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Volumn 9, Issue 1, 1997, Pages 35-49

The role of the Caspase family of cysteine proteases in apoptosis

Author keywords

Apoptosis; Caspase; Cysteine protease

Indexed keywords

ASPARTIC ACID; CYSTEINE PROTEINASE; INTERLEUKIN 1BETA CONVERTING ENZYME;

EID: 0031080248     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1006/smim.1996.0058     Document Type: Article
Times cited : (197)

References (162)
  • 1
    • 0027525104 scopus 로고
    • The C. Elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • 1. Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 75:641-652
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 2
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1β, a protein lacking a signal sequence
    • 2. Rubartelli A, Cozzolino F, Talio M, Sitia R (1990) A novel secretory pathway for interleukin-1β, a protein lacking a signal sequence. EMBO J 9:1503-1510
    • (1990) EMBO J , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 3
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • 3. Cleves AE, Cooper DNW, Barondes SH, Kelly RB (1996) A new pathway for protein export in Saccharomyces cerevisiae. J Cell Biol 133:1017-1026
    • (1996) J Cell Biol , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.W.2    Barondes, S.H.3    Kelly, R.B.4
  • 4
    • 0002136140 scopus 로고    scopus 로고
    • Cytokine convertase inhibitors
    • Henderson B, Bodmer MW, eds CRC Press, Boca Raton
    • 4. Miller DK (1996) Cytokine convertase inhibitors, in Therapeutic Modulation of Cytokines, (Henderson B, Bodmer MW, eds) pp 143-170. CRC Press, Boca Raton
    • (1996) Therapeutic Modulation of Cytokines , pp. 143-170
    • Miller, D.K.1
  • 13
    • 15844393942 scopus 로고    scopus 로고
    • Activation of the native 45-kDa precursor form of interleukin-1 converting enzyme
    • 13. Yamin T-T, Ayala JM, Miller DK (1996) Activation of the native 45-kDa precursor form of Interleukin-1 converting enzyme. J Biol Chem 271:13273-13282
    • (1996) J Biol Chem , vol.271 , pp. 13273-13282
    • Yamin, T.-T.1    Ayala, J.M.2    Miller, D.K.3
  • 14
    • 0028674139 scopus 로고
    • Interleukin-1β converting enzyme
    • 14. Thornberry N (1994) Interleukin-1β converting enzyme. Meth Enzymol 244:615-631
    • (1994) Meth Enzymol , vol.244 , pp. 615-631
    • Thornberry, N.1
  • 15
    • 0028988541 scopus 로고
    • Interleukin-1β converting enzyme requires oligomerization for activity of processed forms in vivo
    • 15. Gu Y, Wu J, Faucheu C, Lalanne J-L, Diu A, Livingston DJ, Su S-S (1995) Interleukin-1β converting enzyme requires oligomerization for activity of processed forms in vivo. EMBO J 14:1923-1931
    • (1995) EMBO J , vol.14 , pp. 1923-1931
    • Gu, Y.1    Wu, J.2    Faucheu, C.3    Lalanne, J.-L.4    Diu, A.5    Livingston, D.J.6    Su, S.-S.7
  • 17
    • 0028169817 scopus 로고
    • Interleukin-1β-converting enzyme is present in monocytic cells as an inactive 45-kDa precursor
    • 17. Ayala JM, Tamin TT, Egger LA, Chin J, Kostura MJ, Miller DK (1994) Interleukin-1β-converting enzyme is present in monocytic cells as an inactive 45-kDa precursor. J Immunol 153:2592-2599
    • (1994) J Immunol , vol.153 , pp. 2592-2599
    • Ayala, J.M.1    Tamin, T.T.2    Egger, L.A.3    Chin, J.4    Kostura, M.J.5    Miller, D.K.6
  • 19
    • 0029048909 scopus 로고
    • Reduction of inflammation and pyrexia in the rat by oral administration of SDZ 224-105, an inhibitor of the interleukin-1β converting enzyme
    • 19. Elford PR, Heng R, Revesz L, MacKenzie AR (1995) Reduction of inflammation and pyrexia in the rat by oral administration of SDZ 224-105, an inhibitor of the interleukin-1β converting enzyme. Br J Pharmacol 115:601-606
    • (1995) Br J Pharmacol , vol.115 , pp. 601-606
    • Elford, P.R.1    Heng, R.2    Revesz, L.3    MacKenzie, A.R.4
  • 24
    • 2642667881 scopus 로고
    • Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases
    • 24. Pickup DJ, Ink BS, Hu W, Ray CA, Joklik WK (1986) Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases. Proc Natl Acad Sci USA 83:7698-7702
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7698-7702
    • Pickup, D.J.1    Ink, B.S.2    Hu, W.3    Ray, C.A.4    Joklik, W.K.5
  • 25
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme
    • 25. Ray CA, Black RA, Kronheim SR, Greenstreet TA, Sleath PR, Salvesen GS, Pickup DJ (1992) Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme. Cell 69:597-604
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvesen, G.S.6    Pickup, D.J.7
  • 27
    • 0029976336 scopus 로고    scopus 로고
    • The mode of death of pig kidney cells infected with cowpox virus is governed by the expression of the crmA gene
    • 27. Ray CA, Pickup DJ (1996) The mode of death of pig kidney cells infected with cowpox virus is governed by the expression of the crmA gene. Virology 217:384-391
    • (1996) Virology , vol.217 , pp. 384-391
    • Ray, C.A.1    Pickup, D.J.2
  • 28
    • 0029056059 scopus 로고
    • Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein
    • 28. Xue D, Horvitz HR (1995) Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein. Nature 377:248-251
    • (1995) Nature , vol.377 , pp. 248-251
    • Xue, D.1    Horvitz, H.R.2
  • 30
    • 0025255636 scopus 로고
    • The Caenorhabditis elegans Genes ced-3 and ced-4 act cell autonomously to cause programmed cell death
    • 30. Yuan J, Horvitz HR (1990) The Caenorhabditis elegans Genes ced-3 and ced-4 act cell autonomously to cause programmed cell death. Dev Biol 138:33-41
    • (1990) Dev Biol , vol.138 , pp. 33-41
    • Yuan, J.1    Horvitz, H.R.2
  • 31
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. Elegans cell death gene ced-3
    • 31. Miura M, Zhu H, Rotello R, Hartweig EA, Yuang J (1993) Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 75:653-660
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartweig, E.A.4    Yuang, J.5
  • 32
    • 0029328602 scopus 로고
    • bcl-2, a novel regulator of cell death
    • 32. Hockenbery DM (1995) bcl-2, a novel regulator of cell death. BioEssays 17:631-638
    • (1995) BioEssays , vol.17 , pp. 631-638
    • Hockenbery, D.M.1
  • 33
    • 0001216397 scopus 로고    scopus 로고
    • Regulation of apoptosis by members of the ice gene family and the Bcl-2 family
    • Bristol JA, Ed. Academic Press, San Diego, CA
    • 33. Miller DK (1996) Regulation of apoptosis by members of the ICE gene family and the Bcl-2 family, in Ann Rep Med Chem (Bristol JA, Ed.) pp 249-268. Academic Press, San Diego, CA
    • (1996) Ann Rep Med Chem , pp. 249-268
    • Miller, D.K.1
  • 35
    • 0029022365 scopus 로고
    • Involvement of an ICE-like protease in Fas-mediated apoptosis
    • 35. Enari M, Hug H, Nagata S (1995) Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 375:78-81
    • (1995) Nature , vol.375 , pp. 78-81
    • Enari, M.1    Hug, H.2    Nagata, S.3
  • 37
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
    • 37. Enari M, Talanian RV, Wong WW, Nagata S (1996) Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis. Nature 380:723-726
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 38
    • 0027999537 scopus 로고
    • Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death
    • 38. Casciola-Rosen LA, Miller DK, Anhalt GJ, Rosen A (1994) Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J Biol Chem 269:30757-30760
    • (1994) J Biol Chem , vol.269 , pp. 30757-30760
    • Casciola-Rosen, L.A.1    Miller, D.K.2    Anhalt, G.J.3    Rosen, A.4
  • 39
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • 39. Lazebnik YA, Kaufmann SH, Desnoyers S, Poirier GG, Earnshaw WC (1994) Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371:346-347
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 42
    • 0029608812 scopus 로고
    • Macrophage apoptosis in the absence of active interleukin-1β-converting enzyme
    • 42. Nett-Fiordalisi M, Tomaselli K, Russell JH, Chaplin DD (1995) Macrophage apoptosis in the absence of active interleukin-1β-converting enzyme. J Leuk Biol 58:717-724
    • (1995) J Leuk Biol , vol.58 , pp. 717-724
    • Nett-Fiordalisi, M.1    Tomaselli, K.2    Russell, J.H.3    Chaplin, D.D.4
  • 43
    • 0028983208 scopus 로고
    • IL-1β converting enzyme (ICE) is not required for apoptosis induced by lymphokine deprivation in an IL-2-dependent T cell line
    • 43. Vasilakos JP, Ghayur T, Carroll RT, Giegel DA, Saunders JM, Quintal L, Keane KM, Shivers BD (1995) IL-1β converting enzyme (ICE) is not required for apoptosis induced by lymphokine deprivation in an IL-2-dependent T cell line. J Immunol 155:3433-3442
    • (1995) J Immunol , vol.155 , pp. 3433-3442
    • Vasilakos, J.P.1    Ghayur, T.2    Carroll, R.T.3    Giegel, D.A.4    Saunders, J.M.5    Quintal, L.6    Keane, K.M.7    Shivers, B.D.8
  • 45
    • 0028797399 scopus 로고
    • The cellular responses to DNA damage
    • 45. Carr AM, Hoekstra MF (1995) The cellular responses to DNA damage. Trends Cell Biol 5:32-40
    • (1995) Trends Cell Biol , vol.5 , pp. 32-40
    • Carr, A.M.1    Hoekstra, M.F.2
  • 47
    • 0029048745 scopus 로고
    • Apoptosis and the cell cycle
    • 47. Meikrantz W, Schlegel R (1995) Apoptosis and the cell cycle. J Cell Biochem 58:160-174
    • (1995) J Cell Biochem , vol.58 , pp. 160-174
    • Meikrantz, W.1    Schlegel, R.2
  • 48
    • 0029136149 scopus 로고
    • Apoptosis in viral infections
    • Maramorosch K, Murphy FA, Shatkin AJ, Eds Academic Press, San Diego
    • 48. Razvi ES, Welsh RM (1995) Apoptosis in viral infections, in Advances in Virus Research (Maramorosch K, Murphy FA, Shatkin AJ, Eds) pp 1-60. Academic Press, San Diego
    • (1995) Advances in Virus Research , pp. 1-60
    • Razvi, E.S.1    Welsh, R.M.2
  • 49
    • 0029891162 scopus 로고    scopus 로고
    • Apoptosis - Molecular mechanisms and biomedical implications
    • 49. McConkey DJ, Zhivotovsky B, Orrenius S (1996) Apoptosis - molecular mechanisms and biomedical implications. Molec Aspects Med 17:1-110
