메뉴 건너뛰기




Volumn 8, Issue 1, 1998, Pages 68-75

The Bcl-2 family and cell death regulation

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CYSTEINE PROTEINASE; CYTOCHROME C; PROTEIN BCL 2; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0031889579     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(98)80064-6     Document Type: Article
Times cited : (120)

References (92)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JFR, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer. 26:1972;239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0028326952 scopus 로고
    • An evolutionary perspective on apoptosis
    • Vaux DL, Haecker G, Strasser A. An evolutionary perspective on apoptosis. Cell. 76:1994;777-779.
    • (1994) Cell , vol.76 , pp. 777-779
    • Vaux, D.L.1    Haecker, G.2    Strasser, A.3
  • 3
    • 0029048498 scopus 로고
    • Life and death during lymphocyte development and function: Evidence for two distinct killing mechanisms
    • Strasser A. Life and death during lymphocyte development and function: evidence for two distinct killing mechanisms. Curr Opin Immunol. 7:1995;228-234.
    • (1995) Curr Opin Immunol , vol.7 , pp. 228-234
    • Strasser, A.1
  • 4
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson MD, Weil M, Raff MC. Programmed cell death in animal development. Cell. 88:1997;347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 5
    • 0028212937 scopus 로고
    • Apoptosis and its role in human disease
    • Barr PJ, Tomei LD. Apoptosis and its role in human disease. Biotechnology. 12:1994;487-493.
    • (1994) Biotechnology , vol.12 , pp. 487-493
    • Barr, P.J.1    Tomei, L.D.2
  • 6
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 7
    • 0030665659 scopus 로고    scopus 로고
    • The role of the bcl-2/ced-9 gene family in cancer and general implications of defects in cell death control in tumourigenesis and resistance to chemotherapy
    • Strasser A, Huang DCS, Vaux DL. The role of the bcl-2/ced-9 gene family in cancer and general implications of defects in cell death control in tumourigenesis and resistance to chemotherapy. Biochim Biophys Acta. 1333:1997;F151-F178.
    • (1997) Biochim Biophys Acta , vol.1333
    • Strasser, A.1    Huang, D.C.S.2    Vaux, D.L.3
  • 9
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis HM, Horvitz HR. Genetic control of programmed cell death in the nematode C. elegans. Cell. 44:1986;817-829.
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 10
    • 0028147070 scopus 로고
    • Programmed cell death in Caenorhabditis elegans
    • Hengartner MO, Horvitz HR. Programmed cell death in Caenorhabditis elegans. Curr Opin Genet Dev. 4:1994;581-586.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 581-586
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 11
    • 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, Ellis HM, Horvitz HR. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell. 75:1993;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
  • 12
    • 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
    • Xue D, Shaham S, Horvitz HR. 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. 10:1996;1073-1083.
    • (1996) Genes Dev , vol.10 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 13
    • 0026582702 scopus 로고
    • Caenorhabditis elegans gene ced-9 protects cells from programmed cell death
    • Hengartner MO, Ellis RE, Horvitz HR. Caenorhabditis elegans gene ced-9 protects cells from programmed cell death. Nature. 356:1992;494-499.
    • (1992) Nature , vol.356 , pp. 494-499
    • Hengartner, M.O.1    Ellis, R.E.2    Horvitz, H.R.3
  • 14
    • 0027050145 scopus 로고
    • Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2
    • Vaux DL, Weissman IL, Kim SK. Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2. Science. 258:1992;1955-1957.
    • (1992) Science , vol.258 , pp. 1955-1957
    • Vaux, D.L.1    Weissman, I.L.2    Kim, S.K.3
  • 15
    • 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. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 76:1994;665-676.
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 17
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to bcl-2
    • Kozopas KM, Yang T, Buchan HL, Zhou P, Craig RW. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to bcl-2. Proc Natl Acad Sci USA. 90:1993;3516-3520.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3    Zhou, P.4    Craig, R.W.5
  • 18
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell. 74:1993;609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 25
    • 0029790857 scopus 로고    scopus 로고
    • Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K
    • of special interest. This paper describes the pro-apoptotic protein Nbk/Bik, identified because of its ability to interact with the adenovirus homologue of Bcl-2, E1B 19K. Like previously identified pro-apoptotic proteins, Nbk/Bik binds to and antagonises the pro-survival function of Bcl-2. The surprising feature of these pro-apoptotic proteins is their lack of overall sequence similarity. These differences may represent their involvement in distinct pathways to apoptosis, perhaps allowing them to interact with diverse upstream signalling molecules.
    • Han J, Sabbatini P, White E. Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K. of special interest Mol Cell Biol. 16:1996;5857-5864 This paper describes the pro-apoptotic protein Nbk/Bik, identified because of its ability to interact with the adenovirus homologue of Bcl-2, E1B 19K. Like previously identified pro-apoptotic proteins, Nbk/Bik binds to and antagonises the pro-survival function of Bcl-2. The surprising feature of these pro-apoptotic proteins is their lack of overall sequence similarity. These differences may represent their involvement in distinct pathways to apoptosis, perhaps allowing them to interact with diverse upstream signalling molecules.
