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Volumn 48, Issue , 1997, Pages 267-281

Apoptosis and disease: Regulation and clinical relevance of programmed cell death

Author keywords

Bcl 2; Homeostasis; Inhibitor of apoptosis; Interleukin 1 converting enzymes; Tumor necrosis factor receptors

Indexed keywords

INTERLEUKIN 1BETA CONVERTING ENZYME; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0031046848     PISSN: 00664219     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.med.48.1.267     Document Type: Review
Times cited : (329)

References (94)
  • 2
    • 0028036918 scopus 로고
    • Autoimmune disease: A problem of defective apoptosis
    • Mountz JD, Wu J, Cheng J, Zhou T. 1994. Autoimmune disease: a problem of defective apoptosis. Arthritis Rheum. 37:1415-20
    • (1994) Arthritis Rheum. , vol.37 , pp. 1415-1420
    • Mountz, J.D.1    Wu, J.2    Cheng, J.3    Zhou, T.4
  • 3
    • 0028240526 scopus 로고
    • Programmed cell death: Implications for neuropsychiatric disorders
    • Margolis RL, Chuang D-M, Post RM. 1994. Programmed cell death: implications for neuropsychiatric disorders. Biol. Psychiatry 35:946-56
    • (1994) Biol. Psychiatry , vol.35 , pp. 946-956
    • Margolis, R.L.1    Chuang, D.-M.2    Post, R.M.3
  • 5
    • 0028025563 scopus 로고
    • Apoptosis in cancer therapy: Crossing the threshold
    • Fisher DE. 1994. Apoptosis in cancer therapy: crossing the threshold. Cell 78:539-42
    • (1994) Cell , vol.78 , pp. 539-542
    • Fisher, D.E.1
  • 7
    • 0022546957 scopus 로고
    • Analysis of the structure, transcription, and protein products of bcl-2, the gene involved in human follicular lymphoma
    • Tsujimoto Y, Croce CM. 1986. Analysis of the structure, transcription, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc. Natl. Acad. Sci USA 83:5214-18
    • (1986) Proc. Natl. Acad. Sci USA , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 8
    • 0027282044 scopus 로고
    • Bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
    • Boise LH, Gonzalez-Garcia M, Postema CE, et al. 1993. Bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell 74:597-608
    • (1993) Cell , vol.74 , pp. 597-608
    • Boise, L.H.1    Gonzalez-Garcia, M.2    Postema, C.E.3
  • 9
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to bcl-2
    • Kozopas KM, Yang T, Buchan HL, et al. 1993. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to bcl-2. Proc. Natl. Acad. Sci. USA 90:3516-20
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3
  • 10
    • 0027326012 scopus 로고
    • Characterization of A1, a novel hematopoietic-specific early-response gene with sequence similarity to bcl-2
    • Lin EY, Orlofsky A, Berger MS, Prystowsky MB. 1993. Characterization of A1, a novel hematopoietic-specific early-response gene with sequence similarity to bcl-2. J. Immunol. 151:1979-88
    • (1993) J. Immunol. , vol.151 , pp. 1979-1988
    • Lin, E.Y.1    Orlofsky, A.2    Berger, M.S.3    Prystowsky, M.B.4
  • 11
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ. 1993. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74:609-19
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 12
    • 0028809209 scopus 로고
    • L and Bcl-2, displaces Bax and promotes cell death
    • L and Bcl-2, displaces Bax and promotes cell death. Cell 80:285-91
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3
  • 13
    • 0028946015 scopus 로고
    • Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K
    • Farrow SN, White JHM, Martinou I, et al. 1995. Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K. Nature 374:731-33
    • (1995) Nature , vol.374 , pp. 731-733
    • Farrow, S.N.1    White, J.H.M.2    Martinou, I.3
  • 14
