-
1
-
-
13344285339
-
Identification and characterization of a new member of the TNF family that induces apoptosis
-
Wiley SR, Schooley K, Smolak PJ, Din WS, Huang CP, Nicholl JK, Sutherland GR, Smith TD, Rauch C, Smith CA, Goodwin RG. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity. 3:1995;673-682.
-
(1995)
Immunity
, vol.3
, pp. 673-682
-
-
Wiley, S.R.1
Schooley, K.2
Smolak, P.J.3
Din, W.S.4
Huang, C.P.5
Nicholl, J.K.6
Sutherland, G.R.7
Smith, T.D.8
Rauch, C.9
Smith, C.A.10
Goodwin, R.G.11
-
2
-
-
17544367410
-
Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
-
Pitti RM, Marsters SA, Ruppert S, Donahue CJ, Moore A, Ashkenazi A. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J Biol Chem. 271:1996;12687-12690.
-
(1996)
J Biol Chem
, vol.271
, pp. 12687-12690
-
-
Pitti, R.M.1
Marsters, S.A.2
Ruppert, S.3
Donahue, C.J.4
Moore, A.5
Ashkenazi, A.6
-
3
-
-
0029969717
-
A death-domain-containing receptor that mediates apoptosis
-
Kitson J, Raven T, Jiang YP, Goeddel DV, Giles KM, Pun KT, Grinham CJ, Brown R, Farrow SN. A death-domain-containing receptor that mediates apoptosis. Nature. 384:1996;372-375.
-
(1996)
Nature
, vol.384
, pp. 372-375
-
-
Kitson, J.1
Raven, T.2
Jiang, Y.P.3
Goeddel, D.V.4
Giles, K.M.5
Pun, K.T.6
Grinham, C.J.7
Brown, R.8
Farrow, S.N.9
-
4
-
-
0030466894
-
Apo-3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-κB
-
Marsters SA, Sheridan JP, Donahue CJ, Pitti RM, Gray CL, Goddard AD, Bauer KD, Ashkenazi A. Apo-3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-κB. Curr Biol. 6:1996;1669-1676.
-
(1996)
Curr Biol
, vol.6
, pp. 1669-1676
-
-
Marsters, S.A.1
Sheridan, J.P.2
Donahue, C.J.3
Pitti, R.M.4
Gray, C.L.5
Goddard, A.D.6
Bauer, K.D.7
Ashkenazi, A.8
-
5
-
-
0030896087
-
TRAMP, a novel apoptosis-mediating receptor with sequence homology to tumor necrosis factor receptor 1 and fas (apo-1/CD95)
-
Bodmer J-L, Burns K, Schneider P, Hofmann K, Steiner V, Thome M, Bornand T, Hahne M, Schroter M, Becker K, et al. TRAMP, a novel apoptosis-mediating receptor with sequence homology to tumor necrosis factor receptor 1 and fas (apo-1/CD95). Immunity. 6:1997;79-88.
-
(1997)
Immunity
, vol.6
, pp. 79-88
-
-
Bodmer, J.-L.1
Burns, K.2
Schneider, P.3
Hofmann, K.4
Steiner, V.5
Thome, M.6
Bornand, T.7
Hahne, M.8
Schroter, M.9
Becker, K.10
-
6
-
-
0030892234
-
Apoptosis by death factor
-
Nagata S. Apoptosis by death factor. Cell. 88:1997;355-365.
-
(1997)
Cell
, vol.88
, pp. 355-365
-
-
Nagata, S.1
-
7
-
-
0030987071
-
Transducing signals of life and death
-
Yuan J. Transducing signals of life and death. Curr Opin Cell Biol. 9:1997;247-251.
-
(1997)
Curr Opin Cell Biol
, vol.9
, pp. 247-251
-
-
Yuan, J.1
-
8
-
-
0028927607
-
The Fas death factor
-
Nagata S, Golstein P. The Fas death factor. Science. 267:1995;1449-1456.
-
(1995)
Science
, vol.267
, pp. 1449-1456
-
-
Nagata, S.1
Golstein, P.2
-
9
-
-
0028864778
-
A role for CD95 ligand in preventing graft rejection
-
Bellgrau D, Gold D, Selawry H, Moore J, Franzusoff A, Duke RC. A role for CD95 ligand in preventing graft rejection. Nature. 377:1995;630-632.
-
(1995)
Nature
, vol.377
, pp. 630-632
-
-
Bellgrau, D.1
Gold, D.2
Selawry, H.3
Moore, J.4
Franzusoff, A.5
Duke, R.C.6
-
10
-
-
0028879109
-
Fas ligand-induced apoptosis as a mechanism of immune privilege
-
Griffith TS, Brunner T, Fletcher SM, Green DR, Ferguson TA. Fas ligand-induced apoptosis as a mechanism of immune privilege. Science. 270:1995;1189-1192.
-
(1995)
Science
, vol.270
, pp. 1189-1192
-
-
Griffith, T.S.1
Brunner, T.2
Fletcher, S.M.3
Green, D.R.4
Ferguson, T.A.5
-
11
-
-
0030298294
-
Dissection of TNF receptor 1 effector function: JNK activation is not linked to apoptosis while NFκB activation prevents cell death
-
Liu C-Z, Hsu H, Goeddel DV. Dissection of TNF receptor 1 effector function: JNK activation is not linked to apoptosis while NFκB activation prevents cell death. Cell. 87:1996;565-576.
-
(1996)
Cell
, vol.87
, pp. 565-576
-
-
Liu, C.-Z.1
Hsu, H.2
Goeddel, D.V.3
-
12
-
-
0029992609
-
Suppression of TNF-α-induced apoptosis by NF-κB
-
of special interest. Similar methods to those used by Wang [13] were used to show that NF-κB activation is part of the anti-apoptotic response employed by TNFα-stimulated cells.
-
Van Antwerp DJ, Martin SJ, Kafri T, Green DR, Verma IM. Suppression of TNF-α-induced apoptosis by NF-κB. of special interest Science. 274:1996;787-789 Similar methods to those used by Wang [13] were used to show that NF-κB activation is part of the anti-apoptotic response employed by TNFα-stimulated cells.
-
(1996)
Science
, vol.274
, pp. 787-789
-
-
Van Antwerp, D.J.1
Martin, S.J.2
Kafri, T.3
Green, D.R.4
Verma, I.M.5
-
13
-
-
0029858387
-
TNF- And cancer therapy-induced apoptosis potentiation by inhibitor of NF-κB
-
of outstanding interest. A superpotent form of IκB, the inhibition of NF-κB, was overexpressed in a tumour cell line to block NF-κB function and demonstrate that it is required for protection from apoptosis mediated by TNF-α. The chemotherapeutic drug daunorubicin and ionizing radiation - but not the drug staurosporine - induce NF-κB as part of a stress response resulting in reduced tumor cell death. By blocking NF-κB, the superpotent form IκB enhanced the apoptotic response to radiation and daunorubicin. The authors suggest that this mechanism may be exploited by tumors to evade cancer treatment and suggest that NF-κB inhibitors may augment radiation and chemotherapy.
