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Volumn 10, Issue 3, 1998, Pages 279-288

Death-inducing functions of ligands of the tumor necrosis factor family: A Sanhedrin verdict

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; TUMOR NECROSIS FACTOR;

EID: 0031805451     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(98)80166-0     Document Type: Article
Times cited : (65)

References (99)
  • 1
    • 0014400299 scopus 로고
    • Cytotoxicity mediated by soluble antigen and lymphocytes in delayed hypersensitivity. III. Analysis of mechanisms
    • Ruddle NH, Waksman BH. Cytotoxicity mediated by soluble antigen and lymphocytes in delayed hypersensitivity. III. Analysis of mechanisms. J Exp Med. 128:1968;1267-1279.
    • (1968) J Exp Med , vol.128 , pp. 1267-1279
    • Ruddle, N.H.1    Waksman, B.H.2
  • 2
    • 0014311519 scopus 로고
    • Lymphocyte in vitro cytotoxicity: Mechanisms of immune and non-immune small lymphocyte mediated target L cell destruction
    • Granger GA, Kolb WP. Lymphocyte in vitro cytotoxicity: mechanisms of immune and non-immune small lymphocyte mediated target L cell destruction. J Immunol. 101:1968;111-120.
    • (1968) J Immunol , vol.101 , pp. 111-120
    • Granger, G.A.1    Kolb, W.P.2
  • 3
    • 0016178412 scopus 로고
    • Human lymphotoxin obtained from established lymphoid lines: Purification characteristics and inhibition by anti-immunoglobulin
    • Amino N, Linn ES, Pysher TJ, Mier R, Moore GE, DeGroot LJ. Human lymphotoxin obtained from established lymphoid lines: purification characteristics and inhibition by anti-immunoglobulin. J Immunol. 113:1974;1334-1345.
    • (1974) J Immunol , vol.113 , pp. 1334-1345
    • Amino, N.1    Linn, E.S.2    Pysher, T.J.3    Mier, R.4    Moore, G.E.5    Degroot, L.J.6
  • 4
    • 0018747910 scopus 로고
    • 51 Cr-labeled allogeneic target cells in vitro: Enhanced lysis by LT complexes associated with lg-like receptor(s)
    • 51 Cr-labeled allogeneic target cells in vitro: enhanced lysis by LT complexes associated with lg-like receptor(s). Cell Immunol. 45:1979;261-275.
    • (1979) Cell Immunol , vol.45 , pp. 261-275
    • Yamamoto, R.S.1    Hiserodt, J.C.2    Granger, G.A.3
  • 5
    • 0029075329 scopus 로고
    • Tumor necrosis factor ligand superfamily: Involvement in the pathology of malignant lymphomas
    • Gruss HJ, Dower SK. Tumor necrosis factor ligand superfamily: involvement in the pathology of malignant lymphomas. Blood. 85:1995;3378-3404.
    • (1995) Blood , vol.85 , pp. 3378-3404
    • Gruss, H.J.1    Dower, S.K.2
  • 6
    • 0030481587 scopus 로고    scopus 로고
    • A decade of accumulated knowledge and emerging answers. The 6th international congress on TNF Rhodes, Greece. May 1996
    • Wallach D. A decade of accumulated knowledge and emerging answers. The 6th international congress on TNF Rhodes, Greece. May 1996. Eur Cytokine Netw. 7:1996;713-724.
    • (1996) Eur Cytokine Netw , vol.7 , pp. 713-724
    • Wallach, D.1
  • 7
    • 0030892234 scopus 로고    scopus 로고
    • 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
  • 9
    • 0031938030 scopus 로고    scopus 로고
    • Downregulation of Fas ligand by shedding
    • of outstanding interest. The soluble form of the Fas/Apo 1-ligand, which is created by proteolytic cleavage of the cell-bound form, is shown in this study to act as competitive inhibitor of the function of the cell-bound form.
    • Tanaka M, Itai T, Adachi M, Nagata S. Downregulation of Fas ligand by shedding. of outstanding interest Nat Med. 4:1998;31-36 The soluble form of the Fas/Apo 1-ligand, which is created by proteolytic cleavage of the cell-bound form, is shown in this study to act as competitive inhibitor of the function of the cell-bound form.
    • (1998) Nat Med , vol.4 , pp. 31-36
    • Tanaka, M.1    Itai, T.2    Adachi, M.3    Nagata, S.4
  • 10
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • of outstanding interest. References by Black et al., 1997 and by Moss et al., 1997 [11] describe for the first time the isolation and cloning of the protease that is associated with the cell surface and is responsible for shedding of cell-surface protein(s).
    • Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slack JL, Wolfson MF, Castner BJ, Stocking KL, Reddy P, Srinivasan S, et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. of outstanding interest Nature. 385:1997;729-733 References by Black et al., 1997 and by Moss et al., 1997 [11] describe for the first time the isolation and cloning of the protease that is associated with the cell surface and is responsible for shedding of cell-surface protein(s).
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slack, J.L.5    Wolfson, M.F.6    Castner, B.J.7    Stocking, K.L.8    Reddy, P.9    Srinivasan, S.10
  • 11
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • of outstanding interest. References by Moss et al., 1997 and by Black et al., 1997 [10] describe for the first time the isolation and cloning of the protease that is associated with the cell surface and is responsible for shedding of cell-surface protein(s).
    • Moss ML, Jin SL, Milla ME, Burkhart W, Carter HL, Chen WJ, Clay WC, Didsbury JR, Hassler D, Hoffman CR, et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. of outstanding interest Nature. 385:1997;733-736 References by Moss et al., 1997 and by Black et al., 1997 [10] describe for the first time the isolation and cloning of the protease that is associated with the cell surface and is responsible for shedding of cell-surface protein(s).
