메뉴 건너뛰기




Volumn 4, Issue SUPPL. 1, 1998, Pages

Dysregulation of apoptosis in cancer

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN BAX; PROTEIN BCL 2;

EID: 0031843732     PISSN: 10814442     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (43)

References (70)
  • 1
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science 1995;267:1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 2
    • 0021821903 scopus 로고
    • Involvement of the bcl-2 gene in human follicular lymphoma
    • Tsujimoto Y, Crossman J, Jaffe E et al. Involvement of the bcl-2 gene in human follicular lymphoma. Science 1985;228:1440-1443.
    • (1985) Science , vol.228 , pp. 1440-1443
    • Tsujimoto, Y.1    Crossman, J.2    Jaffe, E.3
  • 3
    • 0022546957 scopus 로고
    • Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma
    • Tsujimoto Y, Croce CM. Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc Nad Acad Sci USA 1986;83:5214-4218.
    • (1986) Proc Nad Acad Sci USA , vol.83 , pp. 5214-14218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 4
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • Reed JC. Bcl-2 and the regulation of programmed cell death. J Cell Biol 1994;124:1-6.
    • (1994) J Cell Biol , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 5
    • 0028958030 scopus 로고
    • Bcl-2: Prevention of apoptosis as a mechanism of drug resistance
    • Reed JC. Bcl-2: Prevention of apoptosis as a mechanism of drug resistance. Hematol Oncol Clin North Am 1995;9:451-474.
    • (1995) Hematol Oncol Clin North am , vol.9 , pp. 451-474
    • Reed, J.C.1
  • 6
    • 0028292480 scopus 로고
    • Identification of a p53-dependent negative response element in the Bcl-2 gene
    • Miyashita T, Harigai M, Hanada M et al. Identification of a p53-dependent negative response element in the Bcl-2 gene. Cancer Res 1994;54:3131-3135.
    • (1994) Cancer Res , vol.54 , pp. 3131-3135
    • Miyashita, T.1    Harigai, M.2    Hanada, M.3
  • 7
    • 0028963244 scopus 로고
    • Regulation of apoptosis induced by the retinoid N-(4-hydroxyphenyl) retinamide and effect of deregulated bcl-2
    • Delia D, Aiello A, Formelli F et al. Regulation of apoptosis induced by the retinoid N-(4-hydroxyphenyl) retinamide and effect of deregulated bcl-2. Blood 1995;85:359-367.
    • (1995) Blood , vol.85 , pp. 359-367
    • Delia, D.1    Aiello, A.2    Formelli, F.3
  • 8
    • 0343578822 scopus 로고
    • Cell death and the bcl-2 gene
    • Reed JC. Cell death and the bcl-2 gene. Contemp Oncol 1994;4: 29-42.
    • (1994) Contemp Oncol , vol.4 , pp. 29-42
    • Reed, J.C.1
  • 9
    • 0028972616 scopus 로고
    • Regulation of apoptosis by Bcl-2 family proteins and its role in cancer and chemoristance
    • Reed JC. Regulation of apoptosis by Bcl-2 family proteins and its role in cancer and chemoristance. Curr Opin Oncol 1995;7:541-546.
    • (1995) Curr Opin Oncol , vol.7 , pp. 541-546
    • Reed, J.C.1
  • 10
    • 0028973310 scopus 로고
    • Upregulation of bax protein levels in neurons following cerebral ischemia
    • Krajewski S, Mai JK, Krajewska M et al. Upregulation of bax protein levels in neurons following cerebral ischemia. J Neurosci 1995;15:6364-6376.
    • (1995) J Neurosci , vol.15 , pp. 6364-6376
    • Krajewski, S.1    Mai, J.K.2    Krajewska, M.3
  • 11
    • 0027944228 scopus 로고
    • Induction of BAX by genotoxic stress in human cells correlates with normal p53 status and apoptosis
    • Zhan Q, Fan S, Bae I et al. Induction of BAX by genotoxic stress in human cells correlates with normal p53 status and apoptosis. Oncogene 1994;9:3743-3751.
