메뉴 건너뛰기




Volumn 77, Issue 1, 2003, Pages 45-56

The major apoptotic pathway activated and suppressed by poliovirus

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 9; CYTOCHROME C; GUANIDINE; PROTEIN BCL 2; PROTEIN BID;

EID: 0037213269     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.1.45-56.2003     Document Type: Article
Times cited : (74)

References (77)
  • 1
    • 0035146929 scopus 로고    scopus 로고
    • Life-or-death decisions by the Bcl-2 protein family
    • Adams, J. M., and S. Cory. 2001. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem. Sci. 26:61-66.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 61-66
    • Adams, J.M.1    Cory, S.2
  • 2
    • 0035369143 scopus 로고    scopus 로고
    • The mitochondrial apoptosome: A killer unleashed by the cytochrome seas
    • Adrain, C., and S. J. Martin. 2001. The mitochondrial apoptosome: A killer unleashed by the cytochrome seas. Trends Biochem. Sci. 26:390-397.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 390-397
    • Adrain, C.1    Martin, S.J.2
  • 6
    • 0034688231 scopus 로고    scopus 로고
    • Poliovirus protease 3C(pro) kills cells by apoptosis
    • Barco, A., E. Feduchi, and L. Carrasco. 2000. Poliovirus protease 3C(pro) kills cells by apoptosis. Virology 266:352-360.
    • (2000) Virology , vol.266 , pp. 352-360
    • Barco, A.1    Feduchi, E.2    Carrasco, L.3
  • 7
    • 0035182221 scopus 로고    scopus 로고
    • Stress management-heat shock protein-70 and the regulation of apoptosis
    • Beere, H. M., and D. R. Green. 2001. Stress management-heat shock protein-70 and the regulation of apoptosis. Trends Cell Biol. 11:6-10.
    • (2001) Trends Cell Biol. , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 8
    • 0034476896 scopus 로고    scopus 로고
    • An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells hy respiratory syncytial virus
    • Bitko, V., and S. Batik. 2001. An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells hy respiratory syncytial virus. J. Cell. Biochem. 80:441-454.
    • (2001) J. Cell. Biochem. , vol.80 , pp. 441-454
    • Bitko, V.1    Batik, S.2
  • 9
    • 0033047235 scopus 로고    scopus 로고
    • Apoptosis without caspases: An inefficient molecular guillotine?
    • Borner, C., and L. Monney. 1999. Apoptosis without caspases: An inefficient molecular guillotine? Cell Death Differ. 6:497-507
    • (1999) Cell Death Differ. , vol.6 , pp. 497-507
    • Borner, C.1    Monney, L.2
  • 10
    • 0035881713 scopus 로고    scopus 로고
    • New EMBO members' review: Viral and hacterial proteins regulating apoptosis at the mitochondrial level
    • Boya, P., B. Roques, and G. Kroemer. 2001. New EMBO members' review: Viral and hacterial proteins regulating apoptosis at the mitochondrial level. EMBO J. 20:4325-4331.
    • (2001) EMBO J. , vol.20 , pp. 4325-4331
    • Boya, P.1    Roques, B.2    Kroemer, G.3
  • 11
    • 0035368563 scopus 로고    scopus 로고
    • Apoptotic death sensor an organelle's alter ego?
    • Bratton, S. B., and G. M. Cohen. 2001. Apoptotic death sensor an organelle's alter ego? Trends Pharmacol. Sci. 22:306-315.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 306-315
    • Bratton, S.B.1    Cohen, G.M.2
  • 13
    • 0029107952 scopus 로고
    • Modification of membrane permeability by animal viruses
    • Carrasco, L. 1995. Modification of membrane permeability by animal viruses. Adv. Virus. Res. 45:61-112.
    • (1995) Adv. Virus. Res. , vol.45 , pp. 61-112
    • Carrasco, L.1
  • 14
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: Functions and regulation of caspases
    • Chang, H. Y., and X. Yang. 2000. Proteases for cell suicide: Functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 64:821-846.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 15
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by calcium-activated protease calpain can lead to inactivation of caspases
    • Chua, B. T., K. Guo, and P. Li. 2000. Direct cleavage by calcium-activated protease calpain can lead to inactivation of caspases. J. Biol. Chem. 275: 5131-5134.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5131-5134
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 16
    • 0033912936 scopus 로고    scopus 로고
    • The chicken anemia virus derived protein apoptin requires activation of caspases for induction of apoptosis in human tumor cells
    • Danen-van Oorschot, A. A., A. J. van Der Eb, and M. H. Noteborn. 2000. The chicken anemia virus derived protein apoptin requires activation of caspases for induction of apoptosis in human tumor cells. J. Virol. 74:7072-7078.
