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Volumn 8, Issue 10, 2002, Pages 543-560

Peptides in apoptosis research

Author keywords

Anticancer drugs; Apaf 1; Apoptosis; Apoptosis regulators; Apoptosome; Bcl 2; Caspases; IAPs; Programmed cell death; Smac

Indexed keywords

ANTINEOPLASTIC AGENT; APOPTOSIS INHIBITOR; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BENZYLOXYCARBONYLASPARTYLGLUTAMYLVALYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE 10; CASPASE 2; CASPASE 3; CASPASE 3 INHIBITOR; CASPASE 5; CASPASE 7; CASPASE 8; CASPASE 9; CASPASE INHIBITOR; CELL SURFACE RECEPTOR; CYTOKINE; ENZYME ACTIVATOR; ENZYME PRECURSOR; INTERLEUKIN 1BETA CONVERTING ENZYME; PROTEIN BAD; PROTEIN BAK; PROTEIN BCL 2; PROTEIN BCL X; PROTEIN BCL XL; PROTEIN BID; PROTEINASE INHIBITOR; REGULATOR PROTEIN; SYNTHETIC PEPTIDE; TRANSCRIPTION FACTOR; UNINDEXED DRUG; CASPASE; ENZYME INHIBITOR; PEPTIDE;

EID: 0036810764     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.414     Document Type: Review
Times cited : (11)

References (149)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 1972; 26: 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0014575182 scopus 로고
    • Programmed cell death. Activation of lysis by a mechanism involving the synthesis of protein
    • Lockshin RA. Programmed cell death. Activation of lysis by a mechanism involving the synthesis of protein. J. Insect Physiol. 1969; 15: 1505-1516.
    • (1969) J. Insect Physiol , vol.15 , pp. 1505-1516
    • Lockshin, R.A.1
  • 3
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux DV, Korsmeyer SJ. Cell death in development. Cell 1999; 96: 245-254.
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.V.1    Korsmeyer, S.J.2
  • 4
    • 0028929328 scopus 로고
    • Mechanisms and genes of cellular suicide
    • Steller H. Mechanisms and genes of cellular suicide. Science 1995; 267: 1445-1449.
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 5
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature 2000; 407: 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 7
    • 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
  • 8
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson MP. Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 2000; 1: 120-129.
    • (2000) Nat. Rev. Mol. Cell Biol , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 9
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • Johnstone RW, Ruefli AA, Lowe SW. Apoptosis: a link between cancer genetics and chemotherapy. Cell 2002: 108: 153-164.
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 10
    • 0033636355 scopus 로고    scopus 로고
    • Drug discovery opportunities from apoptosis research
    • Reed JC, Tomaselli KJ. Drug discovery opportunities from apoptosis research. Curr. Opin. Biotechnol. 2000; 11: 586-592.
    • (2000) Curr. Opin. Biotechnol , vol.11 , pp. 586-592
    • Reed, J.C.1    Tomaselli, K.J.2
  • 11
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • Nicholson DW. From bench to clinic with apoptosis-based therapeutic agents. Nature 2000; 407: 810-816.
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, D.W.1
  • 12
    • 0028326952 scopus 로고
    • An evolutionary perspective on apoptosis
    • Vaux DL, Haecker G, Strasser A. An evolutionary perspective on apoptosis. Cell 1994; 76: 777-779.
    • (1994) Cell , vol.76 , pp. 777-779
    • Vaux, D.L.1    Haecker, G.2    Strasser, A.3
  • 13
    • 0034652154 scopus 로고    scopus 로고
    • Evolutionary conservation of apoptosis mechanisms: Lepidopteran and baculoviral inhibitor of apoptosis proteins are inhibitors of mammalian caspase-9
    • Huang Q, Deveraux QL, Maeda S, Salvesen GS, Stennicke HR, Hammock BD, Reed JC. Evolutionary conservation of apoptosis mechanisms: lepidopteran and baculoviral inhibitor of apoptosis proteins are inhibitors of mammalian caspase-9. Proc. Natl Acad. Sci. USA 2000; 97: 1427-1432.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1427-1432
    • Huang, Q.1    Deveraux, Q.L.2    Maeda, S.3    Salvesen, G.S.4    Stennicke, H.R.5    Hammock, B.D.6    Reed, J.C.7
  • 14
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science 1998; 281: 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 15
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw WC, Martins LM, Kaufmann SH. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 1999; 68: 383-424.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 16
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: Functions and regulation of caspases
    • Chang HY, Yang X. Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 2000; 64: 821-846.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 17
    • 0035937420 scopus 로고    scopus 로고
    • Cell death inhibition: Keeping caspases in check
    • Goyal L. Cell death inhibition: keeping caspases in check. Cell 2001; 104: 805-808.
