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Volumn 43, Issue 1, 2006, Pages 1-67

BCL2 family of apoptosis-related genes: Functions and clinical implications in cancer

Author keywords

Apoptosis; BAK1; BAX; BBC3; BCL 2; BCL2 gene family; BCL2A1; BCL2L1; BCL2L11; BCL2L12; BCL2L13; BCL2L14; BCL2L2; BCLAF1; BID; BIK; BLK; BMF; BNIP; BNIP1; BNIP2; BNIP3; BOK; BOO DIVA; Cancer; Cancer prognosis; Cancer treatment; ceBNIP3; HRK; MCL1; NIX; PMAIP1; Tumour biomarkers

Indexed keywords

BIOLOGICAL MARKER; MICROTUBULE ASSOCIATED PROTEIN 1; PROTEIN BAX; PROTEIN BCL 2;

EID: 33644928489     PISSN: 10408363     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408360500295626     Document Type: Review
Times cited : (221)

References (484)
  • 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
  • 3
    • 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
  • 4
    • 0032418812 scopus 로고    scopus 로고
    • The critical need for CD4 help in maintaining effective cytotoxic T lymphocyte responses
    • Kalams SA, Walker BD. The critical need for CD4 help in maintaining effective cytotoxic T lymphocyte responses. J Exp Med 1998; 188: 2199-2204.
    • (1998) J Exp Med , vol.188 , pp. 2199-2204
    • Kalams, S.A.1    Walker, B.D.2
  • 5
    • 0031871999 scopus 로고    scopus 로고
    • Traps to catch unwary oncogenes
    • Hueber AO, Evan GI. Traps to catch unwary oncogenes. Trends Genet 1998; 14: 364-367.
    • (1998) Trends Genet , vol.14 , pp. 364-367
    • Hueber, A.O.1    Evan, G.I.2
  • 6
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia - A key regulatory factor in tumour growth
    • Harris AL. Hypoxia - a key regulatory factor in tumour growth. Nat Rev Cancer 2002; 2: 38-47.
    • (2002) Nat Rev Cancer , vol.2 , pp. 38-47
    • Harris, A.L.1
  • 7
    • 0030790430 scopus 로고    scopus 로고
    • Cell death in the regulation of immune responses
    • Winoto A. Cell death in the regulation of immune responses. Curr Opin Immunol 1997; 9: 365-370.
    • (1997) Curr Opin Immunol , vol.9 , pp. 365-370
    • Winoto, A.1
  • 8
    • 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: 321-323.
    • (1994) Nature , vol.369 , pp. 321-323
    • Yin, X.M.1    Oltvai, Z.N.2    Korsmeyer, S.J.3
  • 10
    • 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
  • 11
    • 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
  • 12
    • 0028149786 scopus 로고
    • Checkpoints of dueling dimers foil death wishes
    • Oltvai ZN, Korsmeyer SJ. Checkpoints of dueling dimers foil death wishes. Cell 1994; 79: 189-192.
    • (1994) Cell , vol.79 , pp. 189-192
    • Oltvai, Z.N.1    Korsmeyer, S.J.2
  • 13
    • 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: 25265-25268.
    • (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
  • 14
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery D, Nunez G, Milliman C, Schreiber RD, Korsmeyer SJ. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 1990; 348: 334-336.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 15
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res 1993; 53: 4701-4714.
    • (1993) Cancer Res , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 17
    • 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, Newmeyer DD. 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    Newmeyer, D.D.4
  • 19
    • 0030707613 scopus 로고    scopus 로고
    • Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins
    • Ottilie S, Diaz JL, Home W, Chang J, Wang Y, Wilson G, Chang S, Weeks S, Fritz LC, Oltersdorf T. Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins. J Biol Chem 1997; 272: 30866-30872.
    • (1997) J Biol Chem , vol.272 , pp. 30866-30872
    • Ottilie, S.1    Diaz, J.L.2    Home, W.3    Chang, J.4    Wang, Y.5    Wilson, G.6    Chang, S.7    Weeks, S.8    Fritz, L.C.9    Oltersdorf, T.10
  • 20
    • 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
  • 21
    • 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
  • 23
    • 0021679848 scopus 로고
    • Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation
    • Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM. Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation. Science 1984; 226: 1097-1099.
    • (1984) Science , vol.226 , pp. 1097-1099
    • Tsujimoto, Y.1    Finger, L.R.2    Yunis, J.3    Nowell, P.C.4    Croce, C.M.5
  • 24
    • 0021821903 scopus 로고
    • Involvement of the bcl-2 gene in human follicular lymphoma
    • Tsujimoto Y, Cossman J, Jaffe E, Croce CM. 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    Cossman, J.2    Jaffe, E.3    Croce, C.M.4
  • 25
    • 0021934042 scopus 로고
    • Cloning the chromosomal breakpoint of t(14;18) human lymphomas: Clustering around JH on chromosome 14 and near a transcriptional unit on 18
    • Bakhshi A, Jensen JP, Goldman P, Wright JJ, McBride OW, Epstein AL, Korsmeyer SJ. Cloning the chromosomal breakpoint of t(14;18) human lymphomas: clustering around JH on chromosome 14 and near a transcriptional unit on 18. Cell 1985; 41: 899-906.
    • (1985) Cell , vol.41 , pp. 899-906
    • Bakhshi, A.1    Jensen, J.P.2    Goldman, P.3    Wright, J.J.4    McBride, O.W.5    Epstein, A.L.6    Korsmeyer, S.J.7
  • 26
    • 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 Natl Acad Sci USA 1986; 83: 5214-5218.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 27
    • 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
  • 30
    • 0027977928 scopus 로고
    • The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane
    • Lithgow T, van Driel R, Bertram JF, Strasser A. The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane. Cell Growth Differ 1994; 5: 411-417.
    • (1994) Cell Growth Differ , vol.5 , pp. 411-417
    • Lithgow, T.1    Van Driel, R.2    Bertram, J.F.3    Strasser, A.4
  • 31
    • 0028793279 scopus 로고
    • Localization of the Bcl-2 protein to the outer mitochondrial membrane by electron microscopy
    • Riparbelli MG, Callaini G, Tripodi SA, Cintorino M, Tosi P, Dallai R. Localization of the Bcl-2 protein to the outer mitochondrial membrane by electron microscopy. Exp Cell Res 1995; 221: 363-369.
    • (1995) Exp Cell Res , vol.221 , pp. 363-369
    • Riparbelli, M.G.1    Callaini, G.2    Tripodi, S.A.3    Cintorino, M.4    Tosi, P.5    Dallai, R.6
  • 32
    • 0029032660 scopus 로고
    • Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax
    • Kanada 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: 11962-11969.
    • (1995) J Biol Chem , vol.270 , pp. 11962-11969
    • Kanada, M.1    Aime-Sempe, C.2    Sato, T.3    Reed, J.C.4
  • 33
    • 1442286330 scopus 로고    scopus 로고
    • The role of Bcl-2 family members in tumorigenesis
    • Kirkin V, Joos S, Zornig M. The role of Bcl-2 family members in tumorigenesis. Biochim Biophys Acta 2004; 1644: B229-B249.
    • (2004) Biochim Biophys Acta , vol.1644
    • Kirkin, V.1    Joos, S.2    Zornig, M.3
  • 36
    • 0028178385 scopus 로고
    • bcl-2 protein expression is widespread in the developing nervous system and retained in the adult PNS
    • Merry DE, Veis DJ, Hickey WF, Korsmeyer SJ. bcl-2 protein expression is widespread in the developing nervous system and retained in the adult PNS. Development 1994; 120: 301-311.
    • (1994) Development , vol.120 , pp. 301-311
    • Merry, D.E.1    Veis, D.J.2    Hickey, W.F.3    Korsmeyer, S.J.4
  • 37
    • 0028448483 scopus 로고
    • Bcl-2 is upregulated at the CD4+ CD8+ stage during positive selection and promotes thymocyte differentiation at several control points
    • Linette GP, Grusby MJ, Hedrick SM, Hansen TH, Glimcher LH, Korsmeyer SJ. Bcl-2 is upregulated at the CD4+ CD8+ stage during positive selection and promotes thymocyte differentiation at several control points. Immunity 1994; 1: 197-205.
    • (1994) Immunity , vol.1 , pp. 197-205
    • Linette, G.P.1    Grusby, M.J.2    Hedrick, S.M.3    Hansen, T.H.4    Glimcher, L.H.5    Korsmeyer, S.J.6
  • 38
    • 0027715083 scopus 로고
    • Expression of bcl-2 in fetal tissues suggests a role in morphogenesis
    • LeBrun DP, Warnke RA, Cleary ML. Expression of bcl-2 in fetal tissues suggests a role in morphogenesis. Am J Pathol 1993; 142: 743-753.
    • (1993) Am J Pathol , vol.142 , pp. 743-753
    • LeBrun, D.P.1    Warnke, R.A.2    Cleary, M.L.3
  • 39
    • 0028229760 scopus 로고
    • Bcl-2 protein expression during murine development
    • Novack DV, Korsmeyer SJ. Bcl-2 protein expression during murine development. Am J Pathol 1994; 145: 61-73.
    • (1994) Am J Pathol , vol.145 , pp. 61-73
    • Novack, D.V.1    Korsmeyer, S.J.2
  • 40
    • 1842456916 scopus 로고    scopus 로고
    • Inactivation of bcl-2 results in progressive degeneration of motoneurons, sympathetic and sensory neurons during early postnatal development
    • Michaelidis TM, Sendtner M, Cooper JD, Airaksinen MS, Holtmann B, Meyer M, Thoenen H. Inactivation of bcl-2 results in progressive degeneration of motoneurons, sympathetic and sensory neurons during early postnatal development. Neuron 1996; 17: 75-89.
    • (1996) Neuron , vol.17 , pp. 75-89
    • Michaelidis, T.M.1    Sendtner, M.2    Cooper, J.D.3    Airaksinen, M.S.4    Holtmann, B.5    Meyer, M.6    Thoenen, H.7
  • 44
    • 0029091740 scopus 로고
    • Role of BCL-2 in the survival and function of developing and mature sympathetic neurons
    • Greenlund LJ, Korsmeyer SJ, Johnson EM Jr. Role of BCL-2 in the survival and function of developing and mature sympathetic neurons. Neuron 1995; 15: 649-661.
    • (1995) Neuron , vol.15 , pp. 649-661
    • Greenlund, L.J.1    Korsmeyer, S.J.2    Johnson Jr., E.M.3
  • 45
    • 0028790829 scopus 로고
    • Bcl-2 blocks glucocorticoid- but not Fas- or activation-induced apoptosis in a T cell hybridoma
    • Memon SA, Moreno MB, Petrak D, Zacharchuk CM. Bcl-2 blocks glucocorticoid- but not Fas- or activation-induced apoptosis in a T cell hybridoma. J Immunol 1995; 155: 4644-4652.
    • (1995) J Immunol , vol.155 , pp. 4644-4652
    • Memon, S.A.1    Moreno, M.B.2    Petrak, D.3    Zacharchuk, C.M.4
  • 46
    • 0034001120 scopus 로고    scopus 로고
    • Changes in glucocorticoid-induced apoptosis and in expression of Bcl-2 protein during long-term culture of thymic lymphoma
    • Kobzdej M, MatuszykJ, Ziolo E, Strzadala L. Changes in glucocorticoid-induced apoptosis and in expression of Bcl-2 protein during long-term culture of thymic lymphoma. Arch Immunol Ther Exp 2000; 48: 43-46.
    • (2000) Arch Immunol Ther Exp , vol.48 , pp. 43-46
    • Kobzdej, M.1    Matuszyk, J.2    Ziolo, E.3    Strzadala, L.4
  • 47
    • 0030874326 scopus 로고    scopus 로고
    • The earliest T lineage-committed cells depend on IL-7 for Bcl-2 expression and normal cell cycle progression
    • Von Freeden-Jeffry U, Solvason N, Howard M, Murray R. The earliest T lineage-committed cells depend on IL-7 for Bcl-2 expression and normal cell cycle progression. Immunity 1997; 7: 147-154.
    • (1997) Immunity , vol.7 , pp. 147-154
    • Von Freeden-Jeffry, U.1    Solvason, N.2    Howard, M.3    Murray, R.4
  • 49
    • 0030855164 scopus 로고    scopus 로고
    • Bcl-2 protein inhibits bufalin-induced apoptosis through inhibition of mitogen-activated protein kinase activation in human leukemia U937 cells
    • Watabe M, Kawazoe N, Masuda Y, Nakajo S, Nakaya K. Bcl-2 protein inhibits bufalin-induced apoptosis through inhibition of mitogen-activated protein kinase activation in human leukemia U937 cells. Cancer Res 1997; 57: 3097-3100.
    • (1997) Cancer Res , vol.57 , pp. 3097-3100
    • Watabe, M.1    Kawazoe, N.2    Masuda, Y.3    Nakajo, S.4    Nakaya, K.5
  • 53
    • 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
  • 54
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu Y, Benedict MA, Wu D, Inohara N, Nunez G. Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Natl Acad Sci USA 1998; 95: 4386-4391.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3    Inohara, N.4    Nunez, G.5
  • 55
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • Pan G, O'Rourke K, Dixit VM. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J Biol Chem 1998; 273: 5841-5845.
    • (1998) J Biol Chem , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 56
    • 0033545382 scopus 로고    scopus 로고
    • Bcl-2 regulates amplification of caspase activation by cytochrome c
    • Cosulich SC, Savory PJ, Clarke PR. Bcl-2 regulates amplification of caspase activation by cytochrome c. Curr Biol 1999; 9: 147-150.