    • (2000) J. Virol. , vol.74 , pp. 7072-7078
    • Danen-van Oorschot, A.A.1    Van Der Eb, A.J.2    Noteborn, M.H.3
  • 17
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher, S., and J.-C. Martinou. 2000. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10:369-377.
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.-C.2
  • 18
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins - Suppressors of apoptosis
    • Deveraux, Q. L., and J. C. Reed. 1999. IAP family proteins - Suppressors of apoptosis. Genes Dev. 13:239-252.
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 19
    • 0034925865 scopus 로고    scopus 로고
    • Apoptotic cell death in the pathogenesis of infectious diseases
    • Dockrell, D. H. 2001. Apoptotic cell death in the pathogenesis of infectious diseases. J. Infect. 42:227-234.
    • (2001) J. Infect. , vol.42 , pp. 227-234
    • Dockrell, D.H.1
  • 20
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating 1AP inhibition
    • Du, C., M. Fang, Y. Li, L. Li, and X. Wang. 2000. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating 1AP inhibition. Cell 102:33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 21
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw, W. C., L. M. Martins, and S. H. Kaufmann. 1999. Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68:383-424.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 22
    • 0035884766 scopus 로고    scopus 로고
    • Viruses and apoptosis: Meddling with mitochondria
    • Everett, H., and G. McFadden. 2001. Viruses and apoptosis: Meddling with mitochondria. Virology 288:1-7.
    • (2001) Virology , vol.288 , pp. 1-7
    • Everett, H.1    McFadden, G.2
  • 24
    • 0034722379 scopus 로고    scopus 로고
    • Caspases disrupt the nucleo-cytoplasmic barrier
    • Faleiro, L., and Y. Lazebnik. 2000. Caspases disrupt the nucleo-cytoplasmic barrier. J. Cell Biol. 151:951-959.
    • (2000) J. Cell Biol. , vol.151 , pp. 951-959
    • Faleiro, L.1    Lazebnik, Y.2
  • 27
  • 30
    • 0026729556 scopus 로고
    • Determinants of substrate recognition by poliovirus 2A proteinase
    • Hellen, C. U., C. K. Lee, and E. Wimmer. 1992. Determinants of substrate recognition by poliovirus 2A proteinase. J. Virol. 66:3330-3338.
    • (1992) J. Virol. , vol.66 , pp. 3330-3338
    • Hellen, C.U.1    Lee, C.K.2    Wimmer, E.3
  • 31
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengarther, M. O. 2000. The biochemistry of apoptosis. Nature 407:770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengarther, M.O.1
  • 32
    • 0033635733 scopus 로고    scopus 로고
    • BH3-only proteins - Essential initiators of apoptotic cell death
    • Huang, D. C., and A. Strasser 2000. BH3-only proteins - Essential initiators of apoptotic cell death. Cell 103:839-842.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.1    Strasser, A.2
  • 34
    • 0035899429 scopus 로고    scopus 로고
    • Ionizing radiation but not anticancer drugs causes cell cycle arrest and failure to activate the mitochondrial death pathway in MCF-7 breast carcinoma cells
    • Jänicke, R. U., I. H. Engels, T. Dunkern, B. Kaina, K. Schulze-Osthoff, and A. G. Porter. 2001. Ionizing radiation but not anticancer drugs causes cell cycle arrest and failure to activate the mitochondrial death pathway in MCF-7 breast carcinoma cells. Oncogene 20:5043-5053.
    • (2001) Oncogene , vol.20 , pp. 5043-5053
    • Jänicke, R.U.1    Engels, I.H.2    Dunkern, T.3    Kaina, B.4    Schulze-Osthoff, K.5    Porter, A.G.6
  • 35
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • Jänicke, R. U., M. L. Sprengart, M. R. Wati, and A. G. Porter. 1998. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis J. Biol. Chem. 273:9357-9360.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9357-9360
    • Jänicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 37
    • 0034685633 scopus 로고    scopus 로고
    • Poliovirus induces an early impairment of mitochondrial function by inhibiting succinate dehydrogenase activity
    • Koundouris, A., G. E. Kass, C. R. Johnson, A. Boxall, P. G. Sanders, and M. J. Carter. 2000. Poliovirus induces an early impairment of mitochondrial function by inhibiting succinate dehydrogenase activity. Biochem, Biophys. Res. Commun. 271:610-614.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 610-614
    • Koundouris, A.1    Kass, G.E.2    Johnson, C.R.3    Boxall, A.4    Sanders, P.G.5    Carter, M.J.6
  • 38
    • 0034641898 scopus 로고    scopus 로고
    • CD95's deadly mission in the immune system
    • Krammer, P. H. 2000. CD95's deadly mission in the immune system. Nature 407:789-795.