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Burkhart, W.4    Carter, H.L.5    Chen, W.J.6    Clay, W.C.7    Didsbury, J.R.8    Hassler, D.9    Hoffman, C.R.10
  • 13
    • 0030869432 scopus 로고    scopus 로고
    • Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family
    • of outstanding interest. References by Degli Esposti et al., 1997, Pan et al., 1997 [14], Sheridan et al., 1997 [15] and MacFarlane et al., 1997 [16] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • Degli Esposti MA, Smolak PJ, Walczak H, Waugh J, Huang CP, DuBose RF, Goodwin RG, Smith CA. Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family. of outstanding interest J Exp Med. 186:1997;1165-1170 References by Degli Esposti et al., 1997, Pan et al., 1997 [14], Sheridan et al., 1997 [15] and MacFarlane et al., 1997 [16] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • (1997) J Exp Med , vol.186 , pp. 1165-1170
    • Degli Esposti, M.A.1    Smolak, P.J.2    Walczak, H.3    Waugh, J.4    Huang, C.P.5    Dubose, R.F.6    Goodwin, R.G.7    Smith, C.A.8
  • 14
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a death domain-containing receptor for TRAIL
    • of special interest. References by Pan et al., 1997, Degli Esposti et al., 1997 [13], Sheridan et al., 1997 [15] and MacFarlane et al., 1997 [16] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • Pan G, Ni J, Wei YF, Yu G, Gentz R, Dixit VM. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. of special interest Science. 277:1997;815-818 References by Pan et al., 1997, Degli Esposti et al., 1997 [13], Sheridan et al., 1997 [15] and MacFarlane et al., 1997 [16] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • (1997) Science , vol.277 , pp. 815-818
    • Pan, G.1    Ni, J.2    Wei, Y.F.3    Yu, G.4    Gentz, R.5    Dixit, V.M.6
  • 15
    • 0030792712 scopus 로고    scopus 로고
    • Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors
    • of special interest. References by Sheridan et al., 1997, Degli Esposti et al., 1997 [13], Pan et al., 1997 [14] and MacFarlane et al., 1997 [16] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • Sheridan JP, Marsters SA, Pitti RM, Gurney A, Skubatch M, Baldwin D, Ramakrishnan L, Gray CL, Baker K, Wood WI, et al. Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. of special interest Science. 277:1997;818-821 References by Sheridan et al., 1997, Degli Esposti et al., 1997 [13], Pan et al., 1997 [14] and MacFarlane et al., 1997 [16] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • (1997) Science , vol.277 , pp. 818-821
    • Sheridan, J.P.1    Marsters, S.A.2    Pitti, R.M.3    Gurney, A.4    Skubatch, M.5    Baldwin, D.6    Ramakrishnan, L.7    Gray, C.L.8    Baker, K.9    Wood, W.I.10
  • 16
    • 0030770614 scopus 로고    scopus 로고
    • Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL
    • of special interest. References by MacFarlane et al., 1997, Degli Esposti et al., 1997 [13], Pan et al., 1997 [14] and Sheridan et al., 1997 [15] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • MacFarlane M, Ahmad M, Srinivasula SM, Fernandes Alnemri T, Cohen GM, Alnemri ES. Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL. of special interest J Biol Chem. 272:1997;25417-25420 References by MacFarlane et al., 1997, Degli Esposti et al., 1997 [13], Pan et al., 1997 [14] and Sheridan et al., 1997 [15] describe the cloning of a decoy receptor for TRAIL/Apo2 ligand.
    • (1997) J Biol Chem , vol.272 , pp. 25417-25420
    • MacFarlane, M.1    Ahmad, M.2    Srinivasula, S.M.3    Fernandes Alnemri, T.4    Cohen, G.M.5    Alnemri, E.S.6
  • 17
    • 0031414749 scopus 로고    scopus 로고
    • The novel receptor TRAIL-R4 induced NF-κB and protects against TRAIL-mediated apoptosis, yet retains and incomplete death domain
    • of special interest. References by Degli-Esposti et al., 1997, and Marsters et al., 1997 [18] describe the cloning of a receptor for TRAIL/Apo2 ligand that does not signal for cell death (although it has the ability to signal for other effects) and blocks death induction, apparently by competing with those TRAIL/Apo2 ligand receptors that upon ligand binding signal to cause death.
    • Degli-Esposti MA, Dougall WC, Smolak PJ, Waugh JY, Smith CA, Goodwin RG. The novel receptor TRAIL-R4 induced NF-κB and protects against TRAIL-mediated apoptosis, yet retains and incomplete death domain. of special interest Immunity. 7:1997;813-820 References by Degli-Esposti et al., 1997, and Marsters et al., 1997 [18] describe the cloning of a receptor for TRAIL/Apo2 ligand that does not signal for cell death (although it has the ability to signal for other effects) and blocks death induction, apparently by competing with those TRAIL/Apo2 ligand receptors that upon ligand binding signal to cause death.
    • (1997) Immunity , vol.7 , pp. 813-820
    • Degli-Esposti, M.A.1    Dougall, W.C.2    Smolak, P.J.3    Waugh, J.Y.4    Smith, C.A.5    Goodwin, R.G.6
  • 18
    • 13144265771 scopus 로고    scopus 로고
    • A novel receptor for Apo2L/TRAIL contains a truncated death domain
    • of special interest. References by Marsters et al., 1997, and Degli-Esposti et al., 1997 [17] describe the cloning of a receptor for TRAIL/Apo2 ligand that does not signal for cell death (although it has the ability to signal for other effects) and blocks death induction, apparently by competing with those TRAIL/Apo2 ligand receptors that upon ligand binding signal to cause death.
    • Marsters SA, Sheridan JP, Pitti RM, Hunag A, Skubatch M, Baldwin D, Yan J, Gurney A, Goddard AD, Godowski P, Ashenazi A. A novel receptor for Apo2L/TRAIL contains a truncated death domain. of special interest Curr Biol. 7:1997;1003-1006 References by Marsters et al., 1997, and Degli-Esposti et al., 1997 [17] describe the cloning of a receptor for TRAIL/Apo2 ligand that does not signal for cell death (although it has the ability to signal for other effects) and blocks death induction, apparently by competing with those TRAIL/Apo2 ligand receptors that upon ligand binding signal to cause death.
    • (1997) Curr Biol , vol.7 , pp. 1003-1006
    • Marsters, S.A.1    Sheridan, J.P.2    Pitti, R.M.3    Hunag, A.4    Skubatch, M.5    Baldwin, D.6    Yan, J.7    Gurney, A.8    Goddard, A.D.9    Godowski, P.10    Ashenazi, A.11
  • 19
    • 85088329517 scopus 로고    scopus 로고
    • Cell death: TRAIL and its receptors
    • Golstein P. Cell death: TRAIL and its receptors. Curr Biol. 7:1998;R75-R753.
    • (1998) Curr Biol , vol.7
    • Golstein, P.1
  • 20
    • 0030965162 scopus 로고    scopus 로고
    • Cell death induction by TNF: A matter of self control
    • Wallach D. Cell death induction by TNF: a matter of self control. Trends Biochem Sci. 22:1997;107-146.
    • (1997) Trends Biochem Sci , vol.22 , pp. 107-146
    • Wallach, D.1
  • 22
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang X, Khosravi Far R, Chang HY, Baltimore D. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell. 89:1997;1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 23
    • 0026691240 scopus 로고
    • The A20 Zinc finger protein protects cells from tumor necrosis factor cytotoxicity
    • Opipari AW, Hu HM, Yabkowitz R, Dixit VM. The A20 Zinc finger protein protects cells from tumor necrosis factor cytotoxicity. J Biol Chem. 267:1992;12424-12427.
    • (1992) J Biol Chem , vol.267 , pp. 12424-12427
    • Opipari, A.W.1    Hu, H.M.2    Yabkowitz, R.3    Dixit, V.M.4
  • 24
    • 0000564581 scopus 로고    scopus 로고
    • The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappa B activation
    • of special interest. This provides evidence that A20, which acts as an inhibitor of TNF-receptor signaling, is part of the signaling complex.