    • 0028986876 scopus 로고
    • Induction of apoptosis by the Bcl-2 homologue Bak
    • Chittenden T, Harrington EA, O'Connor R, et al. 1995. Induction of apoptosis by the Bcl-2 homologue Bak. Nature 374:733-36
    • (1995) Nature , vol.374 , pp. 733-736
    • Chittenden, T.1    Harrington, E.A.2    O'Connor, R.3
  • 15
    • 0028904163 scopus 로고
    • Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak
    • Kiefer MC, Brauer MJ, Powers VC, et al. 1995. Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak. Nature 374:736-39
    • (1995) Nature , vol.374 , pp. 736-739
    • Kiefer, M.C.1    Brauer, M.J.2    Powers, V.C.3
  • 16
    • 0028017880 scopus 로고
    • Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system
    • Sato T, Hanada M, Bodrug S, et al. 1994. Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system. Proc. Natl. Acad. Sci. USA 91:9238-42
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9238-9242
    • Sato, T.1    Hanada, M.2    Bodrug, S.3
  • 17
    • 0029097470 scopus 로고
    • Multiple Bcl-2 family members demonstrate competing dimerizations with Bax
    • Sedlak TW, Oltvai ZN, Yang E, et al. 1995. Multiple Bcl-2 family members demonstrate competing dimerizations with Bax. Proc. Natl Acad. Sci. USA 92:7834-38
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7834-7838
    • Sedlak, T.W.1    Oltvai, Z.N.2    Yang, E.3
  • 18
    • 0028206341 scopus 로고
    • BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heter-dimerization with Bax
    • Yin X-M, Oltvai ZN, Korsmeyer SJ. 1994. BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heter-dimerization with Bax. Nature 369:321-23
    • (1994) Nature , vol.369 , pp. 321-323
    • Yin, X.-M.1    Oltvai, Z.N.2    Korsmeyer, S.J.3
  • 19
    • 0028832667 scopus 로고
    • A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions
    • Chittenden T, Flemington C, Houghton AB, et al. 1995. A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. EMBO J. 14:5589-96
    • (1995) EMBO J. , vol.14 , pp. 5589-5596
    • Chittenden, T.1    Flemington, C.2    Houghton, A.B.3
  • 20
    • 0028812606 scopus 로고
    • Bik, a novel death-inducing protein, shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins
    • Boyd JM, Gallo GJ, Elangovan B, et al. 1995. Bik, a novel death-inducing protein, shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins. Oncogene 11:1921-28
    • (1995) Oncogene , vol.11 , pp. 1921-1928
    • Boyd, J.M.1    Gallo, G.J.2    Elangovan, B.3
  • 21
    • 0026582702 scopus 로고
    • C. elegans gene ced-9 protects from programmed cell death
    • Hengartner MO, Ellis RE, Horvitz HR. 1992. C. elegans gene ced-9 protects from programmed cell death. Nature 356:494-99
    • (1992) Nature , vol.356 , pp. 494-499
    • Hengartner, M.O.1    Ellis, R.E.2    Horvitz, H.R.3
  • 22
    • 0028288277 scopus 로고
    • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • Hengartner MO, Horvitz HR. 1994. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell 76:665-76
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 25
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • Yuan J, Shaham S, Ledoux S, et al. 1993. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 75: 641-52
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3
  • 26
    • 0030012008 scopus 로고    scopus 로고
    • Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities
    • Shaham S, Horvitz HR. 1996. Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities. Genes Dev. 10:578-91
    • (1996) Genes Dev. , vol.10 , pp. 578-591
    • Shaham, S.1    Horvitz, H.R.2
  • 27
    • 0029664296 scopus 로고    scopus 로고
    • ICE family proteases: Mediators of all apoptotic cell death?
