메뉴 건너뛰기




Volumn 11, Issue 2, 1999, Pages 255-260

Apoptosis control by death and decoy receptors

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CELL RECEPTOR; FAS ANTIGEN; FAS LIGAND; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 0032910169     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80034-9     Document Type: Article
Times cited : (1171)

References (66)
  • 1
    • 0028929328 scopus 로고
    • Mechanisms and genes of cellular suicide
    • Steller H. Mechanisms and genes of cellular suicide. Science. 267:1995;1445-1449.
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 2
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson M.D., Weil M., Raff M.C. Programmed cell death in animal development. Cell. 88:1997;347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 3
    • 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
  • 4
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • A detailed review of signaling by death receptors; includes nonapoptotic functions.
    • Ashkenazi A., Dixit V.M. Death receptors: signaling and modulation. Science. 281:1998;1305-1308. A detailed review of signaling by death receptors; includes nonapoptotic functions.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 5
    • 0029075329 scopus 로고
    • Tumor necrosis factor ligand superfamily: Involvement in the pathology of malignant lymphomas
    • Gruss H.J., Dower S.K. 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
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 Ligand, a new member of the tumor necrosis factor receptor family
    • Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A. Induction of apoptosis by Apo-2 Ligand, a new member of the tumor necrosis factor receptor 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
  • 8
    • 0031239984 scopus 로고    scopus 로고
    • TRICK2, a new alternatively spliced receptor that transduces the cytotoxic signal from TRAIL
    • Screaton G.R., Mongkolsapaya J., Xu X.N., Cowper A.E., McMichael A.J., Bell J.I. TRICK2, a new alternatively spliced receptor that transduces the cytotoxic signal from TRAIL. Curr Biol. 7:1997;693-696.
    • (1997) Curr Biol , vol.7 , pp. 693-696
    • Screaton, G.R.1    Mongkolsapaya, J.2    Xu, X.N.3    Cowper, A.E.4    McMichael, A.J.5    Bell, J.I.6
  • 10
    • 0031974417 scopus 로고    scopus 로고
    • TRAIL/Apo-2-ligand-induced apoptosis in human T cells
    • Jeramias I., Herr I., Boehler T., Debatin K.M. TRAIL/Apo-2-ligand-induced apoptosis in human T cells. Eur J Immunol. 28:1998;143-152.
    • (1998) Eur J Immunol , vol.28 , pp. 143-152
    • Jeramias, I.1    Herr, I.2    Boehler, T.3    Debatin, K.M.4
  • 11
    • 0030155964 scopus 로고    scopus 로고
    • Activation of apoptosis by Apo-2 ligand is independent of FADD but blocked by CrmA
    • Marsters S., Pitti R., Donahue C., Ruppert S., Bauer K., Ashkenazi A. Activation of apoptosis by Apo-2 ligand is independent of FADD but blocked by CrmA. Curr Biol. 6:1996;750-752.
    • (1996) Curr Biol , vol.6 , pp. 750-752
    • Marsters, S.1    Pitti, R.2    Donahue, C.3    Ruppert, S.4    Bauer, K.5    Ashkenazi, A.6
  • 13
    • 0032169208 scopus 로고    scopus 로고
    • TNF-related apoptosis-inducing ligand (TRAIL) induces apoptosis in Fas ligand-resistant melanoma cells and mediates CD4 T cell killing of target cells
    • Thomas W.D., Hersey P. TNF-related apoptosis-inducing ligand (TRAIL) induces apoptosis in Fas ligand-resistant melanoma cells and mediates CD4 T cell killing of target cells. J Immunol. 161:1998;2195-2200.
    • (1998) J Immunol , vol.161 , pp. 2195-2200
    • Thomas, W.D.1    Hersey, P.2
  • 16
    • 0028353492 scopus 로고
    • The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death
    • Smith C.A., Farrah T., Goodwin R.G. The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell. 76:1994;959-962.