    • Song HY, Rothe M, Goeddel DV. The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappa B activation. of special interest Proc Natl Acad Sci USA. 93:1996;6721-6725 This provides evidence that A20, which acts as an inhibitor of TNF-receptor signaling, is part of the signaling complex.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6721-6725
    • Song, H.Y.1    Rothe, M.2    Goeddel, D.V.3
  • 25
    • 0030026698 scopus 로고    scopus 로고
    • L: A20 zinc finger protein inhibits TNF and IL-1 signaling
    • of special interest. The authors provide evidence that A20 is a wide-ranging inhibitor of TNF function (as well as of the function of IL-1, whose receptor employs parts of the signaling molecules activated by the TNF receptors).
    • Jaattela M, Mouritzen H, Elling F, Bastholm L. L: A20 zinc finger protein inhibits TNF and IL-1 signaling. of special interest J Immunol. 156:1996;1166-1173 The authors provide evidence that A20 is a wide-ranging inhibitor of TNF function (as well as of the function of IL-1, whose receptor employs parts of the signaling molecules activated by the TNF receptors).
    • (1996) J Immunol , vol.156 , pp. 1166-1173
    • Jaattela, M.1    Mouritzen, H.2    Elling, F.3    Bastholm, L.4
  • 26
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • Rothe M, Pan M-G, Henzel WJ, Ayres TM, Goeddel DV. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell. 83:1995;1243-1252.
    • (1995) Cell , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan M-G2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 27
    • 0029953942 scopus 로고    scopus 로고
    • Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors
    • Uren AG, Pakusch M, Hawkins CJ, Puls KL, Vaux DL. Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors. Proc Natl Acad Sci USA. 93:1996;4974-4978.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4974-4978
    • Uren, A.G.1    Pakusch, M.2    Hawkins, C.J.3    Puls, K.L.4    Vaux, D.L.5
  • 28
    • 0030447483 scopus 로고    scopus 로고
    • The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex
    • of special interest. This provides evidence that c-IAP1, an inhibitor of apoptosis that contains a Baculovirus inhibitor of death motif, is recruited to the main death-inducing TNF receptor, the p55 receptor (CD120a).
    • Shu H-B, Takeuchi M, Goeddel DV. The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex. of special interest Proc Natl Acad Sci USA. 93:1996;13973-13978 This provides evidence that c-IAP1, an inhibitor of apoptosis that contains a Baculovirus inhibitor of death motif, is recruited to the main death-inducing TNF receptor, the p55 receptor (CD120a).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13973-13978
    • Shu H-B1    Takeuchi, M.2    Goeddel, D.V.3
  • 29
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • of outstanding interest. This reports that apoptosis inhibitors of the IAP family directly inhibit specific caspases.
    • Devereaux QL, Takahashi R, Salvesen GS, Reed JC. X-linked IAP is a direct inhibitor of cell-death proteases. of outstanding interest Nature. 388:1997;300-304 This reports that apoptosis inhibitors of the IAP family directly inhibit specific caspases.
    • (1997) Nature , vol.388 , pp. 300-304
    • Devereaux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 30
    • 0032478717 scopus 로고    scopus 로고
    • A single BIR domain of XIAP sufficient for inhibiting caspases
    • of special interest. The authors demonstrate that caspase inhibition by IAP family members is mediated by specific Baculovirus inhibitor of death (BIR) motifs within them.
    • Takahashi R, Deveraux Q, Tamm I, Welsh K, Assa-Munt N, Salvesen GS, Reed JC. A single BIR domain of XIAP sufficient for inhibiting caspases. of special interest J Biol Chem. 273:1998;7787-7790 The authors demonstrate that caspase inhibition by IAP family members is mediated by specific Baculovirus inhibitor of death (BIR) motifs within them.
    • (1998) J Biol Chem , vol.273 , pp. 7787-7790
    • Takahashi, R.1    Deveraux, Q.2    Tamm, I.3    Welsh, K.4    Assa-Munt, N.5    Salvesen, G.S.6    Reed, J.C.7
  • 31
    • 0030613758 scopus 로고    scopus 로고
    • NF-κB activation: The 1κB kinase revealed?
    • Stankovski I, Baltimore D. NF-κB activation: the 1κB kinase revealed? Cell. 91:1997;299-302.
    • (1997) Cell , vol.91 , pp. 299-302
    • Stankovski, I.1    Baltimore, D.2
  • 32
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-a-induced cell death
    • of special interest. References by Beg and Baltimore, 1996, Van Antwerp et al., 1996 [33], Wang et al., 1996 [34] and Liu et al., 1996 [35] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • Beg AA, Baltimore D. An essential role for NF-κB in preventing TNF-a-induced cell death. of special interest Science. 274:1996;782-784 References by Beg and Baltimore, 1996, Van Antwerp et al., 1996 [33], Wang et al., 1996 [34] and Liu et al., 1996 [35] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 33
    • 0029992609 scopus 로고    scopus 로고
    • Suppression of TNF-α-induced apoptosis by NF-κB
    • of special interest. References by Van Antwerp et al., 1996, Beg and Baltimore, 1996 [32], Wang et al., 1996 [34] and Liu et al., 1996 [35] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • 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 References by Van Antwerp et al., 1996, Beg and Baltimore, 1996 [32], Wang et al., 1996 [34] and Liu et al., 1996 [35] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • (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
  • 34
    • 0029858387 scopus 로고    scopus 로고
    • TNF- And cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB
    • of special interest. References by Wang et al., 1996, Beg and Baltimore, 1996 [32], Van Antwerp et al., 1996 [33] and Liu et al., 1996 [35] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • Wang C-Y, Mayo MW, Baldwin AS Jr. TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB. of special interest Science. 274:1996;784-787 References by Wang et al., 1996, Beg and Baltimore, 1996 [32], Van Antwerp et al., 1996 [33] and Liu et al., 1996 [35] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • (1996) Science , vol.274 , pp. 784-787
    • Wang C-Y1    Mayo, M.W.2    Baldwin A.S., Jr.3
  • 35
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death
    • of special interest. References by Liu et al., 1996 [35], Beg and Baltimore, 1996 [32], Van Antwerp et al., 1996 [33] and Wang et al., 1996 [34] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • Liu Z-G, Hsu H, Goeddel DV, Karin M. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. of special interest Cell. 87:1996;565-576 References by Liu et al., 1996 [35], Beg and Baltimore, 1996 [32], Van Antwerp et al., 1996 [33] and Wang et al., 1996 [34] indicate that some NF-κB-induced proteins have a protective effect against TNF cytotoxicity and that various cells that are resistant to TNF depend on the activation of NF-κB by TNF for this resistance.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu Z-G1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 36
    • 0030592564 scopus 로고    scopus 로고
    • Expansion or elimination of B cells in vivo: Dual roles for CD40- And Fas (CD95)-ligands modulated by the B cell antigen receptor
    • Rathmell JC, Townsend SE, Xu JC, Flavell RA, Goodnow CC. Expansion or elimination of B cells in vivo: dual roles for CD40- and Fas (CD95)-ligands modulated by the B cell antigen receptor. Cell. 87:1996;319-329.
