-I-induced antiapoptotic signaling requires phosphatidylinositol-3-OH-kinase-dependent and mitogen-activated protein kinase-dependent activation of the transcription factor cAMP response element-binding protein. Circulation. 104:2001;2088-2094.
    • (2001) Circulation , vol.104 , pp. 2088-2094
    • Mehrhof, F.B.1    Muller, F.U.2    Bergmann, M.W.3    Li, P.4    Wang, Y.5    Schmitz, W.6    Dietz, R.7    Von Harsdorf, R.8
  • 221
    • 0032104245 scopus 로고    scopus 로고
    • The extended PKC superfamily
    • Mellor H., Parker P.J. The extended PKC superfamily. Biochem J. 332:1998;281-292.
    • (1998) Biochem J , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 222
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr Sect D. 50:1994;869-873.
    • (1994) Acta Crystallogr Sect D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 224
    • 0034767019 scopus 로고    scopus 로고
    • Caspase-dependent and serine protease-dependent DNA fragmentation of myocytes in the ischemia-reperfused rabbit heart: These inhibitors do not reduce infarct size
    • Minatoguchi S., Kariya T., Uno Y., Arai M., Nishida Y., Hashimoto K., Wang N., Aoyama T., Takemura G., Fujiwara T., Fujiwara H. Caspase-dependent and serine protease-dependent DNA fragmentation of myocytes in the ischemia-reperfused rabbit heart: these inhibitors do not reduce infarct size. Jpn Circ J. 65:2001;907-911.
    • (2001) Jpn Circ J , vol.65 , pp. 907-911
    • Minatoguchi, S.1    Kariya, T.2    Uno, Y.3    Arai, M.4    Nishida, Y.5    Hashimoto, K.6    Wang, N.7    Aoyama, T.8    Takemura, G.9    Fujiwara, T.10    Fujiwara, H.11
  • 225
    • 0032778043 scopus 로고    scopus 로고
    • Pro-B-cell specific transcription and proapoptotic function of protein kinase C η
    • Morrow T.A., Muljo S.A., Zhang J., Hardwick J.M., Schlissel M.S. Pro-B-cell specific transcription and proapoptotic function of protein kinase C η Mol Cell Biol. 19:1999;5608-5618.
    • (1999) Mol Cell Biol , vol.19 , pp. 5608-5618
    • Morrow, T.A.1    Muljo, S.A.2    Zhang, J.3    Hardwick, J.M.4    Schlissel, M.S.5
  • 227
    • 0035834824 scopus 로고    scopus 로고
    • 2+ overload during simulated ischemia and reperfusion: Possible mechanism of cardioprotection
    • 2+ overload during simulated ischemia and reperfusion: possible mechanism of cardioprotection. Circ Res. 89:2001;891-898.
    • (2001) Circ Res , vol.89 , pp. 891-898
    • Murata, M.1    Akao, M.2    O'Rourke, B.3    Marban, E.4
  • 228
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 proteins: Regulation of subcellular localization by molecular interference
    • Muslin A.J., Xing H. 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell Signal. 12:2000;703-709.
    • (2000) Cell Signal , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 229
    • 0034630317 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation
    • Nagata S. Apoptotic DNA fragmentation. Exp Cell Res. 256:2000;12-18.
    • (2000) Exp Cell Res , vol.256 , pp. 12-18
    • Nagata, S.1
  • 230
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families: Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T., Yuan J. Cross-talk between two cysteine protease families: activation of caspase-12 by calpain in apoptosis. J Cell Biol. 150:2000;887-894.
    • (2000) J Cell Biol , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 231
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β Nature. 403:2000;98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 232
  • 234
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A., Smith C.L., Lamensdorf I., Yoon S.-H., Youle R.J. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J Cell Biol. 153:2001;1265-1276.
    • (2001) J Cell Biol , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.-H.4    Youle, R.J.5
  • 235
    • 0023662325 scopus 로고
    • Molecular analysis of mbcl-2: Structure and expression of the murine gene homologous to the human gene involved in follicular lymphoma
    • Negrini M., Silini E., Kozak C., Tsujimoto Y., Croce C.M. Molecular analysis of mbcl-2: structure and expression of the murine gene homologous to the human gene involved in follicular lymphoma. Cell. 49:1987;455-463.
    • (1987) Cell , vol.49 , pp. 455-463
    • Negrini, M.1    Silini, E.2    Kozak, C.3    Tsujimoto, Y.4    Croce, C.M.5
  • 238
    • 0035823571 scopus 로고    scopus 로고
    • The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function
    • Neuss M., Monticone R., Lundberg M.S., Chesley A.T., Fleck E., Crow M.T. The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function. J Biol Chem. 276:2001;33915-33922.
    • (2001) J Biol Chem , vol.276 , pp. 33915-33922
    • Neuss, M.1    Monticone, R.2    Lundberg, M.S.3    Chesley, A.T.4    Fleck, E.5    Crow, M.T.6
  • 239
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct Funct Genet. 11:1991;281-296.
    • (1991) Proteins Struct Funct Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 240
    • 0033290849 scopus 로고    scopus 로고
    • Apoptosis and necrosis: Different execution of the same death
    • Nicotera P., Leist M., Reffando-May E. Apoptosis and necrosis: different execution of the same death. Biochem Soc Symp. 66:1999;69-73.
    • (1999) Biochem Soc Symp , vol.66 , pp. 69-73
    • Nicotera, P.1    Leist, M.2    Reffando-May, E.3
  • 242
    • 0030856469 scopus 로고    scopus 로고
    • Serum levels of soluble form of Fas molecular in patients with congestive heart failure
    • Okuyama M., Yamaguchi S., Nozaki N., Yamaoka M., Shirakabe M., Tomoike H. Serum levels of soluble form of Fas molecular in patients with congestive heart failure. Am J Cardiol. 79:1997;1698-1701.
