-
1
-
-
0015383455
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
16
-
-
0027282044
-
Bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
-
Boise LH, Gonzalez-Garcia M, Postema CE, Ding L, Lindsten T, Turka LA, Mao X, Nunez G, Thompson CB. bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell. 74:1993;597-608.
-
(1993)
Cell
, vol.74
, pp. 597-608
-
-
Boise, L.H.1
Gonzalez-Garcia, M.2
Postema, C.E.3
Ding, L.4
Lindsten, T.5
Turka, L.A.6
Mao, X.7
Nunez, G.8
Thompson, C.B.9
-
17
-
-
0027480450
-
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
-
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
-
19
-
-
0028812606
-
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, Houghton AB, Malstrom S, Avery BJ, Ebb RG, Subramanian T, Chittenden T, Lutz RJ, Chinnadurai G. 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. 11:1995;1921-1928.
-
(1995)
Oncogene
, vol.11
, pp. 1921-1928
-
-
Boyd, J.M.1
Gallo, G.J.2
Elangovan, B.3
Houghton, A.B.4
Malstrom, S.5
Avery, B.J.6
Ebb, R.G.7
Subramanian, T.8
Chittenden, T.9
Lutz, R.J.10
Chinnadurai, G.11
-
20
-
-
0028986876
-
Induction of apoptosis by the Bcl-2 homologue Bak
-
Chittenden T, Harrington EA, O'Connor R, Flemington C, Lutz RJ, Evan GI, Guild BC. Induction of apoptosis by the Bcl-2 homologue Bak. Nature. 374:1995;733-736.
-
(1995)
Nature
, vol.374
, pp. 733-736
-
-
Chittenden, T.1
Harrington, E.A.2
O'Connor, R.3
Flemington, C.4
Lutz, R.J.5
Evan, G.I.6
Guild, B.C.7
-
21
-
-
0028946015
-
Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K
-
Farrow SN, White JHM, Martinou I, Raven T, Pun K-T, Grinham CJ, Martinou J-C, Brown R. Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K. Nature. 374:1995;731-733.
-
(1995)
Nature
, vol.374
, pp. 731-733
-
-
Farrow, S.N.1
White, J.H.M.2
Martinou, I.3
Raven, T.4
Pun K-T5
Grinham, C.J.6
Martinou J-C7
Brown, R.8
-
22
-
-
0028904163
-
Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak
-
Kiefer MC, Brauer MJ, Powers VC, Wu JJ, Umansky SR, Tomei LD, Barr PJ. Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak. Nature. 374:1995;736-739.
-
(1995)
Nature
, vol.374
, pp. 736-739
-
-
Kiefer, M.C.1
Brauer, M.J.2
Powers, V.C.3
Wu, J.J.4
Umansky, S.R.5
Tomei, L.D.6
Barr, P.J.7
-
23
-
-
0028809209
-
L and Bcl-2, displaces Bax and promotes cell death
-
L and Bcl-2, displaces Bax and promotes cell death. Cell. 80:1995;285-291.
-
(1995)
Cell
, vol.80
, pp. 285-291
-
-
Yang, E.1
Zha, J.2
Jockel, J.3
Boise, L.H.4
Thompson, C.B.5
Korsmeyer, S.J.6
-
24
-
-
9544250358
-
Bcl-w, a novel member of the bcl-2 family, promotes cell survival
-
L, is a mammalian pro-survival protein. The discovery of multiple proteins of apparently similar function raises questions as to their different roles in vivo.
-
L, is a mammalian pro-survival protein. The discovery of multiple proteins of apparently similar function raises questions as to their different roles in vivo.
-
(1996)
Oncogene
, vol.13
, pp. 665-675
-
-
Gibson, L.1
Holmgreen, S.2
Huang, D.C.S.3
Bernard, O.4
Copeland, N.G.5
Jenkins, N.A.6
Sutherland, G.R.7
Baker, E.8
Adams, J.M.9
Cory, S.10
-
25
-
-
0029790857
-
Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K
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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
-
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0029807585
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BID: A novel BH3 domain-only death agonist
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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
-
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0030970085
-
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
-
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0030012008
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Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities
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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
-
Molecular ordering of the cell death pathway
-
of special interest. See annotation [32].
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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
-
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0029894283
-
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
-
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
-
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
-
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
-
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0030951345
-
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
-
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0031194404
-
Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis
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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
-
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
-
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0031020227
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
48
-
-
0030893693
-
Herpesvirus saimiri encodes a functional homolog of the human bcl-2 oncogene
-
Nava VE, Cheng EH-Y, Veliuona M, Zou S, Clem RJ, Mayer M, Hardwick JM. Herpesvirus saimiri encodes a functional homolog of the human bcl-2 oncogene. J Virol. 71:1997;4118-4122.