    • (1996) Mol Cell Biol , vol.16 , pp. 5857-5864
    • Han, J.1    Sabbatini, P.2    White, E.3
  • 26
    • 0029807585 scopus 로고    scopus 로고
    • BID: A novel BH3 domain-only death agonist
    • of special interest. This paper describes the cloning of Bid, another pro-apoptotic protein discovered because of its ability to bind to Bcl-2. Like Nbk/Bik, Bid's primary structure has limited features in common with those of other known pro-apoptotic proteins.
    • Wang K, Yin X-M, Chao DT, Milliman CL, Korsmeyer SJ. BID: a novel BH3 domain-only death agonist. of special interest Genes Dev. 10:1996;2859-2869 This paper describes the cloning of Bid, another pro-apoptotic protein discovered because of its ability to bind to Bcl-2. Like Nbk/Bik, Bid's primary structure has limited features in common with those of other known pro-apoptotic proteins.
    • (1996) Genes Dev , vol.10 , pp. 2859-2869
    • Wang, K.1    Yin X-M2    Chao, D.T.3    Milliman, C.L.4    Korsmeyer, S.J.5
  • 27
    • 0030970085 scopus 로고    scopus 로고
    • L
    • of special interest. Describes the pro-apoptotic protein Hrk. This protein, like Nbk/Bik and Bid, was identified because of its ability to interact with anti-apoptotic members of the Bcl-2 protein family.
    • L. of special interest EMBO J. 16:1997;1686-1694 Describes the pro-apoptotic protein Hrk. This protein, like Nbk/Bik and Bid, was identified because of its ability to interact with anti-apoptotic members of the Bcl-2 protein family.
    • (1997) EMBO J , vol.16 , pp. 1686-1694
    • Inohara, N.1    Ding, L.2    Chen, S.3    Noez, G.4
  • 28
    • 0030012008 scopus 로고    scopus 로고
    • Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities
    • of outstanding interest. This paper describes genetic studies which delineated the order in which cell death genes act in the nematode. Specifically, that ced-9 acts upstream of ced-4, and that ced-4 acts upstream of, or parallel to ced-3. These findings provided important clues to interactions between the mammalian homologues of these genes.
    • Shaham S, Horvitz HR. Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities. of outstanding interest Genes Dev. 10:1996;578-591 This paper describes genetic studies which delineated the order in which cell death genes act in the nematode. Specifically, that ced-9 acts upstream of ced-4, and that ced-4 acts upstream of, or parallel to ced-3. These findings provided important clues to interactions between the mammalian homologues of these genes.
    • (1996) Genes Dev , vol.10 , pp. 578-591
    • Shaham, S.1    Horvitz, H.R.2
  • 29
    • 0029912189 scopus 로고    scopus 로고
    • Molecular ordering of the cell death pathway
    • of special interest. See annotation [32].
    • Chinnaiyan AM, Orth K, O'Rourke K, Duan H, Poirier GG, Dixit VM. Molecular ordering of the cell death pathway. of special interest J Biol Chem. 271:1996;4573-4576 See annotation [32].
    • (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
  • 30
    • 0029894283 scopus 로고    scopus 로고
    • L
    • of special interest. See annotation [32].
    • L. of special interest J Biol Chem. 271:1996;17601-17604 See annotation [32].
    • (1996) J Biol Chem , vol.271 , pp. 17601-17604
    • Erhardt, P.1    Cooper, G.M.2
  • 31
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate Lamin A
    • of special interest. See annotation [32].
    • Orth K, Chinnaiyan AM, Garg M, Froelich CJ, Dixit VM. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate Lamin A. of special interest J Biol Chem. 271:1996;16443-16446 See annotation [32].
    • (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
  • 32
    • 0031032105 scopus 로고    scopus 로고
    • Bcl-2 prevents activation of CPP32 cysteine protease and cleavage of poly (ADP-ribose) polymerase and U1-70 kD proteins in staurosporine-mediated apoptosis
    • L act upstream of some caspases and, in this respect, are similar to CED-9, which acts upstream of the caspase CED-3 in C. elegans.
    • L act upstream of some caspases and, in this respect, are similar to CED-9, which acts upstream of the caspase CED-3 in C. elegans.
    • (1997) Cell Death Differ , vol.4 , pp. 34-38
    • Estoppey, S.1    Rodriguez, I.2    Sadoul, R.3    Martinou J-C4
  • 33
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death
    • L complexed with either Bax, Bak or Bik, is unable to bind to CED-4.
    • L complexed with either Bax, Bak or Bik, is unable to bind to CED-4.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, B.R.3    Dixit, V.M.4
  • 34
    • 0030951345 scopus 로고    scopus 로고
    • Direct physical interaction between the Caenorhabditis elegans death proteins ced-3 and ced-4
    • of outstanding interest. The authors find that CED-4 can bind to the caspase CED-3. These experiments followed the identification of a a protein-protein interaction domain termed a caspase recruitment domain (CARD) in CED-3 and CED-4.
    • Irmler M, Hofmann K, Vaux DL, Tschopp J. Direct physical interaction between the Caenorhabditis elegans death proteins ced-3 and ced-4. of outstanding interest FEBS Lett. 406:1997;189-190 The authors find that CED-4 can bind to the caspase CED-3. These experiments followed the identification of a a protein-protein interaction domain termed a caspase recruitment domain (CARD) in CED-3 and CED-4.