-
Wang C-Y, Mayo MW, Baldwin AS Jr. TNF- and cancer therapy-induced apoptosis potentiation by inhibitor of NF-κB. of outstanding interest Science. 274:1996;784-787 A superpotent form of IκB, the inhibition of NF-κB, was overexpressed in a tumour cell line to block NF-κB function and demonstrate that it is required for protection from apoptosis mediated by TNF-α. The chemotherapeutic drug daunorubicin and ionizing radiation - but not the drug staurosporine - induce NF-κB as part of a stress response resulting in reduced tumor cell death. By blocking NF-κB, the superpotent form IκB enhanced the apoptotic response to radiation and daunorubicin. The authors suggest that this mechanism may be exploited by tumors to evade cancer treatment and suggest that NF-κB inhibitors may augment radiation and chemotherapy.
-
(1996)
Science
, vol.274
, pp. 784-787
-
-
Wang, C.-Y.1
Mayo, M.W.2
Baldwin A.S., Jr.3
-
14
-
-
0029976817
-
An essential role for NF-κB in preventing TNF-α-induced cell death
-
of special interest. Using RelA null mouse fibroblasts, which lack NF-κB function, it was shown that TNF-α treatment results in apoptosis mediated by the TNF receptor 1. Cell death was blocked in null fibroblasts transfected with a RelA expression vector, implicating NF-κB activity in the protection of TNF-α-treated cells from apoptosis.
-
Beg AA, Baldwin AS. An essential role for NF-κB in preventing TNF-α-induced cell death. of special interest Science. 274:1996;782-784 Using RelA null mouse fibroblasts, which lack NF-κB function, it was shown that TNF-α treatment results in apoptosis mediated by the TNF receptor 1. Cell death was blocked in null fibroblasts transfected with a RelA expression vector, implicating NF-κB activity in the protection of TNF-α-treated cells from apoptosis.
-
(1996)
Science
, vol.274
, pp. 782-784
-
-
Beg, A.A.1
Baldwin, A.S.2
-
15
-
-
0029664296
-
ICE family proteases: Mediators of all apoptotic cell death?
-
Henkart PA. ICE family proteases: mediators of all apoptotic cell death? Immunity. 4:1996;195-201.
-
(1996)
Immunity
, vol.4
, pp. 195-201
-
-
Henkart, P.A.1
-
17
-
-
0031048545
-
Bcl-2 and the ICE family of apoptotic regulators: Making a connection
-
Rao L, White E. Bcl-2 and the ICE family of apoptotic regulators: making a connection. Curr Opin Genet Dev. 7:1997;52-58.
-
(1997)
Curr Opin Genet Dev
, vol.7
, pp. 52-58
-
-
Rao, L.1
White, E.2
-
18
-
-
0009530192
-
Human ICE/CED-3 protease nomenclature
-
Alnemri ES, Livingston DJ, Nicholson DW, Salvesen G, Thornberry NA, Wong WW, Yuan J. Human ICE/CED-3 protease nomenclature. Cell. 87:1996;171.
-
(1996)
Cell
, vol.87
, pp. 171
-
-
Alnemri, E.S.1
Livingston, D.J.2
Nicholson, D.W.3
Salvesen, G.4
Thornberry, N.A.5
Wong, W.W.6
Yuan, J.7
-
19
-
-
0029758833
-
Cleavage of lamin A by Mch2α but not CPP32: Multiple ICE-related proteases with distinct substrate recognition properties are active in apoptosis
-
Takahashi A, Alnemri ES, Lazebnik YA, Fernandes-Alnemri T, Litwack G, Moir RD, Goldman RD, Poirier GG, Kaufmann SH, Earnshaw WC. Cleavage of lamin A by Mch2α but not CPP32: multiple ICE-related proteases with distinct substrate recognition properties are active in apoptosis. Proc Natl Acad Sci USA. 93:1996;8395-8400.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 8395-8400
-
-
Takahashi, A.1
Alnemri, E.S.2
Lazebnik, Y.A.3
Fernandes-Alnemri, T.4
Litwack, G.5
Moir, R.D.6
Goldman, R.D.7
Poirier, G.G.8
Kaufmann, S.H.9
Earnshaw, W.C.10
-
20
-
-
0029956641
-
Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
-
Kuida K, Zheng TS, NA S-Q, Kuan C-Y, Yang D, Karasuyama H, Rakic P, Flavell RA. 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.-Q.3
Kuan, C.-Y.4
Yang, D.5
Karasuyama, H.6
Rakic, P.7
Flavell, R.A.8
-
21
-
-
0028920863
-
Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme
-
Kuida K, Lippke JA, Ku G, Harding MW, Livingston DJ, Su MS-S, Flavell RA. Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science. 267:1995;2000-2002.
-
(1995)
Science
, vol.267
, pp. 2000-2002
-
-
Kuida, K.1
Lippke, J.A.2
Ku, G.3
Harding, M.W.4
Livingston, D.J.5
Su, M.-S.6
Flavell, R.A.7
-
22
-
-
0028984948
-
Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock
-
Li P, Allen H, Banerjee S, Franklin S, Herzog L, Johnston C, McDowell J, Paskind M, Rodman L, Salfeld J, et al. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell. 80:1995;401-411.
-
(1995)
Cell
, vol.80
, pp. 401-411
-
-
Li, P.1
Allen, H.2
Banerjee, S.3
Franklin, S.4
Herzog, L.5
Johnston, C.6
McDowell, J.7
Paskind, M.8
Rodman, L.9
Salfeld, J.10
-
23
-
-
8944230656
-
Fas-induced activation of the cell death related protease CPP32 is inhibited by ICE family protease inhibitors and by Bcl-2
-
of special interest. Fas-induced apoptosis in Jurkat cells and caspase 3 activation were inhibited by Bcl-2 overexpression as well as with the caspase inhibitor ZVAD-FMK. Thus, Bcl-2 functions either at or upstream of the caspase 3 activation step in Fas-mediated apoptosis.
-
Armstrong RC, Aja T, Xiang J, Gaur S, Krebs J, Hoang K, Bai X, Korsmeyer SJ, Karanewsky DS, Fritz LC, et al. Fas-induced activation of the cell death related protease CPP32 is inhibited by ICE family protease inhibitors and by Bcl-2. of special interest J Biol Chem. 271:1996;16850-16855 Fas-induced apoptosis in Jurkat cells and caspase 3 activation were inhibited by Bcl-2 overexpression as well as with the caspase inhibitor ZVAD-FMK. Thus, Bcl-2 functions either at or upstream of the caspase 3 activation step in Fas-mediated apoptosis.
-
(1996)
J Biol Chem
, vol.271
, pp. 16850-16855
-
-
Armstrong, R.C.1
Aja, T.2
Xiang, J.3
Gaur, S.4
Krebs, J.5
Hoang, K.6
Bai, X.7
Korsmeyer, S.J.8
Karanewsky, D.S.9
Fritz, L.C.10
-
24
-
-
0029912189
-
Molecular ordering of the cell death pathway: Bcl-2 and Bcl-xL function upstream of the CED-3-like apoptotic proteases
-
L were not able to block caspase activation and cell death mediated by the Fas pathway. Although the reasons for this discrepancy are not clear, CrmA was shown to block Fas-induced cell death. The authors speculate that the activation of caspases by different apoptotic stimuli may be controlled by several distinct mechanisms.