    • (1994) Cell , vol.76 , pp. 959-962
    • Smith, C.A.1    Farrah, T.2    Goodwin, R.G.3
  • 17
    • 0027275490 scopus 로고
    • A novel domain within the 55 kd TNF receptor signals cell death
    • Tartaglia L.A., Ayers T.M., Wong G.H.W., Goeddel D.V. A novel domain within the 55 kd TNF receptor signals cell death. Cell. 74:1993;845-853.
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayers, T.M.2    Wong, G.H.W.3    Goeddel, D.V.4
  • 18
    • 0027281373 scopus 로고
    • A novel protein domain required for apoptosis: Mutational analysis of human Fas antigen
    • Itoh N., Nagata S. A novel protein domain required for apoptosis: mutational analysis of human Fas antigen. J Biol Chem. 268:1993;10932-10937.
    • (1993) J Biol Chem , vol.268 , pp. 10932-10937
    • Itoh, N.1    Nagata, S.2
  • 20
    • 0030466894 scopus 로고    scopus 로고
    • Apo3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-κB
    • Marsters S., Sheridan J., Donahue C., Pitti R., Gray C., Goddard A., Bauer K.D., Ashkenazi A. Apo3, 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.1    Sheridan, J.2    Donahue, C.3    Pitti, R.4    Gray, C.5    Goddard, A.6    Bauer, K.D.7    Ashkenazi, A.8
  • 23
    • 0030940538 scopus 로고    scopus 로고
    • LARD: A new lymphoid-specific death domain containing receptor regulated by alternative pre-mRNA splicing
    • Screaton G., Xu X., Olsen A., Cowper A., Tan R., McMichael A., Bell J.I. LARD: a new lymphoid-specific death domain containing receptor regulated by alternative pre-mRNA splicing. Proc Natl Acad Sci USA. 94:1997;4615-4619.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4615-4619
    • Screaton, G.1    Xu, X.2    Olsen, A.3    Cowper, A.4    Tan, R.5    McMichael, A.6    Bell, J.I.7
  • 25
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a new death domain-containing receptor for TRAIL
    • Pan G., Dixit V.M. An antagonist decoy receptor and a new death domain-containing receptor for TRAIL. Science. 277:1997;815-818.
    • (1997) Science , vol.277 , pp. 815-818
    • Pan, G.1    Dixit, V.M.2
  • 34
    • 0032489353 scopus 로고    scopus 로고
    • TRUNDD, a new member of the TRAIL receptor family that antagonizes TRAIL signaling
    • Pan G., Ni J., Yu G.L., Wei Y.F., Dixit V.M. TRUNDD, a new member of the TRAIL receptor family that antagonizes TRAIL signaling. FEBS Lett. 424:1998;41-45.
    • (1998) FEBS Lett , vol.424 , pp. 41-45
    • Pan, G.1    Ni, J.2    Yu, G.L.3    Wei, Y.F.4    Dixit, V.M.5
  • 35
    • 0031414749 scopus 로고    scopus 로고
    • The novel receptor TRAIL-R4 induces NF-κB and protects aginst TRAIL-mediated apoptosis, yet retains an incomplete death domain
    • Degli-Esposti M.A., Dougall W.C., Smolak P.J., Waugh J.Y., Smith C.A., Goodwin R.G. The novel receptor TRAIL-R4 induces NF-κB and protects aginst TRAIL-mediated apoptosis, yet retains an incomplete death domain. Immunity. 7:1997;813-820.
    • (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
  • 37
    • 17444424930 scopus 로고    scopus 로고
    • A secreted decoy receptor that blocks apoptosis-induction by FasL was discovered on the basis of homology to the TNFR family. The gene encoding the decoy is amplified in about half of 35 primary lung and colon cancers studied, which suggests that this decoy receptor may well be involved in immune-evasion by tumors
    • Pitti, R., Marsters, S.A., Lawrence, D.A., Roy, M., Kischkel, F.C., Dowd, P., Huang, A., Donahue, C.J., Sherwood, S.W., Baldwin, D.T. et al.: Genomic amplification of a decoy receptor for Fas ligand in lung and colon cancer. 1998, 396:699-703. A secreted decoy receptor that blocks apoptosis-induction by FasL was discovered on the basis of homology to the TNFR family. The gene encoding the decoy is amplified in about half of 35 primary lung and colon cancers studied, which suggests that this decoy receptor may well be involved in immune-evasion by tumors.