    • (1997) FEBS Lett , vol.406 , pp. 189-190
    • Irmler, M.1    Hofmann, K.2    Vaux, D.L.3    Tschopp, J.4
  • 35
    • 0031194404 scopus 로고    scopus 로고
    • Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis
    • of outstanding interest. The first paper to show that CED-4 is unable to promote CED-3 activation. This activity of CED-4 was inhibited by CED-9, with CED-9 able to bind to CED-4.
    • Seshagiri S, Miller LK. Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis. of outstanding interest Curr Biol. 7:1997;455-460 The first paper to show that CED-4 is unable to promote CED-3 activation. This activity of CED-4 was inhibited by CED-9, with CED-9 able to bind to CED-4.
    • (1997) Curr Biol , vol.7 , pp. 455-460
    • Seshagiri, S.1    Miller, L.K.2
  • 36
    • 0031019739 scopus 로고    scopus 로고
    • Interaction between the C. elegans cell-death regulators CED-9 and CED-4
    • of outstanding interest. Describes the ability of CED-4 to bind to CED-9. The significance of this interaction is established by the analysis of ced-9 mutants, which finds that CED-4 binding correlates with CED-9 pro-survival function.
    • Spector MS, Desnoyers S, Hoeppner DJ, Hengartner MO. Interaction between the C. elegans cell-death regulators CED-9 and CED-4. of outstanding interest Nature. 385:1997;653-656 Describes the ability of CED-4 to bind to CED-9. The significance of this interaction is established by the analysis of ced-9 mutants, which finds that CED-4 binding correlates with CED-9 pro-survival function.
    • (1997) Nature , vol.385 , pp. 653-656
    • Spector, M.S.1    Desnoyers, S.2    Hoeppner, D.J.3    Hengartner, M.O.4
  • 37
    • 0031020227 scopus 로고    scopus 로고
    • Interaction and regulation of subcellular localization of CED-4 by CED-9
    • of outstanding interest. This paper, like [36], focuses on the interaction of CED-4 with CED-9. Confocal microscopy and subcellular fractionation experiments suggest that this interaction allows CED-9 to localise CED-4 to nuclear and organelle membranes. The implication is that this property of CED-9, and perhaps other anti-apoptotic proteins, may be important for its pro-survival function.
    • Wu D, Wallen HD, Nunez G. Interaction and regulation of subcellular localization of CED-4 by CED-9. of outstanding interest Science. 275:1997;1126-1129 This paper, like [36], focuses on the interaction of CED-4 with CED-9. Confocal microscopy and subcellular fractionation experiments suggest that this interaction allows CED-9 to localise CED-4 to nuclear and organelle membranes. The implication is that this property of CED-9, and perhaps other anti-apoptotic proteins, may be important for its pro-survival function.
    • (1997) Science , vol.275 , pp. 1126-1129
    • Wu, D.1    Wallen, H.D.2    Nunez, G.3
  • 38
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of Caspase-3
    • of outstanding interest. This paper describes the purification and subsequent cloning of the protein Apaf-1 from HeLa cell cytosol. This protein was sought because of its ability to trigger caspase-3 activation in the presence of cytochrome c, dATP and Apaf in vitro. The discovery of Apaf-1 had considerable impact on the field of cell death research as it is a much sought after mammalian homologue of CED-4.
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of Caspase-3. of outstanding interest Cell. 90:1997;405-413 This paper describes the purification and subsequent cloning of the protein Apaf-1 from HeLa cell cytosol. This protein was sought because of its ability to trigger caspase-3 activation in the presence of cytochrome c, dATP and Apaf in vitro. The discovery of Apaf-1 had considerable impact on the field of cell death research as it is a much sought after mammalian homologue of CED-4.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 39
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- And TNF receptor-induced cell death
    • of outstanding interest. See annotation [40].
    • Boldin MP, Goncharov TM, Goltsev YV, Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. of outstanding interest Cell. 85:1996;803-815 See annotation [40].
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 40
    • 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
    • of outstanding interest. References [39-40] demonstrate that caspase-8 is recruited to the CD95/Fas and TNRF1 signalling complexes by the cytoplasmic adaptor protein FADD/MORT1. Activation of caspase-8 represents a mechanism by which ligation of these receptors is able to trigger apoptosis.
    • Muzio M, Chinnaiyan AM, Kischkel FC, O'Rourke K, Shevchenko A, Ni J, Scaffidi C, Bretz JD, Zhang M, Gentz R, et al. FLICE, a novel FADD homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/Apo-1) death-inducing signaling complex. of outstanding interest Cell. 85:1996;817-827 References [39-40] demonstrate that caspase-8 is recruited to the CD95/Fas and TNRF1 signalling complexes by the cytoplasmic adaptor protein FADD/MORT1. Activation of caspase-8 represents a mechanism by which ligation of these receptors is able to trigger apoptosis.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3    O'Rourke, K.4    Shevchenko, A.5    Ni, J.6    Scaffidi, C.7    Bretz, J.D.8    Zhang, M.9    Gentz, R.10
  • 41
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan H, Dixit VM. RAIDD is a new 'death' adaptor molecule. Nature. 385:1997;86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 42
    • 0030821826 scopus 로고    scopus 로고
    • Role of CED-4 in the activation of CED-3
    • of outstanding interest. This paper, together with [35], demonstrates that CED-4 stimulates CED-3 autoactivation and identifies ATP and regions of CED-4 and CED-3 as requisites for CED-3 cleavage.