    • (1997) Am J Cardiol , vol.79 , pp. 1698-1701
    • Okuyama, M.1    Yamaguchi, S.2    Nozaki, N.3    Yamaoka, M.4    Shirakabe, M.5    Tomoike, H.6
  • 243
    • 0034634284 scopus 로고    scopus 로고
    • ATP channels in preconditioning
    • ATP channels in preconditioning. Circ Res. 87:2000;845-855.
    • (2000) Circ Res , vol.87 , pp. 845-855
    • O'Rourke, B.1
  • 245
    • 0034966632 scopus 로고    scopus 로고
    • PKCε activation induces dichotomous cardiac phenotypes and modulates PKCε-RACK interactions and RACK expression
    • Pass J.M., Zheng Y., Wead W.B., Zhang J., Li R.C., Bolli R., Ping P. PKCε activation induces dichotomous cardiac phenotypes and modulates PKCε-RACK interactions and RACK expression. Am J Physiol. 280:2001;H946-H955.
    • (2001) Am J Physiol , vol.280
    • Pass, J.M.1    Zheng, Y.2    Wead, W.B.3    Zhang, J.4    Li, R.C.5    Bolli, R.6    Ping, P.7
  • 248
    • 0033824161 scopus 로고    scopus 로고
    • Apoptosis and proliferation of cardiomyocytes in heart failure of different etiologies
    • Petrovic D., Zorc-Pleskovic R., Zorc M. Apoptosis and proliferation of cardiomyocytes in heart failure of different etiologies. Cardiovasc Pathol. 9:1999;149-152.
    • (1999) Cardiovasc Pathol , vol.9 , pp. 149-152
    • Petrovic, D.1    Zorc-Pleskovic, R.2    Zorc, M.3
  • 249
    • 0034705239 scopus 로고    scopus 로고
    • Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes
    • Pham F.H., Sugden P.H., Clerk A. Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes. Circ Res. 86:2000;1252-1258.
    • (2000) Circ Res , vol.86 , pp. 1252-1258
    • Pham, F.H.1    Sugden, P.H.2    Clerk, A.3
  • 251
    • 0035957009 scopus 로고    scopus 로고
    • Inhibition of caspase 1 reduces human myocardial ischemic dysfunction via inhibition of IL-18 and IL-1β
    • Pomerantz B.J., Reznikow L.L., Harken A.H., Dinarello C.A. Inhibition of caspase 1 reduces human myocardial ischemic dysfunction via inhibition of IL-18 and IL-1β Proc Natl Acad Sci USA. 98:2001;2871-2876.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2871-2876
    • Pomerantz, B.J.1    Reznikow, L.L.2    Harken, A.H.3    Dinarello, C.A.4
  • 252
    • 0033601231 scopus 로고    scopus 로고
    • Spontaneous neutrophil apoptosis involves caspase 3-mediated activation of protein kinase C-δ
    • Pongracz J., Webb P., Wang K., Deacon E., Lunn O.J., Lord J.M. Spontaneous neutrophil apoptosis involves caspase 3-mediated activation of protein kinase C-δ J Biol Chem. 274:1999;37329-37334.
    • (1999) J Biol Chem , vol.274 , pp. 37329-37334
    • Pongracz, J.1    Webb, P.2    Wang, K.3    Deacon, E.4    Lunn, O.J.5    Lord, J.M.6
  • 254
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell. 3:1999;287-296.
    • (1999) Mol Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 255
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G., Coultas L., Cheney R.E., Huang D.C., Strasser A. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science. 293:2001;1784-1785.
    • (2001) Science , vol.293 , pp. 1784-1785
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.7    Strasser, A.8
  • 256
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • Qin H., Srinivasula S.M., Wu G., Fernander-Alnemri T., Alnemri E.S., Shi Y. Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. Nature. 399:1999;549-557.
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernander-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 257
    • 0034951169 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, and apoptosis
    • Raha S., Robinson B.H. Mitochondria, oxygen free radicals, and apoptosis. Am J Med Genet. 106:2001;62-70.
    • (2001) Am J Med Genet , vol.106 , pp. 62-70
    • Raha, S.1    Robinson, B.H.2
  • 258
    • 0030695187 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase in interleukin 1 signaling. Physical interaction with the interleukin 1 receptor and requirement in NFκB and AP-1 activation
    • Reddy S.A.G., Huang J.H., Liao W.S.-L. Phosphatidylinositol 3-kinase in interleukin 1 signaling. Physical interaction with the interleukin 1 receptor and requirement in NFκB and AP-1 activation. J Biol Chem. 272:1997;29167-29173.
    • (1997) J Biol Chem , vol.272 , pp. 29167-29173
    • Reddy, S.A.G.1    Huang, J.H.2    Liao, W.S.-L.3
  • 261
    • 0031897739 scopus 로고    scopus 로고
    • Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes
    • Roberg K., Ollinger K. Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes. Am J Pathol. 152:1998;1151-1156.
    • (1998) Am J Pathol , vol.152 , pp. 1151-1156
    • Roberg, K.1    Ollinger, K.2
  • 262
    • 0033436344 scopus 로고    scopus 로고
    • Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis induced by oxidative stress
    • Roberg K., Johansson U., Ollinger K. Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis induced by oxidative stress. Free Radic Biol Med. 27:1999;1228-1237.
    • (1999) Free Radic Biol Med , vol.27 , pp. 1228-1237
    • Roberg, K.1    Johansson, U.2    Ollinger, K.3
  • 264
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel T., Bokoch G.M. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science. 276:1997;1571-1574.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 265
    • 0031907887 scopus 로고    scopus 로고
    • Cutting edge: P21-activated kinase (PAK) is required for Fas-induced JNK activation in Jurkat cells
    • Rudel T., Zenke F.T., Chuang T.-H., Bokoch G.M. Cutting edge: p21-activated kinase (PAK) is required for Fas-induced JNK activation in Jurkat cells. J Immunol. 160:1998;7-11.
    • (1998) J Immunol , vol.160 , pp. 7-11
    • Rudel, T.1    Zenke, F.T.2    Chuang, T.-H.3    Bokoch, G.M.4
  • 266
    • 0035195595 scopus 로고    scopus 로고
    • Inhibition of caspase-3 improves contractile recovery of stunned myocardium, independent of apoptosis-inhibitory effects
    • Ruetten H., Badorff C., Ihling C., Zeiher A.M., Dimmeler S. Inhibition of caspase-3 improves contractile recovery of stunned myocardium, independent of apoptosis-inhibitory effects. J Am Coll Cardiol. 38:2001;2063-2070.
