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Volumn 11, Issue 4, 2006, Pages 459-471

Cell death regulation by B-cell lymphoma protein

Author keywords

Active site; Bcl 2 family; Hematopoietic stem cells; Homology model; Inducible expression; Mutants

Indexed keywords

B CELL LYMPHOMA PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; MUTANT PROTEIN; PROTEIN BCL 2; UNCLASSIFIED DRUG;

EID: 33646395652     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-006-5702-1     Document Type: Article
Times cited : (30)

References (100)
  • 1
    • 0022971142 scopus 로고
    • Cloning and structural analysis of cDNAs for Bcl-2 and a hybrid Bcl-2/immunoglobulin transcript resulting from the t (14;18) translocation
    • Cleary ML, Smith SD, Sklar J. Cloning and structural analysis of cDNAs for Bcl-2 and a hybrid Bcl-2/immunoglobulin transcript resulting from the t (14;18) translocation. Cell 1986; 47: 19-28.
    • (1986) Cell , vol.47 , pp. 19-28
    • Cleary, M.L.1    Smith, S.D.2    Sklar, J.3
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281(5381): 1309-1312.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 5
    • 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
  • 7
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: Regulators of apoptosis or of mitochondrial homeostasis?
    • Heiden VMG, Thompson CB. Bcl-2 proteins: Regulators of apoptosis or of mitochondrial homeostasis? Nat Cell Biol 1999; 1(8): E209-E216.
    • (1999) Nat Cell Biol , vol.1 , Issue.8
    • Heiden, V.M.G.1    Thompson, C.B.2
  • 8
    • 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
  • 10
    • 0028167978 scopus 로고
    • The protein Bcl-2α does not require membrane attachment, but two conserved domains to suppress apoptosis
    • Borner C, Martinou I, Mattmann C. The protein Bcl-2α does not require membrane attachment, but two conserved domains to suppress apoptosis. J Cell Biol 1994; 126: 1059-1068.
    • (1994) J Cell Biol , vol.126 , pp. 1059-1068
    • Borner, C.1    Martinou, I.2    Mattmann, C.3
  • 11
    • 0033549844 scopus 로고    scopus 로고
    • Cloning and characterization of human BAG-1 gene promoter: Upregulation by tumor-derived p 53 mutants
    • Yang X, Tang SC, Pater A. Cloning and characterization of human BAG-1 gene promoter: Upregulation by tumor-derived p 53 mutants. Oncogene 1999; 18: 4546-4553.
    • (1999) Oncogene , vol.18 , pp. 4546-4553
    • Yang, X.1    Tang, S.C.2    Pater, A.3
  • 12
    • 0029942921 scopus 로고    scopus 로고
    • The p53 binding protein 53BP2 also interacts with Bcl-2 and impedes cell cycle progression at G2/M
    • Naumouski L, Cleary ML. The p53 binding protein 53BP2 also interacts with Bcl-2 and impedes cell cycle progression at G2/M. Mol Cell Biol 1996; 16(7): 3884-3892.
    • (1996) Mol Cell Biol , vol.16 , Issue.7 , pp. 3884-3892
    • Naumouski, L.1    Cleary, M.L.2
  • 13
    • 0343457526 scopus 로고    scopus 로고
    • WS Reversible phosphorylation of Bcl-2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A
    • Deng X, Ito T, Carr B, Mumby M, May Jr. WS Reversible phosphorylation of Bcl-2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A. J Biol Chem 1998; 273: 34157-34163.
    • (1998) J Biol Chem , vol.273 , pp. 34157-34163
    • Deng, X.1    Ito, T.2    Carr, B.3    Mumby, M.4    May, Jr.5
  • 14
    • 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
  • 15
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of Bcl-2 to a Bax-like death effector by caspases
    • Cheng EH, Kirsch DG, Clem RJ. Conversion of Bcl-2 to a Bax-like death effector by caspases. Science 1997; 278: 1966-1968.
    • (1997) Science , vol.278 , pp. 1966-1968
    • Cheng, E.H.1    Kirsch, D.G.2    Clem, R.J.3
  • 16
    • 0033603460 scopus 로고    scopus 로고
    • Bcl-2 and caspase inhibition cooperate to inhibit tumor necrosis factor-α-induced cell death in a Bcl-2 cleavage-independent fashion
    • Bryan WJ, Lawrence HB. Bcl-2 and caspase inhibition cooperate to inhibit tumor necrosis factor-α-induced cell death in a Bcl-2 cleavage-independent fashion. J Biol Chem 1999; 274(26): 18552-18558.