    • Henkart PA. 1996. ICE family proteases: mediators of all apoptotic cell death? Immunity 4:195-201
    • (1996) Immunity , vol.4 , pp. 195-201
    • Henkart, P.A.1
  • 28
    • 0030044324 scopus 로고    scopus 로고
    • ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis
    • Duan H, Chinnaiyan AM, Hudson PL, et al. 1996. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 271:1621-25
    • (1996) J. Biol. Chem. , vol.271 , pp. 1621-1625
    • Duan, H.1    Chinnaiyan, A.M.2    Hudson, P.L.3
  • 29
    • 0028107827 scopus 로고
    • Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: A (p20/p10)2 homodimer
    • Walker NP, Talanian RV, Brady KD, et al. 1995. Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer. Cell 78: 343-52
    • (1995) Cell , vol.78 , pp. 343-352
    • Walker, N.P.1    Talanian, R.V.2    Brady, K.D.3
  • 30
    • 0028949537 scopus 로고
    • Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities
    • Alnemri ES, Fernandes-Alnemri T, Litwack G. 1995. Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities. J. Biol. Chem. 270: 4312-17
    • (1995) J. Biol. Chem. , vol.270 , pp. 4312-4317
    • Alnemri, E.S.1    Fernandes-Alnemri, T.2    Litwack, G.3
  • 31
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang L, Miura M, Bergeron L, et al. 1994. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 78:739-50
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3
  • 32
    • 0029025549 scopus 로고
    • Mch2, a new member of the apoptotic CED-3/ICE cysteine protease gene family
    • Fernandes-Alnemri T, Litwack G, Alnemri ES. 1995. Mch2, a new member of the apoptotic CED-3/ICE cysteine protease gene family. Cancer Res. 55:2737-42
    • (1995) Cancer Res. , vol.55 , pp. 2737-2742
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 33
    • 0028984948 scopus 로고
    • Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock
    • Li P, Allen H, Banerjee S, et al. 1995. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 80: 401-11
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1    Allen, H.2    Banerjee, S.3
  • 34
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme
    • Kiuda K, Lippke JA, Ku G, et al. 1995. Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 267:2000-3
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kiuda, K.1    Lippke, J.A.2    Ku, G.3
  • 35
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED3 protease necessary for mammalian apoptosis
    • Nicholson DW, Ali A, Thornberry NA, et al. 1995. Identification and inhibition of the ICE/CED3 protease necessary for mammalian apoptosis. Nature 376:37-43
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1    Ali, A.2    Thornberry, N.A.3
  • 36
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M, Quan LT, O'Rourke K, et al. 1995. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801-9
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3
  • 37
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik YA, Kaufmann SH, Disnoyers S, et al. 1994. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371:346-47
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Disnoyers, S.3
  • 38
    • 0028922462 scopus 로고
    • Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease
    • Wang Z-Q, Auer B, Stingl L, et al. 1995. Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease. Genes Dev. 9:509-20
    • (1995) Genes Dev. , vol.9 , pp. 509-520
    • Wang, Z.-Q.1    Auer, B.2    Stingl, L.3
  • 39
    • 0028087585 scopus 로고
    • Tyrosine kinase activation provides an early and requisite signal for Fas-induced apoptosis
    • Eischen CM, Dick CJ, Leibson PJ. 1994. Tyrosine kinase activation provides an early and requisite signal for Fas-induced apoptosis. J. Immunol. 153:1947-54
    • (1994) J. Immunol. , vol.153 , pp. 1947-1954
    • Eischen, C.M.1    Dick, C.J.2    Leibson, P.J.3
  • 40
    • 0028268215 scopus 로고
    • Programmed cell death and Bcl-2 protection in the absence of a nucleus