    • (1996) Molec Aspects Med , vol.17 , pp. 1-110
    • McConkey, D.J.1    Zhivotovsky, B.2    Orrenius, S.3
  • 50
    • 0030272687 scopus 로고    scopus 로고
    • Diverse molecular provocation of programmed cell death
    • 50. Wertz IE, Hanley MR (1996) Diverse molecular provocation of programmed cell death. TIBS 21:359-364
    • (1996) TIBS , vol.21 , pp. 359-364
    • Wertz, I.E.1    Hanley, M.R.2
  • 53
    • 0028841537 scopus 로고
    • An ICE-like protease is a common mediator of apoptosis induced by diverse stimuli in human monocytic THP.1 cells
    • 53. Zhu H, Fearnhead HO, Cohen GM (1995) An ICE-like protease is a common mediator of apoptosis induced by diverse stimuli in human monocytic THP.1 cells. FEBS Lett 374:303-308
    • (1995) FEBS Lett , vol.374 , pp. 303-308
    • Zhu, H.1    Fearnhead, H.O.2    Cohen, G.M.3
  • 56
    • 0030060075 scopus 로고    scopus 로고
    • Requirement of an ICE-like protease for induction of apoptosis and ceramide generation by REAPER
    • 56. Pronk GJ, Ramer K, Amiri P, Williams LT (1996) Requirement of an ICE-like protease for induction of apoptosis and ceramide generation by REAPER. Science 271:808-810
    • (1996) Science , vol.271 , pp. 808-810
    • Pronk, G.J.1    Ramer, K.2    Amiri, P.3    Williams, L.T.4
  • 57
    • 0029890689 scopus 로고    scopus 로고
    • The contrasting roles of ICE family proteases and interleukin-1β in apoptosis induced by tropic factor withdrawal and by copper/ zinc superoxide dismutase down-regulation
    • 57. Troy CM, Stefanis L, Prochiantz A, Greene LA, Shelanski ML (1996) The contrasting roles of ICE family proteases and interleukin-1β in apoptosis induced by tropic factor withdrawal and by copper/ zinc superoxide dismutase down-regulation. Proc Natl Acad Sci USA 93:5635-5640
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5635-5640
    • Troy, C.M.1    Stefanis, L.2    Prochiantz, A.3    Greene, L.A.4    Shelanski, M.L.5
  • 58
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of Poly(ADP)-ribose polymerase: An early marker of chemotherapy-induced apoptosis
    • 58. Kaufmann SH, Desnoyerws S, Ottaviano Y, Davidson NE, Poirier GG (1993) Specific proteolytic cleavage of Poly(ADP)-ribose polymerase: an early marker of chemotherapy-induced apoptosis. Cancer Res 53:3976-3985
    • (1993) Cancer Res , vol.53 , pp. 3976-3985
    • Kaufmann, S.H.1    Desnoyerws, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 60
    • 14844356354 scopus 로고
    • Degradation of Lamin B1 precedes oligonucleosomal dna fragmentation in apoptotic thymocytes and isolated thymocyte nuclei
    • 60. Neamati N, Fernandez A, Wright S, Kiefer J, McConkey DJ (1995) Degradation of Lamin B1 precedes oligonucleosomal DNA fragmentation in apoptotic thymocytes and isolated thymocyte nuclei. J Immunol 154:3788-3795
    • (1995) J Immunol , vol.154 , pp. 3788-3795
    • Neamati, N.1    Fernandez, A.2    Wright, S.3    Kiefer, J.4    McConkey, D.J.5
  • 61
    • 0028881847 scopus 로고
    • DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis
    • 61. Casciola-Rosen LA, Anhalt GJ, Rosen A (1995) DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis. J Exp Med 182:1625-1634
    • (1995) J Exp Med , vol.182 , pp. 1625-1634
    • Casciola-Rosen, L.A.1    Anhalt, G.J.2    Rosen, A.3
  • 63
    • 0030576945 scopus 로고    scopus 로고
    • CPP32/ Yama/ apopain cleaves the catalytic component of DNA-dependent protein kinase in the holoenzyme
    • 63. Teraoka H, Yumoto Y, Watanabe F, Tsukada K, Suwa A, Enari M, Nagata S (1996) CPP32/ Yama/ apopain cleaves the catalytic component of DNA-dependent protein kinase in the holoenzyme. FEBS Lett 393:1-6
    • (1996) FEBS Lett , vol.393 , pp. 1-6
    • Teraoka, H.1    Yumoto, Y.2    Watanabe, F.3    Tsukada, K.4    Suwa, A.5    Enari, M.6    Nagata, S.7
  • 65
    • 0030058584 scopus 로고    scopus 로고
    • Dynamic changes of NuMA during the cell cycle and possible appearance of a truncated form of numa during apoptosis
    • 65. Hsu H-L, Yeh N-H (1996) Dynamic changes of NuMA during the cell cycle and possible appearance of a truncated form of NuMA during apoptosis. J Cell Sci 109:277-288
    • (1996) J Cell Sci , vol.109 , pp. 277-288
    • Hsu, H.-L.1    Yeh, N.-H.2
  • 67
    • 0028788309 scopus 로고
    • Microfilament reorganization during apoptosis: The role of Gas2, a possible substrate for ICE-like proteases
    • 67. Brancolini C, Benedetti M, Schneider C (1995) Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. EMBO J 14:5179-5190
    • (1995) EMBO J , vol.14 , pp. 5179-5190
    • Brancolini, C.1    Benedetti, M.2    Schneider, C.3
  • 68
    • 0029610432 scopus 로고
    • Identification of actin as a substrate of ICE and an ICE-like protease and involvement of an ICE-like protease but not ICE in VP-16-induced U937 apoptosis
    • 68. Mashima T, Naito M, Fujita N, Noguchi K, Tsuruo T (1995) Identification of actin as a substrate of ICE and an ICE-like protease and involvement of an ICE-like protease but not ICE in VP-16-induced U937 apoptosis. Biochem Biophys Res Commun 217:1185-1192