    • (1999) J Biol Chem , vol.274 , Issue.26 , pp. 18552-18558
    • Bryan, W.J.1    Lawrence, H.B.2
  • 19
    • 0033532543 scopus 로고    scopus 로고
    • Dephosphorylation targets Bcl-2 for ubiquitin-dependent degradation: A link between the apoptosome and the proteosome pathway
    • Dimmler S, Breitschopf K, Haendeler J, Zeiher AM. Dephosphorylation targets Bcl-2 for ubiquitin-dependent degradation: A link between the apoptosome and the proteosome pathway. J Exp Med 1999; 189(11): 1815-1822.
    • (1999) J Exp Med , vol.189 , Issue.11 , pp. 1815-1822
    • Dimmler, S.1    Breitschopf, K.2    Haendeler, J.3    Zeiher, A.M.4
  • 20
    • 0033575320 scopus 로고    scopus 로고
    • Ceramide induces Bcl-2 dephosphorylation via a mechanism involving mitochondrial PP2A
    • Ruvolo PP, Deng X, Ito T, Carr BK, May WS. Ceramide induces Bcl-2 dephosphorylation via a mechanism involving mitochondrial PP2A. J Biol Chem 1999; 274(29): 20296-20300.
    • (1999) J Biol Chem , vol.274 , Issue.29 , pp. 20296-20300
    • Ruvolo, P.P.1    Deng, X.2    Ito, T.3    Carr, B.K.4    May, W.S.5
  • 21
    • 0030901628 scopus 로고    scopus 로고
    • Suppression of signaling through transcription factor NFAT by interaction between calcineurin and Bcl-2
    • Shibasaki F, Kondo E, Akagi T, Mckeon F. Suppression of signaling through transcription factor NFAT by interaction between calcineurin and Bcl-2. Nature 1997; 386: 728-731.
    • (1997) Nature , vol.386 , pp. 728-731
    • Shibasaki, F.1    Kondo, E.2    Akagi, T.3    Mckeon, F.4
  • 22
    • 0033136719 scopus 로고    scopus 로고
    • Self-renewal, differentiation or death: Regulation and manipulation of hematopoietic stem cell fate
    • Domen J, Weissman I. Self-renewal, differentiation or death: Regulation and manipulation of hematopoietic stem cell fate. Molecular Medicine Today 1999; 5(5): 201-208.
    • (1999) Molecular Medicine Today , vol.5 , Issue.5 , pp. 201-208
    • Domen, J.1    Weissman, I.2
  • 24
    • 0027523461 scopus 로고
    • Apoptosis induced by withdrawal of interleukin-3 (IL-3) from an IL-3-dependent hematopoietic cell line is associated with repartitioning of intracellular calcium and is blocked by enforced Bcl-2 oncoprotein production
    • Baffy G, Miyashita T, Williamson Jr. Apoptosis induced by withdrawal of interleukin-3 (IL-3) from an IL-3-dependent hematopoietic cell line is associated with repartitioning of intracellular calcium and is blocked by enforced Bcl-2 oncoprotein production. J Biol Chem 1993; 268(9): 6511-6519.
    • (1993) J Biol Chem , vol.268 , Issue.9 , pp. 6511-6519
    • Baffy, G.1    Miyashita, T.2    Williamson, Jr.3
  • 25
    • 9544246860 scopus 로고    scopus 로고
    • Mitochondrial permeability transition is a central coordinating event of apoptosis
    • Marchetti P. Mitochondrial permeability transition is a central coordinating event of apoptosis. J Exp Med 1996; 184:1155-1160.
    • (1996) J Exp Med , vol.184 , pp. 1155-1160
    • Marchetti, P.1
  • 26
    • 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. PNAS USA 2000; 97: 3100-3105.
    • (2000) PNAS USA , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 27
    • 5244224827 scopus 로고    scopus 로고
    • L, an inhibitor of programmed cell death
    • L, an inhibitor of programmed cell death. Nature 1996; 381: 335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1
  • 28
    • 9844257587 scopus 로고    scopus 로고
    • Inhibition of Bax channel-forming activity by Bcl-2
    • Antonsson B, Conti F, Ciavatta AM, et al. Inhibition of Bax channel-forming activity by Bcl-2. Science 1997; 277(5324): 370-372.