    • Jacobson MD, Burne JF, Raff MC. 1994. Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO J. 13:1899-910
    • (1994) EMBO J. , vol.13 , pp. 1899-1910
    • Jacobson, M.D.1    Burne, J.F.2    Raff, M.C.3
  • 41
    • 0029900295 scopus 로고    scopus 로고
    • The tumor necrosis factor ligand and receptor families
    • Bazzoni F, Beutler B. 1996. The tumor necrosis factor ligand and receptor families. N. Engl. J. Med. 334:1717-25
    • (1996) N. Engl. J. Med. , vol.334 , pp. 1717-1725
    • Bazzoni, F.1    Beutler, B.2
  • 42
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • 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 81:505-12
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 43
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/Apo-1 (CD95) in yeast and causes cell death
    • Stanger BZ, Leder P, Lee T, et al. 1995. RIP: a novel protein containing a death domain that interacts with Fas/Apo-1 (CD95) in yeast and causes cell death. Cell 81:513-23
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.3
  • 44
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu H, Xiong J, Goeddel DV. 1995. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell 81:495-504
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 45
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H, Shu H-B, Pan M-G, Goeddel DV. 1996. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84:299-308
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.-B.2    Pan, M.-G.3    Goeddel, D.V.4
  • 46
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • 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 85:803-15
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 47
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/Apo-1) death-inducing signaling complex (DISC)
    • Muzio M, Chinnaiyan AM, Kischkel FC, et al. 1996. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/Apo-1) death-inducing signaling complex (DISC). Cell 85: 817-27
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 48
    • 0028964917 scopus 로고
    • Fas-induced apoptosis is mediated via a ceramide-initiated Ras signaling pathway
    • Gulbins E, Bissonnette R, Mahboubi A, et al. 1995. Fas-induced apoptosis is mediated via a ceramide-initiated Ras signaling pathway. Immunity 2:341-51
    • (1995) Immunity , vol.2 , pp. 341-351
    • Gulbins, E.1    Bissonnette, R.2    Mahboubi, A.3
  • 49
    • 0347537940 scopus 로고    scopus 로고
    • Requirement for ceramide-initiated SAPK/ JNK signaling in stress-induced apoptosis
    • Nerheij M, Bose R, Lin XH, et al. 1996. Requirement for ceramide-initiated SAPK/ JNK signaling in stress-induced apoptosis. Nature 380:75-79
    • (1996) Nature , vol.380 , pp. 75-79
    • Nerheij, M.1    Bose, R.2    Lin, X.H.3
  • 50
    • 0030060075 scopus 로고    scopus 로고
    • Requirement of an ICE-like protease for induction of apoptosis and ceramide generation by REAPER
    • 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 271:808-10
    • (1996) Science , vol.271 , pp. 808-810
    • Pronk, G.J.1    Ramer, K.2    Amiri, P.3    Williams, L.T.4
  • 51
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe M, Wong SC, Henzel WJ, Goeddel DV. 1994. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 78:681-92
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 52
    • 0028878977 scopus 로고
    • The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family
    • Mosialos G, Birkenbach M, Yalamanchili R, et al. 1995. The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family. Cell 80:389-99
    • (1995) Cell , vol.80 , pp. 389-399
    • Mosialos, G.1    Birkenbach, M.2    Yalamanchili, R.3
  • 53
    • 0028936733 scopus 로고
    • Involvement of CRAF1, a relative of TRAF, in CD40 signaling
    • Chang G, Cleary AM, Ye Z, et al. 1995. Involvement of CRAF1, a relative of TRAF, in CD40 signaling. Science 267: 1494-98
    • (1995) Science , vol.267 , pp. 1494-1498
    • Chang, G.1    Cleary, A.M.2    Ye, Z.3
  • 54
    • 0027943499 scopus 로고