    • Chinnaiyan AM, Chaudhary D, O'Rourke K, Koonin EV, Dixit VM. Role of CED-4 in the activation of CED-3. of outstanding interest Nature. 388:1997;728-729 This paper, together with [35], demonstrates that CED-4 stimulates CED-3 autoactivation and identifies ATP and regions of CED-4 and CED-3 as requisites for CED-3 cleavage.
    • (1997) Nature , vol.388 , pp. 728-729
    • Chinnaiyan, A.M.1    Chaudhary, D.2    O'Rourke, K.3    Koonin, E.V.4    Dixit, V.M.5
  • 43
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu H, Xiong J, Goeddel DV. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell. 81:1995;495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 44
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • of outstanding interest. This paper identifies Daxx as a protein that can bind to the CD95/Fas death domain and activate the JNK pathway, but surprisingly Daxx itself lacks a death domain. Unlike FADD/MORT1, Daxx appears to participate in an apoptotic pathway downstream of CD95/Fas that is Bcl-2-sensitive and does not involve caspase-8 activation.
    • Yang X, Khosravi-Far R, Chang HY, Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. of outstanding interest Cell. 89:1997;1067-1076 This paper identifies Daxx as a protein that can bind to the CD95/Fas death domain and activate the JNK pathway, but surprisingly Daxx itself lacks a death domain. Unlike FADD/MORT1, Daxx appears to participate in an apoptotic pathway downstream of CD95/Fas that is Bcl-2-sensitive and does not involve caspase-8 activation.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 45
    • 0029609086 scopus 로고
    • Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis
    • Strasser A, Harris AW, Huang DCS, Krammer PH, Cory S. Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis. EMBO J. 14:1995;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
  • 46
    • 12644286556 scopus 로고    scopus 로고
    • Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- And TNFR1-induced apoptosis
    • of outstanding interest. See annotation [47].
    • Bertin J, Armstrong RC, Ottilie S, Martin DA, Wang Y, Banks S, Wang G-H, Senkevich TG, Alnemri ES, Moss B, et al. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis. of outstanding interest Proc Natl Acad Sci USA. 94:1996;1172-1176 See annotation [47].
    • (1996) Proc Natl Acad Sci USA , vol.94 , pp. 1172-1176
    • Bertin, J.1    Armstrong, R.C.2    Ottilie, S.3    Martin, D.A.4    Wang, Y.5    Banks, S.6    Wang G-H7    Senkevich, T.G.8    Alnemri, E.S.9    Moss, B.10
  • 47
    • 0030970013 scopus 로고    scopus 로고
    • Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
    • of outstanding interest. References [46,47] describe how some viruses interfere with the defences of the host by producing proteins that block caspase-8 activation downstream of members of the TNF receptor family.
    • Thome M, Schneider P, Hofmann K, Fickenscher H, Meinl E, Neipel F, Mattmann C, Burns K, Bodmer J-L, Schröster M, et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. of outstanding interest Nature. 386:1997;517-521 References [46,47] describe how some viruses interfere with the defences of the host by producing proteins that block caspase-8 activation downstream of members of the TNF receptor family.
    • (1997) Nature , vol.386 , pp. 517-521
    • Thome, M.1    Schneider, P.2    Hofmann, K.3    Fickenscher, H.4    Meinl, E.5    Neipel, F.6    Mattmann, C.7    Burns, K.8    Bodmer J-L9    Schröster, M.10
  • 49
    • 0031017578 scopus 로고    scopus 로고
    • A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak
    • Cheng EH-Y, Nicholas J, Bellows DS, Hayward GS, Guo H-G, Reitz MS, Hardwick JM. A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak. Proc Natl Acad Sci USA. 94:1997;690-694.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 690-694
    • Cheng Eh-Y1    Nicholas, J.2    Bellows, D.S.3    Hayward, G.S.4    Guo H-G5    Reitz, M.S.6    Hardwick, J.M.7
  • 50
    • 0026773471 scopus 로고
    • The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor α
    • White E, Sabbatini P, Debbas M, Wold WSM, Kusher DI, Gooding LR. The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor α Mol Cell Biol. 12:1992;2570-2580.
    • (1992) Mol Cell Biol , vol.12 , pp. 2570-2580
    • White, E.1    Sabbatini, P.2    Debbas, M.3    Wold, W.S.M.4    Kusher, D.I.5    Gooding, L.R.6
  • 51
    • 0031020635 scopus 로고    scopus 로고
    • L and adenovirus protein E1B19kD are functionally equivalent in their ability to inhibit cell death
    • L and adenovirus protein E1B19kD are functionally equivalent in their ability to inhibit cell death. Oncogene. 14:1997;405-414.