    • (1997) Science , vol.277 , Issue.5324 , pp. 370-372
    • Antonsson, B.1    Conti, F.2    Ciavatta, A.M.3
  • 29
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin SA, Lorenzo HK, Zamzami N, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 1999; 397: 441-446.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 30
    • 0344897663 scopus 로고    scopus 로고
    • Bcl-2 on the endoplasmic reticulum: Protecting the mitochondria from a distance
    • Thomenius MJ, Distelhorst CW. Bcl-2 on the endoplasmic reticulum: Protecting the mitochondria from a distance. J Cell Sci 2003; 116: 4493-4499.
    • (2003) J Cell Sci , vol.116 , pp. 4493-4499
    • Thomenius, M.J.1    Distelhorst, C.W.2
  • 32
    • 11144294108 scopus 로고    scopus 로고
    • A transcriptional element in the coding sequence of the human Bcl-2 gene
    • Lang G, Gombert WM, Gould HJ. A transcriptional element in the coding sequence of the human Bcl-2 gene. Immunology 2005; 114: 25-36.
    • (2005) Immunology , vol.114 , pp. 25-36
    • Lang, G.1    Gombert, W.M.2    Gould, H.J.3
  • 33
    • 0023779204 scopus 로고
    • Alternative promoter and exons, somatic mutations and deregulation of the Bcl-2-Ig fusion gene in lymphoma
    • Seto M, Jaeger U, Hockett RD, et al. Alternative promoter and exons, somatic mutations and deregulation of the Bcl-2-Ig fusion gene in lymphoma. EMBO J 1988; 7: 123-131.
    • (1988) EMBO J , vol.7 , pp. 123-131
    • Seto, M.1    Jaeger, U.2    Hockett, R.D.3
  • 34
    • 0025255538 scopus 로고
    • Deregulated Bcl-2 gene expression selectively prolongs survival of growth factor-deprived hematopoietic cell lines
    • Nunez G, London L, Hockenbery D, Alexander M, McKearn JP, Korsmeyer SJ. Deregulated Bcl-2 gene expression selectively prolongs survival of growth factor-deprived hematopoietic cell lines. J Immunol 1990; 144: 3602-3610.
    • (1990) J Immunol , vol.144 , pp. 3602-3610
    • Nunez, G.1    London, L.2    Hockenbery, D.3    Alexander, M.4    McKearn, J.P.5    Korsmeyer, S.J.6
  • 35
    • 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. PNAS USA 1986; 83: 5214-5218.
    • (1986) PNAS USA , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 36
    • 0027427493 scopus 로고
    • Bcl-2 affects survival but not neuronal differentiation of PC12 cells
    • Batistatou A, Merry DE, Korsmeyer SJ, Greene LA. Bcl-2 affects survival but not neuronal differentiation of PC12 cells. J Neurosci 1993; 13: 4422-4428.
    • (1993) J Neurosci , vol.13 , pp. 4422-4428
    • Batistatou, A.1    Merry, D.E.2    Korsmeyer, S.J.3    Greene, L.A.4
  • 37
    • 0029810469 scopus 로고    scopus 로고
    • Induction of Bcl-2 expression by phosphorylated CREB proteins during B-cell activation and rescue from apoptosis
    • Wilson BE, Mochon E, Boxer LM. Induction of Bcl-2 expression by phosphorylated CREB proteins during B-cell activation and rescue from apoptosis. Mol Cell Biol 1996; 16: 5546-5556.
    • (1996) Mol Cell Biol , vol.16 , pp. 5546-5556
    • Wilson, B.E.1    Mochon, E.2    Boxer, L.M.3
  • 38
    • 0033527753 scopus 로고    scopus 로고
    • Mechanisms of transcriptional activation of Bcl-2 gene expression by 17beta-estradiol in breast cancer cells
    • Dong L, Wang W, Wang F, et al. Mechanisms of transcriptional activation of Bcl-2 gene expression by 17beta-estradiol in breast cancer cells. J Biol Chem 1999; 274(45): 32099-32107.
    • (1999) J Biol Chem , vol.274 , Issue.45 , pp. 32099-32107
    • Dong, L.1    Wang, W.2    Wang, F.3
  • 39
    • 0344419987 scopus 로고    scopus 로고
    • Identification of c-Jun as Bcl-2 transcription factor in human uterine endometrium
    • Li ZL, Abe H, Ueki K, Kumagai K, Araki R, Otsuki Y. Identification of c-Jun as Bcl-2 transcription factor in human uterine endometrium. J Histochem Cytochem 2003; 51(12): 1601-1609.