    • (1998) Genomic Amplification of a Decoy Receptor for Fas Ligand in Lung and Colon Cancer , vol.396 , pp. 699-703
    • Pitti, R.1    Marsters, S.A.2    Lawrence, D.A.3    Roy, M.4    Kischkel, F.C.5    Dowd, P.6    Huang, A.7    Donahue, C.J.8    Sherwood, S.W.9    Baldwin, D.T.10
  • 38
    • 0031472042 scopus 로고    scopus 로고
    • Cell death: TRAIL and its receptors
    • Golstein P. Cell death: TRAIL and its receptors. Curr Biol. 7:1997;750-753.
    • (1997) Curr Biol , vol.7 , pp. 750-753
    • Golstein, P.1
  • 40
    • 0032563275 scopus 로고    scopus 로고
    • Identification and functional characterization of DR6, a novel death domain-containing TNF receptor
    • DR6 was discovered on the basis of homology to the TNFR family. DR6 is unique in that it appears to bind the adaptor TRADD but not FADD. This is in contrast to Fas, which binds FADD but not TRADD, and to TNFR1, which binds FADD immediately through TRADD.
    • Pan G., Bauer J.H., Haridas V., Wang S., Liu D., Yu G., Vincenz C., Aggarwal B.B., Ni J., Dixit V.M. Identification and functional characterization of DR6, a novel death domain-containing TNF receptor. FEBS Lett. 431:1998;351-356. DR6 was discovered on the basis of homology to the TNFR family. DR6 is unique in that it appears to bind the adaptor TRADD but not FADD. This is in contrast to Fas, which binds FADD but not TRADD, and to TNFR1, which binds FADD immediately through TRADD.
    • (1998) FEBS Lett , vol.431 , pp. 351-356
    • Pan, G.1    Bauer, J.H.2    Haridas, V.3    Wang, S.4    Liu, D.5    Yu, G.6    Vincenz, C.7    Aggarwal, B.B.8    Ni, J.9    Dixit, V.M.10
  • 41
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science. 281:1998;1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 42
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • 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. Nature. 391:1998;43-50.
    • (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
  • 43
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H., Enari M., Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature. 391:1998;96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 44
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X., Zou H., Slaughter C., Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 45
  • 47
    • 0008206988 scopus 로고    scopus 로고
    • TRAF2 is essential for JNK but not NF-κB activation and regulates lymphocyte proliferation and survival
    • Lee S.Y., Reichlin A., Santana A., Sokol K.A., Nussenzweig M.C., Choi W. TRAF2 is essential for JNK but not NF-κB activation and regulates lymphocyte proliferation and survival. Immunity. 7:1997;703-713.
    • (1997) Immunity , vol.7 , pp. 703-713
    • Lee, S.Y.1    Reichlin, A.2    Santana, A.3    Sokol, K.A.4    Nussenzweig, M.C.5    Choi, W.6
  • 48
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1
    • Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature. 385:1997;540-544.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.L.1    Boldin, M.P.2    Kovalenko, A.V.3    Wallach, D.4
  • 49
    • 0032541652 scopus 로고    scopus 로고
    • Docking IκB kinases
    • Scheidereit C. Docking IκB kinases. Nature. 395:1998;225-226.
    • (1998) Nature , vol.395 , pp. 225-226
    • Scheidereit, C.1
  • 51
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • By knocking out the FADD gene in mice, the authors establish that FADD is essential for apoptosis induction by Fas, TNFR1 and DR3. There are conflicting reports on the ability of the dominant-negative FADD mutants to block apoptosis-induction by Apo2L. This study shows that transfection of FADD-deficient cells with Apo2L receptor DR4 induced apoptosis; thus, FADD is not required for apoptosis signaling through DR4.