-
L were not able to block caspase activation and cell death mediated by the Fas pathway. Although the reasons for this discrepancy are not clear, CrmA was shown to block Fas-induced cell death. The authors speculate that the activation of caspases by different apoptotic stimuli may be controlled by several distinct mechanisms.
-
(1996)
J Biol Chem
, vol.271
, pp. 4573-4576
-
-
Chinnaiyan, A.M.1
Orth, K.2
O'Rourke, K.3
Duan, H.4
Poirer, G.G.5
Dixit, V.M.6
-
25
-
-
0029884711
-
Bcl-2 blocks loss of mitochondrial membrane potential which ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors
-
Shimizu S, Eguchi Y, Kamiike W, Waguri S, Uchiyama Y, Matsuda H, Tsujimoto Y. Bcl-2 blocks loss of mitochondrial membrane potential which ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors. Oncogene. 13:1996;21-29.
-
(1996)
Oncogene
, vol.13
, pp. 21-29
-
-
Shimizu, S.1
Eguchi, Y.2
Kamiike, W.3
Waguri, S.4
Uchiyama, Y.5
Matsuda, H.6
Tsujimoto, Y.7
-
26
-
-
0029906828
-
BAX-induced cell death may not require interleukin 1β-converting enzyme-like proteases
-
of special interest. Overexpression of BAX-induced changes in mitochondrial membrane potential and apoptosis, neither of which were blocked by caspase inhibitors - although DNA fragmentation and cleavage of caspase targets were blocked. These data suggest that Bcl-2 family members are upstream of the caspases and that the known caspases may not be absolutely required for Bax-induced cell death.
-
Xiang J, Chao DT, Korsmeyer SJ. BAX-induced cell death may not require interleukin 1β-converting enzyme-like proteases. of special interest Proc Natl Acad Sci USA. 93:1996;14559-14563 Overexpression of BAX-induced changes in mitochondrial membrane potential and apoptosis, neither of which were blocked by caspase inhibitors - although DNA fragmentation and cleavage of caspase targets were blocked. These data suggest that Bcl-2 family members are upstream of the caspases and that the known caspases may not be absolutely required for Bax-induced cell death.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 14559-14563
-
-
Xiang, J.1
Chao, D.T.2
Korsmeyer, S.J.3
-
27
-
-
0031033274
-
Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak
-
of special interest. Caspase inhibitors could not delay the onset of apoptosis in response to death signals, although the completion of the apoptotic program was delayed. Conversely, the apoptosis inhibitor Bcl-2 and the growth factor IGF-1 delay apoptosis but have no effect on the kinetics of the downstream apoptotic program once it is initiated. Thus, the Bcl-2 family is probably involved in the commitment of the cell to apoptosis, with the caspases being effectors of this process.
-
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. of special interest J Cell Biol. 136:1997;215-227 Caspase inhibitors could not delay the onset of apoptosis in response to death signals, although the completion of the apoptotic program was delayed. Conversely, the apoptosis inhibitor Bcl-2 and the growth factor IGF-1 delay apoptosis but have no effect on the kinetics of the downstream apoptotic program once it is initiated. Thus, the Bcl-2 family is probably involved in the commitment of the cell to apoptosis, with the caspases being effectors of this process.
-
(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
-
28
-
-
0029899181
-
Molecular thanatopsis: A discourse on the BCL2 family and cell death
-
Yang E, Korsmeyer SJ. Molecular thanatopsis: a discourse on the BCL2 family and cell death. Blood. 88:1996;386-401.
-
(1996)
Blood
, vol.88
, pp. 386-401
-
-
Yang, E.1
Korsmeyer, S.J.2
-
29
-
-
0027427492
-
Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair
-
Veis DJ, Sorenson CM, Shutter JR, Korsmeyer SJ. Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell. 75:1993;229-240.
-
(1993)
Cell
, vol.75
, pp. 229-240
-
-
Veis, D.J.1
Sorenson, C.M.2
Shutter, J.R.3
Korsmeyer, S.J.4
-
30
-
-
0028175759
-
Targeted disruption of Bcl-2αβ in mice: Occurrence of gray hair, polycystic kidney disease, and lymphocytopenia
-
Nakayama K, Nakayama K-I, Negishi I, Kuida K, Sawa H, Loh DY. Targeted disruption of Bcl-2αβ in mice: occurrence of gray hair, polycystic kidney disease, and lymphocytopenia. Proc Natl Acad Sci USA. 91:1994;3700-3704.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 3700-3704
-
-
Nakayama, K.1
Nakayama, K.-I.2
Negishi, I.3
Kuida, K.4
Sawa, H.5
Loh, D.Y.6
-
31
-
-
0028859541
-
Bax-deficient mice with lymphoid hyperplasia and male germ cell death
-
Knudson CM, Tung KSK, Tourtellote WG, Brown GAJ, Korsmeyer SJ. Bax-deficient mice with lymphoid hyperplasia and male germ cell death. Science. 270:1995;96-99.
-
(1995)
Science
, vol.270
, pp. 96-99
-
-
Knudson, C.M.1
Tung, K.S.K.2
Tourtellote, W.G.3
Brown, G.A.J.4
Korsmeyer, S.J.5
-
32
-
-
0030245811
-
BAX is required for neuronal death after trophic factor deprivation and during development
-
of special interest. Deletion of the cell-death agonist Bax resulted in reduced sensitivity of neonatal sympathetic and facial motor neurons to factor deprivation induced apoptosis. Furthermore, an increased number of neurons in the superior cervical ganglia and facial nuclei were observed implicating Bax as the major Bcl-2 family member involved in trophic factor deprivation induced neuronal cell death.
-
Deckwerth TL, Elliott JL, Knudson CM, Johnson EM Jr, Snider WD, Korsmeyer SJ. BAX is required for neuronal death after trophic factor deprivation and during development. of special interest Neuron. 17:1996;401-411 Deletion of the cell-death agonist Bax resulted in reduced sensitivity of neonatal sympathetic and facial motor neurons to factor deprivation induced apoptosis. Furthermore, an increased number of neurons in the superior cervical ganglia and facial nuclei were observed implicating Bax as the major Bcl-2 family member involved in trophic factor deprivation induced neuronal cell death.
-
(1996)
Neuron
, vol.17
, pp. 401-411
-
-
Deckwerth, T.L.1
Elliott, J.L.2
Knudson, C.M.3
Johnson E.M., Jr.4
Snider, W.D.5
Korsmeyer, S.J.6
-
33
-
-
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
-
34
-
-
0028206341
-
BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax
-
Yin X-M, Oltvai ZN, Korsmeyer SJ. BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature. 369:1994;321-323.