    • (1997) Oncogene , vol.14 , pp. 405-414
    • Huang, D.C.S.1    Cory, S.2    Strasser, A.3
  • 52
    • 0027260656 scopus 로고
    • Epstein virus-coded BHRF 1 protein, a viral homologue of Bcl-2 protects human B cells from programmed cell death
    • Henderson S, Huen D, Rowe M, Dawson C, Johnson G, Rickinson A. Epstein virus-coded BHRF 1 protein, a viral homologue of Bcl-2 protects human B cells from programmed cell death. Proc Natl Acad Sci USA. 90:1993;8479-8483.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8479-8483
    • Henderson, S.1    Huen, D.2    Rowe, M.3    Dawson, C.4    Johnson, G.5    Rickinson, A.6
  • 53
    • 0030861571 scopus 로고    scopus 로고
    • Bcl-2 and Bax function independently to regulate cell death
    • of special interest. This paper examines cells from Bcl-2-deficient mice, Bax-deficient mice and mice deficient in both proteins for their ability to undergo apoptosis. This work establishes that Bax can promote cell death in the absence of Bcl-2 and that Bcl-2 does not need Bax to promote cell survival.
    • Knudson CM, Korsmeyer SJ. Bcl-2 and Bax function independently to regulate cell death. of special interest Nat Genet. 16:1997;358-363 This paper examines cells from Bcl-2-deficient mice, Bax-deficient mice and mice deficient in both proteins for their ability to undergo apoptosis. This work establishes that Bax can promote cell death in the absence of Bcl-2 and that Bcl-2 does not need Bax to promote cell survival.
    • (1997) Nat Genet , vol.16 , pp. 358-363
    • Knudson, C.M.1    Korsmeyer, S.J.2
  • 57
    • 9844257587 scopus 로고    scopus 로고
    • Inhibition of Bax channel-forming activity by Bcl-2
    • of special interest. This paper shows that a truncated Bax mutant which lacks a carboxy-terminal hydrophobic domain behaves as a pore-forming protein at physiological pH and that Bcl-2 can block the effects of Bax on membranes.
    • Antonsson B, Conti F, Ciavatta A-M, Montessuit S, Lewis S, Martinou I, Bernasconi L, Bernard A, Mermod J-J, Mazzei G, et al. Inhibition of Bax channel-forming activity by Bcl-2. of special interest Science. 277:1997;370-372 This paper shows that a truncated Bax mutant which lacks a carboxy-terminal hydrophobic domain behaves as a pore-forming protein at physiological pH and that Bcl-2 can block the effects of Bax on membranes.
    • (1997) Science , vol.277 , pp. 370-372
    • Antonsson, B.1    Conti, F.2    Ciavatta A-M3    Montessuit, S.4    Lewis, S.5    Martinou, I.6    Bernasconi, L.7    Bernard, A.8    Mermod J-J9    Mazzei, G.10
  • 58
    • 0029906828 scopus 로고    scopus 로고
    • BAX-induced cell death may not require interleukin 1β-converting enzyme-like proteases
    • Xiang J, Chao DT, Korsmeyer SJ. BAX-induced cell death may not require interleukin 1β-converting enzyme-like proteases. Proc Natl Acad Sci USA. 93:1996;14559-14563.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 59
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak
    • McCarthy NJ, Whyte MKB, Gilbert CS, Evan GI. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J Cell Biol. 136:1997;215-227.
    • (1997) J Cell Biol , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.B.2    Gilbert, C.S.3    Evan, G.I.4
  • 60
    • 0024501122 scopus 로고
    • The bcl-2 candidate proto-oncogene product is a 24-kilodalton integral-membrane protein highly expressed in lymphoid cell lines and lymphomas carrying the t(14;18) translocation
    • Chen-Levy Z, Nourse J, Cleary ML. The bcl-2 candidate proto-oncogene product is a 24-kilodalton integral-membrane protein highly expressed in lymphoid cell lines and lymphomas carrying the t(14;18) translocation. Mol Cell Biol. 9:1989;701-710.
    • (1989) Mol Cell Biol , vol.9 , pp. 701-710
    • Chen-Levy, Z.1    Nourse, J.2    Cleary, M.L.3
  • 61
    • 0025213270 scopus 로고
    • Membrane topology of the Bcl-2 proto-oncogenic protein demonstrated in vitro
    • Chen-Levy Z, Cleary ML. Membrane topology of the Bcl-2 proto-oncogenic protein demonstrated in vitro. J Biol Chem. 265:1990;4929-4933.
    • (1990) J Biol Chem , vol.265 , pp. 4929-4933
    • Chen-Levy, Z.1    Cleary, M.L.2
  • 64
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53:1993;4701-4714.
    • (1993) Cancer Res , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 66
    • 0027977928 scopus 로고
    • The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum and the outer mitochondrial membrane
    • Lithgow T, van Driel R, Bertram JF, Strasser A. The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum and the outer mitochondrial membrane. Cell Growth Differ. 5:1994;411-417.
    • (1994) Cell Growth Differ , vol.5 , pp. 411-417
    • Lithgow, T.1    Van Driel, R.2    Bertram, J.F.3    Strasser, A.4
  • 68
    • 0028289951 scopus 로고
    • Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus
    • Nguyen M, Branton PE, Walton PA, Oltvai ZN, Korsmeyer SJ, Shore GC. Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus. J Biol Chem. 269:1994;16521-16524.