    • Yeh W.C., Pompa J.L., McCurrach M.E., Shu H.B., Elia A.J., Shahinian A., Ng M., Wakeham A., Khoo W., Mitchell K.et al. FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science. 279:1998;1954-1958. By knocking out the FADD gene in mice, the authors establish that FADD is essential for apoptosis induction by Fas, TNFR1 and DR3. There are conflicting reports on the ability of the dominant-negative FADD mutants to block apoptosis-induction by Apo2L. This study shows that transfection of FADD-deficient cells with Apo2L receptor DR4 induced apoptosis; thus, FADD is not required for apoptosis signaling through DR4.
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    Pompa, J.L.2    McCurrach, M.E.3    Shu, H.B.4    Elia, A.J.5    Shahinian, A.6    Ng, M.7    Wakeham, A.8    Khoo, W.9    Mitchell, K.10
  • 52
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes
    • Transgenic mice expressing a dominant-negative FADD mutation in T cells show a defect in Fas-induced apoptosis as expected. Suprisingly, these mice also show a defect in the proliferative response to their T cells to antigenic stimulation, which implicates FADD in regulating not only death but also proliferation of cells.
    • Newton K., Harris A.W., Bath M.L., Smith K.G.C., Strasser A. A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes. EMBO J. 17:1998;706-718. Transgenic mice expressing a dominant-negative FADD mutation in T cells show a defect in Fas-induced apoptosis as expected. Suprisingly, these mice also show a defect in the proliferative response to their T cells to antigenic stimulation, which implicates FADD in regulating not only death but also proliferation of cells.
    • (1998) EMBO J , vol.17 , pp. 706-718
    • Newton, K.1    Harris, A.W.2    Bath, M.L.3    Smith, K.G.C.4    Strasser, A.5
  • 53
    • 0032499138 scopus 로고    scopus 로고
    • P53-dependent impairment of T-cell proliferation in FADD dominant-negative transgenic mice
    • This study provides evidence that the dominant-negative FADD impairs activation-induced proliferation of thyrmocytes through a mechanism that appears to involve the p53 tumor suppressor gene.
    • Zornig M., Hueber A.O., Evan G. p53-dependent impairment of T-cell proliferation in FADD dominant-negative transgenic mice. Curr Biol. 8:1998;467-470. This study provides evidence that the dominant-negative FADD impairs activation-induced proliferation of thyrmocytes through a mechanism that appears to involve the p53 tumor suppressor gene.
    • (1998) Curr Biol , vol.8 , pp. 467-470
    • Zornig, M.1    Hueber, A.O.2    Evan, G.3
  • 54
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • By deleting the FADD gene in mice, the authors demonstrate that FADD is essential for apoptosis-induction by Fas and TNFR1. Although Fas or TNFR1 knockouts in the mouse are not lethal FADD gene knockout is, which suggests that FADD has additional roles besides signaling downstream of these latter receptors. Rescue of the mice by the breeding with RAG-1 knockout mice revealed a defect in T cell proliferation in response to antigenic stimulation, which is consistent with the results from transgenic mice expressing dominant-negative FADD.
    • Zhang J., Cado D., Chen A., Kabra N.H., Winoto A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature. 392:1998;296-300. By deleting the FADD gene in mice, the authors demonstrate that FADD is essential for apoptosis-induction by Fas and TNFR1. Although Fas or TNFR1 knockouts in the mouse are not lethal FADD gene knockout is, which suggests that FADD has additional roles besides signaling downstream of these latter receptors. Rescue of the mice by the breeding with RAG-1 knockout mice revealed a defect in T cell proliferation in response to antigenic stimulation, which is consistent with the results from transgenic mice expressing dominant-negative FADD.
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 55
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Caspase-8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally
    • Biochemmical studies have implicated the capase-8 in death signaling by several death receptors. By deleting the mouse capase-8 gene, the authors show that capase-8 plays an essential role in apoptosis-induction by Fas, TNFR1 and DR3.