-
(1994)
Nature
, vol.369
, pp. 321-323
-
-
Yin, X.-M.1
Oltvai, Z.N.2
Korsmeyer, S.J.3
-
35
-
-
0028017880
-
Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system
-
Sato T, Hanada M, Bodrug S, Irie S, Iwama N, Boise LH, Thompson CB, Golemis E, Fong L, Wang H-G, Reed JC. Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system. Proc Natl Acad Sci USA. 91:1994;9238-9242.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 9238-9242
-
-
Sato, T.1
Hanada, M.2
Bodrug, S.3
Irie, S.4
Iwama, N.5
Boise, L.H.6
Thompson, C.B.7
Golemis, E.8
Fong, L.9
Wang, H.-G.10
Reed, J.C.11
-
36
-
-
0029097470
-
Multiple Bcl-2 family members demonstrate selective dimerizations with Bax
-
Sedlak TW, Oltvai ZN, Yang E, Wang K, Boise LH, Thompson CB, Korsmeyer SJ. Multiple Bcl-2 family members demonstrate selective dimerizations with Bax. Proc Natl Acad Sci USA. 92:1995;7834-7838.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 7834-7838
-
-
Sedlak, T.W.1
Oltvai, Z.N.2
Yang, E.3
Wang, K.4
Boise, L.H.5
Thompson, C.B.6
Korsmeyer, S.J.7
-
37
-
-
0030584079
-
Apoptosis meets signal transduction: Elimination of a BAD influence
-
Gajewski TF, Thompson CB. Apoptosis meets signal transduction: elimination of a BAD influence. Cell. 87:1996;589-592.
-
(1996)
Cell
, vol.87
, pp. 589-592
-
-
Gajewski, T.F.1
Thompson, C.B.2
-
38
-
-
0030584088
-
L
-
L and antagonize its function. The phosphorylation status of Bad was dependent on the presence of IL-3.
-
L and antagonize its function. The phosphorylation status of Bad was dependent on the presence of IL-3.
-
(1996)
Cell
, vol.87
, pp. 619-628
-
-
Zha, J.1
Harada, H.2
Yang, E.3
Jockel, J.4
Korsmeyer, S.J.5
-
39
-
-
5244224827
-
L, an inhibitor of programmed cell death
-
L. Domains of the protein previously shown to be involved in protein - protein interactions were shown to form a hydrophobic pocket. Additionally, the molecule shows structural homology with the pore-forming proteins colicin and dipthenia toxin.
-
L. Domains of the protein previously shown to be involved in protein - protein interactions were shown to form a hydrophobic pocket. Additionally, the molecule shows structural homology with the pore-forming proteins colicin and dipthenia toxin.
-
(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.-L.10
-
40
-
-
0028832667
-
A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions
-
Chittenden T, Flemington C, Houghton AB, Ebb RG, Gallo GJ, Elangovan B, Chinnadurai G, Lutz RJ. 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
-
41
-
-
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, Chinnandurai 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
Chinnandurai, G.11
-
42
-
-
0029917541
-
Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
-
Zha H, Aime-Sempe C, Sato T, Reed JC. Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem. 271:1996;7440-7444.
-
(1996)
J Biol Chem
, vol.271
, pp. 7440-7444
-
-
Zha, H.1
Aime-Sempe, C.2
Sato, T.3
Reed, J.C.4
-
43
-
-
0029928885
-
A peptide sequence from Bax that converts Bcl-2 into an activator of apoptosis
-
Hunter JJ, Parslow TG. A peptide sequence from Bax that converts Bcl-2 into an activator of apoptosis. J Biol Chem. 271:1996;8521-8524.
-
(1996)
J Biol Chem
, vol.271
, pp. 8521-8524
-
-
Hunter, J.J.1
Parslow, T.G.2
-
44
-
-
0030614915
-
L-Bak peptide complex: Recognition between regulators of apoptosis
-
L-Bak peptide complex: recognition between regulators of apoptosis. Science. 275:1997;983-986.
-
(1997)
Science
, vol.275
, pp. 983-986
-
-
Sattler, M.1
Liang, H.2
Nettesheim, D.3
Meadows, R.P.4
Harlan, J.E.5
Eberstadt, M.6
Yoon, H.S.7
Shuker, S.B.8
Chang, B.S.9
Minn, A.J.10
-
45
-
-
1842332735
-
L forms an ion channel in synthetic lipid membranes
-
L was homologous to the bacterial pore-forming proteins colicin and diptheria toxin.
-
L was homologous to the bacterial pore-forming proteins colicin and diptheria toxin.
-
(1997)
Nature
, vol.385
, pp. 353-357
-
-
Minn, A.J.1
Velez, P.2
Schendel, S.L.3
Liang, H.4
Muchmore, S.W.5
Fesik, S.W.6
Fill, M.7
Thompson, C.B.8
-
46
-
-
0031008397
-
Channel formation by antiapoptotic protein Bcl-2
-
Schendel SL, Xie Z, Montal MO, Matsuyama S, Montal M, Reed JC. Channel formation by antiapoptotic protein Bcl-2. Proc Natl Acad Sci USA. 94:1977;5113-5118.
-
(1977)
Proc Natl Acad Sci USA
, vol.94
, pp. 5113-5118
-
-
Schendel, S.L.1
Xie, Z.2
Montal, M.O.3
Matsuyama, S.4
Montal, M.5
Reed, J.C.6
-
47
-
-
0028046038
-
Commitment to apoptosis is associated with changes in mitochondrial biogenesis and activity in cell lines conditionally immortalized with simian virus 40
-
Vassiere J-L, Petit P, Risler Y, Mignotte B. Commitment to apoptosis is associated with changes in mitochondrial biogenesis and activity in cell lines conditionally immortalized with simian virus 40. Proc Natl Acad Sci USA. 91:1994;11752-11756.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 11752-11756
-
-
Vassiere, J.-L.1
Petit, P.2
Risler, Y.3
Mignotte, B.4
-
48
-
-
0029036412
-
Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis
-
Petit PX, Lecouer H, Zorn E, Dauguet C, Mignotte B, Gougeon M-L. Alterations in mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis. J Cell Biol. 130:1995;157-167.
-
(1995)
J Cell Biol
, vol.130
, pp. 157-167
-
-
Petit, P.X.1
Lecouer, H.2
Zorn, E.3
Dauguet, C.4
Mignotte, B.5
Gougeon, M.-L.6
-
49
-
-
0029862706
-
Mitochondrial control of nuclear apoptosis
-
of outstanding interest. A reduction in mitochondrial transmembrane potential was shown to be an early event in drug-induced apoptosis induction in extracts from a range of cell lines. Inhibition of the decrease in the mitochondrial transmembrane potential by pharmacological agents or Bcl-2 overexpression prevented nuclear apoptosis in a cell-free system.
-
Zamzami N, Susin SA, Marchetti P, Hirsch T, Gomez-Monterrey I, Castedo M, Kroemer G. Mitochondrial control of nuclear apoptosis. of outstanding interest J Exp Med. 183:1996;1533-1544 A reduction in mitochondrial transmembrane potential was shown to be an early event in drug-induced apoptosis induction in extracts from a range of cell lines. Inhibition of the decrease in the mitochondrial transmembrane potential by pharmacological agents or Bcl-2 overexpression prevented nuclear apoptosis in a cell-free system.