    • (1994) Oncogene , vol.9 , pp. 3743-3751
    • Zhan, Q.1    Fan, S.2    Bae, I.3
  • 12
    • 0028335717 scopus 로고
    • Tumor suppressor p53 is a regulator of BCL-2 and BAX in gene expression in vitro and in vivo
    • Miyashita T, Krajewski S, Krajewska M et al. Tumor suppressor p53 is a regulator of BCL-2 and BAX in gene expression in vitro and in vivo. Oncogene 1994;9:1799-1805.
    • (1994) Oncogene , vol.9 , pp. 1799-1805
    • Miyashita, T.1    Krajewski, S.2    Krajewska, M.3
  • 13
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of human BAX gene
    • Miyashita T, Reed JC. Tumor suppressor p53 is a direct transcriptional activator of human BAX gene. Cell 1995;80:293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 14
    • 0029671112 scopus 로고    scopus 로고
    • γ-Radiation induces upregulation of Bax protein and apoptosis in radiosensitive cells in vivo
    • Kitada S, Krajewski S, Miyashita T et al. γ-Radiation induces upregulation of Bax protein and apoptosis in radiosensitive cells in vivo. Oncogene 1996;12:187-192.
    • (1996) Oncogene , vol.12 , pp. 187-192
    • Kitada, S.1    Krajewski, S.2    Miyashita, T.3
  • 15
    • 0029045784 scopus 로고
    • Reduced expression of pro-apoptotic gene Bax is associated with poor response rates to combination chemotherapy and shorter survival in women with metastatic breast adenocarcinoma
    • Krajewski S, Blomvqvist C, Franssili K et al. Reduced expression of pro-apoptotic gene Bax is associated with poor response rates to combination chemotherapy and shorter survival in women with metastatic breast adenocarcinoma. Cancer Res 1995;55:4471-4478.
    • (1995) Cancer Res , vol.55 , pp. 4471-4478
    • Krajewski, S.1    Blomvqvist, C.2    Franssili, K.3
  • 16
    • 0031030334 scopus 로고    scopus 로고
    • Immunohistochemical analysis of Bax and Bcl-2 in p53-immunopositive breast cancers
    • Krajewski S, Thor AD, Edgerton SM et al. Immunohistochemical analysis of Bax and Bcl-2 in p53-immunopositive breast cancers. Clin Cancer Res 1996;3:199-208.
    • (1996) Clin Cancer Res , vol.3 , pp. 199-208
    • Krajewski, S.1    Thor, A.D.2    Edgerton, S.M.3
  • 17
    • 0030162560 scopus 로고    scopus 로고
    • Balancing cell life and death: Bax, apoptosis, and breast cancer
    • Reed JC. Balancing cell life and death: Bax, apoptosis, and breast cancer. J Clin Invest 1996;97:2403-2404.
    • (1996) J Clin Invest , vol.97 , pp. 2403-2404
    • Reed, J.C.1
  • 18
    • 0029945789 scopus 로고    scopus 로고
    • Elevated expression of Bd-X and reduced Bak in primary colorectal adenocarcinomas
    • Krajewska M, Moss S, Krajewski S et al. Elevated expression of Bd-X and reduced Bak in primary colorectal adenocarcinomas. Cancer Res 1996;56:2422-2427.
    • (1996) Cancer Res , vol.56 , pp. 2422-2427
    • Krajewska, M.1    Moss, S.2    Krajewski, S.3
  • 19
    • 0028206341 scopus 로고
    • BH1 and BH2 domains of bcl-2 are required for inhibition of apoptosis and heterodimerization with bax
    • Yin XM, Oltvai ZN, Korsmeyer SJ. BH1 and BH2 domains of bcl-2 are required for inhibition of apoptosis and heterodimerization with bax. Nature 1994;369:321-333.