    • (2001) J Am Coll Cardiol , vol.38 , pp. 2063-2070
    • Ruetten, H.1    Badorff, C.2    Ihling, C.3    Zeiher, A.M.4    Dimmeler, S.5
  • 267
    • 0035370483 scopus 로고    scopus 로고
    • Regulation and function of the p53 tumor suppressor protein
    • Ryan K.M., Phillips A.C., Vousden K.H. Regulation and function of the p53 tumor suppressor protein. Curr Opin Cell Biol. 13:2001;332-337.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 332-337
    • Ryan, K.M.1    Phillips, A.C.2    Vousden, K.H.3
  • 269
    • 0033955751 scopus 로고    scopus 로고
    • Apoptotic cell death in heart failure
    • Sabbah H.N. Apoptotic cell death in heart failure. Cardiovasc Res. 45:2000;704-712.
    • (2000) Cardiovasc Res , vol.45 , pp. 704-712
    • Sabbah, H.N.1
  • 270
    • 0033841726 scopus 로고    scopus 로고
    • ATP channels in cardioprotection
    • ATP channels in cardioprotection. Basic Res Cardiol. 95:2000;285-289.
    • (2000) Basic Res Cardiol , vol.95 , pp. 285-289
    • Sato, T.1    Marban, E.2
  • 274
    • 0037028646 scopus 로고    scopus 로고
    • Apoptotic pathway activation from mitochondria and death receptors without caspase-3 cleavage in failing human myocardium
    • Scheubel R.J., Bartling B., Simm A., Silber R.-E., Drogaris K., Darmer D., Holtz J. Apoptotic pathway activation from mitochondria and death receptors without caspase-3 cleavage in failing human myocardium. J Am Coll Cardiol. 39:2002;481-488.
    • (2002) J Am Coll Cardiol , vol.39 , pp. 481-488
    • Scheubel, R.J.1    Bartling, B.2    Simm, A.3    Silber, R.-E.4    Drogaris, K.5    Darmer, D.6    Holtz, J.7
  • 275
    • 0032190548 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinase activation in the hypertrophic growth of adult ventricular cardiomyocytes
    • Schluter K.-D., Goldberg Y., Taimor G., Schafer M., Pipier H.M. Role of phosphatidylinositol 3-kinase activation in the hypertrophic growth of adult ventricular cardiomyocytes. Cardiovasc Res. 40:1998;174-181.
    • (1998) Cardiovasc Res , vol.40 , pp. 174-181
    • Schluter, K.-D.1    Goldberg, Y.2    Taimor, G.3    Schafer, M.4    Pipier, H.M.5
  • 276
    • 0035368020 scopus 로고    scopus 로고
    • Distinct roles for extracellular-signal-regulated protein kinase (ERK) mitogen-activated protein kinases and phosphatidylinositol 3-kinase in the regulation of Mcl-1 synthesis
    • Schubert K.M., Duronio V. Distinct roles for extracellular-signal-regulated protein kinase (ERK) mitogen-activated protein kinases and phosphatidylinositol 3-kinase in the regulation of Mcl-1 synthesis. Biochem J. 356:2001;473-480.
    • (2001) Biochem J , vol.356 , pp. 473-480
    • Schubert, K.M.1    Duronio, V.2
  • 277
    • 0035929596 scopus 로고    scopus 로고
    • The tumor suppressor gene PTEN can regulate cardiac hypertrophy and survival
    • Schwartzbauer G., Robbins J. The tumor suppressor gene PTEN can regulate cardiac hypertrophy and survival. J Biol Chem. 276:2001;35786-35793.
    • (2001) J Biol Chem , vol.276 , pp. 35786-35793
    • Schwartzbauer, G.1    Robbins, J.2
  • 278
    • 0035075597 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of ROCK1 induces MLC phosphorylation and apoptotic membrane blebbing
    • Sebbagh M., Renvoize C., Hamelin J., Riche N., Bertoglio J., Breard J. Caspase-3-mediated cleavage of ROCK1 induces MLC phosphorylation and apoptotic membrane blebbing. Nat Cell Biol. 3:2001;346-352.
    • (2001) Nat Cell Biol , vol.3 , pp. 346-352
    • Sebbagh, M.1    Renvoize, C.2    Hamelin, J.3    Riche, N.4    Bertoglio, J.5    Breard, J.6
  • 279
    • 0023779204 scopus 로고
    • Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma
    • Seto M., Jaeger U., Hockett R.D., Graninger W., Bennett S., Goldman P., Korsmeyer S.J. Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma. EMBO J. 7:1988;123-131.
    • (1988) EMBO J , vol.7 , pp. 123-131
    • Seto, M.1    Jaeger, U.2    Hockett, R.D.3    Graninger, W.4    Bennett, S.5    Goldman, P.6    Korsmeyer, S.J.7
  • 280
    • 0033595780 scopus 로고    scopus 로고
    • Loss of molecular interaction between cytochrome c and cardiolipin due to lipid peroxidation
    • Shidoji Y., Hayashi K., Komura S., Ohishi N., Yagi K. Loss of molecular interaction between cytochrome c and cardiolipin due to lipid peroxidation. Biochem Biophys Res Commun. 264:1999;343-347.
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 343-347
    • Shidoji, Y.1    Hayashi, K.2    Komura, S.3    Ohishi, N.4    Yagi, K.5
  • 281
    • 0034697365 scopus 로고    scopus 로고
    • Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu S., Ide T., Yanagida T., Tsujimoto Y. Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J Biol Chem. 275:2000;12321-12325.
