-
1
-
-
2642689658
-
Proteases to die for
-
Cryns V., Yuan J. Proteases to die for. Genes Dev. 12:1998;1551-1570.
-
(1998)
Genes Dev
, vol.12
, pp. 1551-1570
-
-
Cryns, V.1
Yuan, J.2
-
2
-
-
0032563323
-
Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment
-
The authors determined the solution structure of the CARD domain in RAIDD using NMR spectroscopy. The arrangement of six α-helices of CARD is topologically similar to that of DED and the death domain. The surface contains a basic and acidic patch on opposite sites, indicating that CARDs pair through hydrophilic interaction. The modeling results of the CARD domains of caspase-2 and -9, Apaf-1, CED3 and CED-4 show that the basic/acidic surface polarity is highly conserved, suggesting a general mode for CARD-CARD interaction.
-
Chou J.J., Matsuo H., Duan H., Wagner G. Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Cell. 94:1998;171-180. The authors determined the solution structure of the CARD domain in RAIDD using NMR spectroscopy. The arrangement of six α-helices of CARD is topologically similar to that of DED and the death domain. The surface contains a basic and acidic patch on opposite sites, indicating that CARDs pair through hydrophilic interaction. The modeling results of the CARD domains of caspase-2 and -9, Apaf-1, CED3 and CED-4 show that the basic/acidic surface polarity is highly conserved, suggesting a general mode for CARD-CARD interaction.
-
(1998)
Cell
, vol.94
, pp. 171-180
-
-
Chou, J.J.1
Matsuo, H.2
Duan, H.3
Wagner, G.4
-
3
-
-
0032580153
-
NMR structure and mutagenesis of the FADD(Mort1) death-effector domain
-
The authors characterized the solution structure of the DED domain in FADD using NMR spectroscopy. Although the overall structure of FADD DED is similar to the death domain of Fas, the hydrophobic region of FADD DED is vital for its binding to caspase-8 indicating that hydrophobic interaction is important for DED-DED coupling.
-
Eberstadt M., Huang B., Chen Z., Meadows R.P., Ng S-C., Zheng L., Lenardo M.J., Fesik S.W. NMR structure and mutagenesis of the FADD(Mort1) death-effector domain. Nature. 293:1998;941-945. The authors characterized the solution structure of the DED domain in FADD using NMR spectroscopy. Although the overall structure of FADD DED is similar to the death domain of Fas, the hydrophobic region of FADD DED is vital for its binding to caspase-8 indicating that hydrophobic interaction is important for DED-DED coupling.
-
(1998)
Nature
, vol.293
, pp. 941-945
-
-
Eberstadt, M.1
Huang, B.2
Chen, Z.3
Meadows, R.P.4
Ng, S.-C.5
Zheng, L.6
Lenardo, M.J.7
Fesik, S.W.8
-
4
-
-
0030745646
-
Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
-
The authors identified Apaf-1 as a mammalian homolog of the C. elegans cell death gene product CED-4 protein using an elegant biochemical system.
-
Zou H., Henzel W.J., 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. Cell. 90:1997;405-413. The authors identified Apaf-1 as a mammalian homolog of the C. elegans cell death gene product CED-4 protein using an elegant biochemical system.
-
(1997)
Cell
, vol.90
, pp. 405-413
-
-
Zou, H.1
Henzel, W.J.2
Liu, X.3
Lutschg, A.4
Wang, X.5
-
5
-
-
0030715323
-
Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
-
The authors showed that caspase-9 is activated through the interaction with Apaf-1 in the presence of cytochrome c and dATP and established the existence of a caspase cascade from caspase-9 to caspase-3.
-
Li P., Nijhawan D., Brudihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489. The authors showed that caspase-9 is activated through the interaction with Apaf-1 in the presence of cytochrome c and dATP and established the existence of a caspase cascade from caspase-9 to caspase-3.