    • (1994) Nature , vol.369 , pp. 321-333
    • Yin, X.M.1    Oltvai, Z.N.2    Korsmeyer, S.J.3
  • 20
    • 0030026865 scopus 로고    scopus 로고
    • Bax-independent inhibition of apoptosis by Bcl-Xl
    • Cheng EH-Y, Levine B, Boise LH et al. Bax-independent inhibition of apoptosis by Bcl-Xl. Nature 1996;379:554-556.
    • (1996) Nature , vol.379 , pp. 554-556
    • Cheng, E.H.-Y.1    Levine, B.2    Boise, L.H.3
  • 21
    • 0031436251 scopus 로고    scopus 로고
    • Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells
    • Zha H, Reed JC. Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells. J Biol Chem 1997;272:31482-31488.
    • (1997) J Biol Chem , vol.272 , pp. 31482-31488
    • Zha, H.1    Reed, J.C.2
  • 22
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med 1997;3:614-620.
    • (1997) Nat Med , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 23
    • 0029927422 scopus 로고    scopus 로고
    • The role of proteases during apoptosis
    • Patel T, Gores GJ, Kaufmann SH. The role of proteases during apoptosis. FASEB J 1996;10:587-597.
    • (1996) FASEB J , vol.10 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 24
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin SJ, Green DR. Protease activation during apoptosis: death by a thousand cuts? Cell 1995;82:349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 25
    • 0030702084 scopus 로고    scopus 로고
    • Caspase: Intracellular signaling by proteolysis
    • Salvesen G, Dixit VM. Caspase: intracellular signaling by proteolysis. Cell 1997;91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.1    Dixit, V.M.2
  • 27
    • 0029787268 scopus 로고    scopus 로고
    • Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases
    • Orth K, O'Rourke K, Salvesen GS et al. Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases. J Biol Chem 1996;271:20977-20980.
    • (1996) J Biol Chem , vol.271 , pp. 20977-20980
    • Orth, K.1    O'Rourke, K.2    Salvesen, G.S.3
  • 28
    • 0344053451 scopus 로고    scopus 로고
    • Activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
    • Fernandes-Alnemri T, Armstrong RC, Krebs J et al. Activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc Natl Acad Sci USA 1996;93:7464-7469.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7464-7469
    • Fernandes-Alnemri, T.1    Armstrong, R.C.2    Krebs, J.3
  • 29
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995;81:505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 30
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin MP, Varfolomeev EE, Pancer Z et al. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J Biol Chem 1995;270:7795-7798.
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3
  • 31
    • 15844412409 scopus 로고    scopus 로고
    • Flice, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (FAS/APO-1) death inducing signalling complex
    • Muzio M, Chinnaiyan AM, Kischkel FC et al. Flice, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (FAS/APO-1) death inducing signalling complex. Cell 1996;85: 817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 32
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/ APO-I- And TNF receptor-induced cell death
    • Boldin MP, Goncharov TM, Goltsev YV et al. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/ APO-I- and TNF receptor-induced cell death. Cell 1996;85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3
  • 33
    • 0029905073 scopus 로고    scopus 로고
    • Molecular ordering of the fas-apoptic pathway: The fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases
    • Srinivasula S, Ahmad M, Fernandes-Alenri T et al. Molecular ordering of the fas-apoptic pathway: The fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc Natl Acad Sci USA 1996;93: 14486-14491.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14486-14491
    • Srinivasula, S.1    Ahmad, M.2    Fernandes-Alenri, T.3
  • 34
    • 0031018914 scopus 로고    scopus 로고
    • FLICE-induced apoptosis in a cell-free system
    • Muzio M, Salvesen GS, Sizit VM. FLICE-induced apoptosis in a cell-free system. J Biol Chem 1997;272:2952-2956.