    • (1996) Cell , vol.87 , pp. 319-329
    • Rathmell, J.C.1    Townsend, S.E.2    Xu, J.C.3    Flavell, R.A.4    Goodnow, C.C.5
  • 37
    • 0029073035 scopus 로고
    • Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis
    • Sarma V, Lin Z, Clark L, Rust BM, Tewari M, Noelle RJ, Dixit VM. Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis. J Biol Chem. 270:1995;12343-12346.
    • (1995) J Biol Chem , vol.270 , pp. 12343-12346
    • Sarma, V.1    Lin, Z.2    Clark, L.3    Rust, B.M.4    Tewari, M.5    Noelle, R.J.6    Dixit, V.M.7
  • 38
    • 0030067795 scopus 로고    scopus 로고
    • A novel function of CD40: Induction of cell death in transformed cells
    • Hess S, Engelmann H. A novel function of CD40: induction of cell death in transformed cells. J Exp Med. 183:1996;159-167.
    • (1996) J Exp Med , vol.183 , pp. 159-167
    • Hess, S.1    Engelmann, H.2
  • 40
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes
    • of special interest. References by Newton et al., 1998 and Zsrnig et al., 1998 [41] present evidence suggesting that MORT1/FADD, in addition to its role in death induction by receptors of the TNF/NGF family, also has a role in signaling for growth.
    • Newton K, Harris AH, Bath ML, Smith KGC, Strasser A. A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes. of special interest EMBO J. 18:1998;706-718 References by Newton et al., 1998 and Zsrnig et al., 1998 [41] present evidence suggesting that MORT1/FADD, in addition to its role in death induction by receptors of the TNF/NGF family, also has a role in signaling for growth.
    • (1998) EMBO J , vol.18 , pp. 706-718
    • Newton, K.1    Harris, A.H.2    Bath, M.L.3    Smith, K.G.C.4    Strasser, A.5
  • 41
    • 0032499138 scopus 로고    scopus 로고
    • P53-dependent impairment of T-cell proliferation in FADD dominant-negative transgenic mice
    • of special interest. References by Zsrnig et al., 1998 and Newton et al., 1998 [40] present evidence suggesting that MORT1/FADD, in addition to its role in death induction by receptors of the TNF/NGF family, also has a role in signaling for growth.
    • Zsrnig M, Hueber A-O, Evan G. p53-dependent impairment of T-cell proliferation in FADD dominant-negative transgenic mice. of special interest Curr Biol. 8:1998;467-470 References by Zsrnig et al., 1998 and Newton et al., 1998 [40] present evidence suggesting that MORT1/FADD, in addition to its role in death induction by receptors of the TNF/NGF family, also has a role in signaling for growth.
    • (1998) Curr Biol , vol.8 , pp. 467-470
    • Zsrnig, M.1    Hueber A-O2    Evan, G.3
  • 42
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with Fas
    • Sato T, Irie S, Kitada S, Reed JC. FAP-1: a protein tyrosine phosphatase that associates with Fas. Science. 268:1995;411-415.
    • (1995) Science , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 43
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO1- And TNF receptor-induced cell death
    • Boldin MP, Goncharov TM, Goltsev YV, Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO1- and TNF receptor-induced cell death. Cell. 85:1996;803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 46
    • 0030934465 scopus 로고    scopus 로고
    • Fas-associated death domain protein interleukin-1 β-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- And p55-mediated death signaling
    • Vincenz C, Dixit VM. Fas-associated death domain protein interleukin-1 β-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling. J Biol Chem. 272:1997;6578-6583.
    • (1997) J Biol Chem , vol.272 , pp. 6578-6583
    • Vincenz, C.1    Dixit, V.M.2
  • 47
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adapter molecule
    • Duan H, Dixit VM. RAIDD is a new 'death' adapter molecule. Nature. 385:1997;86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 50
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-κB signal
    • of outstanding interest. References by Kelliher et al., 1998, and Ting et al., 1996 [51] provide evidence suggesting that RIP, a death-domain-containing adapter protein that can cause death when overexpressed in cells, does not serve an important role in death induction by Fas/Apo-1 or by TNF and actually contributes to cell resistance to TNF cytotoxicity, being crucial for the TNF-induced activation of NF-κB.
    • Kelliher MA, Grimm S, Ishida Y, Kuo F, Stanger BZ, Leder P. The death domain kinase RIP mediates the TNF-induced NF-κB signal. of outstanding interest Immunity. 8:1998;297-303 References by Kelliher et al., 1998, and Ting et al., 1996 [51] provide evidence suggesting that RIP, a death-domain-containing adapter protein that can cause death when overexpressed in cells, does not serve an important role in death induction by Fas/Apo-1 or by TNF and actually contributes to cell resistance to TNF cytotoxicity, being crucial for the TNF-induced activation of NF-κB.
    • (1998) Immunity , vol.8 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3    Kuo, F.4    Stanger, B.Z.5    Leder, P.6
  • 51
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis
    • of outstanding interest. References by Ting et al., 1996, and Kelliher et al., 1998 [50] provide evidence suggesting that RIP, a death-domain-containing adapter protein that can cause death when overexpressed in cells, does not serve an important role in death induction by Fas/Apo-1 or by TNF and actually contributes to cell resistance to TNF cytotoxicity, being crucial for the TNF-induced activation of NF-κB.
    • Ting AT, Pimentel Muinos FX, Seed B. RIP mediates tumor necrosis factor receptor 1 activation of NF-kappaB but not Fas/APO-1-initiated apoptosis. of outstanding interest EMBO J. 15:1996;6189-6196 References by Ting et al., 1996, and Kelliher et al., 1998 [50] provide evidence suggesting that RIP, a death-domain-containing adapter protein that can cause death when overexpressed in cells, does not serve an important role in death induction by Fas/Apo-1 or by TNF and actually contributes to cell resistance to TNF cytotoxicity, being crucial for the TNF-induced activation of NF-κB.