    • (1999) Curr Biol , vol.9 , pp. 147-150
    • Cosulich, S.C.1    Savory, P.J.2    Clarke, P.R.3
  • 60
    • 0036716281 scopus 로고    scopus 로고
    • The Bc12 family: Regulators of the cellular life-or-death switch
    • Cory S, Adams JM. The Bc12 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2002; 2: 647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 62
    • 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
  • 63
    • 0034605121 scopus 로고    scopus 로고
    • Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release
    • Von Ahsen O, Renken C, Perkins G, Kluck RM, Bossy-Wetzel E, Newmeyer DD. Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release. J Cell Biol 2000; 150: 1027-1036.
    • (2000) J Cell Biol , vol.150 , pp. 1027-1036
    • Von Ahsen, O.1    Renken, C.2    Perkins, G.3    Kluck, R.M.4    Bossy-Wetzel, E.5    Newmeyer, D.D.6
  • 64
    • 0028170778 scopus 로고
    • bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localises to mitochondria
    • Gonzalez-Garcia M, Perez-Ballestero R, Ding L, Duan L, Boise LH, Thompson CB, Nunez G. bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localises to mitochondria. Development 1994; 120: 3033-3042.
    • (1994) Development , vol.120 , pp. 3033-3042
    • Gonzalez-Garcia, M.1    Perez-Ballestero, R.2    Ding, L.3    Duan, L.4    Boise, L.H.5    Thompson, C.B.6    Nunez, G.7
  • 66
    • 0028036895 scopus 로고
    • Immunohistochemical determination of in vivo distribution of Bax, a dominant inhibitor of Bcl-2
    • Krajewski S, Krajewska M, Shabaik A, Miyashita T, Wang HG, Reed JC. Immunohistochemical determination of in vivo distribution of Bax, a dominant inhibitor of Bcl-2. Am J Pathol 1994; 145: 1323-1336.
    • (1994) Am J Pathol , vol.145 , pp. 1323-1336
    • Krajewski, S.1    Krajewska, M.2    Shabaik, A.3    Miyashita, T.4    Wang, H.G.5    Reed, J.C.6
  • 67
    • 0031447458 scopus 로고    scopus 로고
    • A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells
    • Yang XF, Weber GF, Cantor H. A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells. Immunity 1997; 7: 629-639.
    • (1997) Immunity , vol.7 , pp. 629-639
    • Yang, X.F.1    Weber, G.F.2    Cantor, H.3
  • 69
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT, Wolter KG, Youle RJ. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci USA 1997; 94: 3668-3672.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 70
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A, Jockel J, Wei MC, Korsmeyer SJ. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J 1998; 17: 3878-3885.
    • (1998) EMBO J , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 71
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signalling
    • Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signalling. Cell 1999; 96: 615-624.
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 74
    • 0033521537 scopus 로고    scopus 로고
    • Boo, a novel negative regulator of cell death, interacts with Apaf-1
    • Song Q, Kuang Y, Dixit VM, Vincenz C. Boo, a novel negative regulator of cell death, interacts with Apaf-1. EMBO J 1999; 18: 167-178.
    • (1999) EMBO J , vol.18 , pp. 167-178
    • Song, Q.1    Kuang, Y.2    Dixit, V.M.3    Vincenz, C.4
  • 76
    • 0032970003 scopus 로고    scopus 로고
    • Role of PI3-kinase in Bcl-X induction and apoptosis inhibition mediated by IL-3 or IGF-1 in Baf-3 cells
    • Leverrier Y, Thomas J, Mathieu AL, Low W, Blanquier B, Marvel J. Role of PI3-kinase in Bcl-X induction and apoptosis inhibition mediated by IL-3 or IGF-1 in Baf-3 cells. Cell Death Differ 1999; 6: 290-296.
    • (1999) Cell Death Differ , vol.6 , pp. 290-296
    • Leverrier, Y.1    Thomas, J.2    Mathieu, A.L.3    Low, W.4    Blanquier, B.5    Marvel, J.6
  • 77
    • 0032973967 scopus 로고    scopus 로고
    • Nerve growth factor determines survival and death of PC12 cells by regulation of the bcl-x, bax, and caspase-3 genes
    • Rong P, Bennie AM, Epa WR, Barrett GL. Nerve growth factor determines survival and death of PC12 cells by regulation of the bcl-x, bax, and caspase-3 genes. J Neurochem 1999; 72: 2294-2300.
    • (1999) J Neurochem , vol.72 , pp. 2294-2300
    • Rong, P.1    Bennie, A.M.2    Epa, W.R.3    Barrett, G.L.4
  • 78
    • 0029091387 scopus 로고
    • Induction of bcl-x by CD40 engagement rescues sIg-induced apoptosis in murine B cells
    • Wang Z, Karras JG, Howard RG, Rothstein TL. Induction of bcl-x by CD40 engagement rescues sIg-induced apoptosis in murine B cells. J Immunol 1995; 155: 3722-3725.
    • (1995) J Immunol , vol.155 , pp. 3722-3725
    • Wang, Z.1    Karras, J.G.2    Howard, R.G.3    Rothstein, T.L.4
  • 80
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2
    • Kozopas KM, Yang T, Buchan HL, Zhou P, Craig RW. MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2. Proc Natl Acad Sci USA 1993; 90: 3516-3520.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3    Zhou, P.4    Craig, R.W.5
  • 81
    • 0034682837 scopus 로고    scopus 로고
    • MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain
    • Bae J, Leo CP, Hsu SY, Hsueh AJ. MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. J Biol Chem 2000; 275: 25255-25261.
    • (2000) J Biol Chem , vol.275 , pp. 25255-25261
    • Bae, J.1    Leo, C.P.2    Hsu, S.Y.3    Hsueh, A.J.4
  • 82
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis Science 1986; 234: 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 84
    • 0029915856 scopus 로고    scopus 로고
    • MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation
    • Yang T, Buchan HL, Townsend KJ, Craig RW. MCL-1, a member of the BLC-2 family, is induced rapidly in response to signals for cell differentiation or death, but not to signals for cell proliferation. J Cell Physiol 1996; 166: 523-536.
    • (1996) J Cell Physiol , vol.166 , pp. 523-536
    • Yang, T.1    Buchan, H.L.2    Townsend, K.J.3    Craig, R.W.4
  • 85
    • 0032505111 scopus 로고    scopus 로고
    • Expression of the antiapoptotic MCL1 gene product is regulated by a mitogen activated protein kinase-mediated pathway triggered through microtubule disruption and protein kinase C
    • Townsend KJ, Trusty JL, Traupman MA, Eastman A, Craig RW. Expression of the antiapoptotic MCL1 gene product is regulated by a mitogen activated protein kinase-mediated pathway triggered through microtubule disruption and protein kinase C. Oncogene 1998; 17: 1223-1234.
    • (1998) Oncogene , vol.17 , pp. 1223-1234
    • Townsend, K.J.1    Trusty, J.L.2    Traupman, M.A.3    Eastman, A.4    Craig, R.W.5
  • 86
    • 0033868378 scopus 로고    scopus 로고
    • Suppression of PMN apoptosis by hypoxia is dependent on Mcl-1 and MAPK activity
    • Leuenroth SJ, Grutkoski PS, Ayala A, Simms HH. Suppression of PMN apoptosis by hypoxia is dependent on Mcl-1 and MAPK activity. Surgery 2000; 128: 171-177.
    • (2000) Surgery , vol.128 , pp. 171-177
    • Leuenroth, S.J.1    Grutkoski, P.S.2    Ayala, A.3    Simms, H.H.4
  • 87
    • 0034618369 scopus 로고    scopus 로고
    • MEK/ERK signalling pathway regulates the expression of Bcl-2, Bcl-X(L), and Mcl-1 and promotes survival of human pancreatic cancer cells
    • Boucher MJ, Morisset J, Vachon PH, Reed JC, Laine J, Rivard N. MEK/ERK signalling pathway regulates the expression of Bcl-2, Bcl-X(L), and Mcl-1 and promotes survival of human pancreatic cancer cells. J Cell Biochem 2000; 79: 355-369.
    • (2000) J Cell Biochem , vol.79 , pp. 355-369
    • Boucher, M.J.1    Morisset, J.2    Vachon, P.H.3    Reed, J.C.4    Laine, J.5    Rivard, N.6
  • 88
    • 0034704939 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF) suppresses staurosporine-induced apoptosis by inducing mcl-1 via the mitogen-activated protein kinase pathway
    • Leu CM, Chang C, Hu C. Epidermal growth factor (EGF) suppresses staurosporine-induced apoptosis by inducing mcl-1 via the mitogen-activated protein kinase pathway. Oncogene 2000; 19: 1665-1675.
    • (2000) Oncogene , vol.19 , pp. 1665-1675
    • Leu, C.M.1    Chang, C.2    Hu, C.3
  • 89
    • 0032772367 scopus 로고    scopus 로고
    • The antiapoptotic gene mcl-1 is upregulated by the phosphatidylinositol 3-kinase/Akt signalling pathway through a transcription factor complex containing CREB
    • Wang JM, Chao JR, Chen W, Kuo ML, Yen JJ, Yang-Yen HF. The antiapoptotic gene mcl-1 is upregulated by the phosphatidylinositol 3-kinase/Akt signalling pathway through a transcription factor complex containing CREB. Mol Cell Biol 1999; 19: 6195-6206.
    • (1999) Mol Cell Biol , vol.19 , pp. 6195-6206
    • Wang, J.M.1    Chao, J.R.2    Chen, W.3    Kuo, M.L.4    Yen, J.J.5    Yang-Yen, H.F.6
  • 90
    • 0032711250 scopus 로고    scopus 로고
    • IL-6 up-regulates mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway
    • Puthier D, Bataille R, Amiot M. IL-6 up-regulates mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway. Eur J Immunol 1999; 29: 3945-3950.
    • (1999) Eur J Immunol , vol.29 , pp. 3945-3950
    • Puthier, D.1    Bataille, R.2    Amiot, M.3
  • 92
    • 0035876931 scopus 로고    scopus 로고
    • Cooperative regulation of Mcl-1 by Janus kinase/stat and phosphatidylinositol 3-kinase contribute to granulocyte-macrophage colony-stimulating factor-delayed apoptosis in human neutrophils
    • Epling-Burnette PK, Zhong B, Bai F, Jiang K, Bailey RD, Garcia R, Jove R, Djeu JY, Loughran TP Jr, Wei S. Cooperative regulation of Mcl-1 by Janus kinase/stat and phosphatidylinositol 3-kinase contribute to granulocyte- macrophage colony-stimulating factor-delayed apoptosis in human neutrophils. J Immunol 2001; 166: 7486-7495.
    • (2001) J Immunol , vol.166 , pp. 7486-7495
    • Epling-Burnette, P.K.1    Zhong, B.2    Bai, F.3    Jiang, K.4    Bailey, R.D.5    Garcia, R.6    Jove, R.7    Djeu, J.Y.8    Loughran Jr., T.P.9    Wei, S.10
  • 93
    • 0037902100 scopus 로고    scopus 로고
    • Serine phosphorylation of STAT3 is essential for Mcl-1 expression and macrophage survival
    • Liu H, Ma Y, Cole SM, Zander C, Chen KH, KarrasJ, Pope RM. Serine phosphorylation of STAT3 is essential for Mcl-1 expression and macrophage survival. Blood 2003; 102: 344-352.
    • (2003) Blood , vol.102 , pp. 344-352
    • Liu, H.1    Ma, Y.2    Cole, S.M.3    Zander, C.4    Chen, K.H.5    Karras, J.6    Pope, R.M.7
  • 94
    • 0034698122 scopus 로고    scopus 로고
    • Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death
    • Bingle CD, Craig RW, Swales BM, Singleton V, Zhou P, Whyte MK. Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death. J Biol Chem 2000; 275: 22136-22146.
    • (2000) J Biol Chem , vol.275 , pp. 22136-22146
    • Bingle, C.D.1    Craig, R.W.2    Swales, B.M.3    Singleton, V.4    Zhou, P.5    Whyte, M.K.6
  • 95
    • 0028540185 scopus 로고
    • Antiapoptosis potential of bcl-2 oncogene by dephosphorylation
    • Haldar S, Jena N, Croce CM. Antiapoptosis potential of bcl-2 oncogene by dephosphorylation. Biochem Cell Biol 1994; 72: 455-462.
    • (1994) Biochem Cell Biol , vol.72 , pp. 455-462
    • Haldar, S.1    Jena, N.2    Croce, C.M.3
  • 96
    • 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
  • 97
    • 0030959304 scopus 로고    scopus 로고
    • Bcl-2 phosphorylation required for anti-apoptosis function
    • Ito T, Deng X, Carr B, May WS. Bcl-2 phosphorylation required for anti-apoptosis function. J Biol Chem 1997; 272: 11671-11673.
    • (1997) J Biol Chem , vol.272 , pp. 11671-11673
    • Ito, T.1    Deng, X.2    Carr, B.3    May, W.S.4
  • 98
    • 0031035693 scopus 로고    scopus 로고
    • Bcl2 is the guardian of microtubule integrity
    • Haldar S, Basu A, Croce CM. Bcl2 is the guardian of microtubule integrity. Cancer Res 1997; 57: 229-233.
    • (1997) Cancer Res , vol.57 , pp. 229-233
    • Haldar, S.1    Basu, A.2    Croce, C.M.3
  • 99
    • 0032522885 scopus 로고    scopus 로고
    • Serine-70 is one of the critical sites for drug-induced Bcl2 phosphorylation in cancer cells
    • Haldar S, Basu A, Croce CM. Serine-70 is one of the critical sites for drug-induced Bcl2 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
  • 100
    • 0343457526 scopus 로고    scopus 로고
    • Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A
    • Deng X, Ito T, Carr B, Mumby M, May WS Jr. Reversible phosphorylation of Bcl2 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., W.S.5
  • 101
    • 0034647890 scopus 로고    scopus 로고
    • Myeloid cell leukemia 1 is phosphorylated through two distinct pathways, one associated with extracellular signal-regulated kinase activation and the other with G2/M accumulation or protein phosphatase 1/2A inhibition
    • Domina AM, Smith JH, Craig RW. Myeloid cell leukemia 1 is phosphorylated through two distinct pathways, one associated with extracellular signal-regulated kinase activation and the other with G2/M accumulation or protein phosphatase 1/2A inhibition. J Biol Chem 2000; 275: 21688-21694.