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 1185-1192
    • Mashima, T.1    Naito, M.2    Fujita, N.3    Noguchi, K.4    Tsuruo, T.5
  • 69
    • 0029876247 scopus 로고    scopus 로고
    • Cleavage of actin by interleukin-1β-converting enzyme to reverse DNase I inhibition
    • 69. Kayalar C, Ord T, Testa MP, Zhong L-T, Bredesen DE (1996) Cleavage of actin by interleukin-1β-converting enzyme to reverse DNase I inhibition. Proc Natl Acad Sci USA 93:2234-2238
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2234-2238
    • Kayalar, C.1    Ord, T.2    Testa, M.P.3    Zhong, L.-T.4    Bredesen, D.E.5
  • 71
    • 0030023846 scopus 로고    scopus 로고
    • Cleavage of retinoblastoma protein during apoptosis: An interleukin 1β-converting enzyme-like protease as candidate
    • 71. An B, Dou QP (1996) Cleavage of retinoblastoma protein during apoptosis: an interleukin 1β-converting enzyme-like protease as candidate. Cancer Res 56:438-442
    • (1996) Cancer Res , vol.56 , pp. 438-442
    • An, B.1    Dou, Q.P.2
  • 73
    • 0029871920 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis
    • 73. Wang X, Zelenski NG, Yang J, Sakai J, Brown MS, Goldstein JL (1996) Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis. EMBO J 15:1012-1020
    • (1996) EMBO J , vol.15 , pp. 1012-1020
    • Wang, X.1    Zelenski, N.G.2    Yang, J.3    Sakai, J.4    Brown, M.S.5    Goldstein, J.L.6
  • 74
    • 0028833024 scopus 로고
    • Activation of intracellular proteases is an early event in TNF-induced apoptosis
    • 74. Voelkel-Johnson C, Entingh AJ, Wold WS, Gooding LR, Laster SM (1995) Activation of intracellular proteases is an early event in TNF-induced apoptosis. J Immunol 154:1707-1716
    • (1995) J Immunol , vol.154 , pp. 1707-1716
    • Voelkel-Johnson, C.1    Entingh, A.J.2    Wold, W.S.3    Gooding, L.R.4    Laster, S.M.5
  • 75
    • 0029789073 scopus 로고    scopus 로고
    • Selective cleavage of nuclear autoantigens during CD95 (Fas/ APO-1)-mediated T cell apoptosis
    • 75. Casiano CA, Martin SJ, Green DR, Tan EM (1996) Selective cleavage of nuclear autoantigens during CD95 (Fas/ APO-1)-mediated T cell apoptosis. J Exp Med 184:765-770
    • (1996) J Exp Med , vol.184 , pp. 765-770
    • Casiano, C.A.1    Martin, S.J.2    Green, D.R.3    Tan, E.M.4
  • 77
    • 0028978248 scopus 로고
    • Purification of an interleukin-1β converting enzyme-related cysteine protease that cleaves sterol regulatory element-binding proteins between the leucine zipper and transmembrane domains
    • 77. Wang X, Pai J-T, Wiedenfeld EA, Medina JC, Slaughter CA, Goldstein JL, Brown MS (1995) Purification of an interleukin-1β converting enzyme-related cysteine protease that cleaves sterol regulatory element-binding proteins between the leucine zipper and transmembrane domains. J Biol Chem 270:18044-18050
    • (1995) J Biol Chem , vol.270 , pp. 18044-18050
    • Wang, X.1    Pai, J.-T.2    Wiedenfeld, E.A.3    Medina, J.C.4    Slaughter, C.A.5    Goldstein, J.L.6    Brown, M.S.7
  • 78
    • 0029890823 scopus 로고    scopus 로고
    • Apopain/ CPP32 cleaves proteins that are essential for cellular repair: A fundamental principle of apoptotic death
    • 78. Casciola-Rosen L, Nicholson DW, Chong T, Rowan KR, Thornberry NA, Miller DK, Rosen A (1996) Apopain/ CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death. J Exp Med 183:1957-1964
    • (1996) J Exp Med , vol.183 , pp. 1957-1964
    • Casciola-Rosen, L.1    Nicholson, D.W.2    Chong, T.3    Rowan, K.R.4    Thornberry, N.A.5    Miller, D.K.6    Rosen, A.7
  • 80
    • 0001864010 scopus 로고
    • The Merck Gene Indices, a public resource for genomics research
    • 80. Williamson AR, Elliston KO, Sturchio JL (1995) The Merck Gene Indices, a public resource for genomics research, J NIH Res 7:61-63
    • (1995) J NIH Res , vol.7 , pp. 61-63
    • Williamson, A.R.1    Elliston, K.O.2    Sturchio, J.L.3
  • 82
    • 0029787268 scopus 로고    scopus 로고
    • Molecular ordering of apoptotic mammalian CED-3/ ICE-like proteases
    • 82. Orth K, O'Rourke K, Salvesen GS, Dixit VM (1996) Molecular ordering of apoptotic mammalian CED-3/ ICE-like proteases. J Biol Chem 271:20977-20980
    • (1996) J Biol Chem , vol.271 , pp. 20977-20980
    • Orth, K.1    O'Rourke, K.2    Salvesen, G.S.3    Dixit, V.M.4
  • 83
    • 0026763128 scopus 로고
    • Identification of a set of genes with developmentally down-regulated expression in the mouse brain
    • 83. Kumar S, Tomooka Y, Noda M (1982) Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem Biophys Res Commun 185:1155-1161
    • (1982) Biochem Biophys Res Commun , vol.185 , pp. 1155-1161
    • Kumar, S.1    Tomooka, Y.2    Noda, M.3
  • 84
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme
    • 84. Kumar S, Kinoshita M, Noda M, Copeland NG, Jenkins NA (1994) Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme. Genes Dev 8:1613-1626