    • (2001) Cell , vol.104 , pp. 805-808
    • Goyal, L.1
  • 18
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding
    • Chai J, Wu Q, Shiozaki E, Srinivasula SM, Alnemri ES, Shi Y. Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding. Cell 2001; 107: 399-407.
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1    Wu, Q.2    Shiozaki, E.3    Srinivasula, S.M.4    Alnemri, E.S.5    Shi, Y.6
  • 26
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain
    • Huang Y, Park YC, Rich RL, Segal D, Myszka DG, Wu H. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell 2001; 104: 781-790.
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4    Myszka, D.G.5    Wu, H.6
  • 29
    • 0034622936 scopus 로고    scopus 로고
    • Caspase-8 specificity probed at subsite S(4): Crystal structure of the caspase-8-Z-DEVD-cho complex
    • Blanchard H, Donepudi M, Tschopp M, Kodandapani L, Wu JC, Grutter MG. Caspase-8 specificity probed at subsite S(4): crystal structure of the caspase-8-Z-DEVD-cho complex. J. Mol. Biol. 2000; 302: 9-16.
    • (2000) J. Mol. Biol , vol.302 , pp. 9-16
    • Blanchard, H.1    Donepudi, M.2    Tschopp, M.3    Kodandapani, L.4    Wu, J.C.5    Grutter, M.G.6
  • 30
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 31
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 1993; 74: 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 35
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM, Korsmeyer SJ. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 1999; 13: 1899-1911.
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 36
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an 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 an apoptotic protease cascade. Cell 1997; 91: 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
  • 37
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation
    • Acehan D, Jiang X, Morgan DG, Heuser JE, Wang X, Akey CW. Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation. Mol. Cell 2002; 9: 423-432.
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 38
    • 0027537461 scopus 로고
    • An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif
    • Crook NE, Clem RJ, Miller LK. An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif. J. Virol. 1993; 67: 2168-2174.
    • (1993) J. Virol , vol.67 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 39
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux QL, Takahashi R, Salvesen GS, Reed JC. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 1997; 388: 300-304.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 40
    • 0033215040 scopus 로고    scopus 로고
    • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    • Deveraux QL, Leo E, Stennicke HR, Welsh K, Salvesen GS, Reed JC. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J. 1999; 18: 5242-5251.
    • (1999) EMBO J , vol.18 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicke, H.R.3    Welsh, K.4    Salvesen, G.S.5    Reed, J.C.6
  • 41
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins - Suppressors of apoptosis
    • Deveraux QL, Reed JC. IAP family proteins - suppressors of apoptosis. Genes Dev. 1999; 13: 239-252.
    • (1999) Genes Dev , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 42
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102: 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 44
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams JM, Cory S. The Bcl-2 protein family: Arbiters of cell survival. Science 1998; 281: 1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 45
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science 1998; 281: 1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 48
    • 0032568954 scopus 로고    scopus 로고
    • Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c
    • Kuwana T, Smith JJ, Muzio M, Dixit V, Newmeyer DD, Kornbluth S. Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c. J. Biol. Chem. 1998; 273: 16589-16594.
    • (1998) J. Biol. Chem , vol.273 , pp. 16589-16594
    • Kuwana, T.1    Smith, J.J.2    Muzio, M.3    Dixit, V.4    Newmeyer, D.D.5    Kornbluth, S.6
  • 49
    • 0034280579 scopus 로고    scopus 로고
    • Signal transduction mediated by Bid, a pro-death Bcl-2 family proteins, connects the death receptor and mitochondria apoptosis pathways
    • Yin XM. Signal transduction mediated by Bid, a pro-death Bcl-2 family proteins, connects the death receptor and mitochondria apoptosis pathways. Cell Res. 2000; 10: 161-167.