    • (1996) EMBO J , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel Muinos, F.X.2    Seed, B.3
  • 52
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • of special interest. References by Irmler et al., 1997, Shu et al., 1997 [53], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55], Hu et al., 1997 [56] and Han et al., 1987 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • Irmler M, Thome M, Hahne M, Schneider P, Hofmann K, Steiner V, Bodmer JL, Schroter M, Burns K, Mattmann C, et al. Inhibition of death receptor signals by cellular FLIP. of special interest Nature. 388:1997;190-195 References by Irmler et al., 1997, Shu et al., 1997 [53], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55], Hu et al., 1997 [56] and Han et al., 1987 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1    Thome, M.2    Hahne, M.3    Schneider, P.4    Hofmann, K.5    Steiner, V.6    Bodmer, J.L.7    Schroter, M.8    Burns, K.9    Mattmann, C.10
  • 53
    • 0030746740 scopus 로고    scopus 로고
    • Casper is a FADD- And caspase-related inducer of apoptosis
    • of special interest. References by Shu et al., 1997, Irmler et al., 1997 [52], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55], Hu et al., 1997 [56] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • Shu HB, Halpin DR, Goeddel DV. Casper is a FADD- and caspase-related inducer of apoptosis. of special interest Immunity. 6:1997;751-763 References by Shu et al., 1997, Irmler et al., 1997 [52], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55], Hu et al., 1997 [56] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • (1997) Immunity , vol.6 , pp. 751-763
    • Shu, H.B.1    Halpin, D.R.2    Goeddel, D.V.3
  • 54
    • 0030877440 scopus 로고    scopus 로고
    • CASH, a novel caspase homologue with death effector domains
    • of special interest. References by Goltsev et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Srinivasula et al., 1997 [55], Hu et al., 1997 [56] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • Goltsev YV, Kovalenko AV, Arnold E, Varfolomeev EE, Brodianskii VM, Wallach D. CASH, a novel caspase homologue with death effector domains. of special interest J Biol Chem. 272:1997;19641-19644 References by Goltsev et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Srinivasula et al., 1997 [55], Hu et al., 1997 [56] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • (1997) J Biol Chem , vol.272 , pp. 19641-19644
    • Goltsev, Y.V.1    Kovalenko, A.V.2    Arnold, E.3    Varfolomeev, E.E.4    Brodianskii, V.M.5    Wallach, D.6
  • 55
    • 0030810981 scopus 로고    scopus 로고
    • FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis
    • of special interest. References by Srinivasula et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Goltsev et al., 1997 [54], Hu et al., 1997 [56] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes Alnemri T, Croce CM, Litwack G, et al. FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis. of special interest J Biol Chem. 272:1997;18542-18545 References by Srinivasula et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Goltsev et al., 1997 [54], Hu et al., 1997 [56] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • (1997) J Biol Chem , vol.272 , pp. 18542-18545
    • Srinivasula, S.M.1    Ahmad, M.2    Ottilie, S.3    Bullrich, F.4    Banks, S.5    Wang, Y.6    Fernandes Alnemri, T.7    Croce, C.M.8    Litwack, G.9
  • 56
    • 0030841911 scopus 로고    scopus 로고
    • I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- And CD-95-induced apoptosis
    • of special interest. References by Hu et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • Hu S, Vincenz C, Ni J, Gentz R, Dixit VM. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. of special interest J Biol Chem. 272:1997;17255-17257 References by Hu et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55] and Han et al., 1997 [57] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • (1997) J Biol Chem , vol.272 , pp. 17255-17257
    • Hu, S.1    Vincenz, C.2    Ni, J.3    Gentz, R.4    Dixit, V.M.5
  • 57
    • 0030758315 scopus 로고    scopus 로고
    • MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death
    • of special interest. References by Han et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55] and Hu et al., 1997 [56] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • Han DK, Chaudhary PM, Wright ME, Friedman C, Trask B, Riedel R, Baskin D, Schwartz S, Hood L. MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death. of special interest Proc Natl Acad Sci USA. 94:1997;11333-11338 References by Han et al., 1997, Irmler et al., 1997 [52], Shu et al., 1997 [53], Goltsev et al., 1997 [54], Srinivasula et al., 1997 [55] and Hu et al., 1997 [56] describe the cloning of a protein that displays a marked sequence homology to caspase-8 and -10, but lacks several residues that are crucial for caspase activity. This protein can prevent cell death induction by TNF and Fas/Apo1, apparently by competing with caspase-8 and -10 for their binding to the adapter protein MORT1/FADD. In some cells, however, it is capable of triggering cytotoxicity, probably through association with functional caspases, suggesting that it serves a more subtle role than mere inhibition of death induction.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11333-11338
    • Han, D.K.1    Chaudhary, P.M.2    Wright, M.E.3    Friedman, C.4    Trask, B.5    Riedel, R.6    Baskin, D.7    Schwartz, S.8    Hood, L.9
  • 58
    • 0018832418 scopus 로고
    • Injury of neoplastic cells by murine macrophages leads to inhibition of mitochondrial respiration
    • Granger DL, Taintor RR, Cook JL, Hibbs JB Jr. Injury of neoplastic cells by murine macrophages leads to inhibition of mitochondrial respiration. J Clin Invest. 65:1980;357-370.
    • (1980) J Clin Invest , vol.65 , pp. 357-370
    • Granger, D.L.1    Taintor, R.R.2    Cook, J.L.3    Hibbs J.B., Jr.4
  • 59
    • 0020513294 scopus 로고
    • Anti-tumour cytotoxin produced by human monocytes: Studies on its mode of action
    • Matthews N. Anti-tumour cytotoxin produced by human monocytes: studies on its mode of action. Br J Cancer. 48:1983;405-410.
    • (1983) Br J Cancer , vol.48 , pp. 405-410
    • Matthews, N.1
  • 61
    • 0029811838 scopus 로고    scopus 로고
    • Loss of function of cytochrome c in Jurkat cells undergoing fas-mediated apoptosis
    • Krippner A, Matsuno Yagi A, Gottlieb RA, Babior BM. Loss of function of cytochrome c in Jurkat cells undergoing fas-mediated apoptosis. J Biol Chem. 271:1996;21629-21636.
    • (1996) J Biol Chem , vol.271 , pp. 21629-21636
    • Krippner, A.1    Matsuno Yagi, A.2    Gottlieb, R.A.3    Babior, B.M.4
  • 62
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • of outstanding interest. This reports that cytochrome c released by the mitochondria during apoptosis can trigger damage in isolated nuclei, similar to that observed in the apoptotic cells. This is a major step forward in definition of the in vitro system that has allowed identification of Apaf-1 and study of the positive and negative regulation of its function.
    • 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 This reports that cytochrome c released by the mitochondria during apoptosis can trigger damage in isolated nuclei, similar to that observed in the apoptotic cells. This is a major step forward in definition of the in vitro system that has allowed identification of Apaf-1 and study of the positive and negative regulation of its function.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 63
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • 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. Cell. 90:1997;405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 64
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates and apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates and apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 65
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death
    • of outstanding interest. This shows that the anti-apoptotic effect of CED-9 is mediated by its binding to CED-4 and inhibition of CED-3 processing by it. CED-4 also binds in transfected cells to the mammalian caspase 1 and caspase 8.
    • Chinnaiyan AM, O'Rourke K, Lane BR, Dixit VM. Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death. of outstanding interest Science. 275:1997;1122-1126 This shows that the anti-apoptotic effect of CED-9 is mediated by its binding to CED-4 and inhibition of CED-3 processing by it. CED-4 also binds in transfected cells to the mammalian caspase 1 and caspase 8.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, B.R.3    Dixit, V.M.4
  • 66
    • 0031020227 scopus 로고    scopus 로고
    • Interaction and regulation of subcellular localization of CED-4 by CED-9
    • of outstanding interest. The authors demonstrate that the anti-apoptotic effect of CED-9 is mediated by its binding to CED-4.