    • (2000) Nature , vol.407 , pp. 789-795
    • Krammer, P.H.1
  • 39
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeahilization
    • Lassus, P., X. Opilz-Araya, and Y. Lazebnik. 2002. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeahilization. Science 297:1352-1354.
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opilz-Araya, X.2    Lazebnik, Y.3
  • 40
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist, M. and M. Jäättelä. 2001. Four deaths and a funeral: From caspases to alternative mechanisms, Nat. Rev. Mol. Cell. Biol. 2:589-598.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jäättelä, M.2
  • 41
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L. Y., X. Luo, and X. Wang. 2001. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412:95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 42
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., D. Nijhawan, I. Budihardjo, S. M. Srinivasula, M. Ahmad, E. S. Alnemri, and X. Wang. 1997. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 43
    • 0036468550 scopus 로고    scopus 로고
    • Dysfunctional apoptosome activation in ovarian cancer: Implications for chemoresistance
    • Liu, J. R., A. W. Opipari, L. Tan, Y. Jiang, Y. Zhang, H. Tang, and G. Nunez. 2002. Dysfunctional apoptosome activation in ovarian cancer: Implications for chemoresistance. Cancer Res. 62:924-931.
    • (2002) Cancer Res. , vol.62 , pp. 924-931
    • Liu, J.R.1    Opipari, A.W.2    Tan, L.3    Jiang, Y.4    Zhang, Y.5    Tang, H.6    Nunez, G.7
  • 44
    • 0343090469 scopus 로고    scopus 로고
    • Poliovirus induces apoptosis in the human U937 promonocytic cell line
    • López-Goerero, J. A., M. Alonso, F. Martin-Belmonte, and L. Carrasco. 2000. Poliovirus induces apoptosis in the human U937 promonocytic cell line. Virology 272:250-256.
    • (2000) Virology , vol.272 , pp. 250-256
    • López-Goerero, J.A.1    Alonso, M.2    Martin-Belmonte, F.3    Carrasco, L.4
  • 46
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • Meier, P., A. Finch, and G. Evan. 2000. Apoptosis in development. Nature 407:796-801.
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 47
    • 0037072937 scopus 로고    scopus 로고
    • An ER stress-specific caspase cascade in apoptosis: Cytochrome c-independent activation of caspase-9 by caspase-12
    • Morishima, N., K. Nakanishi, H. Takenouchi, T. Shibata, and Y. Yasuhiko. 2002. An ER stress-specific caspase cascade in apoptosis: Cytochrome c-independent activation of caspase-9 by caspase-12, J. Biol. Chem. 277:34287-34294.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 48
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa, T., and J. Yuan. 2000. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J. Cell Biol. 150: 887-894.
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 49
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa, T., H. Zhu, N. Morishima, E. Li, J. Xu, B. A. Yankner, and J. Yuan. 2000. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403:98-103.
    • (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
  • 50
    • 0034795061 scopus 로고    scopus 로고
    • Poliovirus protein 3A inhibits tumor necrosis factor (TNF)-induced apoptosis by eliminating the TNF receptor from the cell surface
    • Neznanov, N., A. Kondratova, K. M. Chumakov, B. Angres, B. Zhumabayeva, V. I. Agol, and A. V. Gudkov. 2001. Poliovirus protein 3A inhibits tumor necrosis factor (TNF)-induced apoptosis by eliminating the TNF receptor from the cell surface. J. Virol. 75:10409-10420.
    • (2001) J. Virol. , vol.75 , pp. 10409-10420
    • Neznanov, N.1    Kondratova, A.2    Chumakov, K.M.3    Angres, B.4    Zhumabayeva, B.5    Agol, V.I.6    Gudkov, A.V.7
  • 52
    • 0031871102 scopus 로고    scopus 로고
    • Viruses and apoptosis
    • O'Brien. 1998. Viruses and apoptosis. J. Gen. Virol. 79:1833-1845.