-
(1996)
J Exp Med
, vol.183
, pp. 1533-1544
-
-
Zamzami, N.1
Susin, S.A.2
Marchetti, P.3
Hirsch, T.4
Gomez-Monterrey, I.5
Castedo, M.6
Kroemer, G.7
-
50
-
-
0030581151
-
Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
-
of outstanding interest. Cell-free cytosol extracts from non-apoptotic cells were triggered with dATP to duplicate some of the features of apoptosis as a means to purify some of the soluble factors that promote cell death. Cytochrome c was released from mitochondria in cell-free extracts and intact cells and, in combination with dATP, could activate apoptotic activity in the cell extracts.
-
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 Cell-free cytosol extracts from non-apoptotic cells were triggered with dATP to duplicate some of the features of apoptosis as a means to purify some of the soluble factors that promote cell death. Cytochrome c was released from mitochondria in cell-free extracts and intact cells and, in combination with dATP, could activate apoptotic activity in the cell extracts.
-
(1996)
Cell
, vol.86
, pp. 147-157
-
-
Liu, X.1
Kim, C.N.2
Yang, J.3
Jemmerson, R.4
Wang, X.5
-
51
-
-
0029811838
-
Loss of function of cytochrome c in Jurkat cells undergoing fas-mediated apoptosis
-
of outstanding interest. Cellular oxygen consumption, a measure of mitochondrial function, was investigated in Jurkat cells undergoing Fas-mediated apoptosis. Both oxygen consumption and cytochrome c function were diminished and these changes preceded nuclear apoptosis. Caspase inhibitors could protect cells from cytochrome c inactivation, although the cytochrome c protein was not degraded during its inactivation. These results indicate that protease activity and loss of cytochrome c function are involved in the reduction of mitochondrial function that occurs in apoptotic cells.
-
Krippner A, Matsuno-Yagi A, Gottlieb RA, Babior BM. Loss of function of cytochrome c in Jurkat cells undergoing fas-mediated apoptosis. of outstanding interest J Biol Chem. 27:1996;21629-21636 Cellular oxygen consumption, a measure of mitochondrial function, was investigated in Jurkat cells undergoing Fas-mediated apoptosis. Both oxygen consumption and cytochrome c function were diminished and these changes preceded nuclear apoptosis. Caspase inhibitors could protect cells from cytochrome c inactivation, although the cytochrome c protein was not degraded during its inactivation. These results indicate that protease activity and loss of cytochrome c function are involved in the reduction of mitochondrial function that occurs in apoptotic cells.
-
(1996)
J Biol Chem
, vol.27
, pp. 21629-21636
-
-
Krippner, A.1
Matsuno-Yagi, A.2
Gottlieb, R.A.3
Babior, B.M.4
-
52
-
-
0031037897
-
The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
-
of outstanding interest. Bcl-2 was shown to block cytochrome c release in a cell-free apoptosis system and in intact cells undergoing apoptosis. Caspase inhibitors could not block cytochrome c release but exogenously added cytochrome c could overcome Bcl-2 inhibition of apoptosis in a cell-free system. Cytochrome c release did not change mitochrondrial membrane potential, suggesting it is a later event in the apoptosis pathway.
-
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 Bcl-2 was shown to block cytochrome c release in a cell-free apoptosis system and in intact cells undergoing apoptosis. Caspase inhibitors could not block cytochrome c release but exogenously added cytochrome c could overcome Bcl-2 inhibition of apoptosis in a cell-free system. Cytochrome c release did not change mitochrondrial membrane potential, suggesting it is a later event in the apoptosis pathway.
-
(1997)
Science
, vol.275
, pp. 1132-1136
-
-
Kluck, R.M.1
Bossy-Wetzel, E.2
Green, D.R.3
Newmeyer, D.D.4
-
53
-
-
0031036872
-
Prevention of apoptosis by Bcl-2: Release of cytochrome C from mitochrondria blocked
-
of special interest. Cytochrome c levels were increased in the cytosol and decreased in the mitochondria of intact cells undergoing apoptosis. Bcl-2 was shown to block cytochrome c release into the cytosol and caspase activation, suggesting that Bcl-2 blockage of cytochrome c release from mitochondria may inhibit the activation of the apoptotic pathway.
-
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 mitochrondria blocked. of special interest Science. 275:1997;1129-1132 Cytochrome c levels were increased in the cytosol and decreased in the mitochondria of intact cells undergoing apoptosis. Bcl-2 was shown to block cytochrome c release into the cytosol and caspase activation, suggesting that Bcl-2 blockage of cytochrome c release from mitochondria may inhibit the activation of the apoptotic pathway.
-
(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.-I.7
Jones, D.P.8
Wang, X.9
-
54
-
-
0031034933
-
Potential involvement of fas and its ligand in the pathogenesis of Hashimoto's thyroiditis
-
of outstanding interest. IL-1β-induced Fas expression in normal thyrocytes where FasL was constitutively expressed resulting in apoptosis. Thyrocytes from Hashimoto's thyroiditis patients, however, contitutively expressed Fas as well as FasL, suggesting that thyrocytes alone - in the absence of infiltrating T lymphocytes - may undergo apoptosis resulting in hypothyroidism.
-
Giordano C, Stassi G, De Maria R, Todaro M, Richiusa P, Papoff G, Ruberti G, Bagnasco M, Testi R, Galluzzo A. Potential involvement of fas and its ligand in the pathogenesis of Hashimoto's thyroiditis. of outstanding interest Science. 275:1997;960-963 IL-1β-induced Fas expression in normal thyrocytes where FasL was constitutively expressed resulting in apoptosis. Thyrocytes from Hashimoto's thyroiditis patients, however, contitutively expressed Fas as well as FasL, suggesting that thyrocytes alone - in the absence of infiltrating T lymphocytes - may undergo apoptosis resulting in hypothyroidism.
-
(1997)
Science
, vol.275
, pp. 960-963
-
-
Giordano, C.1
Stassi, G.2
De Maria, R.3
Todaro, M.4
Richiusa, P.5
Papoff, G.6
Ruberti, G.7
Bagnasco, M.8
Testi, R.9
Galluzzo, A.10
-
55
-
-
10544232277
-
Melanoma cell expression of fas (Apo-1/CD95) ligand: Implications for tumor immune escape
-
of outstanding interest. Clear demonstration that some tumors use the Fas/FasL apoptosis pathway to protect themselves from tumor-infiltrating T lymphocytes. Melanoma cells were shown to express FasL in areas proximal to Fas-expressing T cells. In vitro demonstrations of the ability of the tumor cells expressing FasL, to activate apoptosis of the T lymphocytes, as well as in vivo demonstrations of the increased potency of FasL expressing melanoma cells in normal mice - but not lpr mutant mice - suggest that some tumors may use FasL to create immune privilege.