    • (2000) J Biol Chem , vol.275 , pp. 21688-21694
    • Domina, A.M.1    Smith, J.H.2    Craig, R.W.3
  • 102
    • 0029043811 scopus 로고
    • Immunohistochemical analysis of Mcl-1 protein in human tissues. Differential regulation of Mcl-1 and Bcl-2 protein production suggests a unique role for Mcl-1 in control of programmed cell death in vivo
    • Krajewski S, Bodrug S, Krajewska M, Shabaik A, Gascoyne R, Berean K, Reed JC. Immunohistochemical analysis of Mcl-1 protein in human tissues. Differential regulation of Mcl-1 and Bcl-2 protein production suggests a unique role for Mcl-1 in control of programmed cell death in vivo. Am J Pathol 1995; 146: 1309-1319.
    • (1995) Am J Pathol , vol.146 , pp. 1309-1319
    • Krajewski, S.1    Bodrug, S.2    Krajewska, M.3    Shabaik, A.4    Gascoyne, R.5    Berean, K.6    Reed, J.C.7
  • 103
    • 0036234124 scopus 로고    scopus 로고
    • MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis
    • Craig RW. MCL1 provides a window on the role of the BCL2 family in cell proliferation, differentiation and tumorigenesis. Leukemia 2002; 16: 444-454.
    • (2002) Leukemia , vol.16 , pp. 444-454
    • Craig, R.W.1
  • 104
    • 0028965578 scopus 로고
    • The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2
    • Yang T, Kozopas KM, Craig RW. The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2. J Cell Biol 1995; 128: 1173-1184.
    • (1995) J Cell Biol , vol.128 , pp. 1173-1184
    • Yang, T.1    Kozopas, K.M.2    Craig, R.W.3
  • 105
    • 0032211158 scopus 로고    scopus 로고
    • Mcl-1 in transgenic mice promotes survival in a spectrum of hematopoietic cell types and immortalization in the myeloid lineage
    • Zhou P, Qian L, Bieszczad CK, Noelle R, Binder M, Levy NB, Craig RW. Mcl-1 in transgenic mice promotes survival in a spectrum of hematopoietic cell types and immortalization in the myeloid lineage. Blood 1998; 92: 3226-3239.
    • (1998) Blood , vol.92 , pp. 3226-3239
    • Zhou, P.1    Qian, L.2    Bieszczad, C.K.3    Noelle, R.4    Binder, M.5    Levy, N.B.6    Craig, R.W.7
  • 107
    • 0030033049 scopus 로고    scopus 로고
    • Expression of the Bcl-2 homologue Mcl-1 correlates with survival of peripheral blood B lymphocytes
    • Lomo J, Smeland EB, Krajewski S, Reed JC, Blomhoff HK. Expression of the Bcl-2 homologue Mcl-1 correlates with survival of peripheral blood B lymphocytes. Cancer Res 1996; 56: 40-43.
    • (1996) Cancer Res , vol.56 , pp. 40-43
    • Lomo, J.1    Smeland, E.B.2    Krajewski, S.3    Reed, J.C.4    Blomhoff, H.K.5
  • 108
    • 0030960075 scopus 로고    scopus 로고
    • Interleukin-13 in combination with CD40 ligand potently inhibits apoptosis in human B lymphocytes: Upregulation of Bcl-xL and Mcl-1
    • Lomo J, Blomhoff HK, Jacobsen SE, Krajewski S, Reed JC, Smeland EB. Interleukin-13 in combination with CD40 ligand potently inhibits apoptosis in human B lymphocytes: upregulation of Bcl-xL and Mcl-1. Blood 1997; 89: 4415-4424.
    • (1997) Blood , vol.89 , pp. 4415-4424
    • Lomo, J.1    Blomhoff, H.K.2    Jacobsen, S.E.3    Krajewski, S.4    Reed, J.C.5    Smeland, E.B.6
  • 110
    • 0035127222 scopus 로고    scopus 로고
    • Interferon alpha extends the survival of human myeloma cells through an upregulation of the Mcl-1 anti-apoptotic molecule
    • Puthier D, Thabard W, Rapp M, Etrillard M, HarousseauJ, Bataille R, Amiot M. Interferon alpha extends the survival of human myeloma cells through an upregulation of the Mcl-1 anti-apoptotic molecule. Br J Haematol 2001; 112: 358-363.
    • (2001) Br J Haematol , vol.112 , pp. 358-363
    • Puthier, D.1    Thabard, W.2    Rapp, M.3    Etrillard, M.4    Harousseau, J.5    Bataille, R.6    Amiot, M.7
  • 111
    • 0031876318 scopus 로고    scopus 로고
    • mcl-1 is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signalling pathway and is one component of the GM-CSF viability response
    • Chao JR, Wang JM, Lee SF, Peng HW, Lin YH, Chou CH, LiJC, Huang HM, Chou CK, Kuo ML, Yen JJ, Yang-Yen HF. mcl-1 is an immediate-early gene activated by the granulocyte-macrophage colony-stimulating factor (GM-CSF) signalling pathway and is one component of the GM-CSF viability response. Mol Cell Biol 1998; 18: 4883-4898.
    • (1998) Mol Cell Biol , vol.18 , pp. 4883-4898
    • Chao, J.R.1    Wang, J.M.2    Lee, S.F.3    Peng, H.W.4    Lin, Y.H.5    Chou, C.H.6    Li, J.C.7    Huang, H.M.8    Chou, C.K.9    Kuo, M.L.10    Yen, J.J.11    Yang-Yen, H.F.12
  • 112
    • 0032189802 scopus 로고    scopus 로고
    • Mcl-1 expression in human neutrophils: Regulation by cytokines and correlation with cell survival
    • Moulding DA, Quayle JA, Hart CA, Edwards SW. Mcl-1 expression in human neutrophils: regulation by cytokines and correlation with cell survival. Blood 1998; 92: 2495-2502.
    • (1998) Blood , vol.92 , pp. 2495-2502
    • Moulding, D.A.1    Quayle, J.A.2    Hart, C.A.3    Edwards, S.W.4
  • 114
    • 0032969347 scopus 로고    scopus 로고
    • Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members
    • Holmgreen SP, Huang DC, Adams JM, Cory S. Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members. Cell Death Differ 1999; 6: 525-532.
    • (1999) Cell Death Differ , vol.6 , pp. 525-532
    • Holmgreen, S.P.1    Huang, D.C.2    Adams, J.M.3    Cory, S.4
  • 115
    • 0344492705 scopus 로고    scopus 로고
    • Differential expression of bcl-w and bcl-x messenger RNA in the developing and adult rat nervous system
    • Hamner S, Skoglosa Y, Lindholm D. Differential expression of bcl-w and bcl-x messenger RNA in the developing and adult rat nervous system. Neuroscience 1999; 91: 673-684.
    • (1999) Neuroscience , vol.91 , pp. 673-684
    • Hamner, S.1    Skoglosa, Y.2    Lindholm, D.3
  • 119
    • 0344608883 scopus 로고    scopus 로고
    • The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
    • Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL. The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. EMBO J 2003; 22: 1497-1507.
    • (2003) EMBO J , vol.22 , pp. 1497-1507
    • Hinds, M.G.1    Lackmann, M.2    Skea, G.L.3    Harrison, P.J.4    Huang, D.C.5    Day, C.L.6
  • 122
    • 0034463078 scopus 로고    scopus 로고
    • Bcl-w forms complexes with Bax and Bak, and elevated ratios of Bax/Bcl-w and Bak/Bcl-w correspond to spermatogonial and spermatocyte apoptosis in the testis
    • Yan W, Samson M, Jegou B, Toppari J. Bcl-w forms complexes with Bax and Bak, and elevated ratios of Bax/Bcl-w and Bak/Bcl-w correspond to spermatogonial and spermatocyte apoptosis in the testis. Mol Endocrinol 2000; 14: 682-699.
    • (2000) Mol Endocrinol , vol.14 , pp. 682-699
    • Yan, W.1    Samson, M.2    Jegou, B.3    Toppari, J.4
  • 124
    • 0034624285 scopus 로고    scopus 로고
    • Improvement of the viability of cultured rat neurons by the non-essential amino acids L-serine and glycine that upregulates expression of the anti-apoptotic gene product Bcl-w
    • Yang L, Zhang B, Toku K, Maeda N, Sakanaka M, Tanaka J. Improvement of the viability of cultured rat neurons by the non-essential amino acids L-serine and glycine that upregulates expression of the anti-apoptotic gene product Bcl-w. Neurosci Lett 2000; 295: 97-100.
    • (2000) Neurosci Lett , vol.295 , pp. 97-100
    • Yang, L.1    Zhang, B.2    Toku, K.3    Maeda, N.4    Sakanaka, M.5    Tanaka, J.6
  • 125
    • 0034116079 scopus 로고    scopus 로고
    • Over-expression of the cell death suppressor Bcl-w in ischemic brain: Implications for a neuroprotective role via the mitochondrial pathway
    • Yan C, Chen J, Chen D, Minami M, Pei W, Yin XM, Simon RP. Over-expression of the cell death suppressor Bcl-w in ischemic brain: implications for a neuroprotective role via the mitochondrial pathway. J Cereb Blood Flow Metab 2000; 20: 620-630.
    • (2000) J Cereb Blood Flow Metab , vol.20 , pp. 620-630
    • Yan, C.1    Chen, J.2    Chen, D.3    Minami, M.4    Pei, W.5    Yin, X.M.6    Simon, R.P.7
  • 126
    • 0035929416 scopus 로고    scopus 로고
    • Characterization of NR13-related human cell death regulator, Boo/Diva, in normal and cancer tissues
    • Lee R, Chen J, Matthews CP, McDougall JK, Neiman PE. Characterization of NR13-related human cell death regulator, Boo/Diva, in normal and cancer tissues. Biochim Biophys Acta 2001; 1520: 187-194.
    • (2001) Biochim Biophys Acta , vol.1520 , pp. 187-194
    • Lee, R.1    Chen, J.2    Matthews, C.P.3    McDougall, J.K.4    Neiman, P.E.5
  • 127
    • 0029861518 scopus 로고    scopus 로고
    • Endothelial cell death induced by tumor necrosis factor-alpha is inhibited by the Bcl-2 family member, A1
    • Karsan A, Yee E, Harlan JM. Endothelial cell death induced by tumor necrosis factor-alpha is inhibited by the Bcl-2 family member, A1. J Biol Chem 1996; 271: 27201-27204.
    • (1996) J Biol Chem , vol.271 , pp. 27201-27204
    • Karsan, A.1    Yee, E.2    Harlan, J.M.3
  • 128
    • 0030952952 scopus 로고    scopus 로고
    • GRS, a novel member of the Bcl-2 gene family, is highly expressed in multiple cancer cell lines and in normal leukocytes
    • Kenny JJ, Knobloch TJ, Augustus M, Carter KC, Rosen CA, Lang JC. GRS, a novel member of the Bcl-2 gene family, is highly expressed in multiple cancer cell lines and in normal leukocytes. Oncogene 1997; 14: 997-1001.
    • (1997) Oncogene , vol.14 , pp. 997-1001
    • Kenny, J.J.1    Knobloch, T.J.2    Augustus, M.3    Carter, K.C.4    Rosen, C.A.5    Lang, J.C.6
  • 129
    • 0029915833 scopus 로고    scopus 로고
    • Cloning of human Bcl-2 homologue: Inflammatory cytokines induce human A1 in cultured endothelial cells
    • Karsan A, Yee E, Kaushansky K, Harlan JM. Cloning of human Bcl-2 homologue: inflammatory cytokines induce human A1 in cultured endothelial cells. Blood 1996; 87: 3089-3096.
    • (1996) Blood , vol.87 , pp. 3089-3096
    • Karsan, A.1    Yee, E.2    Kaushansky, K.3    Harlan, J.M.4
  • 130
    • 0032543597 scopus 로고    scopus 로고
    • Functional dissection of Bfl-1, a Bcl-2 homolog: Anti-apoptosis, oncogene-cooperation and cell proliferation activities
    • D'Sa-Eipper C, Chinnadurai G. Functional dissection of Bfl-1, a Bcl-2 homolog: anti-apoptosis, oncogene-cooperation and cell proliferation activities. Oncogene 1998; 16: 3105-3114.
    • (1998) Oncogene , vol.16 , pp. 3105-3114
    • D'Sa-Eipper, C.1    Chinnadurai, G.2
  • 131
    • 0028824266 scopus 로고
    • A novel Bcl-2 related gene, Bfl-1, is overexpressed in stomach cancer and preferentially expressed in bone marrow
    • Choi SS, Park IC, Yun JW, Sung YC, Hong SI, Shin HS. A novel Bcl-2 related gene, Bfl-1, is overexpressed in stomach cancer and preferentially expressed in bone marrow. Oncogene 1995; 11: 1693-1698.
    • (1995) Oncogene , vol.11 , pp. 1693-1698
    • Choi, S.S.1    Park, I.C.2    Yun, J.W.3    Sung, Y.C.4    Hong, S.I.5    Shin, H.S.6
  • 133
    • 0037693201 scopus 로고    scopus 로고
    • Bfl-1S, a novel alternative splice variant of Bfl-1, localises in the nucleus via its C-terminus and prevents cell death
    • Ko JK, Lee MJ, Cho SH, Cho JA, Lee BY, Koh JS, Lee SS, Shim YH, Kim CW. Bfl-1S, a novel alternative splice variant of Bfl-1, localises in the nucleus via its C-terminus and prevents cell death. Oncogene 2003; 22: 2457-2465.