-
(1997)
J Virol
, vol.71
, pp. 4118-4122
-
-
Nava, V.E.1
Cheng Eh-Y2
Veliuona, M.3
Zou, S.4
Clem, R.J.5
Mayer, M.6
Hardwick, J.M.7
-
49
-
-
0031017578
-
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
-
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
-
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
-
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
-
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
-
54
-
-
5244224827
-
L, an inhibitor of programmed cell death
-
L and related proteins may also form membrane pores. This is the first member of the Bcl-2 protein family to have its structure solved.
-
L and related proteins may also form membrane pores. This is the first member of the Bcl-2 protein family to have its structure solved.
-
(1996)
Nature
, vol.381
, pp. 335-341
-
-
Muchmore, S.W.1
Sattler, M.2
Liang, H.3
Meadows, R.P.4
Harlan, J.E.5
Yoon, H.S.6
Nettesheim, D.7
Chang, B.S.8
Thompson, C.B.9
Wong S-L10
-
55
-
-
1842332735
-
L forms an ion channel in synthetic lipid membranes
-
L forms an ion channel in synthetic lipid membranes. Nature. 385:1997;353-357.
-
(1997)
Nature
, vol.385
, pp. 353-357
-
-
Minn, A.J.1
Vélez, P.2
Schendel, S.L.3
Liang, H.4
Muchmore, S.W.5
Fesik, S.W.6
Fill, M.7
Thompson, C.B.8
-
56
-
-
0031008397
-
Channel formation by anti-apoptotic protein Bcl-2
-
Schendel SL, Xie Z, Oblatt-Montal M, Matsuyama S, Montal M, Reed JC. Channel formation by anti-apoptotic protein Bcl-2. Proc Natl Acad Sci USA. 94:1997;5113-5118.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 5113-5118
-
-
Schendel, S.L.1
Xie, Z.2
Oblatt-Montal, M.3
Matsuyama, S.4
Montal, M.5
Reed, J.C.6
-
57
-
-
9844257587
-
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
-
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
-
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
-
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
-
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
-
62
-
-
0027051578
-
Subcellular localization of bcl-2 protein
-
De Jong D, Prins F, van Krieken HHJM, Mason DY, van Ommen G, Kluin PM. Subcellular localization of bcl-2 protein. Curr Topics Microbiol Immunol. 182:1992;287-292.
-
(1992)
Curr Topics Microbiol Immunol
, vol.182
, pp. 287-292
-
-
De Jong, D.1
Prins, F.2
Van Krieken, H.H.J.M.3
Mason, D.Y.4
Van Ommen, G.5
Kluin, P.M.6
-
63
-
-
0026480579
-
Ultrastructural localization of BCL-2 protein
-
Monaghan P, Robertson D, Amos TAS, Dyer MJS, Mason DY, Greaves MF. Ultrastructural localization of BCL-2 protein. J Histochem Cytochem. 40:1992;1819-1825.
-
(1992)
J Histochem Cytochem
, vol.40
, pp. 1819-1825
-
-
Monaghan, P.1
Robertson, D.2
Amos, T.A.S.3
Dyer, M.J.S.4
Mason, D.Y.5
Greaves, M.F.6
-
64
-
-
0027362667
-
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
-
65
-
-
0028157171
-
Subcellular localization of the bcl-2 protein in malignant and normal lymphoid cells
-
De Jong D, Prins FA, Mason DY, Reed JC, van Ommen GB, Kluin PM. Subcellular localization of the bcl-2 protein in malignant and normal lymphoid cells. Cancer Res. 54:1994;256-260.
-
(1994)
Cancer Res
, vol.54
, pp. 256-260
-
-
De Jong, D.1
Prins, F.A.2
Mason, D.Y.3
Reed, J.C.4
Van Ommen, G.B.5
Kluin, P.M.6
-
66
-
-
0027977928
-
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
-
67
-
-
0027485461
-
Bcl-2 functions in an antioxidant pathway to prevent apoptosis
-
Hockenbery DM, Oltvai ZN, Yin X-M, Milliman CL, Korsmeyer S. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell. 74:1993;241-251.
-
(1993)
Cell
, vol.74
, pp. 241-251
-
-
Hockenbery, D.M.1
Oltvai, Z.N.2
Yin X-M3
Milliman, C.L.4
Korsmeyer, S.5
-
68
-
-
0028289951
-
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
-
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
-
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
-
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
-
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
-
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
-
74
-
-
0030610962
-
L as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis
-
L.
-
L.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 6939-6942
-
-
Kharbanda, S.1
Pandey, P.2
Schofield, L.3
Israels, S.4
Roncinske, R.5
Yoshida, K.6
Bharti, A.7
Yuan Z-M8
Saxena, S.9
Weichselbaum, R.10
-
75
-
-
0029950290
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
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