    • (1994) Genes Dev , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 85
    • 0028168593 scopus 로고
    • Ich-1, and Ice/ ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • 85. Wang L, Miura M, Bergeron L, Zhu H, Yuan J (1994) Ich-1, and Ice/ ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 78:739-750
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 86
    • 0028998012 scopus 로고    scopus 로고
    • Inhibition of apoptosis by the expression of antisense Nedd2
    • 86. Kumar S (1996) Inhibition of apoptosis by the expression of antisense Nedd2. FEBS Lett 368:69-72
    • (1996) FEBS Lett , vol.368 , pp. 69-72
    • Kumar, S.1
  • 87
    • 0027973061 scopus 로고
    • CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1β-converting enzyme
    • 87. Fernandes-Alnemri T, Litwack G, Alnemri ES (1994) CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1β-converting enzyme. J Biol Chem 269:30761-30764
    • (1994) J Biol Chem , vol.269 , pp. 30761-30764
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 88
    • 0028990125 scopus 로고
    • Yama/ CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • 88. Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM (1995) Yama/ CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81:801-809
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 89
    • 0029880987 scopus 로고    scopus 로고
    • The caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease
    • 89. Xue D, Shaham S, Horvitz HR (1996) The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes Dev 10:1073-1083
    • (1996) Genes Dev , vol.10 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 90
    • 0029820016 scopus 로고    scopus 로고
    • Activation of the CPP32 protease in apoptosis induced by 1-beta-darabinofuranosylcytosine and other DNA-damaging agents
    • 90. Datta R, Banach D, Kojima H, Talanian RV, Alnemri ES, Wong WW (1996) Activation of the CPP32 protease in apoptosis induced by 1-beta-darabinofuranosylcytosine and other DNA-damaging agents. Blood 88:1936-1943
    • (1996) Blood , vol.88 , pp. 1936-1943
    • Datta, R.1    Banach, D.2    Kojima, H.3    Talanian, R.V.4    Alnemri, E.S.5    Wong, W.W.6
  • 91
    • 0030605878 scopus 로고    scopus 로고
    • Sequential activation of three distinct ICE-like activities in Fas-ligated Jurkat cells
    • 91. Greidinger EL, Miller DK, Yamin T-T, Casciola-Rosen L, Rosen A (1996) Sequential activation of three distinct ICE-like activities in Fas-ligated Jurkat cells. FEBS Lett 390:299-303
    • (1996) FEBS Lett , vol.390 , pp. 299-303
    • Greidinger, E.L.1    Miller, D.K.2    Yamin, T.-T.3    Casciola-Rosen, L.4    Rosen, A.5
  • 95
    • 0029025549 scopus 로고
    • Mch2, a new member of the apoptotic Ced-3/ Ice cysteine protease gene family
    • 95. Fernandes-Alnemri T, Litwack G, Alnemri ES (1995) Mch2, a new member of the apoptotic Ced-3/ Ice cysteine protease gene family. Cancer Res 55:2737-2742
    • (1995) Cancer Res , vol.55 , pp. 2737-2742
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 98
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • 98. Orth K, Chinnaiyan AM, Garg M, Froelich CJ, Dixit VM (1996) The CED-3/ ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J Biol Chem 271:16443-16446
    • (1996) J Biol Chem , vol.271 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, C.J.4    Dixit, V.M.5
  • 99
    • 0030013054 scopus 로고    scopus 로고
    • Purification and characterization of an interleukin-1β-converting enzyme family protease that activates cysteine protease p32 (CPP32)
    • 99. Liu X, CN K, Pohl J, Wang X (1996) Purification and characterization of an interleukin-1β-converting enzyme family protease that activates cysteine protease P32 (CPP32). J Biol Chem 271:13371-13376
    • (1996) J Biol Chem , vol.271 , pp. 13371-13376
    • Liu, X.1    Cn, K.2    Pohl, J.3    Wang, X.4
  • 101
    • 0030044324 scopus 로고    scopus 로고
    • ICE-LAP3, a novel mammalian homolog of the Caenorhabditis elegans cell death protein CED-3 is activated during Fas-and tumor necrosis factor-induced apoptosis
    • 101. Duan H, Chinnaiyan AM, Hudson PL, Wing JP, He W-W, Dixit VM (1996) ICE-LAP3, a novel mammalian homolog of the Caenorhabditis elegans cell death protein CED-3 is activated during Fas-and tumor necrosis factor-induced apoptosis. J Biol Chem 271:1621-1625
    • (1996) J Biol Chem , vol.271 , pp. 1621-1625
    • Duan, H.1    Chinnaiyan, A.M.2    Hudson, P.L.3    Wing, J.P.4    He, W.-W.5    Dixit, V.M.6
  • 102
    • 0030044012 scopus 로고    scopus 로고
    • Identification and characterization of CPP32/ Mch2 homolog 1, a novel cystein protease similar to CPP32
    • 102. Lippke JA, Gu Y, Sarnecki C, Caron PR, Su MS-S (1996) Identification and characterization of CPP32/ Mch2 homolog 1, a novel cystein protease similar to CPP32. J Biol Chem 271:1825-1828
    • (1996) J Biol Chem , vol.271 , pp. 1825-1828
    • Lippke, J.A.1    Gu, Y.2    Sarnecki, C.3    Caron, P.R.4    Su, M.S.-S.5
  • 103