    • (2003) Oncogene , vol.22 , pp. 2457-2465
    • Ko, J.K.1    Lee, M.J.2    Cho, S.H.3    Cho, J.A.4    Lee, B.Y.5    Koh, J.S.6    Lee, S.S.7    Shim, Y.H.8    Kim, C.W.9
  • 134
    • 0031324597 scopus 로고    scopus 로고
    • TNF-alpha induction of A1 expression in human cancer cells
    • Pang XP, Hershman JM, Karsan A. TNF-alpha induction of A1 expression in human cancer cells. Oncol Res 1997; 9: 623-627.
    • (1997) Oncol Res , vol.9 , pp. 623-627
    • Pang, X.P.1    Hershman, J.M.2    Karsan, A.3
  • 136
    • 0030868515 scopus 로고    scopus 로고
    • Mycobacterium bovis Bacillus Calmette Guerin infection prevents apoptosis of resting human monocytes
    • Kremer L, Estaquier J, Brandt E, Ameisen JC, Locht C. Mycobacterium bovis Bacillus Calmette Guerin infection prevents apoptosis of resting human monocytes. Eur J Immunol 1997; 27: 2450-2456.
    • (1997) Eur J Immunol , vol.27 , pp. 2450-2456
    • Kremer, L.1    Estaquier, J.2    Brandt, E.3    Ameisen, J.C.4    Locht, C.5
  • 137
    • 0033168655 scopus 로고    scopus 로고
    • The murine antiapoptotic protein A1 is induced in inflammatory macrophages and constitutively expressed in neutrophils
    • Orlofsky A, Somogyi RD, Weiss LM, Prystowsky MB. The murine antiapoptotic protein A1 is induced in inflammatory macrophages and constitutively expressed in neutrophils. J Immunol 1999; 163: 412-419.
    • (1999) J Immunol , vol.163 , pp. 412-419
    • Orlofsky, A.1    Somogyi, R.D.2    Weiss, L.M.3    Prystowsky, M.B.4
  • 138
    • 0033981935 scopus 로고    scopus 로고
    • In vitro Brucella suis infection prevents the programmed cell death of human monocytic cells
    • Gross A, Terraza A, Ouahrani-Bettache S, Liautard JP, Dornand J. In vitro Brucella suis infection prevents the programmed cell death of human monocytic cells. Infect Immun 2000; 68: 342-351.
    • (2000) Infect Immun , vol.68 , pp. 342-351
    • Gross, A.1    Terraza, A.2    Ouahrani-Bettache, S.3    Liautard, J.P.4    Dornand, J.5
  • 139
    • 0032557564 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces expression of the antiapoptotic proteins Bcl-2 and A1 in vascular endothelial cells
    • Gerber HP, Dixit V, Ferrara N. Vascular endothelial growth factor induces expression of the antiapoptotic proteins Bcl-2 and A1 in vascular endothelial cells. J Biol Chem 1998; 273: 13313-13316.
    • (1998) J Biol Chem , vol.273 , pp. 13313-13316
    • Gerber, H.P.1    Dixit, V.2    Ferrara, N.3
  • 140
    • 0030930196 scopus 로고    scopus 로고
    • STAT5A-deficient mice demonstrate a defect in granulocyte-macrophage colony-stimulating factor-induced proliferation and gene expression
    • Feldman GM, Rosenthal LA, Liu X, Hayes MP, Wynshaw-Boris A, Leonard WJ, Hennighausen L, Finbloom DS. STAT5A-deficient mice demonstrate a defect in granulocyte-macrophage colony-stimulating factor-induced proliferation and gene expression. Blood 1997; 90: 1768-1776.
    • (1997) Blood , vol.90 , pp. 1768-1776
    • Feldman, G.M.1    Rosenthal, L.A.2    Liu, X.3    Hayes, M.P.4    Wynshaw-Boris, A.5    Leonard, W.J.6    Hennighausen, L.7    Finbloom, D.S.8
  • 141
    • 0033529416 scopus 로고    scopus 로고
    • NF-kappaB-mediated up-regulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signalling in B lymphocytes
    • Lee HH, Dadgostar H, Cheng Q, Shu J, Cheng G. NF-kappaB-mediated up-regulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signalling in B lymphocytes. Proc Natl Acad Sci USA 1999; 96: 9136-9141.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9136-9141
    • Lee, H.H.1    Dadgostar, H.2    Cheng, Q.3    Shu, J.4    Cheng, G.5
  • 142
    • 0032588317 scopus 로고    scopus 로고
    • NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis
    • Wang CY, Guttridge DC, Mayo MW, Baldwin AS Jr. NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis. Mol Cell Biol 1999; 19: 5923-5929.
    • (1999) Mol Cell Biol , vol.19 , pp. 5923-5929
    • Wang, C.Y.1    Guttridge, D.C.2    Mayo, M.W.3    Baldwin Jr., A.S.4
  • 143
    • 0033558215 scopus 로고    scopus 로고
    • The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis
    • Zong WX, Edelstein LC, Chen C, Bash J, Gelinas C. The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis. Genes Dev 1999; 13: 382-387.
    • (1999) Genes Dev , vol.13 , pp. 382-387
    • Zong, W.X.1    Edelstein, L.C.2    Chen, C.3    Bash, J.4    Gelinas, C.5
  • 144
    • 0033557805 scopus 로고    scopus 로고
    • Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis
    • Grumont RJ, Rourke IJ, Gerondakis S. Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis. Genes Dev 1999; 13: 400-411.
    • (1999) Genes Dev , vol.13 , pp. 400-411
    • Grumont, R.J.1    Rourke, I.J.2    Gerondakis, S.3
  • 146
    • 0034646702 scopus 로고    scopus 로고
    • Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells
    • Zhang H, Cowan-Jacob SW, Simonen M, Greenhalf W, Heim J, Meyhack B. Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells. J Biol Chem 2000; 275: 11092-11099.
    • (2000) J Biol Chem , vol.275 , pp. 11092-11099
    • Zhang, H.1    Cowan-Jacob, S.W.2    Simonen, M.3    Greenhalf, W.4    Heim, J.5    Meyhack, B.6
  • 147
    • 0034674551 scopus 로고    scopus 로고
    • Al functions at the mitochondria to delay endothelial apoptosis in response to tumor necrosis factor
    • Duriez PJ, Wong F, Dorovini-Zis K, Shahidi R, Karsan A. Al functions at the mitochondria to delay endothelial apoptosis in response to tumor necrosis factor. J Biol Chem 2000; 275: 18099-18107.
    • (2000) J Biol Chem , vol.275 , pp. 18099-18107
    • Duriez, P.J.1    Wong, F.2    Dorovini-Zis, K.3    Shahidi, R.4    Karsan, A.5
  • 148
    • 0037151030 scopus 로고    scopus 로고
    • Bcl-2 family member Bfl-1/A1 sequesters truncated bid to inhibit is collaboration with pro-apoptotic Bak or Bax
    • Werner AB, de Vries E, Tait SW, Bontjer I, Borst J. Bcl-2 family member Bfl-1/A1 sequesters truncated bid to inhibit is collaboration with pro-apoptotic Bak or Bax. J. Biol Chem 2002; 277: 22781-22788.
    • (2002) J Biol Chem , vol.277 , pp. 22781-22788
    • Werner, A.B.1    De Vries, E.2    Tait, S.W.3    Bontjer, I.4    Borst, J.5
  • 149
    • 0029024368 scopus 로고
    • Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of a novel alternatively spliced transcript, BAX delta
    • Apte SS, Mattei MG, Olsen BR. Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of a novel alternatively spliced transcript, BAX delta. Genomics 1995; 26: 592-594.
    • (1995) Genomics , vol.26 , pp. 592-594
    • Apte, S.S.1    Mattei, M.G.2    Olsen, B.R.3
  • 150
    • 0035827622 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax
    • Cuddeback SM, Yamaguchi H, Komatsu K, Miyashita T, Yamada M, Wu C, Singh S, Wang HG. Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax. J Biol Chem 2001; 276: 20559-20565.
    • (2001) J Biol Chem , vol.276 , pp. 20559-20565
    • Cuddeback, S.M.1    Yamaguchi, H.2    Komatsu, K.3    Miyashita, T.4    Yamada, M.5    Wu, C.6    Singh, S.7    Wang, H.G.8
  • 151
    • 0029917541 scopus 로고    scopus 로고
    • Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
    • Zha H, Aime-Sempe C, Sato T, Reed JC. Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem 1996; 271: 7440-7444.
    • (1996) J Biol Chem , vol.271 , pp. 7440-7444
    • Zha, H.1    Aime-Sempe, C.2    Sato, T.3    Reed, J.C.4
  • 153
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T, Reed JC. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 1995; 80: 293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 154
    • 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
  • 156
    • 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
  • 157
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and iritracellular localization
    • Suzuki M, Youle RJ, Tjandra N. Structure of Bax: coregulation of dimer formation and iritracellular localization. Cell 2000; 103: 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 158
    • 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
  • 159
    • 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: 11615-11623.
    • (2001) J Biol Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 160
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A, Bassik MC, Walensky LD, Sorcinelli MD, Weiler S, Korsmeyer SJ. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2002; 2: 183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 165
    • 0037115740 scopus 로고    scopus 로고
    • Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein
    • Roucou X, Montessuit S, Antonsson B, Martinou JC. Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein. Biochem J 2002; 368: 915-921.
    • (2002) Biochem J , vol.368 , pp. 915-921
    • Roucou, X.1    Montessuit, S.2    Antonsson, B.3    Martinou, J.C.4
  • 166
    • 0037458090 scopus 로고    scopus 로고
    • Apoptosis: Mitochondrial membrane permeabilization - The (w)hole story?
    • Zamzami N, Kroemer G. Apoptosis: mitochondrial membrane permeabilization - the (w)hole story? Curr Biol 2003; 13: R71-R73.
    • (2003) Curr Biol , vol.13
    • Zamzami, N.1    Kroemer, G.2
  • 167
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A, Jockel J, Wei MC, Korsmeyer SJ. Enforced dimerization of BAX
    • (1998) EMBO J , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 168
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu YT, Youle RJ. Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem 1997; 272: 13829-13834.
    • (1997) J Biol Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 169
    • 0029906828 scopus 로고    scopus 로고
    • BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases
    • Xiang J, Chao DT, Korsmeyer SJ. BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases. Proc Natl Acad Sci USA 1996; 93: 14559-14563.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 170
    • 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
  • 171
  • 172
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane DM, Bossy-Wetzel E, Waterhouse NJ, Cotter TG, Green DR. Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J Biol Chem 1999; 274: 2225-2233.
    • (1999) J Biol Chem , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 174
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochoridrial transmembrane depolarization
    • Bossy-Wetzel E, Newmeyer DD, Green DR. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochoridrial transmembrane depolarization. EMBO J 1998; 17: 37-49.
    • (1998) EMBO J , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 176
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak
    • McCarthy NJ, Whyte MK, Gilbert CS, Evan GI. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J Cell Biol 1997; 136: 215-227.
    • (1997) J Cell Biol , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.2    Gilbert, C.S.3    Evan, G.I.4
  • 178
    • 0033539507 scopus 로고    scopus 로고
    • Cytokine-mediated Bax deficiency and consequent delayed neutrophil apoptosis: A general mechanism to accumulate effector cells in inflammation
    • Dibbert B, Weber M, Nikolaizik WH, Vogt P, Schoni MH, Blaser K, Simon HU. Cytokine-mediated Bax deficiency and consequent delayed neutrophil apoptosis: a general mechanism to accumulate effector cells in inflammation. Proc Natl Acad Sci USA 1999; 96: 13330-13335.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13330-13335
    • Dibbert, B.1    Weber, M.2    Nikolaizik, W.H.3    Vogt, P.4    Schoni, M.H.5    Blaser, K.6    Simon, H.U.7
  • 179
    • 0033533726 scopus 로고    scopus 로고
    • Relative level of expression of Bax and Bcl-XT, determines the cellular fate of apoptosis/necrosis induced by the overexpression of Bax
    • Shinoura N, Yoshida Y, Asai A, Kirino T, Hamada H. Relative level of expression of Bax and Bcl-XT, determines the cellular fate of apoptosis/necrosis induced by the overexpression of Bax. Oncogene 1999; 18: 5703-5713.
    • (1999) Oncogene , vol.18 , pp. 5703-5713
    • Shinoura, N.1    Yoshida, Y.2    Asai, A.3    Kirino, T.4    Hamada, H.5
  • 185
    • 2342553892 scopus 로고    scopus 로고
    • Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex
    • Leu JI, Dumont P, Hafey M, Murphy ME, George DL. Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex. Nat Cell Biol 2004; 6: 443-450.
    • (2004) Nat Cell Biol , vol.6 , pp. 443-450
    • Leu, J.I.1    Dumont, P.2    Hafey, M.3    Murphy, M.E.4    George, D.L.5
  • 186
    • 0033554620 scopus 로고    scopus 로고
    • The cell death regulatory protein bak is expressed in endothelial cells in inflamed tissues and Is induced by IFN-gamma in vitro
    • Pammer J, Weninger W, Ban J, Wojta J, Tschachler E. The cell death regulatory protein bak is expressed in endothelial cells in inflamed tissues and Is induced by IFN-gamma in vitro. Biochem Biophys Res Commun 1999; 264: 139-143.