    • (1997) J Biol Chem , vol.272 , pp. 2952-2956
    • Muzio, M.1    Salvesen, G.S.2    Sizit, V.M.3
  • 35
    • 0030605023 scopus 로고    scopus 로고
    • Mitochondria and programmed cell death: Back to the future
    • Petit PX, Susin S-A, Zamzami N et al. Mitochondria and programmed cell death: back to the future. FEBS Lett 1996;396:7-13.
    • (1996) FEBS Lett , vol.396 , pp. 7-13
    • Petit, P.X.1    Susin, S.-A.2    Zamzami, N.3
  • 36
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome C
    • Liu X, Kim CN, Yang J et al. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome C. Cell 1996;86:147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3
  • 37
    • 0030745646 scopus 로고    scopus 로고
    • A human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X et al. A human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997;90:405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3
  • 38
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X Bhalla K et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 1997;275:1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 39
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR et al. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 1997;275:1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3
  • 40
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bel-XL, an inhibitor of programmed cell death
    • Muchmore SW, Sattler M, Liang H. X-ray and NMR structure of human Bel-XL, an inhibitor of programmed cell death. Nature 1996;381:335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1    Sattler, M.2    Liang, H.3
  • 41
    • 0030822420 scopus 로고    scopus 로고
    • Crystal structure of rat Bcl-XL: Implications for the function of the Bcl-2 protein family
    • Aritomi M, Kunishima N, Inohara N et al. Crystal structure of rat Bcl-XL: implications for the function of the Bcl-2 protein family. J Biol Chem 1997;272:27886-27892.
    • (1997) J Biol Chem , vol.272 , pp. 27886-27892
    • Aritomi, M.1    Kunishima, N.2    Inohara, N.3
  • 42
    • 0022349252 scopus 로고
    • Requirements for the translocation of diphtheria toxin fragment a across lipid membranes
    • Donovan JJ, Simon MI, Montal M: Requirements for the translocation of diphtheria toxin fragment A across lipid membranes. J Biol Chem 1985;260:8817-8823.
    • (1985) J Biol Chem , vol.260 , pp. 8817-8823
    • Donovan, J.J.1    Simon, M.I.2    Montal, M.3
  • 43
    • 9844257587 scopus 로고    scopus 로고
    • Inhibition of Bax channel-forming activity by Bcl-2
    • Antonsson B, Conti F, Ciavatta A et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 1997;277:370-372.
    • (1997) Science , vol.277 , pp. 370-372
    • Antonsson, B.1    Conti, F.2    Ciavatta, A.3
  • 44
    • 0031019739 scopus 로고    scopus 로고
    • Interaction between the C. elegans cell-death regulators CED-9 and CED-4
    • Spector MS, Desnoyers S, Heoppner DJ et al. Interaction between the C. elegans cell-death regulators CED-9 and CED-4. Nature 1997;385:653-656.
    • (1997) Nature , vol.385 , pp. 653-656
    • Spector, M.S.1    Desnoyers, S.2    Heoppner, D.J.3
  • 45
    • 0031020227 scopus 로고    scopus 로고
    • Interaction and regulation of subcellular localization of CED-4 by CED-9
    • Wu D, Wallen HD, Nunez G. Interaction and regulation of subcellular localization of CED-4 by CED-9. Science 1997;275: 1126-1129.
    • (1997) Science , vol.275 , pp. 1126-1129
    • Wu, D.1    Wallen, H.D.2    Nunez, G.3
  • 46
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death
    • Chinnaiyan AM, O'Rourke K, Lane BR et al. Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death. Science 1997;275:1122-1126.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, B.R.3
  • 47
    • 0031194404 scopus 로고    scopus 로고
    • Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis
    • Seshagiri S, Miller L. Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis. Curr Biol 1997;7:455-460.