-
Hahne M, Rimoldi D, Schroter M, Romero P, Schreier M, French LE, Schneider P, Bornand T, Fontana A, Lienard D, et al. Melanoma cell expression of fas (Apo-1/CD95) ligand: implications for tumor immune escape. of outstanding interest Science. 274:1996;1363-1366 Clear demonstration that some tumors use the Fas/FasL apoptosis pathway to protect themselves from tumor-infiltrating T lymphocytes. Melanoma cells were shown to express FasL in areas proximal to Fas-expressing T cells. In vitro demonstrations of the ability of the tumor cells expressing FasL, to activate apoptosis of the T lymphocytes, as well as in vivo demonstrations of the increased potency of FasL expressing melanoma cells in normal mice - but not lpr mutant mice - suggest that some tumors may use FasL to create immune privilege.
-
(1996)
Science
, vol.274
, pp. 1363-1366
-
-
Hahne, M.1
Rimoldi, D.2
Schroter, M.3
Romero, P.4
Schreier, M.5
French, L.E.6
Schneider, P.7
Bornand, T.8
Fontana, A.9
Lienard, D.10
-
56
-
-
0029808372
-
The Fas counterattack: Fas-mediated T cell killing by colon cancer cells expressing Fas ligand
-
O'Connell J, O'Sullivan GC, Collins JK, Shanahan F. The Fas counterattack: Fas-mediated T cell killing by colon cancer cells expressing Fas ligand. J Exp Med. 184:1996;1075-1082.
-
(1996)
J Exp Med
, vol.184
, pp. 1075-1082
-
-
O'Connell, J.1
O'Sullivan, G.C.2
Collins, J.K.3
Shanahan, F.4
-
57
-
-
16144363507
-
Lymphocyte apoptosis induced by CD95 (APO-1/Fas) ligand-expressing tumor cells-a mechanism of immune evasion?
-
of outstanding interest. Fas protein expression was downregulated in hepatocellular carcinomas but FasL was upregulated. In vitro, these tumor cells were able to trigger apoptosis in Fas-expressing Jurkat cells, suggesting that some tumors may use FasL expression to inhibit immune attack. The authors also suggest that FasL-induction in tumors may result from some types of chemotherapy potentially promoting tumor survival.
-
Strand S, Hofmann WJ, Hug H, Muller M, Otto G, Strand D, Mariani SM, Stremmel W, Krammer PH, Galle PR. Lymphocyte apoptosis induced by CD95 (APO-1/Fas) ligand-expressing tumor cells-a mechanism of immune evasion? of outstanding interest Nat Med. 2:1996;1361-1366 Fas protein expression was downregulated in hepatocellular carcinomas but FasL was upregulated. In vitro, these tumor cells were able to trigger apoptosis in Fas-expressing Jurkat cells, suggesting that some tumors may use FasL expression to inhibit immune attack. The authors also suggest that FasL-induction in tumors may result from some types of chemotherapy potentially promoting tumor survival.
-
(1996)
Nat Med
, vol.2
, pp. 1361-1366
-
-
Strand, S.1
Hofmann, W.J.2
Hug, H.3
Muller, M.4
Otto, G.5
Strand, D.6
Mariani, S.M.7
Stremmel, W.8
Krammer, P.H.9
Galle, P.R.10
-
58
-
-
0030933337
-
Human lung carcinomas express fas ligand
-
Niehans GA, Brunner T, Frizelle SP, Liston JC, Salerno CT, Knapp DJ, Green DR, Kratzke RA. Human lung carcinomas express fas ligand. Cancer Res. 57:1997;1007-1012.
-
(1997)
Cancer Res
, vol.57
, pp. 1007-1012
-
-
Niehans, G.A.1
Brunner, T.2
Frizelle, S.P.3
Liston, J.C.4
Salerno, C.T.5
Knapp, D.J.6
Green, D.R.7
Kratzke, R.A.8
-
59
-
-
0027944206
-
P53 status and the efficacy of cancer therapy in vivo
-
Lowe SW, Bodis S, McClatchey A, Remington L, Ruley HE, Fisher DE, Housman DE, Jacks T. p53 status and the efficacy of cancer therapy in vivo. Science. 266:1994;807-810.
-
(1994)
Science
, vol.266
, pp. 807-810
-
-
Lowe, S.W.1
Bodis, S.2
McClatchey, A.3
Remington, L.4
Ruley, H.E.5
Fisher, D.E.6
Housman, D.E.7
Jacks, T.8
-
60
-
-
0028883179
-
Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
-
Miyashita T, Reed JC. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell. 80:1995;293-299.
-
(1995)
Cell
, vol.80
, pp. 293-299
-
-
Miyashita, T.1
Reed, J.C.2
-
61
-
-
0031018674
-
Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
-
of outstanding interest. The authors identify inactivating mutations of the BAX gene in mutation-prone colon adenocarcinomas that retain wild-type p53, implying that BAX mutations are selected for during tumor progression and that wild-type Bax functions as a tumor suppressor.
-
Rampino N, Yamamoto H, Ionov Y, Li Y, Sawai H, Reed JC, Perucho M. Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. of outstanding interest Science. 275:1997;967-969 The authors identify inactivating mutations of the BAX gene in mutation-prone colon adenocarcinomas that retain wild-type p53, implying that BAX mutations are selected for during tumor progression and that wild-type Bax functions as a tumor suppressor.
-
(1997)
Science
, vol.275
, pp. 967-969
-
-
Rampino, N.1
Yamamoto, H.2
Ionov, Y.3
Li, Y.4
Sawai, H.5
Reed, J.C.6
Perucho, M.7
-
62
-
-
0030938089
-
Bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis
-
McCurrach ME, Connor TMF, Knudson CM, Korsmeyer SJ, Lowe SW. bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis. Proc Natl Acad Sci USA. 94:1997;2345-2349.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 2345-2349
-
-
McCurrach, M.E.1
Connor, T.M.F.2
Knudson, C.M.3
Korsmeyer, S.J.4
Lowe, S.W.5
-
63
-
-
0029868112
-
The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein
-
of outstanding interest. Bax was identified in a yeast-two-hybrid screen for cellular factors that interact with the Bcl-2 homolog E1B 19k. Bax was shown to be activated by p53, to bind to E1B 19k in vitro and in cell lysates, and to antagonize the anti-apoptotic function of E1B 19k. These results indicate that E1B 19k, like Bcl-2 antagonizes p53-mediated apoptosis to promote viral replication with infected cells.
-
Han J, Sabbatini P, Perez D, Rao L, Modha D, White E. The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein. of outstanding interest Genes Dev. 10:1996;461-477 Bax was identified in a yeast-two-hybrid screen for cellular factors that interact with the Bcl-2 homolog E1B 19k. Bax was shown to be activated by p53, to bind to E1B 19k in vitro and in cell lysates, and to antagonize the anti-apoptotic function of E1B 19k. These results indicate that E1B 19k, like Bcl-2 antagonizes p53-mediated apoptosis to promote viral replication with infected cells.
-
(1996)
Genes Dev
, vol.10
, pp. 461-477
-
-
Han, J.1
Sabbatini, P.2
Perez, D.3
Rao, L.4
Modha, D.5
White, E.6
-
64
-
-
0031038137
-
Bax suppresses tumorigenesis and stimulate apoptosis in vivo
-
of outstanding interest. The role of Bax, which is induced in a p53-mediated response to tumor growth in a transgenic brain tumor model, was determined in vivo. Both p53 null and Bax null animals showed increased tumor growth and reduced tumor cell apoptosis, suggesting that Bax may act as a tumor suppressor by contributing to p53-mediated apoptosis.