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 139-143
    • Pammer, J.1    Weninger, W.2    Ban, J.3    Wojta, J.4    Tschachler, E.5
  • 189
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer SJ, Wei MC, Saito M, Weiler S, Oh KJ, Schlesinger PH. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ 2000; 7: 1166-1173.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 191
    • 0035844225 scopus 로고    scopus 로고
    • Neuron-specific Bcl-2 homology 3 domain-only splice variant of Bak is anti-apoptotic in neurons, but pro-apoptotic in non-neuronal cells
    • Sun YF, Yu LY, Saarma M, Timmusk T, Arumae U. Neuron-specific Bcl-2 homology 3 domain-only splice variant of Bak is anti-apoptotic in neurons, but pro-apoptotic in non-neuronal cells. J Biol Chem 2001; 276: 16240-16247.
    • (2001) J Biol Chem , vol.276 , pp. 16240-16247
    • Sun, Y.F.1    Yu, L.Y.2    Saarma, M.3    Timmusk, T.4    Arumae, U.5
  • 192
    • 0001003612 scopus 로고    scopus 로고
    • Bokis a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members
    • Hsu SY, Kaipia A, McGee E, Lomeli M, Hsueh AJ. Bokis a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proc Natl Acad Sci USA 1997; 94: 12401-12406.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12401-12406
    • Hsu, S.Y.1    Kaipia, A.2    McGee, E.3    Lomeli, M.4    Hsueh, A.J.5
  • 193
    • 0032502776 scopus 로고    scopus 로고
    • Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XL
    • Inohara N, Ekhterae D, Garcia I, Carrio R, Merino J, Merry A, Chen S, Nunez G. Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XL. J Biol Chem 1998; 273: 8705-8710.
    • (1998) J Biol Chem , vol.273 , pp. 8705-8710
    • Inohara, N.1    Ekhterae, D.2    Garcia, I.3    Carrio, R.4    Merino, J.5    Merry, A.6    Chen, S.7    Nunez, G.8
  • 194
    • 0028965578 scopus 로고
    • The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2
    • Yang T, Kozopas KM, Craig RW. The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2. J Cell Biol 1995; 128: 1173-1184.
    • (1995) J Cell Biol , vol.128 , pp. 1173-1184
    • Yang, T.1    Kozopas, K.M.2    Craig, R.W.3
  • 196
    • 0034282917 scopus 로고    scopus 로고
    • Drosophila proapoptotic Bcl-2/Bax homologue reveals evolutionary conservation of cell death mechanisms
    • Zhang H, Huang Q, Ke N, Matsuyama S, Hammock B, Godzik A, Reed JC. Drosophila proapoptotic Bcl-2/Bax homologue reveals evolutionary conservation of cell death mechanisms. J Biol Chem 2000; 275: 27303-27306.
    • (2000) J Biol Chem , vol.275 , pp. 27303-27306
    • Zhang, H.1    Huang, Q.2    Ke, N.3    Matsuyama, S.4    Hammock, B.5    Godzik, A.6    Reed, J.C.7
  • 197
    • 0001587938 scopus 로고    scopus 로고
    • A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitro
    • Hsu SY, Hsueh AJ. A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitro. J Biol Chem 1998; 273: 30139-30146.
    • (1998) J Biol Chem , vol.273 , pp. 30139-30146
    • Hsu, S.Y.1    Hsueh, A.J.2
  • 201
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 1995; 80: 285-291.
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boise, L.H.4    Thompson, C.B.5    Korsmeyer, S.J.6
  • 202
    • 14444280882 scopus 로고    scopus 로고
    • Expression and function of a proapoptotic Bcl-2 family member Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary
    • Kaipia A, Hsu SY, Hsueh AJ. Expression and function of a proapoptotic Bcl-2 family member Bcl-XL/Bcl-2-associated death promoter (BAD) in rat ovary. Endocrinology 1997; 138: 5497-5504.
    • (1997) Endocrinology , vol.138 , pp. 5497-5504
    • Kaipia, A.1    Hsu, S.Y.2    Hsueh, A.J.3
  • 203
    • 0034682812 scopus 로고    scopus 로고
    • BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • Tan Y, Demeter MR, Ruan H, Comb MJ. BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J Biol Chem 2000; 275: 25865-25869.
    • (2000) J Biol Chem , vol.275 , pp. 25865-25869
    • Tan, Y.1    Demeter, M.R.2    Ruan, H.3    Comb, M.J.4
  • 204
    • 0034637606 scopus 로고    scopus 로고
    • Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155
    • Zhou XM, Liu Y, Payne G, Lutz RJ, Chittenden T. Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155. J Biol Chem 2000; 275: 25046-25051.
    • (2000) J Biol Chem , vol.275 , pp. 25046-25051
    • Zhou, X.M.1    Liu, Y.2    Payne, G.3    Lutz, R.J.4    Chittenden, T.5
  • 205
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 Proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • Datta SR, Katsov A, Hu L, Petros A, Fesik SW, Yaffe MB, Greenberg ME. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol Cell 2000; 6: 41-51.
    • (2000) Mol Cell , vol.6 , pp. 41-51
    • Datta, S.R.1    Katsov, A.2    Hu, L.3    Petros, A.4    Fesik, S.W.5    Yaffe, M.B.6    Greenberg, M.E.7
  • 206
    • 0034661857 scopus 로고    scopus 로고
    • Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155
    • Lizcano JM, Morrice N, Cohen P. Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. Biochem J 2000; 349: 547-557.
    • (2000) Biochem J , vol.349 , pp. 547-557
    • Lizcano, J.M.1    Morrice, N.2    Cohen, P.3
  • 207
    • 0034699352 scopus 로고    scopus 로고
    • Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival
    • Virdee K, Parone PA, Tolkovsky AM. Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival. Curr Biol 2000; 10: 1151-1154.
    • (2000) Curr Biol , vol.10 , pp. 1151-1154
    • Virdee, K.1    Parone, P.A.2    Tolkovsky, A.M.3
  • 209
    • 3042800912 scopus 로고    scopus 로고
    • Rac1 inhibits apoptosis in human lymphoma cells by stimulating Bad phosphorylation on Ser-75
    • Zhang B, Zhang Y, Shacter E. Rac1 inhibits apoptosis in human lymphoma cells by stimulating Bad phosphorylation on Ser-75. Mol Cell Biol 2004; 24: 6205-6214.
    • (2004) Mol Cell Biol , vol.24 , pp. 6205-6214
    • Zhang, B.1    Zhang, Y.2    Shacter, E.3
  • 210
    • 0038482014 scopus 로고    scopus 로고
    • Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis
    • Won J, Kim DY, La M, Kim D, Meadows GG, Joe CO. Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis. J Biol Chem 2003; 278: 19347-19351.
    • (2003) J Biol Chem , vol.278 , pp. 19347-19351
    • Won, J.1    Kim, D.Y.2    La, M.3    Kim, D.4    Meadows, G.G.5    Joe, C.O.6
  • 211
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, Greenberg ME. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997; 91: 231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 212
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • Del Peso L, Gonzalez-Garcia M, Page C, Herrera R, Nunez. G. 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    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 214
    • 0346995278 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathway-dependent tumor-specific survival signalling in melanoma cells through inactivation of the proapoptotic protein Bad
    • Eisenmann KM, VanBrocklin MW, Staffend NA, Kitchen SM, Koo HM. Mitogen-activated protein kinase pathway-dependent tumor-specific survival signalling in melanoma cells through inactivation of the proapoptotic protein Bad. Cancer Res 2003; 63: 8330-8337.
    • (2003) Cancer Res , vol.63 , pp. 8330-8337
    • Eisenmann, K.M.1    Vanbrocklin, M.W.2    Staffend, N.A.3    Kitchen, S.M.4    Koo, H.M.5
  • 215
    • 3142691373 scopus 로고    scopus 로고
    • Interleukin-7 inactivates the pro-apoptotic protein Bad promoting T cell survival
    • Li WQ, Jiang Q, Khaled AR, Keller JR, Durum SK. Interleukin-7 inactivates the pro-apoptotic protein Bad promoting T cell survival. J Biol Chem 2004; 279: 29160-29166.
    • (2004) J Biol Chem , vol.279 , pp. 29160-29166
    • Li, W.Q.1    Jiang, Q.2    Khaled, A.R.3    Keller, J.R.4    Durum, S.K.5
  • 216
    • 0033581927 scopus 로고    scopus 로고
    • Regulation of BAD phosphorylation at serine 112 by the Ras-mitogen-activated protein kinase pathway
    • Fang X, Yu S, Eder A, Mao M, Bast RC Jr, Boyd D, Mills GB. Regulation of BAD phosphorylation at serine 112 by the Ras-mitogen-activated protein kinase pathway. Oncogene 1999; 18: 6635-6640.
    • (1999) Oncogene , vol.18 , pp. 6635-6640
    • Fang, X.1    Yu, S.2    Eder, A.3    Mao, M.4    Bast Jr., R.C.5    Boyd, D.6    Mills, G.B.7
  • 218
    • 0036660617 scopus 로고    scopus 로고
    • Phenylephrine promotes phosphorylation of Bad in cardiac myocytes through the extracellular signal-regulated kinases 1/2 and protein kinase A
    • Valks DM, Cook SA, Pham FH, Morrison PR, Clerk A, Sugden PH. Phenylephrine promotes phosphorylation of Bad in cardiac myocytes through the extracellular signal-regulated kinases 1/2 and protein kinase A. J Mol Cell Cardiol 2002; 34: 749-763.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 749-763
    • Valks, D.M.1    Cook, S.A.2    Pham, F.H.3    Morrison, P.R.4    Clerk, A.5    Sugden, P.H.6
  • 219
    • 0041631073 scopus 로고    scopus 로고
    • p21-Activated kinase 5 (Pak5) localises to mitochondria and inhibits apoptosis by phosphorylating BAD
    • Cotteret S, Jaffer ZM, Beeser A, ChernoffJ. p21-Activated kinase 5 (Pak5) localises to mitochondria and inhibits apoptosis by phosphorylating BAD. Mol Cell Biol 2003; 23: 5526-5539.
    • (2003) Mol Cell Biol , vol.23 , pp. 5526-5539
    • Cotteret, S.1    Jaffer, Z.M.2    Beeser, A.3    Chernoff, J.4
  • 220
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta SR, Brunet A, Greenberg ME. Cellular survival: a play in three Akts. Genes Dev 1999; 13: 2905-2927.
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 222
    • 0035907371 scopus 로고    scopus 로고
    • p21-activated protein kinase gamma-PAK suppresses programmed cell death of BALB3T3 fibroblasts
    • Jakobi R, Moertl E, Koeppel MA. p21-activated protein kinase gamma-PAK suppresses programmed cell death of BALB3T3 fibroblasts. J Biol Chem 2001; 276: 16624-16634.
    • (2001) J Biol Chem , vol.276 , pp. 16624-16634
    • Jakobi, R.1    Moertl, E.2    Koeppel, M.A.3
  • 223
    • 0035957986 scopus 로고    scopus 로고
    • The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis
    • Gnesutta N, Qu J, Minden A. The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis. J Biol Chem 2001; 276: 14414-14419.
    • (2001) J Biol Chem , vol.276 , pp. 14414-14419
    • Gnesutta, N.1    Qu, J.2    Minden, A.3
  • 224
    • 0041631073 scopus 로고    scopus 로고
    • p21-activated kinase 5 (Pak5) localises to mitochondria and inhibits apoptosis by phosphorylating BAD
    • Cotteret S, Jaffer ZM, Beeser A, Chernoff J. p21-activated kinase 5 (Pak5) localises to mitochondria and inhibits apoptosis by phosphorylating BAD. Mol Cell Biol 2003; 23: 5526-5539.
    • (2003) Mol Cell Biol , vol.23 , pp. 5526-5539
    • Cotteret, S.1    Jaffer, Z.M.2    Beeser, A.3    Chernoff, J.4
  • 225
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, Greenberg ME. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997; 91: 231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 226
    • 0032543578 scopus 로고    scopus 로고
    • The kit receptor promotes cell survival via activation of PI 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136
    • Blume-Jensen P, Janknecht R, Hunter T. The kit receptor promotes cell survival via activation of PI 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136. Curr Biol 1998; 8: 779-782.
    • (1998) Curr Biol , vol.8 , pp. 779-782
    • Blume-Jensen, P.1    Janknecht, R.2    Hunter, T.3
  • 228
    • 0242580961 scopus 로고    scopus 로고
    • The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death
    • Yan B, Zemskova M, Holder S, Chin V, Kraft A, Koskinen PJ, Lilly M. The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death. J Biol Chem 2003; 278: 45358-45367.
    • (2003) J Biol Chem , vol.278 , pp. 45358-45367
    • Yan, B.1    Zemskova, M.2    Holder, S.3    Chin, V.4    Kraft, A.5    Koskinen, P.J.6    Lilly, M.7
  • 229
    • 0038732434 scopus 로고    scopus 로고
    • Overexpression of BAD potentiates sensitivity to tumor necrosis factor-related apoptosis-inducing ligand treatment in the prostatic carcinoma cell line LNCaP
    • Taghiyev AF, Guseva NV, Harada H, Knudson CM, Rokhlin OW, Cohen MB. Overexpression of BAD potentiates sensitivity to tumor necrosis factor-related apoptosis-inducing ligand treatment in the prostatic carcinoma cell line LNCaP. Mol Cancer Res 2003; 1: 500-507.
    • (2003) Mol Cancer Res , vol.1 , pp. 500-507
    • Taghiyev, A.F.1    Guseva, N.V.2    Harada, H.3    Knudson, C.M.4    Rokhlin, O.W.5    Cohen, M.B.6
  • 232
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998; 94: 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 235
    • 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
  • 236
    • 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, Jemmerson R, Wang X. 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    Jemmerson, R.4    Wang, X.5
  • 237
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G, Dallaporta B, Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 1998; 60: 619-642.
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 240
    • 0030970085 scopus 로고    scopus 로고
    • Harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L)
    • Inohara N, Ding L, Chen S, Nunez G. harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L). EMBO J 1997; 16: 1686-1694.