    • Wu D, Wallen HD, Nuez G. Interaction and regulation of subcellular localization of CED-4 by CED-9. of outstanding interest Science. 275:1997;1126-1129 The authors demonstrate that the anti-apoptotic effect of CED-9 is mediated by its binding to CED-4.
    • (1997) Science , vol.275 , pp. 1126-1129
    • Wu, D.1    Wallen, H.D.2    Nuez, G.3
  • 67
    • 0031194404 scopus 로고    scopus 로고
    • Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis
    • of outstanding interest. This reports that the anti-apoptotic effect of CED-9 is mediated by its binding to CED-4 which results in inhibition of CED-3 processing.
    • Seshagiri S, Miller LK. Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis. of outstanding interest Curr Biol. 7:1997;455-60 This reports that the anti-apoptotic effect of CED-9 is mediated by its binding to CED-4 which results in inhibition of CED-3 processing.
    • (1997) Curr Biol , vol.7 , pp. 455-460
    • Seshagiri, S.1    Miller, L.K.2
  • 68
    • 0031582671 scopus 로고    scopus 로고
    • Apoptosis. CED-4 is a stranger no more
    • Hengartner MO. Apoptosis. CED-4 is a stranger no more. Nature. 388:1997;714-715.
    • (1997) Nature , vol.388 , pp. 714-715
    • Hengartner, M.O.1
  • 69
    • 0029899181 scopus 로고    scopus 로고
    • 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
  • 70
    • 0029609086 scopus 로고
    • Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis
    • Strasser A, Harris AW, Huang DC, 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.3    Krammer, P.H.4    Cory, S.5
  • 71
    • 0029976410 scopus 로고    scopus 로고
    • A bcl-2 transgene expressed in hepatocytes protects mice from fulminant liver destruction but not from rapid death induced by anti-Fas antibody injection
    • of special interest. This reports on in vivo evidence for involvement of Bcl-2 in controlling death of hepatocyes induced by Fas/Apo1.
    • Rodriguez I, Matsuura K, Khatib K, Reed JC, Nagata S, Vassalli P. A bcl-2 transgene expressed in hepatocytes protects mice from fulminant liver destruction but not from rapid death induced by anti-Fas antibody injection. of special interest J Exp Med. 183:1996;1031-1036 This reports on in vivo evidence for involvement of Bcl-2 in controlling death of hepatocyes induced by Fas/Apo1.
    • (1996) J Exp Med , vol.183 , pp. 1031-1036
    • Rodriguez, I.1    Matsuura, K.2    Khatib, K.3    Reed, J.C.4    Nagata, S.5    Vassalli, P.6
  • 73
    • 0030994024 scopus 로고    scopus 로고
    • Bcl-x(L) can inhibit apoptosis in cells that have undergone Fas-induced protease activation
    • of special interest. The authors demonstrate evidence that mechanisms acting downstream of the initial caspase activation by Fas/Apo1 are the targets for the protective effect of Bcl-x(L) against apoptosis induced by Fas/Apo1.
    • Boise LH, Thompson CB. Bcl-x(L) can inhibit apoptosis in cells that have undergone Fas-induced protease activation. of special interest Proc Natl Acad Sci USA. 94:1997;3759-6374 The authors demonstrate evidence that mechanisms acting downstream of the initial caspase activation by Fas/Apo1 are the targets for the protective effect of Bcl-x(L) against apoptosis induced by Fas/Apo1.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3759-6374
    • Boise, L.H.1    Thompson, C.B.2
  • 74
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • of special interest. This demonstrates that Bcl-2 can prevent the release of cytochrome c by mitochondria
    • Yang J, Liu X, Bhalla K, Kim CN, Ibrado AM, Cai J, Peng TI, Jones DP, Wang X. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. of special interest Science. 275:1997;1129-1132 This demonstrates that Bcl-2 can prevent the release of cytochrome c by mitochondria.
    • (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
  • 75
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • of special interest. This shows that cytochrome c release from the mitochondria seems to be independent of dissipation of a voltage gradient in the mitochondrial membrane and can be blocked by Bcl-2.
    • 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 special interest Science. 275:1997;1132-1136 This shows that cytochrome c release from the mitochondria seems to be independent of dissipation of a voltage gradient in the mitochondrial membrane and can be blocked by Bcl-2.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 76
    • 0030610962 scopus 로고    scopus 로고
    • Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis
    • of special interest. The authors report that cytochrome c release from the mitochondria can be blocked by Bcl-2.
    • Kharbanda S, Pandey P, Schofield L, Israels S, Roncinske R, Yoshida K, Bharti A, Yuan ZM, Saxena S, Weichselbaum R, et al. Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis. of special interest Proc Natl Acad Sci USA. 94:1997;6939-6942 The authors report that cytochrome c release from the mitochondria can be blocked by Bcl-2.
    • (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.M.8    Saxena, S.9    Weichselbaum, R.10
  • 77
    • 0032539673 scopus 로고    scopus 로고
    • Bcl-2 prevents apoptotic mitochondrial dysfunction by regulating proton flux
    • of special interest. This shows that Bcl-2 prevents dissipation of voltage gradient in the mitochondrial membrane, apparently by affecting proton efflux from the mitochondria.
    • Shimizu S, Eguchi Y, Kamiike W, Funahashi Y, Mignon A, Lacronique V, Matsuda H, Tsujimoto Y. Bcl-2 prevents apoptotic mitochondrial dysfunction by regulating proton flux. of special interest Proc Natl Acad Sci USA. 95:1998;1455-1459 This shows that Bcl-2 prevents dissipation of voltage gradient in the mitochondrial membrane, apparently by affecting proton efflux from the mitochondria.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1455-1459
    • Shimizu, S.1    Eguchi, Y.2    Kamiike, W.3    Funahashi, Y.4    Mignon, A.5    Lacronique, V.6    Matsuda, H.7    Tsujimoto, Y.8
  • 79
    • 0029760303 scopus 로고    scopus 로고
    • Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types
    • of special interest. In this report chimeric Bcl-2 molecules whose membrane-anchoring region was replaced with an anchoring region specific for mitochondria or endoplasmic reticulum endow different cells differentially with resistance to apoptosis, indicating site-specific effects of Bcl-2 within cells.
    • Zhu W, Cowie A, Wasfy GW, Penn LZ, Leber B, Andrews DW. Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types. of special interest EMBO J. 15:1996;4130-4141 In this report chimeric Bcl-2 molecules whose membrane-anchoring region was replaced with an anchoring region specific for mitochondria or endoplasmic reticulum endow different cells differentially with resistance to apoptosis, indicating site-specific effects of Bcl-2 within cells.