-
(1997)
Cell
, vol.91
, pp. 479-489
-
-
Li, P.1
Nijhawan, D.2
Brudihardjo, I.3
Srinivasula, S.M.4
Ahmad, M.5
Alnemri, E.S.6
Wang, X.7
-
6
-
-
0030581151
-
Induction of apoptotic program in cell free extracts: Requirement for dATP and cytochrome c
-
Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell free extracts: requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
-
(1996)
Cell
, vol.86
, pp. 147-157
-
-
Liu, X.1
Kim, C.N.2
Yang, J.3
Jemmerson, R.4
Wang, X.5
-
7
-
-
0032085941
-
Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
-
This paper presents in vitro evidence that Apaf-1 can form oligomers and may facilitate procaspase-9 autoactivation by oligomerizing its precursor molecules, suggesting that oligomerization of procaspases through adapter proteins may be a general mechanism for caspase activation.
-
Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Alnemri E.S. Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell. 1:1998;949-957. This paper presents in vitro evidence that Apaf-1 can form oligomers and may facilitate procaspase-9 autoactivation by oligomerizing its precursor molecules, suggesting that oligomerization of procaspases through adapter proteins may be a general mechanism for caspase activation.
-
(1998)
Mol Cell
, vol.1
, pp. 949-957
-
-
Srinivasula, S.M.1
Ahmad, M.2
Fernandes-Alnemri, T.3
Alnemri, E.S.4
-
8
-
-
0032575723
-
Essential role of CED-4 oligomerization in CED-3 activation and apoptosis
-
The authors demonstrated that oligomerization of CED-3 facilitated by CED-4 is essential for activation of CED-3, suggesting that this mechanism of activation is highly conserved throughout evolution.
-
Yang X., Chang H.Y., Baltimore D. Essential role of CED-4 oligomerization in CED-3 activation and apoptosis. Science. 281:1998;1355-1357. The authors demonstrated that oligomerization of CED-3 facilitated by CED-4 is essential for activation of CED-3, suggesting that this mechanism of activation is highly conserved throughout evolution.
-
(1998)
Science
, vol.281
, pp. 1355-1357
-
-
Yang, X.1
Chang, H.Y.2
Baltimore, D.3
-
9
-
-
0032575714
-
Death receptors: Signaling and modulation
-
Ashkenazi A., Dixit V.M. Death receptors: signaling and modulation. Science. 281:1998;1305-1308.
-
(1998)
Science
, vol.281
, pp. 1305-1308
-
-
Ashkenazi, A.1
Dixit, V.M.2
-
10
-
-
0032579490
-
An induced proximity model for caspase-8 activation
-
Muzio M., Stockwell B.R., Stennicke H.R., Salvesen G.S., Dixit V.M. An induced proximity model for caspase-8 activation. J Biol Chem. 273:1998;2926-2930.
-
(1998)
J Biol Chem
, vol.273
, pp. 2926-2930
-
-
Muzio, M.1
Stockwell, B.R.2
Stennicke, H.R.3
Salvesen, G.S.4
Dixit, V.M.5
-
11
-
-
0032143986
-
Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally
-
Caspase-8 deficient mice show abnormal heart development and hyperemia. EF cells are resistant to apoptosis mediated by death receptors but are sensitive to cytotoxic drugs.
-
Varfolomeev E.E., Schuchmann M., Luria V., Chiannilkulchai N., Beckmann J.S., Mett I.L., Rebrikov D., Brodianski V.M., Kemper O.C., Kollet O.et al. Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity. 9:1998;267-276. Caspase-8 deficient mice show abnormal heart development and hyperemia. EF cells are resistant to apoptosis mediated by death receptors but are sensitive to cytotoxic drugs.
-
(1998)
Immunity
, vol.9
, pp. 267-276
-
-
Varfolomeev, E.E.1
Schuchmann, M.2
Luria, V.3
Chiannilkulchai, N.4
Beckmann, J.S.5
Mett, I.L.6
Rebrikov, D.7
Brodianski, V.M.8
Kemper, O.C.9
Kollet, O.10
-
13
-
-
7144263731
-
FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
-
•].
-
•].
-
(1998)
Science
, vol.279
, pp. 1954-1958
-
-
Yeh, W.C.1
Pompa, J.L.2
McCurrach, M.E.3
Shu, H.B.4
Elia, A.J.5
Shahinian, A.6
Ng, M.7
Wakeham, A.8
Khoo, W.9
Mitchell, K.10
El-Deiry, W.S.11
-
14
-
-
0032493910
-
Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
-
•].