    • A novel RING finger protein interacts with the cytoplasmic domain of CD40
    • Hu HM, O'Rourke K, Boguski MS, Dixit VM. 1994. A novel RING finger protein interacts with the cytoplasmic domain of CD40. J. Biol. Chem. 269:30069-72
    • (1994) J. Biol. Chem. , vol.269 , pp. 30069-30072
    • Hu, H.M.1    O'Rourke, K.2    Boguski, M.S.3    Dixit, V.M.4
  • 55
    • 0028809176 scopus 로고
    • A novel member of the TRAF family of putative signal transducing proteins binds to the cytoplasmic domain of CD40
    • Sato T, Irie S, Reed JC. 1995. A novel member of the TRAF family of putative signal transducing proteins binds to the cytoplasmic domain of CD40. FEBS Lett. 358:113-18
    • (1995) FEBS Lett. , vol.358 , pp. 113-118
    • Sato, T.1    Irie, S.2    Reed, J.C.3
  • 56
    • 0028856787 scopus 로고
    • Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma
    • Regnier CH, Tomasetto C, Moog-Lutz C, et al. 1995. Presence of a new conserved domain in CART1, a novel member of the tumor necrosis factor receptor-associated protein family, which is expressed in breast carcinoma. J. Biol. Chem. 270:25715-21
    • (1995) J. Biol. Chem. , vol.270 , pp. 25715-25721
    • Regnier, C.H.1    Tomasetto, C.2    Moog-Lutz, C.3
  • 57
    • 15844369897 scopus 로고    scopus 로고
    • CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins
    • Gedrich RW, Gilfillan MC, Duckett CS, et al. 1996. CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins. J. Biol. Chem. 271:12852-58
    • (1996) J. Biol. Chem. , vol.271 , pp. 12852-12858
    • Gedrich, R.W.1    Gilfillan, M.C.2    Duckett, C.S.3
  • 58
    • 0028978626 scopus 로고
    • TRAF2-mediated activation of NFκB by TNF receptor 2 and CD40
    • Rothe M, Sarma V, Dixit VM, Goeddel DV. 1995. TRAF2-mediated activation of NFκB by TNF receptor 2 and CD40. Science 269:1424-27
    • (1995) Science , vol.269 , pp. 1424-1427
    • Rothe, M.1    Sarma, V.2    Dixit, V.M.3    Goeddel, D.V.4
  • 59
    • 0028113218 scopus 로고
    • Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins
    • Boyd JM, Malstrom S, Subramanian T, et al. 1994. Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins. Cell 79:341-51
    • (1994) Cell , vol.79 , pp. 341-351
    • Boyd, J.M.1    Malstrom, S.2    Subramanian, T.3
  • 60
    • 0027260656 scopus 로고
    • Epstein-Barr virus-coded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death
    • Henderson S, Huen D, Rowe M, et al. 1993. Epstein-Barr virus-coded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death. Proc. Natl. Acad. Sci. USA 90:8479-83
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8479-8483
    • Henderson, S.1    Huen, D.2    Rowe, M.3
  • 61
    • 0027264124 scopus 로고
    • An African swine fever virus gene with similarity to the proto-oncogen bcl-2 and the Epstein-Barr virus gene BHRF1
    • Nielan JG, Lu Z, Afonzo L, et al. 1993. An African swine fever virus gene with similarity to the proto-oncogen bcl-2 and the Epstein-Barr virus gene BHRF1. J. Virol. 67:4391-94
    • (1993) J. Virol. , vol.67 , pp. 4391-4394
    • Nielan, J.G.1    Lu, Z.2    Afonzo, L.3
  • 62
    • 0025772343 scopus 로고
    • Induction of Bcl-2 expression by Epstein-Barr virus latent membrane protein 1 protects infected B cells from programmed cell death
    • Henderson S, Rowe M, Gregory C, et al. 1991. Induction of Bcl-2 expression by Epstein-Barr virus latent membrane protein 1 protects infected B cells from programmed cell death. Cell 65:1107-15
    • (1991) Cell , vol.65 , pp. 1107-1115
    • Henderson, S.1    Rowe, M.2    Gregory, C.3
  • 63
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme
    • Ray CA, Black RA, Kronheim SR, et al. 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
  • 64
    • 0028817947 scopus 로고
    • Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35
    • Bump NJ, Hackett M, Hugunin M, et al. 1995. Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35. Science 269:1885-88
    • (1995) Science , vol.269 , pp. 1885-1888