    • (2000) Cell Res , vol.10 , pp. 161-167
    • Yin, X.M.1
  • 50
    • 0030897988 scopus 로고    scopus 로고
    • Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases
    • Margolin N, Raybuck SA, Wilson KP, Chen W, Fox T, Gu Y, Livingston DJ. Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases. J. Biol. Chem. 1997; 272: 7223-7228.
    • (1997) J. Biol. Chem , vol.272 , pp. 7223-7228
    • Margolin, N.1    Raybuck, S.A.2    Wilson, K.P.3    Chen, W.4    Fox, T.5    Gu, Y.6    Livingston, D.J.7
  • 55
    • 0022508987 scopus 로고
    • A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma
    • Humphries MJ, Olden K, Yamada KM. A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells. Science 1986: 233: 467-470.
    • (1986) Cells Science , vol.233 , pp. 467-470
    • Humphries, M.J.1    Olden, K.2    Yamada, K.M.3
  • 56
    • 0028670833 scopus 로고
    • Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels
    • Brooks PC, Montgomery AM, Rosenfeld M, Reisfeld RA, Hu T, Klier G, Cheresh DA. Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. Cell 1994; 79: 1157-1164.
    • (1994) Cell , vol.79 , pp. 1157-1164
    • Brooks, P.C.1    Montgomery, A.M.2    Rosenfeld, M.3    Reisfeld, R.A.4    Hu, T.5    Klier, G.6    Cheresh, D.A.7
  • 64
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme
    • Ray CA, Black RA, Kronheim SR, Greenstreet TA, Sleath PR, Salvesen GS, Pickup DJ. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell 1992; 69: 597-604.
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvesen, G.S.6    Pickup, D.J.7
  • 65
    • 0026344133 scopus 로고
    • Prevention of apoptosis by a baculovirus gene during infection of insect cells
    • Clem RJ, Fechheimer M, Miller LK. Prevention of apoptosis by a baculovirus gene during infection of insect cells. Science 1991; 254: 1388-1390.
    • (1991) Science , vol.254 , pp. 1388-1390
    • Clem, R.J.1    Fechheimer, M.2    Miller, L.K.3
  • 66
    • 0029583176 scopus 로고
    • Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death
    • Hay BA, Wassarman DA, Rubin GM. Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death. Cell 1995; 83: 1253-1262.
    • (1995) Cell , vol.83 , pp. 1253-1262
    • Hay, B.A.1    Wassarman, D.A.2    Rubin, G.M.3
  • 67
    • 0032078249 scopus 로고    scopus 로고
    • Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts
    • Uren AG, Coulson EJ, Vaux DL. Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts. Trends Biochem. Sci. 1998; 23: 159-162.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 159-162
    • Uren, A.G.1    Coulson, E.J.2    Vaux, D.L.3
  • 68
    • 0032410818 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) and their emerging role in cancer
    • LaCasse EC, Baird S, Korneluk RG, MacKenzie AE. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene 1998; 17: 3247-3259.
    • (1998) Oncogene , vol.17 , pp. 3247-3259
    • LaCasse, E.C.1    Baird, S.2    Korneluk, R.G.3    MacKenzie, A.E.4
  • 72
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai JJ, Du CY, Wu JW, Kyin S, Wang XD, Shi YG. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 2000; 406: 855-862.
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.J.1    Du, C.Y.2    Wu, J.W.3    Kyin, S.4    Wang, X.D.5    Shi, Y.G.6
  • 77
    • 0035039678 scopus 로고    scopus 로고
    • A structural view of mitochondria-mediated apoptosis
    • Shi Y. A structural view of mitochondria-mediated apoptosis. Nat Struct Biol. 2001; 8: 394-401.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 394-401
    • Shi, Y.1
  • 80
    • 0030954209 scopus 로고    scopus 로고
    • The CARD domain: A new apoptotic signalling motif
    • Hofmann K, Bucher P, Tschopp J. The CARD domain: a new apoptotic signalling motif. Trends Biochem. Sci. 1997; 22: 155-156.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 155-156
    • Hofmann, K.1    Bucher, P.2    Tschopp, J.3
  • 81
    • 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 1997; 90: 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
  • 82
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H, Li Y, Liu X, Wang X. An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 1999; 274: 11 549-11 556.