    • (1996) EMBO J , vol.15 , pp. 4130-4141
    • Zhu, W.1    Cowie, A.2    Wasfy, G.W.3    Penn, L.Z.4    Leber, B.5    Andrews, D.W.6
  • 80
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
    • of special interest. Here a detailed structural analysis of Bcl-xL reveals arrangement of α-helical regions in it which resembles the membrane translocation domain in bacterial toxins.
    • Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, et al. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. of special interest Nature. 381:1996;335-341 Here a detailed structural analysis of Bcl-xL reveals arrangement of α-helical regions in it which resembles the membrane translocation domain in bacterial toxins.
    • (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
  • 81
    • 1842332735 scopus 로고    scopus 로고
    • Bcl-x(L) forms an ion channel in synthetic lipid membranes
    • of special interest. References by Minn et al., 1997, Schendel et al., 1997 [82] and Schlesinger et al., 1997 [83] show that the Bcl-2 family members have an intrinsic ability to form pores in artificial membranes in vitro with somewhat different features for the anti- and pro-apoptotic members.
    • Minn AJ, Velez P, Schendel SL, Liang H, Muchmore SW, Fesik SW, Fill M, Thompson CB. Bcl-x(L) forms an ion channel in synthetic lipid membranes. of special interest Nature. 385:1997;353-357 References by Minn et al., 1997, Schendel et al., 1997 [82] and Schlesinger et al., 1997 [83] show that the Bcl-2 family members have an intrinsic ability to form pores in artificial membranes in vitro with somewhat different features for the anti- and pro-apoptotic members.
    • (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
  • 82
    • 0031008397 scopus 로고    scopus 로고
    • Channel formation by antiapoptotic protein Bcl-2
    • of special interest. References by Schendel et al., 1997, Minn et al., 1997 [81] and Schlesinger et al., 1997 [83] show that the Bcl-2 family members have an intrinsic ability to form pores in artificial membranes in vitro with somewhat different features for the anti- and pro-apoptotic members.
    • Schendel SL, Xie Z, Montal MO, Matsuyama S, Montal M, Reed JC. Channel formation by antiapoptotic protein Bcl-2. of special interest Proc Natl Acad Sci USA. 94:1997;5113-5118 References by Schendel et al., 1997, Minn et al., 1997 [81] and Schlesinger et al., 1997 [83] show that the Bcl-2 family members have an intrinsic ability to form pores in artificial membranes in vitro with somewhat different features for the anti- and pro-apoptotic members.
    • (1997) 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
  • 83
    • 0030779846 scopus 로고    scopus 로고
    • Comparison of the ion channel characteristics of proapoptotic BAX and antiapoptotic BCL-2
    • of special interest. References by Schlesinger et al., 1997, Minn et al., 1997 [81] and Schendel et al., 1997 [82] show that the Bcl-2 family members have an intrinsic ability to form pores in artificial membranes in vitro with somewhat different features for the anti- and pro-apoptotic members.
    • Schlesinger PH, Gross A, Yin XM, Yamamoto K, Saito M, Waksman G, Korsemeyer SJ. Comparison of the ion channel characteristics of proapoptotic BAX and antiapoptotic BCL-2. of special interest Proc Natl Acad Sci USA. 94:1997;11357-11362 References by Schlesinger et al., 1997, Minn et al., 1997 [81] and Schendel et al., 1997 [82] show that the Bcl-2 family members have an intrinsic ability to form pores in artificial membranes in vitro with somewhat different features for the anti- and pro-apoptotic members.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11357-11362
    • Schlesinger, P.H.1    Gross, A.2    Yin, X.M.3    Yamamoto, K.4    Saito, M.5    Waksman, G.6    Korsemeyer, S.J.7
  • 84
    • 9844257587 scopus 로고    scopus 로고
    • Inhibition of Bax channel-forming activity by Bcl-2
    • of special interest. The authors demonstrate the intrinsic channel-forming property of Bcl-2 family members differs from that of the pro-apoptotic ones. Bcl-2 can prevent channel formation by Bax in vitro.
    • Antonsson B, Conti F, Ciavatta A, 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 The authors demonstrate the intrinsic channel-forming property of Bcl-2 family members differs from that of the pro-apoptotic ones. Bcl-2 can prevent channel formation by Bax in vitro.
    • (1997) Science , vol.277 , pp. 370-372
    • Antonsson, B.1    Conti, F.2    Ciavatta, A.3    Montessuit, S.4    Lewis, S.5    Martinou, I.6    Bernasconi, L.7    Bernard, A.8    Mermod J-J9    Mazzei, G.10
  • 85
    • 0031993196 scopus 로고    scopus 로고
    • 1-ATPase proton pump is required for function of the proapoptotic protein Bax in yeast and mammalian cells
    • 1-ATPase proton pump is required for function of the proapoptotic protein Bax in yeast and mammalian cells. Mol Cell Biol. 1:1998;327-336.
    • (1998) Mol Cell Biol , vol.1 , pp. 327-336
    • Matsuyama, S.1    Xu, Q.2    Velours, J.3    Reed, J.C.4
  • 86
    • 0031993255 scopus 로고    scopus 로고
    • Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast
    • Xu Q, Reed JC. Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Mol Cell Biol. 1:1998;337-346.
    • (1998) Mol Cell Biol , vol.1 , pp. 337-346
    • Xu, Q.1    Reed, J.C.2
  • 87
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • L. Mutation of the phosphorylation site enhances the pro-apoptotic function of Bax.
    • L. Mutation of the phosphorylation site enhances the pro-apoptotic function of Bax.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 88
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • of special interest. References by del Peso et al., 1997, and Datta et al., 1997 [89] indicate that survival-factor-induced phosphorylation and inactivation of Bad is mediated by the serine/threonine protein kinase Akt which is activated by the phosphatidylinositide 3-kinase.
    • Del Peso L, Gonzalez Garcia M, Page C, Herrera R, Nunez G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. of special interest Science. 278:1997;687-689 References by del Peso et al., 1997, and Datta et al., 1997 [89] indicate that survival-factor-induced phosphorylation and inactivation of Bad is mediated by the serine/threonine protein kinase Akt which is activated by the phosphatidylinositide 3-kinase.
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 89
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • of special interest. References by Datta et al., 1997, and del Peso et al., 1997 [88] indicate that survival factor-induced phosphorylation and inactivation of Bad is mediated by the serine/threonine protein kinase Akt which is activated by the phosphatidylinositide 3-kinase.
    • Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, Greenberg ME. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. of special interest Cell. 91:1997;231-241 References by Datta et al., 1997, and del Peso et al., 1997 [88] indicate that survival factor-induced phosphorylation and inactivation of Bad is mediated by the serine/threonine protein kinase Akt which is activated by the phosphatidylinositide 3-kinase.
    • (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
  • 90
    • 0345498292 scopus 로고    scopus 로고
    • Bcl-2 targets the protein kinase Raf-1 to mitochondria
    • of special interest. The authors show that the serine/threonine protein kinase Raf-1, which can phosphorylate Bad, binds to Bcl-2 and, when recruited to the mitochondria, enhances survival.