-
•].
-
(1998)
Cell
, vol.94
, pp. 325-337
-
-
Kuida, K.1
Haydar, T.F.2
Kuan, C.3
Gu, Y.4
Taya, C.5
Karasuyama, H.6
Su, M.S.7
Rakic, P.8
Flavell, R.A.9
-
15
-
-
0029956641
-
Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
-
Kuida K., Zheng T.S., Na S., Kuan C., Yang D., Karasuyama H., Rakic P., Flavell R.A. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature. 384:1996;368-372.
-
(1996)
Nature
, vol.384
, pp. 368-372
-
-
Kuida, K.1
Zheng, T.S.2
Na, S.3
Kuan, C.4
Yang, D.5
Karasuyama, H.6
Rakic, P.7
Flavell, R.A.8
-
16
-
-
15644364847
-
Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
-
Caspase-3 deficient mice have abnormal brain development. Cells are resistant to apoptosis induced by a variety of stimuli including death receptors, cytotoxic drugs. Dying cells show defects in chromatin condensation and DNA fragmentation.
-
Woo M., Hakem R., Soengas M.S., Duncan G.S., Shahinian A., Kagi D., Hakem A., McCurrach M., Khoo W., Kaufman S.A.et al. Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev. 12:1998;806-819. Caspase-3 deficient mice have abnormal brain development. Cells are resistant to apoptosis induced by a variety of stimuli including death receptors, cytotoxic drugs. Dying cells show defects in chromatin condensation and DNA fragmentation.
-
(1998)
Genes Dev
, vol.12
, pp. 806-819
-
-
Woo, M.1
Hakem, R.2
Soengas, M.S.3
Duncan, G.S.4
Shahinian, A.5
Kagi, D.6
Hakem, A.7
McCurrach, M.8
Khoo, W.9
Kaufman, S.A.10
-
17
-
-
0032493870
-
Differential requirement for caspase 9 in apoptotic pathways in vivo
-
•].
-
•].
-
(1998)
Cell
, vol.94
, pp. 339-352
-
-
Hakem, R.1
Hakem, A.2
Duncan, G.S.3
Henderson, J.T.4
Woo, M.5
Soengas, M.S.6
Elia, A.7
De La Pompa, J.L.8
Kagi, D.9
Khoo, W.10
-
18
-
-
0032544564
-
Apaf1 is required for mitochondrial pathways of apoptosis and brain development
-
•].
-
•].
-
(1998)
Cell
, vol.94
, pp. 739-750
-
-
Yoshida, H.1
Kong, Y.2
Yoshida, R.3
Elia, A.J.4
Hakem, A.5
Hakem, R.6
Penninger, J.M.7
Mak, T.W.8
-
20
-
-
0032524885
-
The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9
-
The author identified the C. elegans protein EGL-1 as a BH3-domain-containing protein, and demonstrated that EGL-1 is a component of general cell death machinery.
-
Conradt B., Horvitz H.R. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell. 93:1998;519-529. The author identified the C. elegans protein EGL-1 as a BH3-domain-containing protein, and demonstrated that EGL-1 is a component of general cell death machinery.
-
(1998)
Cell
, vol.93
, pp. 519-529
-
-
Conradt, B.1
Horvitz, H.R.2
-
21
-
-
0032555697
-
Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
-
••] identified BID, a pro-apoptotic Bcl-2 member, as a proximal substrate of caspase-8 and a mediator of mitochondrial damage in Fas death pathway.
-
••] identified BID, a pro-apoptotic Bcl-2 member, as a proximal substrate of caspase-8 and a mediator of mitochondrial damage in Fas death pathway.
-
(1998)
Cell
, vol.94
, pp. 491-501
-
-
Li, H.1
Zhu, H.2
Xu, C.3
Yuan, J.4
-
22
-
-
0029807585
-
BID: A novel BH3 domain-only death agonist
-
Wang K., Yin X-M., Chao D.T., Milliman C.L., Korsmeyer S.J. BID: a novel BH3 domain-only death agonist. Genes Dev. 10:1996;2859-2869.