    • (1999) J. Biol. Chem , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 83
    • 0030741528 scopus 로고    scopus 로고
    • Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system
    • Kluck RM, Martin SJ, Hoffman BM, Zhou JS, Green DR, Newmeyer DD. Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. EMBO J. 1997; 16: 4639-4649.
    • (1997) EMBO J , vol.16 , pp. 4639-4649
    • Kluck, R.M.1    Martin, S.J.2    Hoffman, B.M.3    Zhou, J.S.4    Green, D.R.5    Newmeyer, D.D.6
  • 84
    • 0035918306 scopus 로고    scopus 로고
    • A mutational epitope for cytochrome C binding to the apoptosis protease activation factor-1
    • Yu T, Wang X, Purring-Koch C, Wei Y, McLendon GL. A mutational epitope for cytochrome C binding to the apoptosis protease activation factor-1. J. Biol. Chem. 2001; 276: 13 034-13 038.
    • (2001) J. Biol. Chem , vol.276 , pp. 13034-13038
    • Yu, T.1    Wang, X.2    Purring-Koch, C.3    Wei, Y.4    McLendon, G.L.5
  • 86
    • 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 1998; 94: 481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 87
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists
    • McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell 1999; 96: 625-634.
    • (1999) Cell , vol.96 , pp. 625-634
    • McDonnell, J.M.1    Fushman, D.2    Milliman, C.L.3    Korsmeyer, S.J.4    Cowburn, D.5
  • 88
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • Chou JJ, Li HL, Salvesen GS, Yuan JY, Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell 1999; 96: 615-624.
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.L.2    Salvesen, G.S.3    Yuan, J.Y.4    Wagner, G.5
  • 90
    • 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, Ishibashi Y, Ohta S, Morikawa K. Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family. J. Biol. Chem. 1997; 272: 27 886-27 892.
    • (1997) J. Biol. Chem , vol.272 , pp. 27886-27892
    • Aritomi, M.1    Kunishima, N.2    Inohara, N.3    Ishibashi, Y.4    Ohta, S.5    Morikawa, K.6
  • 91
    • 0033713002 scopus 로고    scopus 로고
    • Structure of bax. Coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, Tjandra N. Structure of bax. Coregulation of dimer formation and intracellular localization. Cell 2000; 103: 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 95
    • 0027525536 scopus 로고
    • Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence
    • Nguyen M, Millar DG, Yong VW, Korsmeyer SJ, Shore GC. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 1993; 268: 25 265-25 268.
    • (1993) J. Biol. Chem , vol.268 , pp. 25265-25268
    • Nguyen, M.1    Millar, D.G.2    Yong, V.W.3    Korsmeyer, S.J.4    Shore, G.C.5
  • 96
    • 0028242493 scopus 로고
    • Assembly of Bcl-2 into microsomal and outer mitochondrial membranes
    • Janiak F, Leber B, Andrews DW. Assembly of Bcl-2 into microsomal and outer mitochondrial membranes. J. Biol. Chem. 1994; 269: 9842-9849.
    • (1994) J. Biol. Chem , vol.269 , pp. 9842-9849
    • Janiak, F.1    Leber, B.2    Andrews, D.W.3
  • 99
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved Bid targets mitochondria and is required for cytochrome c release, while Bcl-xL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross A, Yin XM, Wang K, Wei MC, Jockel J, Milliman C, Erdjument-Bromage H, Tempst P, Korsmeyer SJ. Caspase cleaved Bid targets mitochondria and is required for cytochrome c release, while Bcl-xL prevents this release but not tumor necrosis factor-R1/Fas death. J. Biol. Chem. 1999; 274: 1156-1163.