    • (1997) EMBO J , vol.16 , pp. 1686-1694
    • Inohara, N.1    Ding, L.2    Chen, S.3    Nunez, G.4
  • 241
    • 0030854775 scopus 로고    scopus 로고
    • Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death
    • Imaizumi K, Tsuda M, Imai Y, Wanaka A, Takagi T, Tohyama M. Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death. J Biol Chem 1997; 272: 18842-18848.
    • (1997) J Biol Chem , vol.272 , pp. 18842-18848
    • Imaizumi, K.1    Tsuda, M.2    Imai, Y.3    Wanaka, A.4    Takagi, T.5    Tohyama, M.6
  • 242
    • 0034194365 scopus 로고    scopus 로고
    • Specific and rapid induction of the proapoptotic protein Hrk after growth factor withdrawal in hematopoietic progenitor cells
    • Sanz C, Benito A, Inohara N, Ekhterae D, Nunez G, Fernandez-Luna JL. Specific and rapid induction of the proapoptotic protein Hrk after growth factor withdrawal in hematopoietic progenitor cells. Blood 2000; 95: 2742-2747.
    • (2000) Blood , vol.95 , pp. 2742-2747
    • Sanz, C.1    Benito, A.2    Inohara, N.3    Ekhterae, D.4    Nunez, G.5    Fernandez-Luna, J.L.6
  • 243
    • 0033583218 scopus 로고    scopus 로고
    • The cell death-promoting gene DP5, which interacts with the BCL2 family, is induced during neuronal apoptosis following exposure to amyloid beta protein
    • Imaizumi K, Morihara T, Mori Y, Katayama T, Tsuda M, Furuyama T, Wanaka A, Takeda M, Tohyama M. The cell death-promoting gene DP5, which interacts with the BCL2 family, is induced during neuronal apoptosis following exposure to amyloid beta protein. J Biol Chem 1999; 274: 7975-7981.
    • (1999) J Biol Chem , vol.274 , pp. 7975-7981
    • Imaizumi, K.1    Morihara, T.2    Mori, Y.3    Katayama, T.4    Tsuda, M.5    Furuyama, T.6    Wanaka, A.7    Takeda, M.8    Tohyama, M.9
  • 244
    • 0035851204 scopus 로고    scopus 로고
    • BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons
    • Harris CA, Johnson EM Jr. BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons. J Biol Chem 2001; 276: 37754-377560.
    • (2001) J Biol Chem , vol.276 , pp. 37754-377560
    • Harris, C.A.1    Johnson Jr., E.M.2
  • 245
    • 0035834274 scopus 로고    scopus 로고
    • Upregulation of the pro-apoptotic BH3-only peptide harakiri in spinal neurons of amyotrophic lateral sclerosis patients
    • Shinoe T, Wanaka A, Nikaido T, Kanazawa K, Shimizu J, Imaizumi K, Kanazawa I. Upregulation of the pro-apoptotic BH3-only peptide harakiri in spinal neurons of amyotrophic lateral sclerosis patients. Neurosci Lett 2001; 313: 153-157.
    • (2001) Neurosci Lett , vol.313 , pp. 153-157
    • Shinoe, T.1    Wanaka, A.2    Nikaido, T.3    Kanazawa, K.4    Shimizu, J.5    Imaizumi, K.6    Kanazawa, I.7
  • 246
    • 0037169186 scopus 로고    scopus 로고
    • Up-regulation of Hrk, a regulator of cell death, in retinal ganglion cells of axotomized rat retina
    • Wakabayashi T, Kosaka J, Hommura S. Up-regulation of Hrk, a regulator of cell death, in retinal ganglion cells of axotomized rat retina. Neurosci Lett 2002; 318: 77-80.
    • (2002) Neurosci Lett , vol.318 , pp. 77-80
    • Wakabayashi, T.1    Kosaka, J.2    Hommura, S.3
  • 247
    • 0034194365 scopus 로고    scopus 로고
    • Specific and rapid induction of the proapoptotic protein Hrk after growth factor withdrawal in hematopoietic progenitor cells
    • Sanz C, Benito A, Inohara N, Ekhterae D, Nunez G, Fernandez-LunaJL. Specific and rapid induction of the proapoptotic protein Hrk after growth factor withdrawal in hematopoietic progenitor cells. Blood 2000; 95: 2742-2747.
    • (2000) Blood , vol.95 , pp. 2742-2747
    • Sanz, C.1    Benito, A.2    Inohara, N.3    Ekhterae, D.4    Nunez, G.5    Fernandez-Luna, J.L.6
  • 248
    • 0037367272 scopus 로고    scopus 로고
    • Expression of apoptosis-related genes during human preimplantation embryo development: Potential roles for the Harakiri gene product and Caspase-3 in blastomere fragmentation
    • Jurisicora A, Antenos M, Varmuza S, Tilly JL, Casper RF. Expression of apoptosis-related genes during human preimplantation embryo development: potential roles for the Harakiri gene product and Caspase-3 in blastomere fragmentation. Mol Hum Reprod 2003; 9: 133-141.
    • (2003) Mol Hum Reprod , vol.9 , pp. 133-141
    • Jurisicora, A.1    Antenos, M.2    Varmuza, S.3    Tilly, J.L.4    Casper, R.F.5
  • 249
    • 0035341218 scopus 로고    scopus 로고
    • Interleukin 3-dependent activation of DREAM is involved in transcriptional silencing of the apoptotic Hrk gene in hematopoietic progenitor cells
    • Sanz C, Mellstrom B, Link WA, Naranjo JR, Fernandez-Luna JL. Interleukin 3-dependent activation of DREAM is involved in transcriptional silencing of the apoptotic Hrk gene in hematopoietic progenitor cells. EMBO J 2001; 20: 2286-2292.
    • (2001) EMBO J , vol.20 , pp. 2286-2292
    • Sanz, C.1    Mellstrom, B.2    Link, W.A.3    Naranjo, J.R.4    Fernandez-Luna, J.L.5
  • 252
    • 0032161337 scopus 로고    scopus 로고
    • BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members
    • Hsu SY, Lin P, Hsueh AJ. BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. Mol Endocrinol 1998; 12: 1432-1440.
    • (1998) Mol Endocrinol , vol.12 , pp. 1432-1440
    • Hsu, S.Y.1    Lin, P.2    Hsueh, A.J.3
  • 255
    • 0033607506 scopus 로고    scopus 로고
    • Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity
    • Bouillet P, Metcalf D, Huang DC, Tarlinton DM, Kay TW, Kontgen F, Adams JM, Strasser A. Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science 1999; 286: 1735-1738.
    • (1999) Science , vol.286 , pp. 1735-1738
    • Bouillet, P.1    Metcalf, D.2    Huang, D.C.3    Tarlinton, D.M.4    Kay, T.W.5    Kontgen, F.6    Adams, J.M.7    Strasser, A.8
  • 257
    • 0035135349 scopus 로고    scopus 로고
    • Downregulation of Bim, a proapoptotic relative of Bcl-2, is a pivotal step in cytokine-initiated survival signalling in murine hematopoietic progenitors
    • Shinjyo T, Kuribara R, Inukai T, Hosoi H, Kinoshita T, Miyajima A, Houghton PJ, Look AT, Ozawa K, Inaba T. Downregulation of Bim, a proapoptotic relative of Bcl-2, is a pivotal step in cytokine-initiated survival signalling in murine hematopoietic progenitors. Mol Cell Biol 2001; 21: 854-864.
    • (2001) Mol Cell Biol , vol.21 , pp. 854-864
    • Shinjyo, T.1    Kuribara, R.2    Inukai, T.3    Hosoi, H.4    Kinoshita, T.5    Miyajima, A.6    Houghton, P.J.7    Look, A.T.8    Ozawa, K.9    Inaba, T.10
  • 258
    • 0035049449 scopus 로고    scopus 로고
    • Dominant-negative c-Jun promotes neuronal survival by reducing BIM expression and inhibiting mitochondrial cytochrome c release
    • Whitfield J, Neame SJ, Paquet L, Bernard O, Ham J. Dominant-negative c-Jun promotes neuronal survival by reducing BIM expression and inhibiting mitochondrial cytochrome c release. Neuron 2001; 29: 629-643.
    • (2001) Neuron , vol.29 , pp. 629-643
    • Whitfield, J.1    Neame, S.J.2    Paquet, L.3    Bernard, O.4    Ham, J.5
  • 260
    • 0035977077 scopus 로고    scopus 로고
    • Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family
    • Mami U, Miyashita T, Shikama Y, Tadokoro K, Yamada M. Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family. FEBS Lett 2001; 509: 135-141.
    • (2001) FEBS Lett , vol.509 , pp. 135-141
    • Mami, U.1    Miyashita, T.2    Shikama, Y.3    Tadokoro, K.4    Yamada, M.5
  • 261
    • 0037092570 scopus 로고    scopus 로고
    • Identification and characterization of Bimgamma, a novel proapoptotic BH3-only splice variant of Bim
    • Liu JW, Chandra D, Tang SH, Chopra D, Tang DG. Identification and characterization of Bimgamma, a novel proapoptotic BH3-only splice variant of Bim. Cancer Res 2002; 62: 2976-2981.
    • (2002) Cancer Res , vol.62 , pp. 2976-2981
    • Liu, J.W.1    Chandra, D.2    Tang, S.H.3    Chopra, D.4    Tang, D.G.5
  • 262
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 1999; 3: 287-296.
    • (1999) Mol Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 263
    • 0034609737 scopus 로고    scopus 로고
    • Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1
    • Dijkers PF, Medema RH, Lammers JW, Koenderman L, Coffer PJ. Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. Curr Biol 2000; 10: 1201-1204.
    • (2000) Curr Biol , vol.10 , pp. 1201-1204
    • Dijkers, P.F.1    Medema, R.H.2    Lammers, J.W.3    Koenderman, L.4    Coffer, P.J.5
  • 266
    • 1542275411 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases 1/2 are serum-stimulated "Bim(EL) kinases" that bind to the BH3-only protein Bim(EL) causing its phosphorylation and turnover
    • Ley R, Ewings KE, Hadfield K, Howes E, Balmanno K, Cook SJ. Extracellular signal-regulated kinases 1/2 are serum-stimulated "Bim(EL) kinases" that bind to the BH3-only protein Bim(EL) causing its phosphorylation and turnover. J Biol Chem 2004; 279: 8837-8847.
    • (2004) J Biol Chem , vol.279 , pp. 8837-8847
    • Ley, R.1    Ewings, K.E.2    Hadfield, K.3    Howes, E.4    Balmanno, K.5    Cook, S.J.6
  • 267
    • 0842342610 scopus 로고    scopus 로고
    • Caspase cleavage of BimEL triggers a positive feedback amplification of apoptotic signalling
    • Chen D, Zhou Q. Caspase cleavage of BimEL triggers a positive feedback amplification of apoptotic signalling. Proc Natl Acad Sci USA 2004; 101: 1235-1240.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1235-1240
    • Chen, D.1    Zhou, Q.2
  • 268
    • 0242521470 scopus 로고    scopus 로고
    • Phosphorylation of Bim-EL by Erk1/2 on serine 69 promotes its degradation via the proteasome pathway and regulates its proapoptotic function
    • Luciano F, Jacquel A, Colosetti P, Herrant M, Cagnol S, Pages G, Auberger P. Phosphorylation of Bim-EL by Erk1/2 on serine 69 promotes its degradation via the proteasome pathway and regulates its proapoptotic function. Oncogene 2003; 22: 6785-6793.
    • (2003) Oncogene , vol.22 , pp. 6785-6793
    • Luciano, F.1    Jacquel, A.2    Colosetti, P.3    Herrant, M.4    Cagnol, S.5    Pages, G.6    Auberger, P.7
  • 271
    • 0036097786 scopus 로고    scopus 로고
    • Keeping killers on a tight leash: Transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins
    • Puthalakath H, Strasser A. Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins. Cell Death Differ 2002; 9: 505-512.
    • (2002) Cell Death Differ , vol.9 , pp. 505-512
    • Puthalakath, H.1    Strasser, A.2
  • 273
    • 0035049449 scopus 로고    scopus 로고
    • Dominant-negative c-Jun promotes neuronal survival by reducing BIM expression and inhibiting mitochoridrial cytochrome c release
    • Whitfield J, Neame SJ, Paquet L, Bernard O, Ham J. Dominant-negative c-Jun promotes neuronal survival by reducing BIM expression and inhibiting mitochoridrial cytochrome c release. Neuron 2001; 29: 629-643.
    • (2001) Neuron , vol.29 , pp. 629-643
    • Whitfield, J.1    Neame, S.J.2    Paquet, L.3    Bernard, O.4    Ham, J.5
  • 275
    • 0035851204 scopus 로고    scopus 로고
    • BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons
    • Harris CA, Johnson EM Jr. BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons. J Biol Chem 2001; 276: 37754-37760.
    • (2001) J Biol Chem , vol.276 , pp. 37754-37760
    • Harris, C.A.1    Johnson Jr., E.M.2
  • 279
    • 0037017396 scopus 로고    scopus 로고
    • FKHR-L1 can act as a critical effector of cell death induced by cytokine withdrawal: Protein kinase B-enhanced cell survival through maintenance of mitochondrial integrity
    • Dijkers PF, Birkenkamp KU, Lam EW, Thomas NS, Lammers JW, Koenderman L, Coffer PJ. FKHR-L1 can act as a critical effector of cell death induced by cytokine withdrawal: protein kinase B-enhanced cell survival through maintenance of mitochondrial integrity. J Cell Biol 2002; 156: 531-542.