-
(1996)
Genes Dev
, vol.10
, pp. 2859-2869
-
-
Wang, K.1
Yin, X.-M.2
Chao, D.T.3
Milliman, C.L.4
Korsmeyer, S.J.5
-
24
-
-
0030854775
-
Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death
-
Imaizumi K., Tsuda M., Imai Y., Wanaka A., Takagi T., Tohyyama M. Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death. J Biol Chem. 272:1997;18842-18848.
-
(1997)
J Biol Chem
, vol.272
, pp. 18842-18848
-
-
Imaizumi, K.1
Tsuda, M.2
Imai, Y.3
Wanaka, A.4
Takagi, T.5
Tohyyama, M.6
-
25
-
-
0032519859
-
Bax involvement in p53-mediated neuronal cell death
-
Xiang H., Kinoshita Y., Knudson C.M., Korsmeyer S.J., Schwartzkroin P.A., Morrison R.S. Bax involvement in p53-mediated neuronal cell death. J Neurosci. 18:1998;1363-1373.
-
(1998)
J Neurosci
, vol.18
, pp. 1363-1373
-
-
Xiang, H.1
Kinoshita, Y.2
Knudson, C.M.3
Korsmeyer, S.J.4
Schwartzkroin, P.A.5
Morrison, R.S.6
-
27
-
-
0030702123
-
Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
-
••] identified the death agonist BAD as a substrate of protein kinase Akt. The findings defined a mechanism by which growth factors directly inactivate a component of cell death machinery.
-
••] identified the death agonist BAD as a substrate of protein kinase Akt. The findings defined a mechanism by which growth factors directly inactivate a component of cell death machinery.
-
(1997)
Cell
, vol.91
, pp. 231-241
-
-
Datta, S.R.1
Dudek, H.2
Tao, X.3
Masters, S.4
Fu, H.5
Gotoh, Y.6
Greenberg, M.E.7
-
29
-
-
0030780106
-
Movement of Bax from the cytosol to mitochondria during apoptosis
-
Wolter K.G., Hsu Y., Smith C.L., Nechushtan A., Xi X., Youle R.J. Movement of Bax from the cytosol to mitochondria during apoptosis. J Cell Biol. 139:1997;1281-1292.
-
(1997)
J Cell Biol
, vol.139
, pp. 1281-1292
-
-
Wolter, K.G.1
Hsu, Y.2
Smith, C.L.3
Nechushtan, A.4
Xi, X.5
Youle, R.J.6
-
30
-
-
0028832667
-
A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions
-
Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J., Elangovan B., Chinnadurai G., Lutz R.J. A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. EMBO J. 14:1995;5589-5596.
-
(1995)
EMBO J
, vol.14
, pp. 5589-5596
-
-
Chittenden, T.1
Flemington, C.2
Houghton, A.B.3
Ebb, R.G.4
Gallo, G.J.5
Elangovan, B.6
Chinnadurai, G.7
Lutz, R.J.8
-
31
-
-
0030861571
-
Bcl-2 and Bax function independently to regulate cell death
-
The authors provide genetic evidence that Bax may function independently of Bcl-2.
-
Knudson C.M., Korsmeyer S.J. Bcl-2 and Bax function independently to regulate cell death. Nat Genet. 16:1997;358-363. The authors provide genetic evidence that Bax may function independently of Bcl-2.
-
(1997)
Nat Genet
, vol.16
, pp. 358-363
-
-
Knudson, C.M.1
Korsmeyer, S.J.2
-
32
-
-
0032566649
-
Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis
-
Marzo I., Brenner C., Zamzami N., Jurgensmeier J.M., Susin S.A., Vieira H.L.A., Prevost M.C., Xie Z., Matsuyama S., Reed J.C., Kroemer G. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science. 281:1998;2027-2031.
-
(1998)
Science
, vol.281
, pp. 2027-2031
-
-
Marzo, I.1
Brenner, C.2
Zamzami, N.3
Jurgensmeier, J.M.4
Susin, S.A.5
Vieira, H.L.A.6
Prevost, M.C.7
Xie, Z.8
Matsuyama, S.9
Reed, J.C.10
Kroemer, G.11
-
33
-
-
0032080197
-
Defects in regulation of apoptosis in caspase 2-deficient mice
-
Caspase-2 knockout mice have excess oocytes and defects in certain kinds of apoptosis.