    • (2003) J Histochem Cytochem , vol.51 , Issue.12 , pp. 1601-1609
    • Li, Z.L.1    Abe, H.2    Ueki, K.3    Kumagai, K.4    Araki, R.5    Otsuki, Y.6
  • 40
    • 0028322169 scopus 로고
    • Cyclic Bcl-2 gene expression in human uterine endometrium during menstrual cycle
    • Otsuki Y, Misaki O, Sugimoto O, Ito Y, Tsujimoto Y, Akao Y. Cyclic Bcl-2 gene expression in human uterine endometrium during menstrual cycle. Lancet 1994; 344: 28-29.
    • (1994) Lancet , vol.344 , pp. 28-29
    • Otsuki, Y.1    Misaki, O.2    Sugimoto, O.3    Ito, Y.4    Tsujimoto, Y.5    Akao, Y.6
  • 41
    • 0030000059 scopus 로고    scopus 로고
    • What role does apoptosis play in progression of renal disease?
    • Savill J, Mooney A, Hughes J. What role does apoptosis play in progression of renal disease? Curr Opin Nephrol Hypertens 1996; 5(4): 369-374.
    • (1996) Curr Opin Nephrol Hypertens , vol.5 , Issue.4 , pp. 369-374
    • Savill, J.1    Mooney, A.2    Hughes, J.3
  • 42
    • 0027286622 scopus 로고
    • A negative regulatory element in the Bcl-2 5′-untranslated region inhibits expression from an upstream promoter
    • Young RL, Korsmeyer SJ. A negative regulatory element in the Bcl-2 5′-untranslated region inhibits expression from an upstream promoter. Mol Cell Biol 1993; 13(6): 3686-3697.
    • (1993) Mol Cell Biol , vol.13 , Issue.6 , pp. 3686-3697
    • Young, R.L.1    Korsmeyer, S.J.2
  • 43
    • 0028292480 scopus 로고
    • Identification of a p53-dependent negative response element in the Bcl-2 gene
    • Miyashita T, Harigai M, Hanada M, Reed JC. Identification of a p53-dependent negative response element in the Bcl-2 gene. Cancer Res 1994a; 54: 3131-3135.
    • (1994) Cancer Res , vol.54 , pp. 3131-3135
    • Miyashita, T.1    Harigai, M.2    Hanada, M.3    Reed, J.C.4
  • 44
    • 0028335717 scopus 로고
    • Tumor suppressor p53 is a regulator of Bcl-2 and Bax 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 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
  • 45
    • 0033957550 scopus 로고    scopus 로고
    • A conserved AU-rich element in the 3′ untranslated region of Bcl-2 mRNA is endowed with a destabilizing function that is involved in Bcl-2 down-regulation during apoptosis
    • Schiavone I, Rosini P, Quattrone A, Donnini M, Lapucci A, Citti L. A conserved AU-rich element in the 3′ untranslated region of Bcl-2 mRNA is endowed with a destabilizing function that is involved in Bcl-2 down-regulation during apoptosis. The FASEB Journal 2000; 14: 174-184.
    • (2000) The FASEB Journal , vol.14 , pp. 174-184
    • Schiavone, I.1    Rosini, P.2    Quattrone, A.3    Donnini, M.4    Lapucci, A.5    Citti, L.6
  • 46
    • 0024501122 scopus 로고
    • The Bcl -2 candidate proto-oncogene product is a 24-kilodalton integral-membrane protein highly expressed in lymphoid cell lines and lymphomas carrying the t(14;18) translocation
    • Chen-Levy Z, Nourse J, Cleary ML. The Bcl -2 candidate proto-oncogene product is a 24-kilodalton integral-membrane protein highly expressed in lymphoid cell lines and lymphomas carrying the t(14;18) translocation. Mol Cell Biol 1989; 9: 701-710.
    • (1989) Mol Cell Biol , vol.9 , pp. 701-710
    • Chen-Levy, Z.1    Nourse, J.2    Cleary, M.L.3
  • 47
    • 1442310957 scopus 로고    scopus 로고
    • Structural biology of the Bcl-2 family of proteins
    • Biochimica et Biophysica Acta
    • Petros AM, Olejniczak ET, Fesik SW. Structural biology of the Bcl-2 family of proteins. Biochimica et Biophysica Acta. Molecul Cell Research 2004; 1644: 83-94.