    • Wang HG, Rapp UR, Reed JC. Bcl-2 targets the protein kinase Raf-1 to mitochondria. of special interest Cell. 87:1996;629-638 The authors show that the serine/threonine protein kinase Raf-1, which can phosphorylate Bad, binds to Bcl-2 and, when recruited to the mitochondria, enhances survival.
    • (1996) Cell , vol.87 , pp. 629-638
    • Wang, H.G.1    Rapp, U.R.2    Reed, J.C.3
  • 91
    • 0031041089 scopus 로고    scopus 로고
    • Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2
    • L even though it has no effect on their ability to bind to the pro-apoptotic Bcl-2 homolog, Bax. The findings suggest that the function of the anti-apoptotic Bcl-2 analogs is subject to down-regulation by phosphorylation, similarly to the function of the pro-apoptotic ones.
    • L even though it has no effect on their ability to bind to the pro-apoptotic Bcl-2 homolog, Bax. The findings suggest that the function of the anti-apoptotic Bcl-2 analogs is subject to down-regulation by phosphorylation, similarly to the function of the pro-apoptotic ones.
    • (1997) EMBO J , vol.16 , pp. 968-977
    • Chang, B.S.1    Minn, A.J.2    Muchmore, S.W.3    Fesik, S.W.4    Thompson, C.B.5
  • 92
    • 0032576757 scopus 로고    scopus 로고
    • Injected cytochrome c induces apoptosis
    • of outstanding interest. References by Zhivotovsky et al., 1998, and Rossé et al. [93] show that not only the release of cytochrome c but also the apoptotic effect which it has when released to the cytoplasm can be blocked by anti-apoptotic Bcl-2 analogs.
    • Zhivotovsky B, Orrenius S, Brustugun OT, Dskeland SO. Injected cytochrome c induces apoptosis. of outstanding interest Nature. 391:1998;449-450 References by Zhivotovsky et al., 1998, and Rossé et al. [93] show that not only the release of cytochrome c but also the apoptotic effect which it has when released to the cytoplasm can be blocked by anti-apoptotic Bcl-2 analogs.
    • (1998) Nature , vol.391 , pp. 449-450
    • Zhivotovsky, B.1    Orrenius, S.2    Brustugun, O.T.3    Dskeland, S.O.4
  • 93
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c
    • of outstanding interest. References by Rossé et al., 1998, and
    • Rossé T, Olivier R, Monney L, Rager M, Conus S, Fellay I, Jansen B, Borner C. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. of outstanding interest Nature. 391:1998;496-499 References by Rossé et al., 1998, and Zhivotovsky et al., 1998 [92] show that not only the release of cytochrome c but also the apoptotic effect which it has when released to the cytoplasm can be blocked by anti-apoptotic Bcl-2 analogs.
    • (1998) Nature , vol.391 , pp. 496-499
    • Rossé, T.1    Olivier, R.2    Monney, L.3    Rager, M.4    Conus, S.5    Fellay, I.6    Jansen, B.7    Borner, C.8
  • 94
    • 0032489390 scopus 로고    scopus 로고
    • L, and Apaf-1 form a ternary complex
    • L is found to bind to the CED-4 analog Apaf-1 and thereby block the activation of caspase-9 by the latter.
    • L is found to bind to the CED-4 analog Apaf-1 and thereby block the activation of caspase-9 by the latter.
    • (1998) J Biol Chem , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 95
    • 0030705234 scopus 로고    scopus 로고
    • P28 Bap31, a Bcl-2/Bcl-XL- And procaspase-8-associated protein in the endoplasmic reticulum
    • of special interest. The authors report the cloning of an ER-associated protein whose function may allow molecular changes that occur in the ER to trigger apoptosis and in the ER-associated Bcl-2 analogs to control this triggering.
    • Ng FW, Nguyen M, Kwan T, Branton PE, Nicholson DW, Cromlish JA, Shore GC. p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum. of special interest J Cell Biol. 139:1997;327-338 The authors report the cloning of an ER-associated protein whose function may allow molecular changes that occur in the ER to trigger apoptosis and in the ER-associated Bcl-2 analogs to control this triggering.
    • (1997) J Cell Biol , vol.139 , pp. 327-338
    • Ng, F.W.1    Nguyen, M.2    Kwan, T.3    Branton, P.E.4    Nicholson, D.W.5    Cromlish, J.A.6    Shore, G.C.7
  • 96
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • of special interest. References by Liu et al. 1997, Enari et al., 1998 [97] and Sakahira et al., 1998 [98] describe the isolation and cloning of an inhibitor of a DNase (the cloning of which is also described by Enari et al. and Sakahira et al.) which is apparently involved in apoptotic DNA degradation. Cleavage of this inhibitor by caspases set in motion the function of the DNase.
    • 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 special interest Cell. 89:1997;175-184 References by Liu et al. 1997, Enari et al., 1998 [97] and Sakahira et al., 1998 [98] describe the isolation and cloning of an inhibitor of a DNase (the cloning of which is also described by Enari et al. and Sakahira et al.) which is apparently involved in apoptotic DNA degradation. Cleavage of this inhibitor by caspases set in motion the function of the DNase.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 97
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis and its inhibitor ICAD
    • of outstanding interest. References by Enari et al., 1998, Liu et al., 1997 [96] and Sakahira et al., 1998 [98] describe the isolation and cloning of an inhibitor of a DNase (the cloning of which is also described by Enari et al. and Sakahira et al.) which is apparently involved in apoptotic DNA degradation. Cleavage of this inhibitor by caspases set in motion the function of the DNase.
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, Nagata S. A caspase-activated DNase that degrades DNA during apoptosis and its inhibitor ICAD. of outstanding interest Nature. 391:1998;43-50 References by Enari et al., 1998, Liu et al., 1997 [96] and Sakahira et al., 1998 [98] describe the isolation and cloning of an inhibitor of a DNase (the cloning of which is also described by Enari et al. and Sakahira et al.) which is apparently involved in apoptotic DNA degradation. Cleavage of this inhibitor by caspases set in motion the function of the DNase.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 98
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • of outstanding interest. References by Sakahira et al., 1998, Liu et al. 1997 [96] and Enari et al., 1998 [97] describe the isolation and cloning of an inhibitor of a DNase (the cloning of which is also described by Enari et al. and Sakahira et al.) which is apparently involved in apoptotic DNa degradation. Cleavage of this inhibitor by caspases set in motion the function of the DNase.
    • Sakahira H, Enari M, Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. of outstanding interest Nature. 391:1998;96-99 References by Sakahira et al., 1998, Liu et al. 1997 [96] and Enari et al., 1998 [97] describe the isolation and cloning of an inhibitor of a DNase (the cloning of which is also described by Enari et al. and Sakahira et al.) which is apparently involved in apoptotic DNa degradation. Cleavage of this inhibitor by caspases set in motion the function of the DNase.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3


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