    • (2000) J Biol Chem , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 282
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S., Konishi A., Kodama T., Tsujimoto Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc Natl Acad Sci USA. 97:2000;3100-3105.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 284
    • 17544368001 scopus 로고    scopus 로고
    • An additional form of rat Bcl-x, Bcl-xβ, generated by an unspliced RNA, promotes apoptosis in promyeloid cells
    • Shiraiwa N., Inohara N., Okad S., Yuzaki M., Shoji S., Ohta S. An additional form of rat Bcl-x, Bcl-xβ, generated by an unspliced RNA, promotes apoptosis in promyeloid cells. J Biol Chem. 271:1996;13258-13265.
    • (1996) J Biol Chem , vol.271 , pp. 13258-13265
    • Shiraiwa, N.1    Inohara, N.2    Okad, S.3    Yuzaki, M.4    Shoji, S.5    Ohta, S.6
  • 285
    • 0035663296 scopus 로고    scopus 로고
    • Dissociation of Bax from a Bcl-2/Bax heterodimer triggered by phosphorylation of serine 70 of Bcl-2
    • Shitashige M., Toi M., Yano T., Shibata M., Matsuo Y., Shibasaki F. Dissociation of Bax from a Bcl-2/Bax heterodimer triggered by phosphorylation of serine 70 of Bcl-2. J Biochem. 130:2001;741-748.
    • (2001) J Biochem , vol.130 , pp. 741-748
    • Shitashige, M.1    Toi, M.2    Yano, T.3    Shibata, M.4    Matsuo, Y.5    Shibasaki, F.6
  • 286
    • 0032190473 scopus 로고    scopus 로고
    • Role of protein kinase C as a cellular mediator of ischemic preconditioning: A critical review
    • Simkhovich B.Z., Przyklenk K., Kloner R.A. Role of protein kinase C as a cellular mediator of ischemic preconditioning: a critical review. Cardiovasc Res. 40:1998;9-22.
    • (1998) Cardiovasc Res , vol.40 , pp. 9-22
    • Simkhovich, B.Z.1    Przyklenk, K.2    Kloner, R.A.3
  • 287
    • 0033038491 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-κB p65/RelA subunit
    • Sizemore N., Leung S., Stark G.R. Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-κB p65/RelA subunit. Mol Cell Biol. 19:1999;4798-4805.
    • (1999) Mol Cell Biol , vol.19 , pp. 4798-4805
    • Sizemore, N.1    Leung, S.2    Stark, G.R.3
  • 289
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct non-redundant roles during the demolition phase of apoptosis
    • Slee E.A., Adrain C., Martin S.J. Executioner caspase-3, -6, and -7 perform distinct non-redundant roles during the demolition phase of apoptosis. J Biol Chem. 276:2001;7320-7326.
    • (2001) J Biol Chem , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 291
    • 0031259075 scopus 로고    scopus 로고
    • NADPH-oxidase-dependent superoxide production by myocyte-derived H9c2 cells: Influence of ischemia, heat shock, cycloheximide and cytochalasin D
    • Souren J.E., Van Der Mast C., Van Wijk R. NADPH-oxidase-dependent superoxide production by myocyte-derived H9c2 cells: influence of ischemia, heat shock, cycloheximide and cytochalasin D. J Mol Cell Cardiol. 29:1997;2803-2812.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 2803-2812
    • Souren, J.E.1    Van Der Mast, C.2    Van Wijk, R.3
  • 292
    • 0033104331 scopus 로고    scopus 로고
    • Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis
    • Srinivasula S.M., Ahman M., Guo Y., Lazebnik Y., Fernandes-Alnemri T., Alnemri E.S. Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis. Cancer Res. 59:1999;999-1002.
    • (1999) Cancer Res , vol.59 , pp. 999-1002
    • Srinivasula, S.M.1    Ahman, M.2    Guo, Y.3    Lazebnik, Y.4    Fernandes-Alnemri, T.5    Alnemri, E.S.6
  • 294
    • 0033616709 scopus 로고    scopus 로고
    • Deletion of the loop region of Bcl-2 completely blocks paclitaxel-induced apoptosis
    • Srivastave R.K., Mi Q.S., Hardwick J.M., Longo D.L. Deletion of the loop region of Bcl-2 completely blocks paclitaxel-induced apoptosis. Proc Natl Acad Sci USA. 96:1999;3775-3780.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3775-3780
    • Srivastave, R.K.1    Mi, Q.S.2    Hardwick, J.M.3    Longo, D.L.4
  • 295
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite references of human caspases 1, 3, 6, 7 and 8
    • Stennicke H.R., Renatus M., Meldal M., Salvesen G.S. Internally quenched fluorescent peptide substrates disclose the subsite references of human caspases 1, 3, 6, 7 and 8. Biochem J. 350:2000;563-568.
    • (2000) Biochem J , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 298
    • 0031669940 scopus 로고    scopus 로고
    • Cellular mechanisms of cardiac hypertrophy
    • Sugden P.H., Clerk A. Cellular mechanisms of cardiac hypertrophy. J Mol Med. 76:1998;725-746.
    • (1998) J Mol Med , vol.76 , pp. 725-746
    • Sugden, P.H.1    Clerk, A.2
  • 299
    • 0032563677 scopus 로고    scopus 로고
    • "Stress-responsive" mitogen-activated protein kinases in the myocardium
    • Sugden P.H., Clerk A. "Stress-responsive" mitogen-activated protein kinases in the myocardium. Circ Res. 83:1998;345-352.
    • (1998) Circ Res , vol.83 , pp. 345-352
    • Sugden, P.H.1    Clerk, A.2
  • 300
    • 0035919723 scopus 로고    scopus 로고
    • Solution structure of the tumor necrosis factor receptor-1 death domain
    • Sukits S.F., Lin L.-L., Hsu S., Malakian K., Powers R., Xu G.-Y. Solution structure of the tumor necrosis factor receptor-1 death domain. J Mol Biol. 310:2001;895-906.
    • (2001) J Mol Biol , vol.310 , pp. 895-906
    • Sukits, S.F.1    Lin, L.-L.2    Hsu, S.3    Malakian, K.4    Powers, R.5    Xu, G.-Y.6
  • 302
  • 303
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell. 103:2000;645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 304
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki Y., Imai Y., Nakayama H., Takahashi K., Takio K., Takahashi R. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell. 8:2001;613-621.