    • (2004) Molecul Cell Research , vol.1644 , pp. 83-94
    • Petros, A.M.1    Olejniczak, E.T.2    Fesik, S.W.3
  • 49
    • 21244476053 scopus 로고    scopus 로고
    • Structural conservation of residues in BH1 and BH2 domains of Bcl-2 family proteins
    • Jul 4
    • Gurudutta GU, Verma YK, Singh VK, et al. Structural conservation of residues in BH1 and BH2 domains of Bcl-2 family proteins. FEBS Lett 2005 Jul 4; 579(17): 3503-3507.
    • (2005) FEBS Lett , vol.579 , Issue.17 , pp. 3503-3507
    • Gurudutta, G.U.1    Verma, Y.K.2    Singh, V.K.3
  • 50
    • 0028540362 scopus 로고
    • Dissection of functional domains in Bcl-2α by site-directed mutagenesis
    • Borner C. Dissection of functional domains in Bcl-2α by site-directed mutagenesis. Biochem Cell Biol 1994; 72: 463-469.
    • (1994) Biochem Cell Biol , vol.72 , pp. 463-469
    • Borner, C.1
  • 51
    • 0030995943 scopus 로고    scopus 로고
    • A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members
    • Diaz JL. A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members. J Biol Chem 1996; 272(17): 11350-11355.
    • (1996) J Biol Chem , vol.272 , Issue.17 , pp. 11350-11355
    • Diaz, J.L.1
  • 52
    • 0030614915 scopus 로고    scopus 로고
    • L-Bak peptide complex: Recognition between regulators of apoptosis
    • L-Bak peptide complex: Recognition between regulators of apoptosis. Science 1997; 275: 983-986.
    • (1997) Science , vol.275 , pp. 983-986
    • Fesik, S.W.1
  • 53
    • 0031436251 scopus 로고    scopus 로고
    • Heterodimerization independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells
    • Zha H. 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
  • 54
    • 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
  • 55
    • 0029937303 scopus 로고    scopus 로고
    • Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1
    • Wang HG, Takayama S, Rapp UR, Reed JC. Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1. PNAS USA 1996; 93: 7063-7068.
    • (1996) PNAS USA , vol.93 , pp. 7063-7068
    • Wang, H.G.1    Takayama, S.2    Rapp, U.R.3    Reed, J.C.4
  • 57
    • 0029843941 scopus 로고    scopus 로고
    • Cross talk between cell death and cell cycle progression: Bcl-2 regulates NFAT-mediated activation
    • Linette GP, Li Y, Roth K, Korsmeyer SJ. Cross talk between cell death and cell cycle progression: Bcl-2 regulates NFAT-mediated activation. PNAS USA 1996; 93: 9545-9552.
    • (1996) PNAS USA , vol.93 , pp. 9545-9552
    • Linette, G.P.1    Li, Y.2    Roth, K.3    Korsmeyer, S.J.4
  • 58
    • 0029619087 scopus 로고
    • NF-M (chicken C/EBPb) induces eosinophilic differentiation and apoptosis in a hematopoietic progenitor cell line
    • Müller C, Kowenz-Leutz E, Grieser-Ade S, Graf T, Leutz A. NF-M (chicken C/EBPb) induces eosinophilic differentiation and apoptosis in a hematopoietic progenitor cell line. EMBO J 1995; 14: 6127-6135.
    • (1995) EMBO J , vol.14 , pp. 6127-6135
    • Müller, C.1    Kowenz-Leutz, E.2    Grieser-Ade, S.3    Graf, T.4    Leutz, A.5
  • 62
    • 0042220409 scopus 로고    scopus 로고
    • L/Bim fragment complex: Implications for Bim function
    • L/Bim fragment complex: Implications for Bim function. Immunity 2003; 19: 341-352.
    • (2003) Immunity , vol.19 , pp. 341-352
    • Liu, X.1
  • 63
    • 0034644508 scopus 로고    scopus 로고
    • Insight into programmed cell death through structural biology
    • Fesik SW. Insight into programmed cell death through structural biology. Cell 2000; 103: 273-282.
    • (2000) Cell , vol.103 , pp. 273-282
    • Fesik, S.W.1
  • 64
    • 0041885229 scopus 로고    scopus 로고
    • Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2
    • Huang Q. Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2. J Mol Biol 2003; 332: 1123-1130.
    • (2003) J Mol Biol , vol.332 , pp. 1123-1130
    • Huang, Q.1
  • 65
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative p rotein modelling
    • Peitsch MC. ProMod and Swiss-Model: Internet-based tools for automated comparative p rotein modelling. Biochem Soc Trans 1996; 24: 274-279.