    • (1994) J Biol Chem , vol.269 , pp. 16521-16524
    • Nguyen, M.1    Branton, P.E.2    Walton, P.A.3    Oltvai, Z.N.4    Korsmeyer, S.J.5    Shore, G.C.6
  • 69
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • of outstanding interest. The authors of this paper describe a cell-free system in which cytochrome c is essential for caspase-3 activation and demonstrates that cytochrome c levels in the cytosol increase when cells are induced to undergo apoptosis with staurosporine.
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. of outstanding interest Cell. 86:1996;147-157 The authors of this paper describe a cell-free system in which cytochrome c is essential for caspase-3 activation and demonstrates that cytochrome c levels in the cytosol increase when cells are induced to undergo apoptosis with staurosporine.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 70
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • of outstanding interest. The authors demonstrate that cytochrome c released from mitochondria in a Xenopus cell-free system is able to trigger caspase-3 activation in the presence of other cytosolic factors. Bcl-2 prevents this cytochrome c release and associated apoptotic changes. These observations infer that Bcl-2 promotes cell survival by regulating caspase activation.
    • Kluck RM, Bossy Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. of outstanding interest Science. 275:1997;1132-1136 The authors demonstrate that cytochrome c released from mitochondria in a Xenopus cell-free system is able to trigger caspase-3 activation in the presence of other cytosolic factors. Bcl-2 prevents this cytochrome c release and associated apoptotic changes. These observations infer that Bcl-2 promotes cell survival by regulating caspase activation.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 71
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • of outstanding interest. This reference describes the release of cytochrome c from the mitochondria of cells induced to undergo apoptosis by staurosporine treatment. The dependence of the apoptotic program on cytochrome c release was demonstrated by the inability of cell free extracts depleted of cytochrome c to initiate caspase-mediated cleavage events. Bcl-2 was shown to block cytochrome c release and apoptosis, indicating that this may be an important aspect of its pro-survival function.
    • Yang J, Liu X, Bhalla K, Kim CN, Ibrado AM, Cai J, Peng T-I, Jones DP, Wang X. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. of outstanding interest Science. 275:1997;1129-1132 This reference describes the release of cytochrome c from the mitochondria of cells induced to undergo apoptosis by staurosporine treatment. The dependence of the apoptotic program on cytochrome c release was demonstrated by the inability of cell free extracts depleted of cytochrome c to initiate caspase-mediated cleavage events. Bcl-2 was shown to block cytochrome c release and apoptosis, indicating that this may be an important aspect of its pro-survival function.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6    Peng T-I7    Jones, D.P.8    Wang, X.9
  • 72
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • of outstanding interest. The paper details the discovery of a protein, DFF, that is a substrate of caspase-3 and that is activated by proteolytic cleavage. Active DFF promotes internucleosomal DNA fragmentation in isolated nuclei, but not having endonuclease activity itself must activate a downstream endonuclease. This finding therefore elucidates a route form caspases to DNA fragmentation, a commonly observed feature in apoptotic cells.
    • Liu X, Zou H, Slaughter C, Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. of outstanding interest Cell. 89:1997;175-184 The paper details the discovery of a protein, DFF, that is a substrate of caspase-3 and that is activated by proteolytic cleavage. Active DFF promotes internucleosomal DNA fragmentation in isolated nuclei, but not having endonuclease activity itself must activate a downstream endonuclease. This finding therefore elucidates a route form caspases to DNA fragmentation, a commonly observed feature in apoptotic cells.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 73
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • of outstanding interest. This paper demonstrates that the serine-threonine kinase PAK2 is activated by caspase-3 cleavage and that some of the morphological changes characteristic of apoptotic cells are blocked by a dominant-negative PAK2 mutant.
    • Rudel T, Bokoch GM. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. of outstanding interest Science. 276:1997;1571-1574 This paper demonstrates that the serine-threonine kinase PAK2 is activated by caspase-3 cleavage and that some of the morphological changes characteristic of apoptotic cells are blocked by a dominant-negative PAK2 mutant.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 75
    • 0029950290 scopus 로고    scopus 로고
    • Bcl-2 inhibits the mitochondrial release of an apoptogenic protease
    • of special interest. This paper describes a 50kDa protease, AIF, that is released from mitochondria induced to undergo permeability transition in a cell-free system. AIF can trigger caspase-3 activation and internucleosomal DNA fragmentation in isolation and its release from mitochondria is blocked by Bcl-2.
    • Susin SA, Zamzami N, Castedo M, Hirsch T, Marchetti P, Macho A, Daugas E, Geuskens M, Kroemer G. Bcl-2 inhibits the mitochondrial release of an apoptogenic protease. of special interest J Exp Med. 184:1996;1331-1341 This paper describes a 50kDa protease, AIF, that is released from mitochondria induced to undergo permeability transition in a cell-free system. AIF can trigger caspase-3 activation and internucleosomal DNA fragmentation in isolation and its release from mitochondria is blocked by Bcl-2.