    • (2001) Mol Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 305
    • 0035920126 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes
    • Suzuki Y., Nakabayashi Y., Nakata K., Reed J.C., Takahashi R. X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes. J Biol Chem. 276:2001;27058-27063.
    • (2001) J Biol Chem , vol.276 , pp. 27058-27063
    • Suzuki, Y.1    Nakabayashi, Y.2    Nakata, K.3    Reed, J.C.4    Takahashi, R.5
  • 306
    • 0033563738 scopus 로고    scopus 로고
    • Fas antigen modulates ultraviolet B-induced apoptosis of SVHK cells: Sequential activation of caspases 8, 3, and 1 in the apoptotic process
    • Takahashi H., Nakamura S., Asano K., Kinouchi M., Ishida-Yamamoto A., Izuka H. Fas antigen modulates ultraviolet B-induced apoptosis of SVHK cells: sequential activation of caspases 8, 3, and 1 in the apoptotic process. Exp Cell Res. 249:1999;291-298.
    • (1999) Exp Cell Res , vol.249 , pp. 291-298
    • Takahashi, H.1    Nakamura, S.2    Asano, K.3    Kinouchi, M.4    Ishida-Yamamoto, A.5    Izuka, H.6
  • 307
    • 0034705485 scopus 로고    scopus 로고
    • Transgenic overexpression of constitutively active protein kinase C ε causes concentric cardiac hypertrophy
    • Takeishi Y., Ping P., Bolli R., Kirkpatrick D.L., Hoit B.D., Walsh R.A. Transgenic overexpression of constitutively active protein kinase C ε causes concentric cardiac hypertrophy. Circ Res. 86:2000;1218-1223.
    • (2000) Circ Res , vol.86 , pp. 1218-1223
    • Takeishi, Y.1    Ping, P.2    Bolli, R.3    Kirkpatrick, D.L.4    Hoit, B.D.5    Walsh, R.A.6
  • 308
    • 0034682812 scopus 로고    scopus 로고
    • BAD Ser-155 phosphorylation regulates BAD:Bcl-XL interaction and cell survival
    • Tan Y., Demeter M.R., Ruan H., Comb M.J. BAD Ser-155 phosphorylation regulates BAD:Bcl-XL interaction and cell survival. J Biol Chem. 275:2000;25865-25869.
    • (2000) J Biol Chem , vol.275 , pp. 25865-25869
    • Tan, Y.1    Demeter, M.R.2    Ruan, H.3    Comb, M.J.4
  • 309
    • 0027935409 scopus 로고
    • Hypoxia induces apoptosis with enhanced expression of Fas antigen messenger RNA in cultured neonatal rat cardiomyocytes
    • Tanaka M., Ito H., Adachi S., Akimoto H., Nishikawa T., Kasajima T., Marumo F., Hiroe M. Hypoxia induces apoptosis with enhanced expression of Fas antigen messenger RNA in cultured neonatal rat cardiomyocytes. Circ Res. 75:1994;426-433.
    • (1994) Circ Res , vol.75 , pp. 426-433
    • Tanaka, M.1    Ito, H.2    Adachi, S.3    Akimoto, H.4    Nishikawa, T.5    Kasajima, T.6    Marumo, F.7    Hiroe, M.8
  • 310
    • 0037134491 scopus 로고    scopus 로고
    • The forkhead transcription factor AFX activates apoptosis by induction of the BCL-6 transcriptional repressor
    • Tang T.T.-L., Dowbenko D., Jackson A., Toney L., Lewin D.A., Dent A.L., Lasky L.A. The forkhead transcription factor AFX activates apoptosis by induction of the BCL-6 transcriptional repressor. J Biol Chem. 277:2002;14255-14265.
    • (2002) J Biol Chem , vol.277 , pp. 14255-14265
    • Tang, T.T.-L.1    Dowbenko, D.2    Jackson, A.3    Toney, L.4    Lewin, D.A.5    Dent, A.L.6    Lasky, L.A.7
  • 312
    • 0034597496 scopus 로고    scopus 로고
    • P53 mediates bcl-2 phosphorylation and apoptosis via activation of the Cdc42/JNK1 pathway
    • Thomas A., Giesler T., White E. p53 mediates bcl-2 phosphorylation and apoptosis via activation of the Cdc42/JNK1 pathway. Oncogene. 19:2000;5259-5269.
    • (2000) Oncogene , vol.19 , pp. 5259-5269
    • Thomas, A.1    Giesler, T.2    White, E.3
  • 313
    • 0030896559 scopus 로고    scopus 로고
    • Differential effects of protein kinase C, Ras, and Raf-1 kinase on the induction of the cardiac B-type natriuretic peptide gene through a critical promoter-proximal M-CAT element
    • Thuerauf D.J., Glembotski C.C. Differential effects of protein kinase C, Ras, and Raf-1 kinase on the induction of the cardiac B-type natriuretic peptide gene through a critical promoter-proximal M-CAT element. J Biol Chem. 272:1997;7464-7472.
    • (1997) J Biol Chem , vol.272 , pp. 7464-7472
    • Thuerauf, D.J.1    Glembotski, C.C.2
  • 314
    • 0030701607 scopus 로고    scopus 로고
    • Fas induces cytoplasmic apoptosis responses and activation of the MKK7-JNK/SAPK and MKK6-p38 pathways independent of CPP32-like proteases
    • Toyoshima F., Moriguchi T., Nishida E. Fas induces cytoplasmic apoptosis responses and activation of the MKK7-JNK/SAPK and MKK6-p38 pathways independent of CPP32-like proteases. J Cell Biol. 139:1997;1005-1015.
    • (1997) J Cell Biol , vol.139 , pp. 1005-1015
    • Toyoshima, F.1    Moriguchi, T.2    Nishida, E.3
  • 316
    • 0031726359 scopus 로고    scopus 로고
    • Inhibition of Fas death signals by FLIPs
    • Tschopp J., Irmler M., Thome M. Inhibition of Fas death signals by FLIPs. Curr Biol. 10:1998;552-558.