    • (1999) J. Biol. Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3    Wei, M.C.4    Jockel, J.5    Milliman, C.6    Erdjument-Bromage, H.7    Tempst, P.8    Korsmeyer, S.J.9
  • 100
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, Bcl-X(L) sequester BH3 domain-only molecules preventing Bax- and Bak-mediated mitochondrial apoptosis
    • Cheng EH, Wei MC, Weiler S, Flavell RA, Mak TW, Lindsten T, Korsmeyer SJ. BCL-2, Bcl-X(L) sequester BH3 domain-only molecules preventing Bax- and Bak-mediated mitochondrial apoptosis. Mol. Cell 2001; 8: 705-711.
    • (2001) Mol. Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 102
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol. Cell. Biol. 2000; 20: 929-935.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 108
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B, Montessuit S, Lauper S, Eskes R, Martinou JC. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem J. 2000; 345: 271-278.
    • (2000) Biochem. J , vol.345 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 110
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, Tsujimoto Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl Acad. Sci. USA 1998; 95: 14 681-14 686.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 112
    • 0033559998 scopus 로고    scopus 로고
    • Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement
    • Priault M, Chaudhuri B, Clow A, Camougrand N, Manon S. Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement. Eur. J. Biochem. 1999; 260: 684-691.
    • (1999) Eur. J. Biochem , vol.260 , pp. 684-691
    • Priault, M.1    Chaudhuri, B.2    Clow, A.3    Camougrand, N.4    Manon, S.5
  • 113
    • 0034697365 scopus 로고    scopus 로고
    • Electro-physiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu S, Ide T, Yanagida T, Tsujimoto Y. Electro-physiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J. Biol. Chem. 2000; 275: 12 321-12 325.
    • (2000) J. Biol. Chem , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 114
    • 0034618269 scopus 로고    scopus 로고
    • Bax and Bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator
    • Shimizu S, Shinohara Y, Tsujimoto Y. Bax and Bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator. Oncogene 2000; 19: 4309-4318.
    • (2000) Oncogene , vol.19 , pp. 4309-4318
    • Shimizu, S.1    Shinohara, Y.2    Tsujimoto, Y.3
  • 116
    • 0035181345 scopus 로고    scopus 로고
    • Synthetic peptides and non-peptidic molecules as probes of structure and function of Bcl-2 family proteins and modulators of apoptosis
    • Liu D, Huang Z. Synthetic peptides and non-peptidic molecules as probes of structure and function of Bcl-2 family proteins and modulators of apoptosis. Apoptosis 2001; 6: 453-462.
    • (2001) Apoptosis , vol.6 , pp. 453-462
    • Liu, D.1    Huang, Z.2
  • 117
    • 0033785313 scopus 로고    scopus 로고
    • Apoptosis and cancer: Strategies for integrating programmed cell death
    • Reed CJ. Apoptosis and cancer: strategies for integrating programmed cell death. Semin. Hematol. 2000; 37: 9-16.
    • (2000) Semin. Hematol , vol.37 , pp. 9-16
    • Reed, C.J.1
  • 119
    • 0032481346 scopus 로고    scopus 로고
    • The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4
    • Huang DCS, Adams JM, Cory S. The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. EMBO J. 1998; 17: 1029-1039.
    • (1998) EMBO J , vol.17 , pp. 1029-1039
    • Huang, D.C.S.1    Adams, J.M.2    Cory, S.3
  • 120
    • 0029789955 scopus 로고    scopus 로고
    • Evidence for alpha-helical conformation of an essential N-terminal region in the human Bcl2 protein
    • Lee LC, Hunter JJ, Mujeeb A, Turck C, Parslow TG. Evidence for alpha-helical conformation of an essential N-terminal region in the human Bcl2 protein. J. Biol. Chem. 1996; 271: 23 284-23 288.
    • (1996) J. Biol. Chem , vol.271 , pp. 23284-23288
    • Lee, L.C.1    Hunter, J.J.2    Mujeeb, A.3    Turck, C.4    Parslow, T.G.5
  • 121
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S, Konishi A, Kodama T, Tsujimoto Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc. Natl Acad. Sci. USA 2000; 97: 3100-3105.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 122
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M, Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 1999; 399: 483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 123
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
    • Green M, Loewenstein PM. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 1988; 55: 1179-1188.