    • (1996) Biochem Soc Trans , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 67
    • 1242337339 scopus 로고    scopus 로고
    • Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands
    • Day CL, Puthalakath H, Skea G, et al. Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. Biochem J 2004; 377(3): 597-605.
    • (2004) Biochem J , vol.377 , Issue.3 , pp. 597-605
    • Day, C.L.1    Puthalakath, H.2    Skea, G.3
  • 69
    • 0033499801 scopus 로고    scopus 로고
    • Bcl-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G2/M
    • Yamamoto K, Ichijo H, Korsmeyer SJ. Bcl-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G2/M. Molecul Cellular Biol 1999; 19(12): 8469-8478.
    • (1999) Molecul Cellular Biol , vol.19 , Issue.12 , pp. 8469-8478
    • Yamamoto, K.1    Ichijo, H.2    Korsmeyer, S.J.3
  • 70
    • 0035073292 scopus 로고    scopus 로고
    • Phosphorylation of Bcl-2 and regulation of apoptosis
    • Ruvolo PP, Deng X, May WS Jr. Phosphorylation of Bcl-2 and regulation of apoptosis. Leukemia 2001; 15: 515-522.
    • (2001) Leukemia , vol.15 , pp. 515-522
    • Ruvolo, P.P.1    Deng, X.2    May Jr., W.3
  • 71
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • Meier P, Finch A, Evan G. Apoptosis in development. Nature 2000; 407: 796-801.
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 72
    • 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
  • 73
    • 0029056675 scopus 로고
    • Inactivation of Bcl-2 by phosphorylation
    • Haldar S, Jena N, Croce CM. Inactivation of Bcl-2 by phosphorylation. PNAS USA 1995; 92: 4507-4511.
    • (1995) PNAS USA , vol.92 , pp. 4507-4511
    • Haldar, S.1    Jena, N.2    Croce, C.M.3
  • 74
    • 0029964257 scopus 로고    scopus 로고
    • Taxol induces Bcl-2 phosphorylation and death of prostate cancer cells
    • Haldar S, Chintapalli J, Croce CM. Taxol induces Bcl-2 phosphorylation and death of prostate cancer cells. Cancer Res 1996; 56: 1253-1255.
    • (1996) Cancer Res , vol.56 , pp. 1253-1255
    • Haldar, S.1    Chintapalli, J.2    Croce, C.M.3
  • 75
    • 0032522885 scopus 로고    scopus 로고
    • Serine-70 is one of the critical sites for drug-induced Bcl-2 phosphorylation in cancer cells
    • Haldar S, Basu A, Croce CM. Serine-70 is one of the critical sites for drug-induced Bcl-2 phosphorylation in cancer cells. Cancer Res 1998; 58: 1609-1615.
    • (1998) Cancer Res , vol.58 , pp. 1609-1615
    • Haldar, S.1    Basu, A.2    Croce, C.M.3
  • 76
    • 0029913172 scopus 로고    scopus 로고
    • Taxol-induced apoptosis and phosphorylation of Bcl-2 protein involves c-Raf-1 and represents a novel c-Raf-1 signal transduction pathway
    • Blagosklonny MV, Schulte T, Nguyen P, Trepel J, Neckers LM. Taxol-induced apoptosis and phosphorylation of Bcl-2 protein involves c-Raf-1 and represents a novel c-Raf-1 signal transduction pathway. Cancer Res 1996; 56: 1851-1854.
    • (1996) Cancer Res , vol.56 , pp. 1851-1854
    • Blagosklonny, M.V.1    Schulte, T.2    Nguyen, P.3    Trepel, J.4    Neckers, L.M.5
  • 77
    • 0031036307 scopus 로고    scopus 로고
    • Raf-1/Bcl-2 phosphorylation: A step from microtubule damage to cell death
    • Blagosklonny MV, Giannakakou P, El-Deiry WS, et al. Raf-1/Bcl-2 phosphorylation: A step from microtubule damage to cell death. Cancer Res 57: 130-135.
    • Cancer Res , vol.57 , pp. 130-135
    • Blagosklonny, M.V.1    Giannakakou, P.2    El-Deiry, W.S.3
  • 78
    • 0032776120 scopus 로고    scopus 로고
    • Mitogen activated protein kinase pathway is dispensable for microtubule-active drug-induced Raf-1/Bcl-2 phosphorylation and apoptosis in leukemia cells
    • Blagosklonny MV, Chuman Y, Bergan RC, Fojo T. Mitogen activated protein kinase pathway is dispensable for microtubule-active drug-induced Raf-1/Bcl-2 phosphorylation and apoptosis in leukemia cells. Leukemia 1999; 13: 1028-1036.