-
Yin C, Knudson CM, Korsmeyer SJ, Van Dyke T. Bax suppresses tumorigenesis and stimulate apoptosis in vivo. of outstanding interest Nature. 385:1997;637-640 The role of Bax, which is induced in a p53-mediated response to tumor growth in a transgenic brain tumor model, was determined in vivo. Both p53 null and Bax null animals showed increased tumor growth and reduced tumor cell apoptosis, suggesting that Bax may act as a tumor suppressor by contributing to p53-mediated apoptosis.
-
(1997)
Nature
, vol.385
, pp. 637-640
-
-
Yin, C.1
Knudson, C.M.2
Korsmeyer, S.J.3
Van Dyke, T.4
-
66
-
-
0031054439
-
Kaposi's sarcoma-associated herpesvirus encodes a functional Bcl-2 homologue
-
Sarid R, Sato T, Bohenzky RA, Russo JJ, Chang Y. Kaposi's sarcoma-associated herpesvirus encodes a functional Bcl-2 homologue. Nat Med. 3:1997;293-297.
-
(1997)
Nat Med
, vol.3
, pp. 293-297
-
-
Sarid, R.1
Sato, T.2
Bohenzky, R.A.3
Russo, J.J.4
Chang, Y.5
-
67
-
-
0030970013
-
Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
-
of outstanding interest. A novel viral apoptosis-inhibition strategy is described in which vFLIPs bind to the FADD protein to prevent its recruitment of caspase 8 to the Fas/FasL complex, TRAMP, or the TRAIL receptor. It is suggested that the resultant inhibition of apoptosis may promote higher virus production and contribute to the persistence and oncogenicity of the viruses producing vFLIPs.
-
Thome M, Schneider P, Hofmann K, Fickenscher H, Meinl E, Neipel F, Mattmann C, Burns K, Bodmer J-L, Schroter M, et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. of outstanding interest Nature. 386:1997;517-521 A novel viral apoptosis-inhibition strategy is described in which vFLIPs bind to the FADD protein to prevent its recruitment of caspase 8 to the Fas/FasL complex, TRAMP, or the TRAIL receptor. It is suggested that the resultant inhibition of apoptosis may promote higher virus production and contribute to the persistence and oncogenicity of the viruses producing vFLIPs.
-
(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.-L.9
Schroter, M.10
-
68
-
-
0029025441
-
Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome
-
Fisher GH, Rosenberg FJ, Straus SE, Dale JK, Middleton LA, Lin AY, Strober W, Lenardo MJ, Puck JM. Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome. Cell. 81:1995;935-946.
-
(1995)
Cell
, vol.81
, pp. 935-946
-
-
Fisher, G.H.1
Rosenberg, F.J.2
Straus, S.E.3
Dale, J.K.4
Middleton, L.A.5
Lin, A.Y.6
Strober, W.7
Lenardo, M.J.8
Puck, J.M.9
-
69
-
-
0029006893
-
Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity
-
Rieux-Laucat F, Le Deist F, Hivroz C, Roberts IA, Debatin KM, Fischer A, de Villartay J. Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity. Science. 268:1995;1347-1349.
-
(1995)
Science
, vol.268
, pp. 1347-1349
-
-
Rieux-Laucat, F.1
Le Deist, F.2
Hivroz, C.3
Roberts, I.A.4
Debatin, K.M.5
Fischer, A.6
De Villartay, J.7
-
70
-
-
0030614415
-
Clinical immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis
-
Sneller MC, Wang J, Dale JK, Strober W, Middelton LA, Choi Y, Fleisher TA, Lim MS, Jaffe ES, Puck JM, et al. Clinical immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis. Blood. 89:1997;1341-1348.
-
(1997)
Blood
, vol.89
, pp. 1341-1348
-
-
Sneller, M.C.1
Wang, J.2
Dale, J.K.3
Strober, W.4
Middelton, L.A.5
Choi, Y.6
Fleisher, T.A.7
Lim, M.S.8
Jaffe, E.S.9
Puck, J.M.10
-
71
-
-
0029802697
-
Fas gene mutation in the Canale-Smith syndrome, an inherited lymphoproliferative disorder associated with autoimmunity
-
Drappa J, Vaishnaw AK, Sullivan KE, Chu J-L, Elkon KB. Fas gene mutation in the Canale-Smith syndrome, an inherited lymphoproliferative disorder associated with autoimmunity. New Eng J Med. 335:1996;1643-1649.
-
(1996)
New Eng J Med
, vol.335
, pp. 1643-1649
-
-
Drappa, J.1
Vaishnaw, A.K.2
Sullivan, K.E.3
Chu, J.-L.4
Elkon, K.B.5
-
72
-
-
0030972396
-
Transgenic expression of CD95 ligand on islet β cell induces a granulocytic infiltration but does not confer immune privilege upon islet allografts
-
of special interest. An attempt to use FasL to confer immune privilege on grafted pancreas failed because it promoted granulocyte infiltration and destruction of the graft, indicating that FasL may have a proinflammatory role in some situations.
-
Allison J, Georgiou HM, Strasser A, Vaux DL. Transgenic expression of CD95 ligand on islet β cell induces a granulocytic infiltration but does not confer immune privilege upon islet allografts. of special interest Proc Natl Acad Sci USA. 94:1997;3943-3947 An attempt to use FasL to confer immune privilege on grafted pancreas failed because it promoted granulocyte infiltration and destruction of the graft, indicating that FasL may have a proinflammatory role in some situations.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 3943-3947
-
-
Allison, J.1
Georgiou, H.M.2
Strasser, A.3
Vaux, D.L.4
-
73
-
-
0030890721
-
The role of fas in autoimmune diabetes
-
of outstanding interest. In an attempt to protect pancreatic B islet cells from autoimmune destruction by cytotoxic T lymphocytes, the authors expressed FasL on islets which inadvertently promoted their death. The detection of Fas upregulation on the surface of islet exposed to cytotoxic T lymphocytes, however, indicated that the Fas/FasL-triggered apoptosis pathway is the major mechanism of cell destruction in autoimmune diabetes.
-
Chervonsky AV, Wang Y, Wong FS, Visintin I, Flavell RA, Janeway JCA, Matis LA. The role of fas in autoimmune diabetes. of outstanding interest Cell. 89:1997;17-24 In an attempt to protect pancreatic B islet cells from autoimmune destruction by cytotoxic T lymphocytes, the authors expressed FasL on islets which inadvertently promoted their death. The detection of Fas upregulation on the surface of islet exposed to cytotoxic T lymphocytes, however, indicated that the Fas/FasL-triggered apoptosis pathway is the major mechanism of cell destruction in autoimmune diabetes.