    • Bump, N.J.1    Hackett, M.2    Hugunin, M.3
  • 65
    • 0028896092 scopus 로고
    • The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy
    • Roy N, Mahadevan MS, McLean M, et al. 1995. The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy. Cell 80:167-78
    • (1995) Cell , vol.80 , pp. 167-178
    • Roy, N.1    Mahadevan, M.S.2    McLean, M.3
  • 66
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan M-G, Henzel WJ, et al. 1995. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83: 1243-52
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.-G.2    Henzel, W.J.3
  • 67
    • 15844425961 scopus 로고    scopus 로고
    • A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors
    • Duckett CS, Nava VE, Gedrich RW, et al. 1996. A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors. EMBO J. 15: 2685-94
    • (1996) EMBO J. , vol.15 , pp. 2685-2694
    • Duckett, C.S.1    Nava, V.E.2    Gedrich, R.W.3
  • 68
    • 13344278692 scopus 로고    scopus 로고
    • Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes
    • Liston P, Roy N, Tamai K, et al. 1996. Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes. Nature 379:349-53
    • (1996) Nature , vol.379 , pp. 349-353
    • Liston, P.1    Roy, N.2    Tamai, K.3
  • 69
    • 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
    • Uren AG, Pakusch M, Hawkins CJ, et al. 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 93:4974-78
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4974-4978
    • Uren, A.G.1    Pakusch, M.2    Hawkins, C.J.3
  • 70
    • 0026688162 scopus 로고
    • Apoptotic cell death induced by c-myc is inhibited by Bcl-2
    • Bissonnette RP, Echeverri F, Mahboubi A, Green DR. 1992. Apoptotic cell death induced by c-myc is inhibited by Bcl-2. Nature 359:552-54
    • (1992) Nature , vol.359 , pp. 552-554
    • Bissonnette, R.P.1    Echeverri, F.2    Mahboubi, A.3    Green, D.R.4
  • 71
    • 0027451668 scopus 로고
    • P53-dependent apoptosis modulates the cytotoxicity of anticancer agents
    • Lowe SW, Ruley HE, Jacks T, Housman DE. 1993. P53-dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 74:957-67
    • (1993) Cell , vol.74 , pp. 957-967
    • Lowe, S.W.1    Ruley, H.E.2    Jacks, T.3    Housman, D.E.4
  • 72
    • 0028169994 scopus 로고
    • P53-dependent apoptosis suppresses tumor growth and progression in vivo
    • Symonds H, Krall L, Remington L, et al. 1994. P53-dependent apoptosis suppresses tumor growth and progression in vivo. Cell 78:703-11
    • (1994) Cell , vol.78 , pp. 703-711
    • Symonds, H.1    Krall, L.2    Remington, L.3
  • 74
    • 0026760426 scopus 로고
    • Requirement for a functional Rb-1 gene in murine development
    • Clarke A, Maandag E, van Roon M, et al. 1992. Requirement for a functional Rb-1 gene in murine development. Nature 359: 328-30
    • (1992) Nature , vol.359 , pp. 328-330
    • Clarke, A.1    Maandag, E.2    Van Roon, M.3
  • 75
    • 0026744563 scopus 로고
    • Mice deficient for Rb are nonviable and show defects in neurogenesis and haematopoiesis
    • Lee EY-HP, Chang C-Y, Hu N, et al. 1992. Mice deficient for Rb are nonviable and show defects in neurogenesis and haematopoiesis. Nature 359:288-94
    • (1992) Nature , vol.359 , pp. 288-294
    • Lee, E.Y.-H.P.1    Chang, C.-Y.2    Hu, N.3
  • 76
    • 0026702996 scopus 로고
    • Effects of an Rb mutation in the mouse
    • Jacks T, Fazeli A, Schmitt E, et al. 1992. Effects of an Rb mutation in the mouse. Nature 359:295-300
    • (1992) Nature , vol.359 , pp. 295-300
    • Jacks, T.1    Fazeli, A.2    Schmitt, E.3
  • 77
    • 0029888359 scopus 로고    scopus 로고
    • Tumor induction and tissue atrophy in mice lacking E2F-1
    • Yamasaki L, Jacks T, Bronson R, et al. 1996. Tumor induction and tissue atrophy in mice lacking E2F-1. Cell 85:537-48
    • (1996) Cell , vol.85 , pp. 537-548
    • Yamasaki, L.1    Jacks, T.2    Bronson, R.3
  • 78
    • 0029949784 scopus 로고    scopus 로고