    • (1999) Leukemia , vol.13 , pp. 1028-1036
    • Blagosklonny, M.V.1    Chuman, Y.2    Bergan, R.C.3    Fojo, T.4
  • 79
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun YA. The sphingomyelin cycle and the second messenger function of ceramide. J Biol Chem 1994; 269: 3125-3128.
    • (1994) J Biol Chem , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 81
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson DW, Ali A, Thornberry NA, et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 1995; 376: 37-43.
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1    Ali, A.2    Thornberry, N.A.3
  • 82
    • 0033603460 scopus 로고    scopus 로고
    • Bcl-2 and caspase inhibition cooperate to inhibit tumor necrosis factor-induced cell death in a Bcl-2 cleavage-independent fashion
    • Johnson BW, Boise LH. Bcl-2 and caspase inhibition cooperate to inhibit tumor necrosis factor-induced cell death in a Bcl-2 cleavage-independent fashion. J Biol Chem 1999; 274(26): 18552-18558.
    • (1999) J Biol Chem , vol.274 , Issue.26 , pp. 18552-18558
    • Johnson, B.W.1    Boise, L.H.2
  • 83
    • 0027314703 scopus 로고
    • Mature T cells of autoimmune lpr/lpr mice have a defect in antigen-stimulated suicide
    • Russel JH, Rush B, Weaver C, Wang R. Mature T cells of autoimmune lpr/lpr mice have a defect in antigen-stimulated suicide. PNAS USA 1993; 90: 4409-4413.
    • (1993) PNAS USA , vol.90 , pp. 4409-4413
    • Russel, J.H.1    Rush, B.2    Weaver, C.3    Wang, R.4
  • 84
    • 0028883850 scopus 로고
    • Cytotoxicity dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel FC, Hellbardt S, Behrmann I, et al. Cytotoxicity dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995; 14: 5579-5588.
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3
  • 85
    • 0033603460 scopus 로고    scopus 로고
    • Bcl-2 and caspase inhibitor (zVAD-fmk) cooperate to inhibit tumor necrosis factor-α-induced cell death in a Bcl-2 cleavage independent fashion
    • Johnson BW, Boise LH. Bcl-2 and caspase inhibitor (zVAD-fmk) cooperate to inhibit tumor necrosis factor-α-induced cell death in a Bcl-2 cleavage independent fashion. J Biol Chem 1999; 274(26): 18552-18558.
    • (1999) J Biol Chem , vol.274 , Issue.26 , pp. 18552-18558
    • Johnson, B.W.1    Boise, L.H.2
  • 87
    • 0031017578 scopus 로고    scopus 로고
    • A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak
    • Cheng EHY, Nicholas J, Bellows DS, Hayward GS, Guo HG, Reitz MS, et al. A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak. PNAS USA 1997; 94: 690-694.
    • (1997) PNAS USA , vol.94 , pp. 690-694
    • Cheng, E.H.Y.1    Nicholas, J.2    Bellows, D.S.3    Hayward, G.S.4    Guo, H.G.5    Reitz, M.S.6
  • 88
    • 0023786047 scopus 로고
    • Bcl-2 gene promotes hamatopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
    • Vaux DL, Cory S, Adams JM. Bcl-2 gene promotes hamatopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature 1988; 335: 440-442.
    • (1988) Nature , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 89
    • 0031587848 scopus 로고    scopus 로고
    • Enforced expression of Bcl-2 in monocytes rescues macrophages and partially reverses osteopetrosis in op/op mice
    • Lagasse E, Weissman IL. Enforced expression of Bcl-2 in monocytes rescues macrophages and partially reverses osteopetrosis in op/op mice. Cell 1997; 89(7): 1021-1031.
    • (1997) Cell , vol.89 , Issue.7 , pp. 1021-1031
    • Lagasse, E.1    Weissman, I.L.2
  • 91
    • 0030255449 scopus 로고    scopus 로고
    • Mechanisms of Bcl-2 family protein function and dysfunction in health and disease
    • Reed JC. Mechanisms of Bcl-2 family protein function and dysfunction in health and disease. Behring Inst Mit 1996; 97: 72-100.