-
(1997)
Cell
, vol.89
, pp. 17-24
-
-
Chervonsky, A.V.1
Wang, Y.2
Wong, F.S.3
Visintin, I.4
Flavell, R.A.5
Janeway, J.C.A.6
Matis, L.A.7
-
75
-
-
0031042972
-
Antitumor effect of locally produced CD95 ligand
-
of special interest. This group expressed FasL on tumor that does not make Fas to facilitate tumor rejection in a mouse model. Neutrophils caused rejection of the tumor, suggesting that FasL has a proinflammatory role but T-cell-mediated immunity was also obtained. Thus, local expression of FasL may target tumor cells that do not express Fas for destruction by activation of the inflammatory response.
-
Seino K-I, Kayagaki N, Okumura K, Yagita H. Antitumor effect of locally produced CD95 ligand. of special interest Nat Med. 3:1997;165-170 This group expressed FasL on tumor that does not make Fas to facilitate tumor rejection in a mouse model. Neutrophils caused rejection of the tumor, suggesting that FasL has a proinflammatory role but T-cell-mediated immunity was also obtained. Thus, local expression of FasL may target tumor cells that do not express Fas for destruction by activation of the inflammatory response.
-
(1997)
Nat Med
, vol.3
, pp. 165-170
-
-
Seino, K.-I.1
Kayagaki, N.2
Okumura, K.3
Yagita, H.4
-
76
-
-
0030017476
-
Prevention of islet allograft rejection with engineered myoblasts expressing fasL in mice
-
Lau HT, Yu M, Fontana A, Stoeckert CJ Jr. Prevention of islet allograft rejection with engineered myoblasts expressing fasL in mice. Science. 273:1996;109-112.
-
(1996)
Science
, vol.273
, pp. 109-112
-
-
Lau, H.T.1
Yu, M.2
Fontana, A.3
Stoeckert C.J., Jr.4
-
77
-
-
0027291205
-
Lethal effect of the anti-fas antibody in mice
-
Ogasawara J, Watanabe-Fukunaga R, Adachi M, Matsuzawa A, Kasugai T, Kitamura Y, Itoh N, Suda T, Nagata S. Lethal effect of the anti-fas antibody in mice. Nature. 364:1993;806-809.
-
(1993)
Nature
, vol.364
, pp. 806-809
-
-
Ogasawara, J.1
Watanabe-Fukunaga, R.2
Adachi, M.3
Matsuzawa, A.4
Kasugai, T.5
Kitamura, Y.6
Itoh, N.7
Suda, T.8
Nagata, S.9
-
78
-
-
0028783367
-
Involvement of the CD95 (APO-1/Fas) receptor and ligand in liver damage
-
Galle PR. Involvement of the CD95 (APO-1/Fas) receptor and ligand in liver damage. J Exp Med. 182:1995;1223-1230.
-
(1995)
J Exp Med
, vol.182
, pp. 1223-1230
-
-
Galle, P.R.1
-
79
-
-
13344268993
-
Fas ligand in human serum
-
of special interest. A soluble form of FasL was produced by cleavage with an unknown matrix metalloproteinase-like enzyme in patients with large granular lymphocytic leukemia and natural killer cell lymphoma but not in healthy people. These tumors constitutively expressed FasL, although peripheral natural killer cells from healthy people only express it upon activation. The authors suggest that the systemic tissue damage associated with these tumors may result in part from the soluble FasL produced by them.
-
Tanaka M, Suda T, Haze K, Nakamura N, Sato K, Kimura F, Motoyoshi K, Mizuki M, Tagawa S, Ohga S, et al. Fas ligand in human serum. of special interest Nat Med. 2:1996;317-322 A soluble form of FasL was produced by cleavage with an unknown matrix metalloproteinase-like enzyme in patients with large granular lymphocytic leukemia and natural killer cell lymphoma but not in healthy people. These tumors constitutively expressed FasL, although peripheral natural killer cells from healthy people only express it upon activation. The authors suggest that the systemic tissue damage associated with these tumors may result in part from the soluble FasL produced by them.
-
(1996)
Nat Med
, vol.2
, pp. 317-322
-
-
Tanaka, M.1
Suda, T.2
Haze, K.3
Nakamura, N.4
Sato, K.5
Kimura, F.6
Motoyoshi, K.7
Mizuki, M.8
Tagawa, S.9
Ohga, S.10
-
80
-
-
0030999750
-
Apoptosis and the dilemma of cancer chemotherapy
-
Hannun YA. Apoptosis and the dilemma of cancer chemotherapy. Blood. 89:1997;1845-1853.
-
(1997)
Blood
, vol.89
, pp. 1845-1853
-
-
Hannun, Y.A.1
-
81
-
-
0030897001
-
Selection for drug resistance results in resistance to fas-mediated apoptosis
-
of outstanding interest. Drug-resistant tumor cell lines were shown to exhibit resistance to Fas-mediated apoptosis, suggesting that chemotherapeutic drug-induced cell death and physiological apoptosis share common downstream effectors. These results imply that strategies to treat drug-resistant tumors by exploiting apoptosis induction may not succeed.
-
Landowski TH, Gleason-Guzman MC, Dalton WS. Selection for drug resistance results in resistance to fas-mediated apoptosis. of outstanding interest Blood. 89:1997;1854-1861 Drug-resistant tumor cell lines were shown to exhibit resistance to Fas-mediated apoptosis, suggesting that chemotherapeutic drug-induced cell death and physiological apoptosis share common downstream effectors. These results imply that strategies to treat drug-resistant tumors by exploiting apoptosis induction may not succeed.
-
(1997)
Blood
, vol.89
, pp. 1854-1861
-
-
Landowski, T.H.1
Gleason-Guzman, M.C.2
Dalton, W.S.3
-
82
-
-
0344188096
-
An adenovirus mutant that replicates selectively in p53-deficient human tumor cells
-
of outstanding interest. An adenovirus mutant was characterized, injected into a p53-deficient human tumors growing within nude mice, and shown to shrink the tumor, suggesting that it may be useful against some human tumors. The idea of using a mutant adenovirus to kill p53-deficient tumors by its normal replication cycle has promise requiring further trials.
-
Bischoff JR, Kirn DH, Williams A, Heise C, Horn S, Muna M, Ng L, Nye JA, Sampson-Johannes A, Fattaey A, McCormick F. An adenovirus mutant that replicates selectively in p53-deficient human tumor cells. of outstanding interest Science. 274:1996;373-376 An adenovirus mutant was characterized, injected into a p53-deficient human tumors growing within nude mice, and shown to shrink the tumor, suggesting that it may be useful against some human tumors. The idea of using a mutant adenovirus to kill p53-deficient tumors by its normal replication cycle has promise requiring further trials.
-
(1996)
Science
, vol.274
, pp. 373-376
-
-
Bischoff, J.R.1
Kirn, D.H.2
Williams, A.3
Heise, C.4
Horn, S.5
Muna, M.6
Ng, L.7
Nye, J.A.8
Sampson-Johannes, A.9
Fattaey, A.10
McCormick, F.11
-
83
-
-
0029828847
-
Will a twist of viral fate lead to a new cancer treatment?
-
Pennisi E. Will a twist of viral fate lead to a new cancer treatment? Science. 274:1996;342-343.
-
(1996)
Science
, vol.274
, pp. 342-343
-
-
Pennisi, E.1
|