    • (1996) J Exp Med , vol.184 , pp. 1331-1341
    • Susin, S.A.1    Zamzami, N.2    Castedo, M.3    Hirsch, T.4    Marchetti, P.5    MacHo, A.6    Daugas, E.7    Geuskens, M.8    Kroemer, G.9
  • 76
    • 0023786047 scopus 로고
    • Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
    • Vaux DL, Cory S, Adams JM. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature. 335:1988;440-442.
    • (1988) Nature , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 77
    • 0031127855 scopus 로고    scopus 로고
    • Mouse vaginal opening is an apoptosis-dependent process which can be prevented by the overexpression of Bcl2
    • Rodriguez I, Araki K, Khatib K, Martinou J-C, Vassalli P. Mouse vaginal opening is an apoptosis-dependent process which can be prevented by the overexpression of Bcl2. Dev Biol. 184:1997;115-121.
    • (1997) Dev Biol , vol.184 , pp. 115-121
    • Rodriguez, I.1    Araki, K.2    Khatib, K.3    Martinou J-C4    Vassalli, P.5
  • 78
    • 0030003958 scopus 로고    scopus 로고
    • Inhibition of testicular germ cell apoptosis and differentiation in mice misexpressing Bcl-2 in spermatogonia
    • Furuchi T, Masuko K, Nishimune Y, Obinata M, Matsui Y. Inhibition of testicular germ cell apoptosis and differentiation in mice misexpressing Bcl-2 in spermatogonia. Development. 122:1996;1703-1709.
    • (1996) Development , vol.122 , pp. 1703-1709
    • Furuchi, T.1    Masuko, K.2    Nishimune, Y.3    Obinata, M.4    Matsui, Y.5
  • 79
    • 0030975776 scopus 로고    scopus 로고
    • An early and massive wave of germinal cell apoptosis is required for the development of functional spermatogenesis
    • Rodriguez I, Ody C, Araki K, Garcia I, Vassalli P. An early and massive wave of germinal cell apoptosis is required for the development of functional spermatogenesis. EMBO J. 16:1997;2262-2270.
    • (1997) EMBO J , vol.16 , pp. 2262-2270
    • Rodriguez, I.1    Ody, C.2    Araki, K.3    Garcia, I.4    Vassalli, P.5
  • 80
    • 0028297141 scopus 로고
    • Bcl-2 expression promotes B but not T lymphoid development in scid mice
    • Strasser A, Harris AW, Corcoran LM, Cory S. bcl-2 expression promotes B but not T lymphoid development in scid mice. Nature. 368:1994;457-460.
    • (1994) Nature , vol.368 , pp. 457-460
    • Strasser, A.1    Harris, A.W.2    Corcoran, L.M.3    Cory, S.4
  • 81
    • 0030939476 scopus 로고    scopus 로고
    • Constitutive Bcl-2 expression during immunoglobulin heavy chain-promoted B cell differentiation expands novel precursor B cells
    • Young F, Mizoguchi E, Bhan AK, Alt FW. Constitutive Bcl-2 expression during immunoglobulin heavy chain-promoted B cell differentiation expands novel precursor B cells. Immunity. 6:1997;23-33.
    • (1997) Immunity , vol.6 , pp. 23-33
    • Young, F.1    Mizoguchi, E.2    Bhan, A.K.3    Alt, F.W.4
  • 82
    • 0030608977 scopus 로고    scopus 로고
    • Cell survival and cell differentiation during B lymphopoiesis are subject to distinct control
    • Tarlinton DM, Corcoran LM, Strasser A. Cell survival and cell differentiation during B lymphopoiesis are subject to distinct control. Int Immunol. 9:1997;1481-1494.
    • (1997) Int Immunol , vol.9 , pp. 1481-1494
    • Tarlinton, D.M.1    Corcoran, L.M.2    Strasser, A.3
  • 83
    • 0031587848 scopus 로고    scopus 로고
    • Enforced expression of Bcl-2 in monocytes rescues macrophages and partially reverses osteopetrosis in op/op mice
    • of outstanding interest. See annotation [86].
    • Lagasse E, Weissman IL. Enforced expression of Bcl-2 in monocytes rescues macrophages and partially reverses osteopetrosis in op/op mice. of outstanding interest Cell. 89:1997;1021-1031 See annotation [86].
    • (1997) Cell , vol.89 , pp. 1021-1031
    • Lagasse, E.1    Weissman, I.L.2
  • 84
    • 0031587826 scopus 로고    scopus 로고
    • Bcl-2 rescues T lymphopoiesis in Interleukin-7 receptor-deficient mice
    • of outstanding interest. See annotation [86].
    • Akashi K, Kondo M, von Freeden-Jeffry U, Murray R, Weissman IL. Bcl-2 rescues T lymphopoiesis in Interleukin-7 receptor-deficient mice. of outstanding interest Cell. 89:1997;1033-1041 See annotation [86].
    • (1997) Cell , vol.89 , pp. 1033-1041
    • Akashi, K.1    Kondo, M.2    Von Freeden-Jeffry, U.3    Murray, R.4    Weissman, I.L.5
  • 86
    • 0030787787 scopus 로고    scopus 로고
    • Bcl-2 rescues T lymphopoiesis, but not B or NK cell development, in common γ chain-deficient mice
    • of outstanding interest. The authors of references [83-86] describe how a bcl-2 transgene can rescue some of the defects associated with cytokine or cytokine receptor deficient animals. They indicate that the essential role of some cytokines may be to provide cells with a survival signal.