    • (1997) Curr Biol , vol.7 , pp. 455-460
    • Seshagiri, S.1    Miller, L.2
  • 48
    • 0030785790 scopus 로고    scopus 로고
    • The central executioner of apoptosis: Multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- And ceramide-induced apoptosis
    • Susin S, Zamzami N, Castedo M et al. The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis. J Exp Med 1997;186:25-37.
    • (1997) J Exp Med , vol.186 , pp. 25-37
    • Susin, S.1    Zamzami, N.2    Castedo, M.3
  • 49
    • 0344250039 scopus 로고    scopus 로고
    • The permeability transition pore complex: A target for apoptosis regulation by caspases and Bcl-2-related proteins
    • in press
    • Marzo I, Brenner C, Zamzami N et al. The permeability transition pore complex: a target for apoptosis regulation by caspases and Bcl-2-related proteins. Nat Med 1997 (in press).
    • Nat Med , pp. 1997
    • Marzo, I.1    Brenner, C.2    Zamzami, N.3
  • 50
    • 0030949563 scopus 로고    scopus 로고
    • Resistance of cultured peripheral T cells towards activation-induced cell death involves a lack of recruitment of FLICE (MACH/caspase 8) to die CD95 death-inducing signalling complex
    • Peter ME, Kischkel FC, Scheuerpflug CG et al. Resistance of cultured peripheral T cells towards activation-induced cell death involves a lack of recruitment of FLICE (MACH/caspase 8) to die CD95 death-inducing signalling complex. Eur J Immunol 1997; 27:1207-1212.
    • (1997) Eur J Immunol , vol.27 , pp. 1207-1212
    • Peter, M.E.1    Kischkel, F.C.2    Scheuerpflug, C.G.3
  • 51
    • 0029935682 scopus 로고    scopus 로고
    • Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug induced apoptosis in leukemia cells
    • Friesen C, Herr I, Krammer PH et al. Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug induced apoptosis in leukemia cells. Nat Med 1996;2:574-577.
    • (1996) Nat Med , vol.2 , pp. 574-577
    • Friesen, C.1    Herr, I.2    Krammer, P.H.3
  • 52
    • 0030808385 scopus 로고    scopus 로고
    • Thymineless death in colon carcinoma cells is mediated via fas signaling
    • Houghton JA, Haarwood FG, Tillman DM. Thymineless death in colon carcinoma cells is mediated via fas signaling. Proc Natl Acad Sci USA 1997;94:8144-8149.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8144-8149
    • Houghton, J.A.1    Haarwood, F.G.2    Tillman, D.M.3
  • 53
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed JC. Double identity for proteins of the Bcl-2 family. Nature 1997;387:773-776.
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.C.1
  • 55
    • 0345498292 scopus 로고    scopus 로고
    • Bcl-2 targets the protein kinase Raf-1 to mitochondria
    • Wang HG, Rapp UR, Reed JC. Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell 1996;87:629-638.
    • (1996) Cell , vol.87 , pp. 629-638
    • Wang, H.G.1    Rapp, U.R.2    Reed, J.C.3
  • 56
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • Del Peso L, González-Garcia M, Page C et al. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 1997;278:687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    González-Garcia, M.2    Page, C.3
  • 57
    • 0030871891 scopus 로고    scopus 로고
    • BAG-1 modulates the chaperone activity of Hsp70/Hsc70
    • Takayama S, Bimston DN, Matsuzawa S et al. BAG-1 modulates the chaperone activity of Hsp70/Hsc70. EMBOJ 1997;16:4887-4896.
    • (1997) EMBOJ , vol.16 , pp. 4887-4896
    • Takayama, S.1    Bimston, D.N.2    Matsuzawa, S.3
  • 58
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: A novel Bcl-2 binding protein with anti-cell death activity
    • Takayama S, Sato T, Krajewski S et al. Cloning and functional analysis of BAG-1: a novel Bcl-2 binding protein with anti-cell death activity. Cell 1995;80:279-284.