    • (1996) Behring Inst Mit , vol.97 , pp. 72-100
    • Reed, J.C.1
  • 92
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch SM, Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol 1994; 124: 619-626.
    • (1994) J Cell Biol , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 93
    • 0032055166 scopus 로고    scopus 로고
    • Systemic overexpression of Bcl-2 in the hematopoietic system protects transgenic mice from the consequences of lethal irradiation
    • Domen J, Gandy KL. Systemic overexpression of Bcl-2 in the hematopoietic system protects transgenic mice from the consequences of lethal irradiation. Blood 1998; 91: 2272-2282.
    • (1998) Blood , vol.91 , pp. 2272-2282
    • Domen, J.1    Gandy, K.L.2
  • 94
    • 0030901212 scopus 로고    scopus 로고
    • Integration patterns of HTLV-I provirus in relation to the clinical course of ATL: Frequent clonal change at crisis from indolent disease
    • Tsukasaki K, Tsushima H, Yamamura M, et al. Integration patterns of HTLV-I provirus in relation to the clinical course of ATL: Frequent clonal change at crisis from indolent disease. Blood 1997; 89(3): 948-956.
    • (1997) Blood , vol.89 , Issue.3 , pp. 948-956
    • Tsukasaki, K.1    Tsushima, H.2    Yamamura, M.3
  • 95
    • 0033561090 scopus 로고    scopus 로고
    • Optimal proliferation of a hematopoietic progenitor cell line requires either costimulation with stem cell factor or increase of receptor expression that can be replaced by overexpression of Bcl-2
    • Huang HM, Li JC, Hsieh YC, Yen HFY, Yen JJY. Optimal proliferation of a hematopoietic progenitor cell line requires either costimulation with stem cell factor or increase of receptor expression that can be replaced by overexpression of Bcl-2. Blood 1999; 93(8): 2569-2577.
    • (1999) Blood , vol.93 , Issue.8 , pp. 2569-2577
    • Huang, H.M.1    Li, J.C.2    Hsieh, Y.C.3    Yen, H.F.Y.4    Yen, J.J.Y.5
  • 96
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen M, Bujard H. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. PNAS USA 1992; 89(12): 5547-5551.
    • (1992) PNAS USA , vol.89 , Issue.12 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 97
    • 0032533236 scopus 로고    scopus 로고
    • Two new pseudopod morphologies displayed by the human hematopoietic kG-1a progenitor cell line and by primary human CD34 cells
    • Francis K, Ramakrishna R, Holloway W, Palsson BO. Two new pseudopod morphologies displayed by the human hematopoietic kG-1a progenitor cell line and by primary human CD34 cells. Blood 1998; 92(10): 3616-3623.
    • (1998) Blood , vol.92 , Issue.10 , pp. 3616-3623
    • Francis, K.1    Ramakrishna, R.2    Holloway, W.3    Palsson, B.O.4
  • 98
    • 0028939862 scopus 로고
    • The genetic regulation of apoptosis
    • Wyllie AH. The genetic regulation of apoptosis. Curr Opin Gen Dev 1995; 5: 97-104.
    • (1995) Curr Opin Gen Dev , vol.5 , pp. 97-104
    • Wyllie, A.H.1
  • 99
    • 0034652115 scopus 로고    scopus 로고
    • Survival function of ERk1/2 as IL-3 activated, staurosporine-resistant Bcl-2 kinases
    • Deng X, Ruvolo P, Carr B, May Jr WS. Survival function of ERk1/2 as IL-3 activated, staurosporine-resistant Bcl-2 kinases. PNAS USA 2000; 97(4): 1578-1583.
    • (2000) PNAS USA , vol.97 , Issue.4 , pp. 1578-1583
    • Deng, X.1    Ruvolo, P.2    Carr, B.3    May Jr., W.S.4
  • 100
    • 4644305430 scopus 로고    scopus 로고
    • Phase II study of ISIS 3521, an antisense oligodeoxynucleotide to protein kinase C alpha, in patients with previously treated low-grade non-Hodgkin's lymphoma
    • Rao S, Watkins S, Cunningham D, et al. Phase II study of ISIS 3521, an antisense oligodeoxynucleotide to protein kinase C alpha, in patients with previously treated low-grade non-Hodgkin's lymphoma. Ann Oncol 1997; 15: 1413-1418.
    • (1997) Ann Oncol , vol.15 , pp. 1413-1418
    • Rao, S.1    Watkins, S.2    Cunningham, D.3


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