    • (1998) Curr Biol , vol.10 , pp. 552-558
    • Tschopp, J.1    Irmler, M.2    Thome, M.3
  • 317
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk B., Turk D., Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim Biophys Acta. 1477:2000;98-111.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 319
    • 0034280126 scopus 로고    scopus 로고
    • Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer
    • Tyas L., Brophy V.A., Pope A., Rivett A.J., Tavare J.M. Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer. EMBO Rep. 1:2000;266-270.
    • (2000) EMBO Rep , vol.1 , pp. 266-270
    • Tyas, L.1    Brophy, V.A.2    Pope, A.3    Rivett, A.J.4    Tavare, J.M.5
  • 320
    • 0035977077 scopus 로고    scopus 로고
    • Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family
    • Miyashita T., Shikama Y., Tadokoro K., Yamada M. Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family. FEBS Lett. 509:2001;135-141.
    • (2001) FEBS Lett , vol.509 , pp. 135-141
    • Miyashita, T.1    Shikama, Y.2    Tadokoro, K.3    Yamada, M.4
  • 321
  • 322
    • 0036660617 scopus 로고    scopus 로고
    • Phenylephrine promotes phosphorylation of Bad in cardiac myocytes through the extracellular signal-regulated kinases 1/22 and protein kinase A
    • Valks D.M., Cook S.A., Pham F.H., Morrison P.R., Clerk A., Sugden P.H. Phenylephrine promotes phosphorylation of Bad in cardiac myocytes through the extracellular signal-regulated kinases 1/22 and protein kinase A. J Mol Cell Cardiol. 34:2002;749-763.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 749-763
    • Valks, D.M.1    Cook, S.A.2    Pham, F.H.3    Morrison, P.R.4    Clerk, A.5    Sugden, P.H.6
  • 324
    • 0033574536 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase pathway is required for activation-induced cell death of T cells
    • van den Brink M.R.M., Kapeller R., Pratt J.C., Chang J., Burakoff S.J. The extracellular signal-regulated kinase pathway is required for activation-induced cell death of T cells. J Biol Chem. 274:1999;11178-11185.
    • (1999) J Biol Chem , vol.274 , pp. 11178-11185
    • Van den Brink, M.R.M.1    Kapeller, R.2    Pratt, J.C.3    Chang, J.4    Burakoff, S.J.5
  • 325
    • 0031239737 scopus 로고    scopus 로고
    • Significant levels of oxidants are generated by isolated cardiomyocytes during ischemia prior to reperfusion
    • Vanden Hoek T.L., Li C., Shao Z., Schumacker P.T., Becker L.B. Significant levels of oxidants are generated by isolated cardiomyocytes during ischemia prior to reperfusion. J Mol Cell Cardiol. 29:1997;2571-2583.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 2571-2583
    • Vanden Hoek, T.L.1    Li, C.2    Shao, Z.3    Schumacker, P.T.4    Becker, L.B.5
  • 326
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck B., Alessi D.R. The PI3K-PDK1 connection: more than just a road to PKB. Biochem J. 346:2000;561-576.
    • (2000) Biochem J , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 327
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • Vanhaesebroeck B., Waterfield M.D. Signaling by distinct classes of phosphoinositide 3-kinases. Exp Cell Res. 253:1999;239-254.
    • (1999) Exp Cell Res , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 329
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen A.M., Ekert P.G., Pakusch M., Silke J., Connolly L.M., Reid G.E., Moritz R.L., Simpson R.J. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell. 102:2000;43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6    Moritz, R.L.7    Simpson, R.J.8
  • 331
    • 0034699352 scopus 로고    scopus 로고
    • Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival
    • Virdee K., Parone P.A., Tolkovsky A.M. Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival. Curr Biol. 10:2000;1151-1154.
    • (2000) Curr Biol , vol.10 , pp. 1151-1154
    • Virdee, K.1    Parone, P.A.2    Tolkovsky, A.M.3
  • 332
    • 0033535974 scopus 로고    scopus 로고
    • Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis
    • von Harsdorf R., Li P.-F., Dietz R. Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis. Circulation. 99:1999;2934-2941.
    • (1999) Circulation , vol.99 , pp. 2934-2941
    • Von Harsdorf, R.1    Li, P.-F.2    Dietz, R.3
  • 333
    • 0032582669 scopus 로고    scopus 로고
    • Cleavage and activation of p21-activated protein kinase γ-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity
    • Walter B.N., Huang Z., Jakobi R., Tuazon P.T., Alnemri E.S., Litwack G., Traugh J.A. Cleavage and activation of p21-activated protein kinase γ-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity. J Biol Chem. 273:1998;28733-28739.
    • (1998) J Biol Chem , vol.273 , pp. 28733-28739
    • Walter, B.N.1    Huang, Z.2    Jakobi, R.3    Tuazon, P.T.4    Alnemri, E.S.5    Litwack, G.6    Traugh, J.A.7
  • 334
    • 0034913884 scopus 로고    scopus 로고
    • Metallothionein inhibits doxorubicin-induced mitochondrial cytochrome c release and caspase-3 activation in cardiomyocytes
    • Wang G.W., Klein J.B., Kang Y.J. Metallothionein inhibits doxorubicin-induced mitochondrial cytochrome c release and caspase-3 activation in cardiomyocytes. J Pharmacol Exp Ther. 298:2001;461-468.
    • (2001) J Pharmacol Exp Ther , vol.298 , pp. 461-468
    • Wang, G.W.1    Klein, J.B.2    Kang, Y.J.3
  • 335
    • 0034077189 scopus 로고    scopus 로고
    • Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies
    • Wang J., Lenardo M.J. Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies. J Cell Sci. 113:2000;753-757.
    • (2000) J Cell Sci , vol.113 , pp. 753-757
    • Wang, J.1    Lenardo, M.J.2
  • 336
    • 0032494175 scopus 로고    scopus 로고
    • Regulation of cardiomyocyte apoptotic signaling by insulin-like growth factor I
    • Wang L., Ma W., Markovich R., Chen J.W., Wang P.H. Regulation of cardiomyocyte apoptotic signaling by insulin-like growth factor I. Circ Res. 83:1998;516-522.