    • 0029895343 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a second apoptosis-related cystein protease that cleaves and activates sterol regulatory element binding proteins
    • 103. Pai JT, Brown MS, Goldstein JL (1996) Purification and cDNA cloning of a second apoptosis-related cystein protease that cleaves and activates sterol regulatory element binding proteins. Proc Natl Acad Sci USA 93:5437-5442
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5437-5442
    • Pai, J.T.1    Brown, M.S.2    Goldstein, J.L.3
  • 104
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/ FADD-interacting protease, in Fas/ APO-1-and TNF receptor-induced cell death
    • 104. Boldin MP, Goncharov TM, Goltsev YV, Wallach D (1996) Involvement of MACH, a novel MORT1/ FADD-interacting protease, in Fas/ APO-1-and TNF receptor-induced cell death. Cell 85:803-815
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 106
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domains of Fas/ APO1 contains a sequence motif related to the death domain
    • 106. Boldin MP, Varfolomeev EE, Pancer Z, Mett IL, Camonis JH, Wallach D (1995) A novel protein that interacts with the death domains of Fas/ APO1 contains a sequence motif related to the death domain. J Biol Chem 270:7795-7798
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 107
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • 107. Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM (1995) FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81:505-512
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 109
    • 0028843735 scopus 로고
    • A region of the 75 kDa neurotrophin receptor homologous to the death domains of TNFR-1 and Fas
    • 109. Chapman BS (1995) A region of the 75 kDa neurotrophin receptor homologous to the death domains of TNFR-1 and Fas. FEBS Lett 374:216-220
    • (1995) FEBS Lett , vol.374 , pp. 216-220
    • Chapman, B.S.1
  • 111
    • 0030008812 scopus 로고    scopus 로고
    • ICE-LAP6, a novel member of the ICE/ Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B
    • 111. Duan H, Orth K, Chinnaiyan AM, Poirier GG, Froelich GJ, He W-W, Dixit VM (1996) ICE-LAP6, a novel member of the ICE/ Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B. J Biol Chem 271:16720-16724
    • (1996) J Biol Chem , vol.271 , pp. 16720-16724
    • Duan, H.1    Orth, K.2    Chinnaiyan, A.M.3    Poirier, G.G.4    Froelich, G.J.5    He, W.-W.6    Dixit, V.M.7
  • 113
    • 0029808205 scopus 로고    scopus 로고
    • Identification and characterization of Ich-3, a member of the Interleukin-1β converting enzyme (ICE)/ Ced-3 family and an upstream regulator of ICE
    • 113. Wang S, Miura M, Jung Y-k, Zhu H, Gagliardini V, Shi L, Greenberg AH, Yuan J (1996) Identification and characterization of Ich-3, a member of the Interleukin-1β converting enzyme (ICE)/ Ced-3 family and an upstream regulator of ICE. J Biol Chem 271:20580-20587
    • (1996) J Biol Chem , vol.271 , pp. 20580-20587
    • Wang, S.1    Miura, M.2    Jung, Y.-K.3    Zhu, H.4    Gagliardini, V.5    Shi, L.6    Greenberg, A.H.7    Yuan, J.8
  • 114
    • 0028932731 scopus 로고
    • The CTL's kiss of death
    • 114. Berke G (1995) The CTL's kiss of death. Cell 81:9-12
    • (1995) Cell , vol.81 , pp. 9-12
    • Berke, G.1
  • 116
    • 0029521162 scopus 로고
    • Mechanisms of lysis by cytotoxic T cells
    • 115a. Atkinson EA, Bleackley RC (1995) Mechanisms of lysis by cytotoxic T cells. Crit Rev Immunol 15:359-384
    • (1995) Crit Rev Immunol , vol.15 , pp. 359-384
    • Atkinson, E.A.1    Bleackley, R.C.2
  • 119
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • 118. Darmon AJ, Nicholson DW, Bleackley RC (1995) Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 377:446-448
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 123
    • 0028597986 scopus 로고
    • The cytotoxic T cell proteinase granzyme B does not activate interleukin-1β-converting enzyme
    • 122. Darmon AJ, Ehrman N, Caputo A, Fujinaga J, Bleackley RC (1994) The cytotoxic T cell proteinase granzyme B does not activate interleukin-1β-converting enzyme. J Biol Chem 269:32043-32046
    • (1994) J Biol Chem , vol.269 , pp. 32043-32046
    • Darmon, A.J.1    Ehrman, N.2    Caputo, A.3    Fujinaga, J.4    Bleackley, R.C.5
  • 125
    • 0029114963 scopus 로고
    • Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway
    • 124. Miura M, Friedlander RM, Yuan Y (1995) Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway. Proc Natl Acad Sci USA 92:8318-8322
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8318-8322
    • Miura, M.1    Friedlander, R.M.2    Yuan, Y.3
  • 126
    • 0028873964 scopus 로고
    • Fas-and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product
    • 125. Tewari M, Dixit VM (1995) Fas-and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product. J Biol Chem 270:3255-3260
    • (1995) J Biol Chem , vol.270 , pp. 3255-3260
    • Tewari, M.1    Dixit, V.M.2
  • 127
    • 0029120118 scopus 로고
    • CrmA, poxvirus-encoded serpin, inhibits cytotoxic T-lymphocyte-mediated apoptosis