    • (2002) J Cell Biol , vol.156 , pp. 531-542
    • Dijkers, P.F.1    Birkenkamp, K.U.2    Lam, E.W.3    Thomas, N.S.4    Lammers, J.W.5    Koenderman, L.6    Coffer, P.J.7
  • 280
    • 0037094096 scopus 로고    scopus 로고
    • The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2
    • Stahl M, Dijkers PF, Kops GJ, Lens SM, Coffer PJ, Burgering BM, Medema RH. The forkhead transcription factor FoxO regulates transcription of p27Kip1 and Bim in response to IL-2. J Immunol 2002; 168: 5024-5031.
    • (2002) J Immunol , vol.168 , pp. 5024-5031
    • Stahl, M.1    Dijkers, P.F.2    Kops, G.J.3    Lens, S.M.4    Coffer, P.J.5    Burgering, B.M.6    Medema, R.H.7
  • 281
    • 1542327683 scopus 로고    scopus 로고
    • Regulation of expression of Bcl-2 protein family member Bim by T cell receptor triggering
    • Sandalova E, Wei CH, Masucci MG, Levitsky V. Regulation of expression of Bcl-2 protein family member Bim by T cell receptor triggering. Proc Natl Acad Sci USA 2004; 101: 3011-3016.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3011-3016
    • Sandalova, E.1    Wei, C.H.2    Masucci, M.G.3    Levitsky, V.4
  • 283
    • 0032511994 scopus 로고    scopus 로고
    • Regulation of apoptosis by a Caenorhabditis elegans BNIP3 homolog
    • Yasuda M, D'Sa-Eipper C, Gong XL, Chinnadurai G. Regulation of apoptosis by a Caenorhabditis elegans BNIP3 homolog. Oncogene 1998; 17: 2525-2530.
    • (1998) Oncogene , vol.17 , pp. 2525-2530
    • Yasuda, M.1    D'Sa-Eipper, C.2    Gong, X.L.3    Chinnadurai, G.4
  • 284
    • 0034676339 scopus 로고    scopus 로고
    • The C. elegans orthologue ceBNIP3 interacts with CED-9 and CED-3 but kills through a BH3- and caspase-independent mechanism
    • Cizeau J, Ray R, Chen G, Gietz RD, Greenberg AH. The C. elegans orthologue ceBNIP3 interacts with CED-9 and CED-3 but kills through a BH3- and caspase-independent mechanism. Oncogene 2000; 19: 5453-5463.
    • (2000) Oncogene , vol.19 , pp. 5453-5463
    • Cizeau, J.1    Ray, R.2    Chen, G.3    Gietz, R.D.4    Greenberg, A.H.5
  • 285
    • 0032995799 scopus 로고    scopus 로고
    • Novel BNIP1 variants and their interaction with BCL2 family members
    • Zhang H, Heim J, Meyhack B. Novel BNIP1 variants and their interaction with BCL2 family members. FEBS Lett 1999; 448: 23-27.
    • (1999) FEBS Lett , vol.448 , pp. 23-27
    • Zhang, H.1    Heim, J.2    Meyhack, B.3
  • 286
    • 0034604073 scopus 로고    scopus 로고
    • Functional identification of the apoptosis effector BH3 domain in cellular protein BNIP1
    • Yasuda M, Chinnadurai G. Functional identification of the apoptosis effector BH3 domain in cellular protein BNIP1. Oncogene 2000; 19: 2363-2367.
    • (2000) Oncogene , vol.19 , pp. 2363-2367
    • Yasuda, M.1    Chinnadurai, G.2
  • 287
    • 0030975797 scopus 로고    scopus 로고
    • Identification of estrogen-responsive genes in neuroblastoma SK-ER3 cells
    • Garnier M, Di Lorenzo D, Albertini A, Maggi A. Identification of estrogen-responsive genes in neuroblastoma SK-ER3 cells. J Neurosci 1997; 17: 4591-4599.
    • (1997) J Neurosci , vol.17 , pp. 4591-4599
    • Garnier, M.1    Di Lorenzo, D.2    Albertini, A.3    Maggi, A.4
  • 288
    • 0036510580 scopus 로고    scopus 로고
    • The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a novel apoptosis-inducing sequence
    • Zhou YT, Soh UJ, Shang X, Guy GR, Low BC.The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a novel apoptosis-inducing sequence. J Biol Chem 2002; 277: 7483-7492.
    • (2002) J Biol Chem , vol.277 , pp. 7483-7492
    • Zhou, Y.T.1    Soh, U.J.2    Shang, X.3    Guy, G.R.4    Low, B.C.5
  • 292
    • 0344407043 scopus 로고    scopus 로고
    • The apoptosis-associated protein BNIPL interacts with the two cell proliferation-related proteins, MIF and GFER
    • Shen L, Hu J, Lu H, Wu M, Qin W, Wan D, Li YY, Gu J. The apoptosis-associated protein BNIPL interacts with the two cell proliferation-related proteins, MIF and GFER. FEBS Lett 2003; 540: 86-90.
    • (2003) FEBS Lett , vol.540 , pp. 86-90
    • Shen, L.1    Hu, J.2    Lu, H.3    Wu, M.4    Qin, W.5    Wan, D.6    Li, Y.Y.7    Gu, J.8
  • 295
    • 0032524656 scopus 로고    scopus 로고
    • Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence
    • Yasuda M, Theodorakis P, Subramanian T, Chinnadurai G. Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence. J Biol Chem 1998; 273: 12415-12421.
    • (1998) J Biol Chem , vol.273 , pp. 12415-12421
    • Yasuda, M.1    Theodorakis, P.2    Subramanian, T.3    Chinnadurai, G.4
  • 298
    • 0034702841 scopus 로고    scopus 로고
    • Structural analysis of the human pro-apoptotic gene Bik: Chromosomal localization, genomic organization and localization of promoter sequences
    • Verma S, Budarf ML, Emanuel BS, Chinnadurai G. Structural analysis of the human pro-apoptotic gene Bik: chromosomal localization, genomic organization and localization of promoter sequences. Gene 2000; 254: 157-162.
    • (2000) Gene , vol.254 , pp. 157-162
    • Verma, S.1    Budarf, M.L.2    Emanuel, B.S.3    Chinnadurai, G.4
  • 299
    • 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, et al. 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
  • 300
    • 0033179162 scopus 로고    scopus 로고
    • Expression of the death gene Bik/Nbk promotes sensitivity to drug-induced apoptosis in corticosteroid-resistant T-cell lymphoma and prevents tumor growth in severe combined immunodeficient mice
    • Daniel PT, Pun KT, Ritschel S, Sturm I, Holler J, Dorken B, Brown R. Expression of the death gene Bik/Nbk promotes sensitivity to drug-induced apoptosis in corticosteroid-resistant T-cell lymphoma and prevents tumor growth in severe combined immunodeficient mice. Blood 1999; 94: 1100-1107.
    • (1999) Blood , vol.94 , pp. 1100-1107
    • Daniel, P.T.1    Pun, K.T.2    Ritschel, S.3    Sturm, I.4    Holler, J.5    Dorken, B.6    Brown, R.7
  • 301
    • 85047699843 scopus 로고    scopus 로고
    • Induction and endoplasmic reticulum location of BIK/NBK in response to apoptotic signalling by E1A and p53
    • Mathai JP, Germain M, Marcellus RC, Shore GC. Induction and endoplasmic reticulum location of BIK/NBK in response to apoptotic signalling by E1A and p53. Oncogene 2002; 21: 2534-2544.
    • (2002) Oncogene , vol.21 , pp. 2534-2544
    • Mathai, J.P.1    Germain, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 303
    • 0029790857 scopus 로고    scopus 로고
    • Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K
    • Han J, Sabbatini P, White E. Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K. Mol Cell Biol 1996; 16: 5857-5864.
    • (1996) Mol Cell Biol , vol.16 , pp. 5857-5864
    • Han, J.1    Sabbatini, P.2    White, E.3
  • 304
    • 0030783109 scopus 로고    scopus 로고
    • Functional dissection of the pro-apoptotic protein Bik. Heterodimerization with anti-apoptosis proteins is insufficient for induction of cell death
    • Elangovan B, Chinnadurai G. Functional dissection of the pro-apoptotic protein Bik. Heterodimerization with anti-apoptosis proteins is insufficient for induction of cell death. J Biol Chem 1997; 272: 24494-24498.
    • (1997) J Biol Chem , vol.272 , pp. 24494-24498
    • Elangovan, B.1    Chinnadurai, G.2
  • 305
    • 0035895944 scopus 로고    scopus 로고
    • Phosphorylation of the pro-apoptotic protein BIK: Mapping of phosphorylation sites and effect on apoptosis
    • Verma S, Zhao LJ, Chinnadurai G. Phosphorylation of the pro-apoptotic protein BIK: mapping of phosphorylation sites and effect on apoptosis. J Biol Chem 2001; 276: 4671-4676.
    • (2001) J Biol Chem , vol.276 , pp. 4671-4676
    • Verma, S.1    Zhao, L.J.2    Chinnadurai, G.3
  • 306
    • 0030910584 scopus 로고    scopus 로고
    • Bik and Bak induce apoptosis downstream of CrmA but upstream of inhibitor of apoptosis
    • Orth K, Dixit VM. Bik and Bak induce apoptosis downstream of CrmA but upstream of inhibitor of apoptosis. J Biol Chem 1997; 272: 8841-8844.
    • (1997) J Biol Chem , vol.272 , pp. 8841-8844
    • Orth, K.1    Dixit, V.M.2
  • 307
    • 0035873781 scopus 로고    scopus 로고
    • Involvement of bik, a proapoptotic member of the bcl-2 family, in surface igm-mediated b cell apoptosis
    • Jiang A, Clark EA. Involvement of bik, a proapoptotic member of the bcl-2 family, in surface igm-mediated b cell apoptosis. J Immunol 2001; 166: 6025-6033.
    • (2001) J Immunol , vol.166 , pp. 6025-6033
    • Jiang, A.1    Clark, E.A.2
  • 308
    • 0035284812 scopus 로고    scopus 로고
    • Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells
    • Marshansky V, Wang X, Bertrand R, Luo H, Duguid W, Chinnadurai G, Kanaan N, Vu MD, Wu J. Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells. J Immunol 2001; 166: 3130-3142.
    • (2001) J Immunol , vol.166 , pp. 3130-3142
    • Marshansky, V.1    Wang, X.2    Bertrand, R.3    Luo, H.4    Duguid, W.5    Chinnadurai, G.6    Kanaan, N.7    Vu, M.D.8    Wu, J.9
  • 309
    • 0032478614 scopus 로고    scopus 로고
    • Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist
    • Hegde R, Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES. Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist. J Biol Chem 1998; 273: 7783-7786.
    • (1998) J Biol Chem , vol.273 , pp. 7783-7786
    • Hegde, R.1    Srinivasula, S.M.2    Ahmad, M.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5
  • 310
    • 18644374360 scopus 로고    scopus 로고
    • Activation of multidomain and BH3-only proapoptotic Bcl-2 family members in p53-defective cells
    • Paquet C, Schmitt E, Beauchemin M, Bertrand R. Activation of multidomain and BH3-only proapoptotic Bcl-2 family members in p53-defective cells. Apoptosis 2004; 9: 815-831.
    • (2004) Apoptosis , vol.9 , pp. 815-831
    • Paquet, C.1    Schmitt, E.2    Beauchemin, M.3    Bertrand, R.4
  • 312
    • 0037462454 scopus 로고    scopus 로고
    • Liver tumor development. c-Jun antagonizes the proapoptotic acthity of p53
    • Eferl R, Ricci R Kenner L, Zenz R, David JP, Rath M, Wagner EF. Liver tumor development. c-Jun antagonizes the proapoptotic acthity of p53. Cell 2003; 112: 181-192.
    • (2003) Cell , vol.112 , pp. 181-192
    • Eferl, R.1    Ricci, R.2    Kenner, L.3    Zenz, R.4    David, J.P.5    Rath, M.6    Wagner, E.F.7
  • 315
    • 0346655211 scopus 로고    scopus 로고
    • BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1alpha
    • Kim JY, Ahn HJ, Ryu JH, Suk K, Park JH. BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1alpha. J Exp Med 2004; 199: 113-124.
    • (2004) J Exp Med , vol.199 , pp. 113-124
    • Kim, J.Y.1    Ahn, H.J.2    Ryu, J.H.3    Suk, K.4    Park, J.H.5
  • 318
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 1999; 3: 287-296.
    • (1999) Mol Cell , vol.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 319
    • 0037418238 scopus 로고    scopus 로고
    • JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
    • Lei K, Davis RJ. JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. Proc Natl Acad Sci USA 2003; 100: 2432-2437.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2432-2437
    • Lei, K.1    Davis, R.J.2
  • 320
    • 0742306876 scopus 로고    scopus 로고
    • Expression and transcrip-tional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells
    • Morales AA, Olsson A, Celsing F, Osterborg A, Jondal M, Osorio LM. Expression and transcrip-tional regulation of functionally distinct Bmf isoforms in B-chronic lymphocytic leukemia cells. Leukemia 2004; 18: 41-47.
    • (2004) Leukemia , vol.18 , pp. 41-47
    • Morales, A.A.1    Olsson, A.2    Celsing, F.3    Osterborg, A.4    Jondal, M.5    Osorio, L.M.6
  • 328
  • 329
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano K, Vousden KH. PUMA, a novel proapoptotic gene, is induced by p53. Mol Cell 2001; 7: 683-694.
    • (2001) Mol Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 332
    • 0141757205 scopus 로고    scopus 로고
    • Bax conformational change is a crucial step for PUMA-mediated apoptosis in human leukemia
    • Liu FT, Newland AC, Jia L. Bax conformational change is a crucial step for PUMA-mediated apoptosis in human leukemia. Biochem Biophys Res Commun 2003; 310: 956-962.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 956-962
    • Liu, F.T.1    Newland, A.C.2    Jia, L.3
  • 333
    • 0030605415 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1
    • Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N. Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res 1996; 3: 17-24.