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 124
    • 0032556686 scopus 로고    scopus 로고
    • Neuroprotection with Bcl-2(20-34) peptide against trauma
    • Panizzon KL, Shin D, Frautschy S, Wallis PA. Neuroprotection with Bcl-2(20-34) peptide against trauma. Neuroreport 1998; 9: 4131-4136.
    • (1998) Neuroreport , vol.9 , pp. 4131-4136
    • Panizzon, K.L.1    Shin, D.2    Frautschy, S.3    Wallis, P.A.4
  • 125
    • 0029928885 scopus 로고    scopus 로고
    • A peptide sequence from Bax that converts Bcl-2 into an activator of apoptosis
    • Hunter JJ, Parslow TG. A peptide sequence from Bax that converts Bcl-2 into an activator of apoptosis. J. Biol. Chem. 1996; 271: 8521-8524.
    • (1996) J. Biol. Chem , vol.271 , pp. 8521-8524
    • Hunter, J.J.1    Parslow, T.G.2
  • 128
    • 0028812606 scopus 로고
    • Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins
    • Boyd JM, Gallo GJ, Elangovan B, Houghton AB, Malstrom S, Avery BJ, Ebb RG, Subramanian T, Chittenden T, Lutz RJ. Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins. Oncogene 1995; 11: 1921-1928.
    • (1995) Oncogene , vol.11 , pp. 1921-1928
    • Boyd, J.M.1    Gallo, G.J.2    Elangovan, B.3    Houghton, A.B.4    Malstrom, S.5    Avery, B.J.6    Ebb, R.G.7    Subramanian, T.8    Chittenden, T.9    Lutz, R.J.10
  • 129
    • 0029032660 scopus 로고
    • Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax
    • Hanada M, Aime-Sempe C, Sato T, Reed JC. Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax. J. Biol. Chem. 1995; 270: 11 962-11 969.
    • (1995) J. Biol. Chem , vol.270 , pp. 11962-11969
    • Hanada, M.1    Aime-Sempe, C.2    Sato, T.3    Reed, J.C.4
  • 130
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz V, Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 1995; 245: 275-296.
    • (1995) J. Mol. Biol , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 131
    • 0035886913 scopus 로고    scopus 로고
    • Design and evolution of a miniature Bcl-2 binding protein
    • Chin JW, Schepartz A. Design and evolution of a miniature Bcl-2 binding protein. Angew. Chem. 2001: 40: 3806-3809.
    • (2001) Angew. Chem , vol.40 , pp. 3806-3809
    • Chin, J.W.1    Schepartz, A.2
  • 132
    • 0020584172 scopus 로고
    • Conformational flexibility in a small globular hormone: X-ray analysis of avian pancreatic polypeptide at 0.98-Å resolution
    • Glover I, Haneef I, Pitts J, Wood S, Moss D, Tickle I, Blundell T. Conformational flexibility in a small globular hormone: x-ray analysis of avian pancreatic polypeptide at 0.98-Å resolution. Biopolymers 1983; 22: 293-304.
    • (1983) Biopolymers , vol.22 , pp. 293-304
    • Glover, I.1    Haneef, I.2    Pitts, J.3    Wood, S.4    Moss, D.5    Tickle, I.6    Blundell, T.7
  • 133
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi D, Calvet S, Trembleau A, Brunissen A, Chassaing G, Prochiantz A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 1996; 271: 18 188-18 193.
    • (1996) J. Biol. Chem , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 134
    • 0033531926 scopus 로고    scopus 로고
    • Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases
    • Holinger EP, Chittenden T, Lutz RJ. Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. J. Biol. Chem. 1999; 274: 13 298-13 304.
    • (1999) J. Biol. Chem , vol.274 , pp. 13298-13304
    • Holinger, E.P.1    Chittenden, T.2    Lutz, R.J.3
  • 137
    • 0034681110 scopus 로고    scopus 로고
    • Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity
    • Shimizu S, Tsujimoto Y. Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proc. Natl Acad. Sci. USA 2000; 97: 577-582.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 577-582
    • Shimizu, S.1    Tsujimoto, Y.2
  • 138
    • 0035851110 scopus 로고    scopus 로고
    • BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability
    • Polster BM, Kinnally KW, Fiskum G. BH3 death domain peptide induces cell type-selective mitochondrial outer membrane permeability. J. Biol. Chem. 2001; 276: 37 887-37 894.