    • 126. Tewari M, Telford WG, Miller RA, Dixit VM (1995) CrmA, poxvirus-encoded serpin, inhibits cytotoxic T-lymphocyte-mediated apoptosis. J Biol Chem 270:22705-22708
    • (1995) J Biol Chem , vol.270 , pp. 22705-22708
    • Tewari, M.1    Telford, W.G.2    Miller, R.A.3    Dixit, V.M.4
  • 129
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • 128. Hockenbery D, Nunez G, Milliman C, Schreiber RD, Korsmeyer SJ (1990) Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348:334-336
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 130
    • 0027362667 scopus 로고
    • Investigations of the subcellular distribution of the BCL-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum and outer mitochondrial membranes
    • 129. Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC (1993) Investigations of the subcellular distribution of the BCL-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum and outer mitochondrial membranes. Cancer Res 53:4701-4714
    • (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
  • 131
    • 0028149786 scopus 로고
    • Checkpoints of dueling dimers foil death wishes
    • 130. Oltvai ZN, Korsmeyer SJ (1994) Checkpoints of dueling dimers foil death wishes. Cell 79:189-192
    • (1994) Cell , vol.79 , pp. 189-192
    • Oltvai, Z.N.1    Korsmeyer, S.J.2
  • 132
    • 0028206341 scopus 로고
    • BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax
    • 131. Yin X-M, Oltvai ZN, Korsmeyer SJ (1994) BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature 369:321-323
    • (1994) Nature , vol.369 , pp. 321-323
    • Yin, X.-M.1    Oltvai, Z.N.2    Korsmeyer, S.J.3
  • 136
    • 0026574178 scopus 로고
    • Diphtheria-toxin - Membrane interaction and membrane translocation
    • 135. London E (1992) Diphtheria-toxin - membrane interaction and membrane translocation. Biochim Biophys Acta 1113:25-51
    • (1992) Biochim Biophys Acta , vol.1113 , pp. 25-51
    • London, E.1
  • 137
    • 0027443116 scopus 로고
    • Rendering a membrane - Protein soluble in water - A common packing motif in bacterial protein toxins
    • 136. Parker MW, Pattus F (1993) Rendering a membrane - protein soluble in water - a common packing motif in bacterial protein toxins. TIBS 18:391-395
    • (1993) TIBS , vol.18 , pp. 391-395
    • Parker, M.W.1    Pattus, F.2
  • 138
    • 0029886877 scopus 로고    scopus 로고
    • 2+ fluxes to inhibit apoptosis in thapsigargin-and glucocorticoid-treated mouse lymphoma cells
    • 2+ fluxes to inhibit apoptosis in thapsigargin-and glucocorticoid-treated mouse lymphoma cells. Cell Calcium 19:473-483
    • (1996) Cell Calcium , vol.19 , pp. 473-483
    • Distelhorst, C.W.1    McCormick, T.S.2
  • 139
    • 0029912189 scopus 로고    scopus 로고
    • Molecular ordering of the cell death pathway. Bcl-2 and Bcl-xl function upstream of the CED-3 like apoptotic proteases
    • 138. Chinnaiyan AM, Orth K, O'Rourke K, Duan H, Poirier GG, Dixit VM (1996) Molecular ordering of the cell death pathway. Bcl-2 and Bcl-xL function upstream of the CED-3 like apoptotic proteases. J Biol Chem 271:4573-4576
    • (1996) J Biol Chem , vol.271 , pp. 4573-4576
    • Chinnaiyan, A.M.1    Orth, K.2    O'Rourke, K.3    Duan, H.4    Poirier, G.G.5    Dixit, V.M.6
  • 140
    • 0030220462 scopus 로고    scopus 로고
    • Bcl-2 regulates activation of apoptotic proteases in a cell-free system
    • 139. Cosulich SC, Green S, Clarke PR (1996) Bcl-2 regulates activation of apoptotic proteases in a cell-free system. Curr Biol 6:997-1005
    • (1996) Curr Biol , vol.6 , pp. 997-1005
    • Cosulich, S.C.1    Green, S.2    Clarke, P.R.3
  • 141
  • 142
    • 0029609086 scopus 로고
    • Bcl-2 and Fas/ APO-1 regulate distinct pathways to lymphocyte apoptosis
    • 141. Strasser A, Harris AW, Huang DCS, Krammer PH, Cory S (1995) Bcl-2 and Fas/ APO-1 regulate distinct pathways to lymphocyte apoptosis. EMBO J 14:6136-6147
    • (1995) EMBO J , vol.14 , pp. 6136-6147
    • Strasser, A.1    Harris, A.W.2    Huang, D.C.S.3    Krammer, P.H.4    Cory, S.5
  • 144
    • 0025852746 scopus 로고
    • The E1B oncogene of adenovirus confers cellular resistance to cytotoxicity of tumor necrosis factor and monoclonal anti-fas antibody
    • 143. Hashimoto SA, Ishii A, Yonehara S (1991) The E1B oncogene of adenovirus confers cellular resistance to cytotoxicity of tumor necrosis factor and monoclonal anti-Fas antibody. Int Immunol 3:343-351
    • (1991) Int Immunol , vol.3 , pp. 343-351
    • Hashimoto, S.A.1    Ishii, A.2    Yonehara, S.3
  • 145
    • 0028059445 scopus 로고
    • Functional complementation of the Adenovirus E1B 19K protein with Bcl-2 in the inhibition of infected cells
    • 144. Chiou S-K, Tseng C-C, Rao L, White E (1994) Functional complementation of the Adenovirus E1B 19K protein with Bcl-2 in the inhibition of infected cells. J Virol 68:6553-6566
    • (1994) J Virol , vol.68 , pp. 6553-6566
    • Chiou, S.-K.1    Tseng, C.-C.2    Rao, L.3    White, E.4
  • 147