    • (1995) Cell , vol.80 , pp. 279-284
    • Takayama, S.1    Sato, T.2    Krajewski, S.3
  • 59
    • 0030614915 scopus 로고    scopus 로고
    • Structure of Bcl-xL-Bak peptide complex: Recognition between regulators of apoptosis
    • Sattler M, Liang H, Nettesheim D et al. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 1997;275:983-986.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3
  • 60
    • 1842332735 scopus 로고    scopus 로고
    • L forms an ion channel in synthetic lipid membranes
    • L forms an ion channel in synthetic lipid membranes. Nature 1997;385:353-357.
    • (1997) Nature , vol.385 , pp. 353-357
    • Minn, A.J.1    Velez, P.2    Schendel, S.L.3
  • 61
    • 0031008397 scopus 로고    scopus 로고
    • Channel formation by anti-apoptotic protein Bcl-2
    • Schendel SL, Xie Z, Montal MO et al. Channel formation by anti-apoptotic protein Bcl-2. Proc Natl Acad Sci USA 1997;94:5113-5118.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5113-5118
    • Schendel, S.L.1    Xie, Z.2    Montal, M.O.3
  • 62
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell death proteases
    • Deveraux Q, Takahashi R, Salvesen GS et al. X-linked IAP is a direct inhibitor of cell death proteases. Nature 1997;388:300-303.
    • (1997) Nature , vol.388 , pp. 300-303
    • Deveraux, Q.1    Takahashi, R.2    Salvesen, G.S.3
  • 63
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N, Deveraux QL, Takahashi R et al. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J 1997; 16:6914-6925.
    • (1997) EMBO J , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3
  • 64
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini G, Adida C, Altieri D. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997;3: 917-921.
    • (1997) Nat Med , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.3
  • 65
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Imler M, Thome M, Hahne M et al. Inhibition of death receptor signals by cellular FLIP. Nature 1997;388:190-195.
    • (1997) Nature , vol.388 , pp. 190-195
    • Imler, M.1    Thome, M.2    Hahne, M.3
  • 66
    • 0030810981 scopus 로고    scopus 로고
    • FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas-TNFR1-induced apoptosis
    • Srinivasula SM, Ahmad M, Ottilie S et al. FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas-TNFR1-induced apoptosis. J Biol Chem 1997;272:18542-18545.
    • (1997) J Biol Chem , vol.272 , pp. 18542-18545
    • Srinivasula, S.M.1    Ahmad, M.2    Ottilie, S.3
  • 67
    • 0029882175 scopus 로고    scopus 로고
    • Programmed cell death in peripheral lymphocytes from HIV-infected persons
    • Gougeon M-L, Lecoeur H, Dulioust A et al. Programmed cell death in peripheral lymphocytes from HIV-infected persons. J Immunol 1996;156:3509-3520.
    • (1996) J Immunol , vol.156 , pp. 3509-3520
    • Gougeon, M.-L.1    Lecoeur, H.2    Dulioust, A.3
  • 68
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with Fas
    • Sato T, Irie S, Kitada S et al. FAP-1: A protein tyrosine phosphatase that associates with Fas. Science 1995;268:411-415.
    • (1995) Science , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3
  • 69
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang X, Khosravi-Far R, Chang HY et al. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 1997;89:1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3
  • 70
    • 0030888599 scopus 로고    scopus 로고
    • The molecular interaction of Fas and FAP-1: A tripeptide blocker of human Fas interaction with FAP-1 promotes Fas-induced apoptosis
    • Yanagisawa J, Takahashi M, Kanki H et al. The molecular interaction of Fas and FAP-1: a tripeptide blocker of human Fas interaction with FAP-1 promotes Fas-induced apoptosis. J Biol Chem 1997;272:8539-8545.
    • (1997) J Biol Chem , vol.272 , pp. 8539-8545
    • Yanagisawa, J.1    Takahashi, M.2    Kanki, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.