    • E2F-1 functions in mice to promote apoptosis and suppress proliferation
    • Field SJ, Tsai F-Y, Kuo F, et al. 1996. E2F-1 functions in mice to promote apoptosis and suppress proliferation. Cell 85:549-61
    • (1996) Cell , vol.85 , pp. 549-561
    • Field, S.J.1    Tsai, F.-Y.2    Kuo, F.3
  • 79
    • 0027489384 scopus 로고
    • Clinical implications of the p53 tumor-suppressor gene
    • Harris CC, Hollstein M. 1993. Clinical implications of the p53 tumor-suppressor gene. N. Engl. J. Med. 329:1318-27
    • (1993) N. Engl. J. Med. , vol.329 , pp. 1318-1327
    • Harris, C.C.1    Hollstein, M.2
  • 80
    • 0027944206 scopus 로고
    • P53 status and the efficacy of cancer therapy in vivo
    • Lowe SW, Bodis S, McClatchey A, et al. 1994. P53 status and the efficacy of cancer therapy in vivo. Science 266:807-10
    • (1994) Science , vol.266 , pp. 807-810
    • Lowe, S.W.1    Bodis, S.2    McClatchey, A.3
  • 81
    • 0026781986 scopus 로고
    • Bcl-2 gene transfer increases relative resistance of S49.1 and WEHI7.2 lymphoid cells to cell death and DNA fragmentation induced by glucocorticoids and multiple chemotherapeutic drugs
    • Miyashita T, Reed JC. 1992. Bcl-2 gene transfer increases relative resistance of S49.1 and WEHI7.2 lymphoid cells to cell death and DNA fragmentation induced by glucocorticoids and multiple chemotherapeutic drugs. Cancer Res. 52:5407-11
    • (1992) Cancer Res. , vol.52 , pp. 5407-5411
    • Miyashita, T.1    Reed, J.C.2
  • 82
    • 0027389763 scopus 로고
    • Bcl-2 oncoprotein blocks chemotherapy-induced apoptosis in a human leukemia cell line
    • Miyashita T, Reed JC. 1993. Bcl-2 oncoprotein blocks chemotherapy-induced apoptosis in a human leukemia cell line. Blood 81:151-57
    • (1993) Blood , vol.81 , pp. 151-157
    • Miyashita, T.1    Reed, J.C.2
  • 83
    • 0027196091 scopus 로고
    • Constitutive expression of human bcl-2 modulates nitrogen mustard and camptothecin induced apoptosis
    • Walton MI, Whysong D, O'Connor PM, et al. 1993. Constitutive expression of human bcl-2 modulates nitrogen mustard and camptothecin induced apoptosis. Cancer Res. 53:1853-61
    • (1993) Cancer Res. , vol.53 , pp. 1853-1861
    • Walton, M.I.1    Whysong, D.2    O'Connor, P.M.3
  • 84
    • 0027279128 scopus 로고
    • Bcl-2 modulation of apoptosis induced by anticancer drugs: Resistance to thymidylate stress is independent of classical resistance pathways
    • Fisher TC, Milner AE, Gregory CD, et al. 1993. Bcl-2 modulation of apoptosis induced by anticancer drugs: resistance to thymidylate stress is independent of classical resistance pathways. Cancer Res. 53: 3321-26
    • (1993) Cancer Res. , vol.53 , pp. 3321-3326
    • Fisher, T.C.1    Milner, A.E.2    Gregory, C.D.3
  • 85
    • 0028322065 scopus 로고
    • Bcl-2 inhibits chemotherapy-induced apoptosis in neuroblastoma
    • Dole M, Nunez G, Merchant AK, et al. 1994. Bcl-2 inhibits chemotherapy-induced apoptosis in neuroblastoma. Cancer Res. 54:3253-59
    • (1994) Cancer Res. , vol.54 , pp. 3253-3259
    • Dole, M.1    Nunez, G.2    Merchant, A.K.3
  • 86
    • 0028987830 scopus 로고
    • L by cytotoxic drug exposure confers resistance to ionizing radiation-induced internucleosomal DNA fragmentation
    • L by cytotoxic drug exposure confers resistance to ionizing radiation-induced internucleosomal DNA fragmentation. Cell Growth Differ. 6:363-70
    • (1995) Cell Growth Differ. , vol.6 , pp. 363-370
    • Datta, R.1    Manome, Y.2    Taneja, N.3
  • 88
    • 0027164144 scopus 로고
    • High expression of Bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy
    • Campos L, Rouault JP, Sabido O, et al. 1993. High expression of Bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy. Blood 81:3091-96
    • (1993) Blood , vol.81 , pp. 3091-3096
    • Campos, L.1    Rouault, J.P.2    Sabido, O.3
  • 89
    • 8044251593 scopus 로고    scopus 로고
    • Expression of the bcl-x gene in primary human breast cancer: Association with high tumor grade and nodal metastases
    • Abstr.