    • Varfolomeev E.E., Schuchmann M., Luria V., Chiannilkulchai N., Beckmann J.S., Mett I.L., Rebrikov D., Brodianski V.M., Kemper O.C., Kollet O.et al. Targeted disruption of the mouse Caspase-8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity. 9:1998;267-276. Biochemmical studies have implicated the capase-8 in death signaling by several death receptors. By deleting the mouse capase-8 gene, the authors show that capase-8 plays an essential role in apoptosis-induction by Fas, TNFR1 and DR3.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3    Chiannilkulchai, N.4    Beckmann, J.S.5    Mett, I.L.6    Rebrikov, D.7    Brodianski, V.M.8    Kemper, O.C.9    Kollet, O.10
  • 56
    • 0032505127 scopus 로고    scopus 로고
    • Essential requirement for caspase 8/FLICE in the initiation of the Fas-induced apoptotic cascade
    • The authors isolated a mutant human T cell line that is deficient in capase-8. Using this cell line, they show that in the absence of capase-8, Fas-induced apoptosis is abolished completely; suprisingly TNF-induced apoptosis is only partially prevented.
    • Juo P., Kuo C.J., Yuan J., Blenis J. Essential requirement for caspase 8/FLICE in the initiation of the Fas-induced apoptotic cascade. Curr Biol. 8:1998;1001-1008. The authors isolated a mutant human T cell line that is deficient in capase-8. Using this cell line, they show that in the absence of capase-8, Fas-induced apoptosis is abolished completely; suprisingly TNF-induced apoptosis is only partially prevented.
    • (1998) Curr Biol , vol.8 , pp. 1001-1008
    • Juo, P.1    Kuo, C.J.2    Yuan, J.3    Blenis, J.4
  • 57
    • 15644364847 scopus 로고    scopus 로고
    • Essential contribution of caspase-3/CPP32 to apoptosis and its associated nuclear changes
    • Results with caspase-3-deficient cells implicate this capase in the nuclear changes that occur during apoptosis induced by Fas-ligation and other apototic stimuli.
    • Woo M., Hakem R., Soengas M.S., Duncan G.S., Shahinian A., Kagi D., Hakem A., McCurrach M., Khoo W., Kaufman S.A.et al. Essential contribution of caspase-3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev. 12:1998;806-819. Results with caspase-3-deficient cells implicate this capase in the nuclear changes that occur during apoptosis induced by Fas-ligation and other apototic stimuli.
    • (1998) Genes Dev , vol.12 , pp. 806-819
    • Woo, M.1    Hakem, R.2    Soengas, M.S.3    Duncan, G.S.4    Shahinian, A.5    Kagi, D.6    Hakem, A.7    McCurrach, M.8    Khoo, W.9    Kaufman, S.A.10
  • 58
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 60
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome C release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome C release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 61
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 62
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F., Alvarez-Bolado G., Meyer B.I., Roth K.A., Gruss P. Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell. 94:1998;727-737.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 66
    • 0032531817 scopus 로고    scopus 로고
    • DEDD, a novel death effector domian-containing protein, targeted to the nucleus
    • DEDD was identified by virtue of its homology to the death effector domains of FADD and capase-8. Unlike other adaptor molecules, DEDD moves from the cytoplasm to the nucleus upon Fas-ligation; this, together with an ability to inhibit transcription in a reconstituted system, suggests a possible molecular mechanism for shutting down gene expression in cells which are undergoing apoptotic death.
    • Stegh A.H., Schickling O., Ehret A., Scaffidi C., Peterhansel C., Hofmann T.G., Grummt I., Krammer P.H., Peter M.E. DEDD, a novel death effector domian-containing protein, targeted to the nucleus. EMBO J. 17:1998;5974-5986. DEDD was identified by virtue of its homology to the death effector domains of FADD and capase-8. Unlike other adaptor molecules, DEDD moves from the cytoplasm to the nucleus upon Fas-ligation; this, together with an ability to inhibit transcription in a reconstituted system, suggests a possible molecular mechanism for shutting down gene expression in cells which are undergoing apoptotic death.
    • (1998) EMBO J , vol.17 , pp. 5974-5986
    • Stegh, A.H.1    Schickling, O.2    Ehret, A.3    Scaffidi, C.4    Peterhansel, C.5    Hofmann, T.G.6    Grummt, I.7    Krammer, P.H.8    Peter, M.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.