    • (1998) Circ Res , vol.83 , pp. 516-522
    • Wang, L.1    Ma, W.2    Markovich, R.3    Chen, J.W.4    Wang, P.H.5
  • 337
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang Z. The expanding role of mitochondria in apoptosis. Genes Dev. 15:2001;2922-2933.
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, Z.1
  • 338
    • 0032103332 scopus 로고    scopus 로고
    • Ets transcription factors: Nuclear effectors of the Ras MAP-kinase signaling pathway
    • Wasylyk B., Hagman J., Gutierrez-Hartmann A. Ets transcription factors: nuclear effectors of the Ras MAP-kinase signaling pathway. Trends Biochem Sci. 23:1998;213-216.
    • (1998) Trends Biochem Sci , vol.23 , pp. 213-216
    • Wasylyk, B.1    Hagman, J.2    Gutierrez-Hartmann, A.3
  • 339
    • 0032728077 scopus 로고    scopus 로고
    • Hypoxia-activated apoptosis of cardiac myocytes requires reoxygenation of a pH shift and is independent of p53
    • Webster K.A., Discher D.J., Kaiser S., Hernandez O., Sato B., Bishopric N.H. Hypoxia-activated apoptosis of cardiac myocytes requires reoxygenation of a pH shift and is independent of p53. J Clin Invest. 104:1999;239-252.
    • (1999) J Clin Invest , vol.104 , pp. 239-252
    • Webster, K.A.1    Discher, D.J.2    Kaiser, S.3    Hernandez, O.4    Sato, B.5    Bishopric, N.H.6
  • 342
    • 0031239584 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 182 of p38 mitogen-activated protein kinase correlates with the protection of preconditioning in the rabbit heart
    • Weinbrenner C., Liu G.-S., Cohen M.V., Downey J.M. Phosphorylation of tyrosine 182 of p38 mitogen-activated protein kinase correlates with the protection of preconditioning in the rabbit heart. J Mol Cell Cardiol. 29:1997;2383-2391.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 2383-2391
    • Weinbrenner, C.1    Liu, G.-S.2    Cohen, M.V.3    Downey, J.M.4
  • 343
  • 344
    • 0029808748 scopus 로고    scopus 로고
    • Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
    • Whitmarsh A.J., Davis R.J. Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways. J Mol Med. 74:1996;589-607.
    • (1996) J Mol Med , vol.74 , pp. 589-607
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 345
    • 0029810469 scopus 로고    scopus 로고
    • Induction of Bcl-2 expression by phosphorylated CREB proteins during B-cell activation and rescue from apoptosis
    • Wilson B.E., Mochon E., Boxer L.M. Induction of Bcl-2 expression by phosphorylated CREB proteins during B-cell activation and rescue from apoptosis. Mol Cell Biol. 16:1996;5546-5556.
    • (1996) Mol Cell Biol , vol.16 , pp. 5546-5556
    • Wilson, B.E.1    Mochon, E.2    Boxer, L.M.3
  • 346
    • 0033575255 scopus 로고    scopus 로고
    • Suicidal tendencies: Apoptotic cell death by caspase family proteinases
    • Wolf B.B., Green D.R. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J Biol Chem. 274:1999;20049-20052.
    • (1999) J Biol Chem , vol.274 , pp. 20049-20052
    • Wolf, B.B.1    Green, D.R.2
  • 347
    • 0034646172 scopus 로고    scopus 로고
    • The cardiac Fas (APO-1/CD95) receptor/Fas ligand system. Relation to diastolic wall stress in volume-overload hypertrophy in vivo and activation of the transcription factor AP-1 in cardiac myocytes
    • Wollert K.C., Heineke J., Wetermann J., Lüdde M., Fiedler B., Zierhut W., Laurent D., Bauer M.K.A., Schulze-Osthoff K., Drexler H. The cardiac Fas (APO-1/CD95) receptor/Fas ligand system. Relation to diastolic wall stress in volume-overload hypertrophy in vivo and activation of the transcription factor AP-1 in cardiac myocytes. Circulation. 101:2000;1172-1178.
    • (2000) Circulation , vol.101 , pp. 1172-1178
    • Wollert, K.C.1    Heineke, J.2    Wetermann, J.3    Lüdde, M.4    Fiedler, B.5    Zierhut, W.6    Laurent, D.7    Bauer, M.K.A.8    Schulze-Osthoff, K.9    Drexler, H.10
  • 348
    • 0034193138 scopus 로고    scopus 로고
    • Cleavage of Bax enhances its cell death function
    • Wood D.E., Newcomb E.W. Cleavage of Bax enhances its cell death function. Exp Cell Res. 256:2000;375-382.
    • (2000) Exp Cell Res , vol.256 , pp. 375-382
    • Wood, D.E.1    Newcomb, E.W.2
  • 349
    • 0030954131 scopus 로고    scopus 로고
    • Atrial natriuretic peptide induces apoptosis in neonatal rat cardiac myocytes
    • Wu C.F., Bishopric N.H., Pratt R.E. Atrial natriuretic peptide induces apoptosis in neonatal rat cardiac myocytes. J Biol Chem. 272:1997;14860-14866.
    • (1997) J Biol Chem , vol.272 , pp. 14860-14866
    • Wu, C.F.1    Bishopric, N.H.2    Pratt, R.E.3
  • 350
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • Wu G., Chai J., Suber T.L., Wu J.W., Du C., Wang X., Shi Y. Structural basis of IAP recognition by Smac/DIABLO. Nature. 408:2000;1008-1012.
    • (2000) Nature , vol.408 , pp. 1008-1012
    • Wu, G.1    Chai, J.2    Suber, T.L.3    Wu, J.W.4    Du, C.5    Wang, X.6    Shi, Y.7
  • 351
    • 0034704134 scopus 로고    scopus 로고
    • Expression of constitutively active phosphatidylinositol 3-kinase inhibits activation of caspase 3 and apoptosis in cardiac muscle cells
    • Wu W., Lee W.L., Wu Y.Y., Chen D., Liu T.J., Jang A., Sharma P.M., Wang P.H. Expression of constitutively active phosphatidylinositol 3-kinase inhibits activation of caspase 3 and apoptosis in cardiac muscle cells. J Biol Chem. 275:2000;40113-40119.