    • Olopade OI, Adeyanju MO, Safa AR, et al. 1996. Expression of the bcl-x gene in primary human breast cancer: association with high tumor grade and nodal metastases. ASCO Proc. 15:162 (Abstr.)
    • (1996) ASCO Proc. , vol.15 , pp. 162
    • Olopade, O.I.1    Adeyanju, M.O.2    Safa, A.R.3
  • 90
    • 0345483911 scopus 로고    scopus 로고
    • Phase 1 bcl-2 antisense trial: Preliminary results
    • Abstr.
    • Webb A, Cunningham D, Cotter F, et al. 1996. Phase 1 bcl-2 antisense trial: preliminary results. Ann. Oncol. 7(3):32 (Abstr.)
    • (1996) Ann. Oncol. , vol.7 , Issue.3 , pp. 32
    • Webb, A.1    Cunningham, D.2    Cotter, F.3
  • 91
    • 0028215537 scopus 로고
    • T cell deletion in high antigen dose therapy of autoimmune encephalomyelitis
    • Critchfield JM, Racke MK, Zuniga-Pflucker JC, et al. 1994. T cell deletion in high antigen dose therapy of autoimmune encephalomyelitis. Science 263:1139-43
    • (1994) Science , vol.263 , pp. 1139-1143
    • Critchfield, J.M.1    Racke, M.K.2    Zuniga-Pflucker, J.C.3
  • 92
    • 0023759046 scopus 로고
    • Lymphocyte activation by HIV-1 envelope glycoprotein
    • Kornfield H, Cruikshank WW, Pyle SW, et al. 1988. Lymphocyte activation by HIV-1 envelope glycoprotein. Nature 335:445-48
    • (1988) Nature , vol.335 , pp. 445-448
    • Kornfield, H.1    Cruikshank, W.W.2    Pyle, S.W.3
  • 93
    • 0026784923 scopus 로고
    • Crosslinking CD4 by human immunodeficiency virus gp 120 primes T cells for activation-induced apoptosis
    • Banda NK, Bernier J, Kurahara DK, et al. 1992. Crosslinking CD4 by human immunodeficiency virus gp 120 primes T cells for activation-induced apoptosis. J. Exp. Med. 176:1099-106
    • (1992) J. Exp. Med. , vol.176 , pp. 1099-1106
    • Banda, N.K.1    Bernier, J.2    Kurahara, D.K.3
  • 94
    • 0029062573 scopus 로고
    • Induction of apoptosis in uninfected lymphocytes by HIV-1 Tat protein
    • Li CJ, Friedman DJ, Wang C, et al. 1995. Induction of apoptosis in uninfected lymphocytes by HIV-1 Tat protein. Science 268:429-31
    • (1995) Science , vol.268 , pp. 429-431
    • Li, C.J.1    Friedman, D.J.2    Wang, C.3


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