-
Bergeron L., Perez G.I., Macdonald G., Shi L., Sun Y., Jurisicova A., Varmuza S., Latham K.E., Flaws J.A., Salter J.C.et al. Defects in regulation of apoptosis in caspase 2-deficient mice. Genes Dev. 12:1998;1304-1314. Caspase-2 knockout mice have excess oocytes and defects in certain kinds of apoptosis.
-
(1998)
Genes Dev
, vol.12
, pp. 1304-1314
-
-
Bergeron, L.1
Perez, G.I.2
Macdonald, G.3
Shi, L.4
Sun, Y.5
Jurisicova, A.6
Varmuza, S.7
Latham, K.E.8
Flaws, J.A.9
Salter, J.C.10
-
34
-
-
0027166048
-
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
-
Oltvai Z.N., Milliman C.L., Korsmeyer S.J. 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
-
35
-
-
0028946015
-
Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K
-
Farrow S.N., White J.H., Martinou I., Raven T., Pun K.T., Grinham C.J., 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.2
Martinou, I.3
Raven, T.4
Pun, K.T.5
Grinham, C.J.6
Martinou, J.C.7
Brown, R.8
-
36
-
-
0028986876
-
Induction of apoptosis by the Bcl-2 homologue Bak
-
Chittenden T., Harrington E.A., O'Connor R., Flemington C., Lutz R.J., Evan G.I., Guild B.C. 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
-
37
-
-
0028904163
-
Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak
-
Kiefer M.C., Brauer M.J., Powers V.C., Wu J.J., Umansky S.R., Tomei L.D., Barr P.J. 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
-
38
-
-
0001003612
-
Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members
-
Hsu S.Y., Kaipia A., McGee E., Lomeli M., Hsueh A.J. Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proc Natl Acad Sci USA. 94:1997;12401-12406.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 12401-12406
-
-
Hsu, S.Y.1
Kaipia, A.2
McGee, E.3
Lomeli, M.4
Hsueh, A.J.5
-
39
-
-
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
-
40
-
-
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 J.M., Gallo G.J., Elangovan B., Houghton A.B., Malstrom S., Avery B.J., Ebb R.G., Subramanian T., Chittenden T., Lutz R.J.et al. 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
-
41
-
-
0029790857
-
Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K
-
Han J., Sabbatini P., White E. Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K. Mol Cell Biol. 16:1996;5857-5864.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 5857-5864
-
-
Han, J.1
Sabbatini, P.2
White, E.3
-
44
-
-
0032518787
-
Bim, a novel member of the Bcl-2 family that promotes apoptosis
-
O'Connor L., Strasser A., O'Reilly L.A., Hausmann G., Adams J.M., Cory S., Huang D.C. Bim, a novel member of the Bcl-2 family that promotes apoptosis. EMBO J. 17:1998;384-395.
-
(1998)
EMBO J
, vol.17
, pp. 384-395
-
-
O'Connor, L.1
Strasser, A.2
O'Reilly, L.A.3
Hausmann, G.4
Adams, J.M.5
Cory, S.6
Huang, D.C.7
-
45
-
-
0032161337
-
BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members
-
Hsu S.Y., Lin P., Hsueh A.J. BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. Mol Endocrinol. 12:1998;1432-1440.
-
(1998)
Mol Endocrinol
, vol.12
, pp. 1432-1440
-
-
Hsu, S.Y.1
Lin, P.2
Hsueh, A.J.3
-
46
-
-
0031455410
-
The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis
-
Chen G., Ray R., Dubik D., Shi L., Cizeau J., Bleackley R.C., Saxena S., Gietz R.D., Greenberg A.H. The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis. J Exp Med. 186:1997;1975-1983.
-
(1997)
J Exp Med
, vol.186
, pp. 1975-1983
-
-
Chen, G.1
Ray, R.2
Dubik, D.3
Shi, L.4
Cizeau, J.5
Bleackley, R.C.6
Saxena, S.7
Gietz, R.D.8
Greenberg, A.H.9
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