    • (2001) J. Biol. Chem , vol.276 , pp. 37887-37894
    • Polster, B.M.1    Kinnally, K.W.2    Fiskum, G.3
  • 139
    • 0031871330 scopus 로고    scopus 로고
    • A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal
    • Isenmann S, Khew-Goodall Y, Gamble J, Vadas M, Wattenberg BW. A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal. Mol. Biol. Cell 1998; 9: 1649-1660.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1649-1660
    • Isenmann, S.1    Khew-Goodall, Y.2    Gamble, J.3    Vadas, M.4    Wattenberg, B.W.5
  • 140
    • 0034661510 scopus 로고    scopus 로고
    • Targeting and insertion of C-terminally anchored proteins to the mitochondrial outer membrane is specific and saturable but does not strictly require ATP or molecular chaperones
    • Lan L, Isenmann S, Wattenberg BW. Targeting and insertion of C-terminally anchored proteins to the mitochondrial outer membrane is specific and saturable but does not strictly require ATP or molecular chaperones. Biochem. J. 2000; 349: 611-621.
    • (2000) Biochem. J , vol.349 , pp. 611-621
    • Lan, L.1    Isenmann, S.2    Wattenberg, B.W.3
  • 141
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A, Smith CL, Hsu YT, Youle RJ. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 1999; 18: 2330-2341.
    • (1999) EMBO J , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 142
    • 0040185619 scopus 로고    scopus 로고
    • Study of the secondary structure of the C-terminal domain of the antiapoptotic protein bcl-2 and its interaction with model membranes
    • Martinez-Senac MM, Corbalan-Garcia S, Gomez-Fernandez JC. Study of the secondary structure of the C-terminal domain of the antiapoptotic protein bcl-2 and its interaction with model membranes. Biochemistry 2000; 39: 7744-7752.
    • (2000) Biochemistry , vol.39 , pp. 7744-7752
    • Martinez-Senac, M.M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 143
    • 0035928830 scopus 로고    scopus 로고
    • Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes
    • Martinez-Senac MM, Corbalan-Garcia S, Gomez-Fernandez JC. Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes. Biochemistry 2001; 40: 9983-9992.
    • (2001) Biochemistry , vol.40 , pp. 9983-9992
    • Martinez-Senac, M.M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 144
    • 0036220239 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the pro-apoptotic protein bak and its interaction with model membranes
    • Martinez-Senac MM, Corbalan-Garcia S, Gomez-Fernandez JC. The structure of the C-terminal domain of the pro-apoptotic protein bak and its interaction with model membranes. Biophys. J. 2002; 82: 233-243.
    • (2002) Biophys. J , vol.82 , pp. 233-243
    • Martinez-Senac, M.M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 145
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B, Montessuit S, Sanchez B, Martinou JC. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J. Biol. Chem. 2001; 276: 11 615-11 623.
    • (2001) J. Biol. Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 147
    • 0029742260 scopus 로고    scopus 로고
    • Grim, a novel cell death gene in Drosophila
    • Chen P, Nordstrom W, Gish B, Abrams JM. Grim, a novel cell death gene in Drosophila. Genes Dev. 1996; 10: 1773-1782.
    • (1996) Genes Dev , vol.10 , pp. 1773-1782
    • Chen, P.1    Nordstrom, W.2    Gish, B.3    Abrams, J.M.4
  • 148
    • 0029910069 scopus 로고    scopus 로고
    • Apoptotic activity of REAPER is distinct from signaling by the tumor necrosis factor receptor 1 death domain
    • Chen P, Lee P, Otto L, Abrams J. Apoptotic activity of REAPER is distinct from signaling by the tumor necrosis factor receptor 1 death domain. J. Biol. Chem. 1996; 271: 25 735-25 737.
    • (1996) J. Biol. Chem , vol.271 , pp. 25735-25737
    • Chen, P.1    Lee, P.2    Otto, L.3    Abrams, J.4


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