    • (1998) J. Gen. Virol. , vol.79 , pp. 1833-1845
    • O'Brien1
  • 54
    • 0025011840 scopus 로고
    • Proteolytic processing of picornaviral polyprotein
    • Palmenberg, A. C. 1990. Proteolytic processing of picornaviral polyprotein. Annu. Rev. Microbiol. 44:603-623.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 603-623
    • Palmenberg, A.C.1
  • 55
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • Pan, G., K. O'Rourke, and V. M. Dixit. 1998. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J. Biol. Chem. 273:5841-5845.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 59
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • Rodriguez, J., and Y. Lazehnik. 1999. Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev. 13:3179-3184
    • (1999) Genes Dev. , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazehnik, Y.2
  • 61
    • 0034802046 scopus 로고    scopus 로고
    • Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex
    • Rust, R. C., L. Landmann, R. Gosert, B. L. Tang, W. Hong, H. P. Hauri, D. Egger, and K. Bienz. 2001. Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex. J. Virol. 75:9808-9818.
    • (2001) J. Virol. , vol.75 , pp. 9808-9818
    • Rust, R.C.1    Landmann, L.2    Gosert, R.3    Tang, B.L.4    Hong, W.5    Hauri, H.P.6    Egger, D.7    Bienz, K.8
  • 62
    • 0035039678 scopus 로고    scopus 로고
    • A structural view of mitochondria-mediated apoptosis
    • Shi, Y. 2001. A structural view of mitochondria-mediated apoptosis. Nat. Struct. Biol. 8:394-401.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 394-401
    • Shi, Y.1
  • 63
    • 0037134511 scopus 로고    scopus 로고
    • Anti-apoptotic activity of the free caspase recruitment domain of procaspase-9: A novel endogenous rescue pathway in cell death
    • Stephanou, A., T. M. Scarabelli, R. A. Knight, and D. S. Latchman. 2002. Anti-apoptotic activity of the free caspase recruitment domain of procaspase-9: A novel endogenous rescue pathway in cell death. J. Biol. Chem. 277:13693-13699.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13693-13699
    • Stephanou, A.1    Scarabelli, T.M.2    Knight, R.A.3    Latchman, D.S.4
  • 65
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki, Y., Y. Imai, H. Nakayama, K. Takahashi, K. Takio, and R. Takahashi. 2001. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell 8:613-621.
    • (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
  • 66
    • 0034737736 scopus 로고    scopus 로고
    • Caspase-3-activation and Bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis
    • Tang, D., J. M. Lahti, and V. J. Kidd. 2000. Caspase-3-activation and Bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis. J. Biol. Chem. 275:9303-9307.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9303-9307
    • Tang, D.1    Lahti, J.M.2    Kidd, V.J.3
  • 67
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N. A., and Y. Lazebnik. 1998. Caspases: Enemies within. Science 281:1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 68
    • 0020678133 scopus 로고
    • Intertypic recombination in poliovirus: Genetic and biochemical studies
    • Tolskaya, E. A., L. I. Romanova, M. S. Kolesnikova, and V. I. Agol. 1983. Intertypic recombination in poliovirus: Genetic and biochemical studies. Virology 124:121-132.
    • (1983) Virology , vol.124 , pp. 121-132
    • Tolskaya, E.A.1    Romanova, L.I.2    Kolesnikova, M.S.3    Agol, V.I.4
  • 72
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux, D. L., and S. J. Korsmeyer. 1999. Cell death in development. Cell 96:245-254.
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 73
    • 0034921727 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs
    • Verhagen, A. M., E. J. Coulson, and D. L. Vaux. 2001. Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs. Genome Biol. 2:3009.1-3009, 10.
    • (2001) Genome Biol. , vol.2 , pp. 30091-300910
    • Verhagen, A.M.1    Coulson, E.J.2    Vaux, D.L.3
  • 75
    • 0030965162 scopus 로고    scopus 로고
    • Cell death induction by TNF: A matter of self control
    • Wallach, D. 1997. Cell death induction by TNF: A matter of self control. Trends Biochem. Sci. 22:107-109.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 107-109
    • Wallach, D.1
  • 76
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami, N., and G. Kroemer. 2001. The mitochondrion in apoptosis: How Pandora's box opens. Nat. Rev. Mol. Cell. Biol. 2:67-71.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 77
    • 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., J. Chou, R. S. Olea, J. Yuan, and G. Wagner. 1999. 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 96:11265-11270.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.