    • 0026344133 scopus 로고
    • Prevention of apoptosis by a baculovirus gene during infection of insect cells
    • 146. Clem RJ, Fechheimer M, Miller LJ (1991) Prevention of apoptosis by a baculovirus gene during infection of insect cells. Science 254:1388-1390
    • (1991) Science , vol.254 , pp. 1388-1390
    • Clem, R.J.1    Fechheimer, M.2    Miller, L.J.3
  • 148
    • 0027430789 scopus 로고
    • Expression of the baculovirus p35 gene inhibits mammalian neural cell death
    • 147. Rabizadeh S, LaCount DJ, Friesen PD, Bredesen DE (1993) Expression of the baculovirus p35 gene inhibits mammalian neural cell death. J Neurochem 61:2318-2321
    • (1993) J Neurochem , vol.61 , pp. 2318-2321
    • Rabizadeh, S.1    LaCount, D.J.2    Friesen, P.D.3    Bredesen, D.E.4
  • 149
    • 0028271740 scopus 로고
    • Baculovirus p35 prevents developmentally programmed cell death and rescues a ced-9 mutant in the nematode Caenorhabditis elegans
    • 148. Sugimoto A, Friesen PD, Rothman JH (1994) Baculovirus p35 prevents developmentally programmed cell death and rescues a ced-9 mutant in the nematode Caenorhabditis elegans. EMBO J 13:2023-2028
    • (1994) EMBO J , vol.13 , pp. 2023-2028
    • Sugimoto, A.1    Friesen, P.D.2    Rothman, J.H.3
  • 150
    • 0029058323 scopus 로고
    • The baculovirus p35 protein inhibits Fas-and tumor necrosis factor-induced apoptosis
    • 149. Beidler DR, Tewari M, Friesen PD, Poirier G, Dixit VM (1995) The baculovirus p35 protein inhibits Fas-and tumor necrosis factor-induced apoptosis. J Biol Chem 270:16526-16528
    • (1995) J Biol Chem , vol.270 , pp. 16526-16528
    • Beidler, D.R.1    Tewari, M.2    Friesen, P.D.3    Poirier, G.4    Dixit, V.M.5
  • 152
  • 153
    • 0000281927 scopus 로고
    • Molecular interaction of baculovirus p35 and interleukin-1β converting enzyme (ICE): Proposed mechanism for the regulation of an apoptotic pathway
    • 152. Bump NJ, Brady K, Ghayur T, Hugunin M, Li P, Licari P, Miller LK, Wong WW (1995) Molecular interaction of baculovirus p35 and interleukin-1β converting enzyme (ICE): proposed mechanism for the regulation of an apoptotic pathway. J Cell Biochem 19B:294
    • (1995) J Cell Biochem , vol.19 B , pp. 294
    • Bump, N.J.1    Brady, K.2    Ghayur, T.3    Hugunin, M.4    Li, P.5    Licari, P.6    Miller, L.K.7    Wong, W.W.8
  • 154
    • 0027537461 scopus 로고
    • An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif
    • 153. Crook NE, Clem RJ, Miller LK (1993) An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif. J Virol 67:2168-2174
    • (1993) J Virol , vol.67 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 155
    • 0028274132 scopus 로고
    • An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/ His sequence motifs
    • 154. Birnbaum MJ, Clem RJ, Miller LK (1994) An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/ His sequence motifs. J Virol 68:2521-2528
    • (1994) J Virol , vol.68 , pp. 2521-2528
    • Birnbaum, M.J.1    Clem, R.J.2    Miller, L.K.3
  • 156
    • 0027990727 scopus 로고
    • Control of programmed cell death by the baculovirus genes p35 and iap
    • 155. Clem RJ, Miller LJ (1994) Control of programmed cell death by the baculovirus genes p35 and iap. Mol Cell Biol 14:5212-5222
    • (1994) Mol Cell Biol , vol.14 , pp. 5212-5222
    • Clem, R.J.1    Miller, L.J.2
  • 158
    • 0029583176 scopus 로고
    • Drosophila homologs of Baculovirus inhibitor of apoptosis proteins function to block cell death
    • 157. Hay BA, Wassarman DA, Rubin GM (1995) Drosophila homologs of Baculovirus inhibitor of apoptosis proteins function to block cell death. Cell 83:1253-1262
    • (1995) Cell , vol.83 , pp. 1253-1262
    • Hay, B.A.1    Wassarman, D.A.2    Rubin, G.M.3
  • 159
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signalling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • 158. Rothe M, Pan M-G, Henzel WJ, Ayres TM, Goeddel DV (1995) The TNFR2-TRAF signalling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83:1243-1252
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.-G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 161
    • 0029953942 scopus 로고    scopus 로고
    • Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/ or bind tumor necrosis factor receptor-associated factors
    • 160. Uren AG, Pakusch M, Hawkins CJ, Puls KL, Vaux DL (1996) Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/ or bind tumor necrosis factor receptor-associated factors. Proc Natl Acad Sci USA 93:4974-4978
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4974-4978
    • Uren, A.G.1    Pakusch, M.2    Hawkins, C.J.3    Puls, K.L.4    Vaux, D.L.5
  • 162
    • 0028149332 scopus 로고
    • Apoptotic cell death induced by intracellular proteolysis
    • 161. Williams MS, Henkart PA (1994) Apoptotic cell death induced by intracellular proteolysis. J Immunol 153:4247-4255
    • (1994) J Immunol , vol.153 , pp. 4247-4255
    • Williams, M.S.1    Henkart, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.