    • (2000) J Biol Chem , vol.275 , pp. 40113-40119
    • Wu, W.1    Lee, W.L.2    Wu, Y.Y.3    Chen, D.4    Liu, T.J.5    Jang, A.6    Sharma, P.M.7    Wang, P.H.8
  • 352
    • 0035936023 scopus 로고    scopus 로고
    • The protein kinase PKB/Akt regulates cell survival and apoptosis by inhibiting Bax conformational change
    • Yamaguchi H., Wang H.-G. The protein kinase PKB/Akt regulates cell survival and apoptosis by inhibiting Bax conformational change. Oncogene. 20:2001;7779-7786.
    • (2001) Oncogene , vol.20 , pp. 7779-7786
    • Yamaguchi, H.1    Wang, H.-G.2
  • 354
    • 0034776026 scopus 로고    scopus 로고
    • Chelerythrine rapidly induces apoptosis through generation of reactive oxygen species in cardiac myocytes
    • Yamamoto S., Seta K., Morisco C., Vatner S.F., Sadoshima J. Chelerythrine rapidly induces apoptosis through generation of reactive oxygen species in cardiac myocytes. J Mol Cell Cardiol. 33:2001;1829-1848.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1829-1848
    • Yamamoto, S.1    Seta, K.2    Morisco, C.3    Vatner, S.F.4    Sadoshima, J.5
  • 355
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang X., Khozravi-Far R., Chang H.Y., Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell. 89:1997;1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khozravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 356
    • 0031447458 scopus 로고    scopus 로고
    • A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells
    • Yang X.-F., Weber G.F., Cantor H. A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells. Immunity. 7:1997;629-639.
    • (1997) Immunity , vol.7 , pp. 629-639
    • Yang, X.-F.1    Weber, G.F.2    Cantor, H.3
  • 357
    • 0032570292 scopus 로고    scopus 로고
    • Attenuation of ischaemia/reperfusion injury in rats by a caspase inhibitor
    • Yaoita H., Ogawa K., Maehara K., Muruyama Y. Attenuation of ischaemia/reperfusion injury in rats by a caspase inhibitor. Circulation. 97:1998;276-281.
    • (1998) Circulation , vol.97 , pp. 276-281
    • Yaoita, H.1    Ogawa, K.2    Maehara, K.3    Muruyama, Y.4
  • 358
    • 0033980348 scopus 로고    scopus 로고
    • Apoptosis in relevant clinical situations: Contribution of apoptosis in myocardial infarction
    • Yaoita H., Ogawa K., Maehara K., Maruyama Y. Apoptosis in relevant clinical situations: contribution of apoptosis in myocardial infarction. Cardiovasc Res. 45:2000;630-641.
    • (2000) Cardiovasc Res , vol.45 , pp. 630-641
    • Yaoita, H.1    Ogawa, K.2    Maehara, K.3    Maruyama, Y.4
  • 360
    • 0033944665 scopus 로고    scopus 로고
    • Bid, a critical mediator for apoptosis induced by the activation of Fas/TNF-R1 death receptors in hepatocytes
    • Yin X.M. Bid, a critical mediator for apoptosis induced by the activation of Fas/TNF-R1 death receptors in hepatocytes. J Mol Med. 78:2000;203-211.
    • (2000) J Mol Med , vol.78 , pp. 203-211
    • Yin, X.M.1
  • 362
    • 0033613210 scopus 로고    scopus 로고
    • Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: A structural basis for specific adaptor/caspase interaction
    • Zhou P., Chou J., Olea R.S., Yuan J., Wagner G. Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction. Proc Natl Acad Sci USA. 96:1999;11265-11270.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11265-11270
    • Zhou, P.1    Chou, J.2    Olea, R.S.3    Yuan, J.4    Wagner, G.5
  • 363
    • 0034637606 scopus 로고    scopus 로고
    • Growth factors inactivate the cell death promoter, BAD, by phosphorylation of its BH3 domain on serine 155
    • Zhou X.-M., Liu Y., Payne G., Lutz R.J., Chittenden T. Growth factors inactivate the cell death promoter, BAD, by phosphorylation of its BH3 domain on serine 155. J Biol Chem. 275:2000;25046-25051.
    • (2000) J Biol Chem , vol.275 , pp. 25046-25051
    • Zhou, X.-M.1    Liu, Y.2    Payne, G.3    Lutz, R.J.4    Chittenden, T.5
  • 364
    • 0033828720 scopus 로고    scopus 로고
    • Phenylephrine protects neonatal rat cardiomyocytes from hypoxia and serum deprivation-induced apoptosis
    • Zhu H., McElwee-Witmer S., Perrone M., Clark K.L., Zilberstein A. Phenylephrine protects neonatal rat cardiomyocytes from hypoxia and serum deprivation-induced apoptosis. Cell Death Differ. 7:2000;773-784.
    • (2000) Cell Death Differ , vol.7 , pp. 773-784
    • Zhu, H.1    McElwee-Witmer, S.2    Perrone, M.3    Clark, K.L.4    Zilberstein, A.5
  • 365
    • 0034985121 scopus 로고    scopus 로고
    • A cellular survival switch: Poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription
    • Ziegler M., Oei S.L. A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription. Bioessays. 23:2001;543-548.
    • (2001) Bioessays , vol.23 , pp. 543-548
    • Ziegler, M.1    Oei, S.L.2
  • 366
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong W.-X., Lindsten T., Ross A.J., MacGregor G.R., Thompson C.B. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15:2001;1481-1486.
    • (2001) Genes Dev , vol.15 , pp. 1481-1486
    • Zong, W.-X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 367
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H., Henzel W.J., Liu X., Lutschg A., Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 90:1997;405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.