    • Kondo M, Akashi K, Domen J, Sugamura K, Weissman IL. Bcl-2 rescues T lymphopoiesis, but not B or NK cell development, in common γ chain-deficient mice. of outstanding interest Immunity. 7:1997;155-162 The authors of references [83-86] describe how a bcl-2 transgene can rescue some of the defects associated with cytokine or cytokine receptor deficient animals. They indicate that the essential role of some cytokines may be to provide cells with a survival signal.
    • (1997) Immunity , vol.7 , pp. 155-162
    • Kondo, M.1    Akashi, K.2    Domen, J.3    Sugamura, K.4    Weissman, I.L.5
  • 87
    • 0030874326 scopus 로고    scopus 로고
    • The earliest T lineage-committed cells depend on IL-7 for Bcl-2 expression and normal cell cycle progression
    • of special interest. This reference examines Bcl-2 expression in immature thymocytes from IL-7-deficient mice. Loss of Bcl-2 expression is found to correlate with the early defect in T cell development in these mice suggesting that Bcl-2 may be an important downstream target of the IL-7 receptor in these cells.
    • Von Freeden-Jeffry U, Solvason N, Howard M, Murray R. The earliest T lineage-committed cells depend on IL-7 for Bcl-2 expression and normal cell cycle progression. of special interest Immunity. 7:1997;147-154 This reference examines Bcl-2 expression in immature thymocytes from IL-7-deficient mice. Loss of Bcl-2 expression is found to correlate with the early defect in T cell development in these mice suggesting that Bcl-2 may be an important downstream target of the IL-7 receptor in these cells.
    • (1997) Immunity , vol.7 , pp. 147-154
    • Von Freeden-Jeffry, U.1    Solvason, N.2    Howard, M.3    Murray, R.4
  • 88
    • 0031569965 scopus 로고    scopus 로고
    • The Fas-deficient SCID mouse exhibits the development of T cells in the thymus
    • Yasutomo K, Maeda K-I, Hisaeda H, Good RA, Kuroda Y, Himeno K. The Fas-deficient SCID mouse exhibits the development of T cells in the thymus. J Immunol. 158:1997;4729-4733.
    • (1997) J Immunol , vol.158 , pp. 4729-4733
    • Yasutomo, K.1    Maeda K-I2    Hisaeda, H.3    Good, R.A.4    Kuroda, Y.5    Himeno, K.6
  • 89
    • 0030756459 scopus 로고    scopus 로고
    • Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Kostic V, Jackson-Lewis V, de Bilbao F, Dubois-Dauphin M, Przedborski S. Bcl-2: prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis. Science. 277:1997;559-562.
    • (1997) Science , vol.277 , pp. 559-562
    • Kostic, V.1    Jackson-Lewis, V.2    De Bilbao, F.3    Dubois-Dauphin, M.4    Przedborski, S.5
  • 90
    • 0025752461 scopus 로고
    • Two C. elegans genes control the programmed deaths of specific cells in the pharynx
    • Ellis RE, Horvitz HR. Two C. elegans genes control the programmed deaths of specific cells in the pharynx. Development. 112:1991;591-603.
    • (1991) Development , vol.112 , pp. 591-603
    • Ellis, R.E.1    Horvitz, H.R.2
  • 91
    • 0029761433 scopus 로고    scopus 로고
    • Transcriptional regulator of programmed cell death encoded by Caenorhabditis elegans gene ces-2
    • of special interest. This paper describes the cloning and characterisation of CES-2, a transcription factor that acts upstream of CED-3, CED-4 and CED-9 in the nematode cell death pathway.
    • Metzstein MM, Hengartner MO, Tsung N, Ellis RE, Horvitz HR. Transcriptional regulator of programmed cell death encoded by Caenorhabditis elegans gene ces-2. of special interest Nature. 382:1996;545-547 This paper describes the cloning and characterisation of CES-2, a transcription factor that acts upstream of CED-3, CED-4 and CED-9 in the nematode cell death pathway.
    • (1996) Nature , vol.382 , pp. 545-547
    • Metzstein, M.M.1    Hengartner, M.O.2    Tsung, N.3    Ellis, R.E.4    Horvitz, H.R.5
  • 92
    • 0031038137 scopus 로고    scopus 로고
    • Bax suppresses tumorigenesis and stimulates apoptosis in vivo
    • of outstanding interest. This paper demonstrates for the first time that Bax is a tumour-suppressor protein which acts downstream of the tumour-suppressor p53.
    • Yin C, Knudson CM, Korsmeyer SJ, Van Dyke T. Bax suppresses tumorigenesis and stimulates apoptosis in vivo. of outstanding interest Nature. 385:1997;637-640 This paper demonstrates for the first time that Bax is a tumour-suppressor protein which acts downstream of the tumour-suppressor p53.
    • (1997) Nature , vol.385 , pp. 637-640
    • Yin, C.1    Knudson, C.M.2    Korsmeyer, S.J.3    Van Dyke, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.