    • (1996) DNA Res , vol.3 , pp. 17-24
    • Nagase, T.1    Seki, N.2    Ishikawa, K.3    Tanaka, A.4    Nomura, N.5
  • 334
    • 0033008195 scopus 로고    scopus 로고
    • Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins
    • Kasof GM, Goyal L, White E. Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins. Mol Cell Biol 1999; 19: 4390-4404.
    • (1999) Mol Cell Biol , vol.19 , pp. 4390-4404
    • Kasof, G.M.1    Goyal, L.2    White, E.3
  • 336
    • 1542284570 scopus 로고    scopus 로고
    • Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy
    • Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y. Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy. Eur J Biochem 2004; 271: 1035-1045.
    • (2004) Eur J Biochem , vol.271 , pp. 1035-1045
    • Haraguchi, T.1    Holaska, J.M.2    Yamane, M.3    Koujin, T.4    Hashiguchi, N.5    Mori, C.6    Wilson, K.L.7    Hiraoka, Y.8
  • 337
    • 0035377522 scopus 로고    scopus 로고
    • Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension
    • Kataoka T, Holler N, Micheau O, Martinon F, Tinel A, Hofmann K, Tschopp J. Bcl-rambo, a novel Bcl-2 homologue that induces apoptosis via its unique C-terminal extension. J Biol Chem 2001; 276: 19548-19554.
    • (2001) J Biol Chem , vol.276 , pp. 19548-19554
    • Kataoka, T.1    Holler, N.2    Micheau, O.3    Martinon, F.4    Tinel, A.5    Hofmann, K.6    Tschopp, J.7
  • 338
    • 0037448427 scopus 로고    scopus 로고
    • Bcl-rambo beta, a special splicing variant with an insertion of an Alu-like cassette, promotes etoposide- and Taxol-induced cell death
    • Yi P, Zhang W, Zhai Z, Miao L, Wang Y, Wu M. Bcl-rambo beta, a special splicing variant with an insertion of an Alu-like cassette, promotes etoposide- and Taxol-induced cell death. FEBS Lett 2003; 534: 61-68.
    • (2003) FEBS Lett , vol.534 , pp. 61-68
    • Yi, P.1    Zhang, W.2    Zhai, Z.3    Miao, L.4    Wang, Y.5    Wu, M.6
  • 339
    • 0035951886 scopus 로고    scopus 로고
    • Bcl-G, a novel pro-apoptotic member of the Bcl-2 family
    • Guo B, Godzik A, Reed JC. Bcl-G, a novel pro-apoptotic member of the Bcl-2 family. J Biol Chem 2001; 276: 2780-2785.
    • (2001) J Biol Chem , vol.276 , pp. 2780-2785
    • Guo, B.1    Godzik, A.2    Reed, J.C.3
  • 340
    • 0036119568 scopus 로고    scopus 로고
    • A detailed transcriptional map of the chromosome 12p12 tumour suppressor locus
    • Montpetit A, Boily G, Sinnett D. A detailed transcriptional map of the chromosome 12p12 tumour suppressor locus. Eur J Hum Genet 2002; 10: 62-71.
    • (2002) Eur J Hum Genet , vol.10 , pp. 62-71
    • Montpetit, A.1    Boily, G.2    Sinnett, D.3
  • 341
    • 0142025135 scopus 로고    scopus 로고
    • Characterization of ubiquitin-like polypeptide acceptor protein, a novel pro-apoptotic member of the Bcl2 family
    • Nakamura M, Tanigawa Y. Characterization of ubiquitin-like polypeptide acceptor protein, a novel pro-apoptotic member of the Bcl2 family. Eur J Biochem 2003; 270: 4052-4058.
    • (2003) Eur J Biochem , vol.270 , pp. 4052-4058
    • Nakamura, M.1    Tanigawa, Y.2
  • 342
    • 0035951847 scopus 로고    scopus 로고
    • MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains
    • Tan KO, Tan KM, Chan SL, Yee KS, Bevort M, Ang KC, Yu VC. MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains. J Biol Chem 2001; 276: 2802-2807.
    • (2001) J Biol Chem , vol.276 , pp. 2802-2807
    • Tan, K.O.1    Tan, K.M.2    Chan, S.L.3    Yee, K.S.4    Bevort, M.5    Ang, K.C.6    Yu, V.C.7
  • 343
    • 0035855629 scopus 로고    scopus 로고
    • Nrh, a human homologue of Nr-13 associates with Bcl-Xs and is an inhibitor of apoptosis
    • Aouacheria A, Arnaud E, Venet S, Lalle P, Gouy M, Rigal D, Gillet G. Nrh, a human homologue of Nr-13 associates with Bcl-Xs and is an inhibitor of apoptosis. Oncogene 2001; 20: 5846-5855.
    • (2001) Oncogene , vol.20 , pp. 5846-5855
    • Aouacheria, A.1    Arnaud, E.2    Venet, S.3    Lalle, P.4    Gouy, M.5    Rigal, D.6    Gillet, G.7
  • 344
    • 0035918260 scopus 로고    scopus 로고
    • Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak
    • Ke N, Godzik A, Reed JC. Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak. J Biol Chem 2001; 276: 12481-12484.
    • (2001) J Biol Chem , vol.276 , pp. 12481-12484
    • Ke, N.1    Godzik, A.2    Reed, J.C.3
  • 346
    • 0035504106 scopus 로고    scopus 로고
    • Bcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks apoptosis in the mitochondria death pathway but not in the death receptor pathway
    • Zhang H, Holzgreve W, De Geyter C. Bcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks apoptosis in the mitochondria death pathway but not in the death receptor pathway. Hum Mol Genet 2001; 10: 2329-2339.
    • (2001) Hum Mol Genet , vol.10 , pp. 2329-2339
    • Zhang, H.1    Holzgreve, W.2    De Geyter, C.3
  • 347
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 1986; 234: 364.
    • (1986) Science , vol.234 , pp. 364
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 348
    • 0030901628 scopus 로고    scopus 로고
    • Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and BCL-2
    • Shibasaki F, Kondo E, Akagi T, McKeon F. Suppression of signalling through transcription factor NF-AT by interactions 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
  • 349
    • 0031596370 scopus 로고    scopus 로고
    • BCL-2, RAF-1 and mitochondrial regulation of apoptosis
    • Wng HG, Reed JC. BCL-2, RAF-1 and mitochondrial regulation of apoptosis. Biofactors 1998; 8: 13-16.
    • (1998) Biofactors , vol.8 , pp. 13-16
    • Wng, H.G.1    Reed, J.C.2
  • 350
    • 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 DC, Adams JM, Gory 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; 117: 1029-1103.
    • (1998) EMBO J , vol.117 , pp. 1029-1103
    • Huang, D.C.1    Adams, J.M.2    Gory, S.3
  • 351
    • 0035280247 scopus 로고    scopus 로고
    • Molecular cloning, physical mapping, and expression analysis of a novel gene, BCL2L12, encoding a proline-rich protein with a highly conserved BH2 domain of the Bcl-2 family
    • Scorilas A, Kyriakopoulou L, Yousef GM, Ashworth LK Kwamie A, Diamandis EP. Molecular cloning, physical mapping, and expression analysis of a novel gene, BCL2L12, encoding a proline-rich protein with a highly conserved BH2 domain of the Bcl-2 family. Genomics 2001; 72: 217-221.
    • (2001) Genomics , vol.72 , pp. 217-221
    • Scorilas, A.1    Kyriakopoulou, L.2    Yousef, G.M.3    Ashworth, L.K.4    Kwamie, A.5    Diamandis, E.P.6
  • 352
    • 0025211917 scopus 로고
    • Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src
    • Hirai H, Varmus HE. Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src. Mol Cell Biol 1990; 10: 1307-1318.
    • (1990) Mol Cell Biol , vol.10 , pp. 1307-1318
    • Hirai, H.1    Varmus, H.E.2
  • 353
    • 0029878631 scopus 로고    scopus 로고
    • Cubital tunnel surgery. Complications and treatment of failures
    • Jackson LC, Hotchkiss RN. Cubital tunnel surgery. Complications and treatment of failures. Hand Clin 1996; 12: 449-456.
    • (1996) Hand Clin , vol.12 , pp. 449-456
    • Jackson, L.C.1    Hotchkiss, R.N.2
  • 355
    • 0028853727 scopus 로고
    • Immunoreactivity for Bcl-2 protein within neurons in the Alzheimer's disease brain increases with disease severity
    • Satou T, Cummings BJ, Cotman CW. Immunoreactivity for Bcl-2 protein within neurons in the Alzheimer's disease brain increases with disease severity. Brain Res 1995; 697: 35-43.
    • (1995) Brain Res , vol.697 , pp. 35-43
    • Satou, T.1    Cummings, B.J.2    Cotman, C.W.3
  • 356
    • 0033976201 scopus 로고    scopus 로고
    • Developmental expression of Bcl-2 protein in human cortex
    • Jarskog LF, Gilmore JH. Developmental expression of Bcl-2 protein in human cortex. Brain Res Dev Brain Res 2000; 119: 225-230.
    • (2000) Brain Res Dev Brain Res , vol.119 , pp. 225-230
    • Jarskog, L.F.1    Gilmore, J.H.2
  • 357
    • 0033520151 scopus 로고    scopus 로고
    • Bcl-X(L) inhibits apoptosis and necrosis produced by Alzheimer's beta-amyloidl-40 peptide in PC12 cells
    • Tan J, Town T, Placzek A, Kundtz A, Yu H, Mullan M. Bcl-X(L) inhibits apoptosis and necrosis produced by Alzheimer's beta-amyloidl-40 peptide in PC12 cells. Neurosci Lett 1999; 272: 5-8.
    • (1999) Neurosci Lett , vol.272 , pp. 5-8
    • Tan, J.1    Town, T.2    Placzek, A.3    Kundtz, A.4    Yu, H.5    Mullan, M.6
  • 358
    • 0035805391 scopus 로고    scopus 로고
    • Expression of apoptosis related proteins in brains of patients with Alzheimer's disease
    • Engidawork E, Gulesserian T, Seidl R, Cairns N, Lubec G. Expression of apoptosis related proteins in brains of patients with Alzheimer's disease. Neurosci Lett 2001; 303: 79-82.
    • (2001) Neurosci Lett , vol.303 , pp. 79-82
    • Engidawork, E.1    Gulesserian, T.2    Seidl, R.3    Cairns, N.4    Lubec, G.5
  • 361
    • 0027250808 scopus 로고
    • How does HIV cause AIDS?
    • Weiss RA. How does HIV cause AIDS? Science 1993; 260: 1273-1279.
    • (1993) Science , vol.260 , pp. 1273-1279
    • Weiss, R.A.1
  • 362
    • 0030877601 scopus 로고    scopus 로고
    • Modulation of Bcl-2 protein by CD4 cross-linking: A possible mechanism for lymphocyte apoptosis in human immunodeficiency virus infection and for rescue of apoptosis by interleukin-2
    • Hashimoto F, Oyaizu N, Kalyanaraman VS, Pahwa S. Modulation of Bcl-2 protein by CD4 cross-linking: a possible mechanism for lymphocyte apoptosis in human immunodeficiency virus infection and for rescue of apoptosis by interleukin-2. Blood 1997; 90: 745-753.
    • (1997) Blood , vol.90 , pp. 745-753
    • Hashimoto, F.1    Oyaizu, N.2    Kalyanaraman, V.S.3    Pahwa, S.4
  • 363
    • 0032989293 scopus 로고    scopus 로고
    • Downregulation of Bcl-2, but not of Bax or Bcl-x, is associated with T lymphocyte apoptosis in HIV infection and restored by antiretroviral therapy or by interleukin 2
    • Regamey N, Harr T, Battegay M, Erb P. Downregulation of Bcl-2, but not of Bax or Bcl-x, is associated with T lymphocyte apoptosis in HIV infection and restored by antiretroviral therapy or by interleukin 2. AIDS Res Hum Retroviruses 1999; 15: 803-810.
    • (1999) AIDS Res Hum Retroviruses , vol.15 , pp. 803-810
    • Regamey, N.1    Harr, T.2    Battegay, M.3    Erb, P.4
  • 364
    • 0031872690 scopus 로고    scopus 로고
    • High levels of HIV-1 replication show a clear correlation with downmodulation of Bcl-2 protein in peripheral blood lymphocytes of HIV-1-seropositive subjects
    • Re M, Gibellini D, Aschbacher R, Vignoli M, Furlini G, Ramazzotti E, Bertolaso L, La Placa M. High levels of HIV-1 replication show a clear correlation with downmodulation of Bcl-2 protein in peripheral blood lymphocytes of HIV-1-seropositive subjects. J Med Virol 1998; 56: 66-73.
    • (1998) J Med Virol , vol.56 , pp. 66-73
    • Re, M.1    Gibellini, D.2    Aschbacher, R.3    Vignoli, M.4    Furlini, G.5    Ramazzotti, E.6    Bertolaso, L.7    La Placa, M.8
  • 365
    • 0029985912 scopus 로고    scopus 로고
    • Fas and Fas ligand in embryos and adult mice: Ligand expression in several immune-privileged tissues and coexpression in adult tissues characterized by apoptotic cell turnover
    • French LE, Hahne M, Viard I, Radlgruber G, Zanone R, Becker K, Muller C, Tschopp J. Fas and Fas ligand in embryos and adult mice: ligand expression in several immune-privileged tissues and coexpression in adult tissues characterized by apoptotic cell turnover. J Cell Biol 1996; 133: 335-343.
    • (1996) J Cell Biol , vol.133 , pp. 335-343
    • French, L.E.1    Hahne, M.2    Viard, I.3    Radlgruber, G.4    Zanone, R.5    Becker, K.6    Muller, C.7    Tschopp, J.8
  • 370
    • 0032907268 scopus 로고    scopus 로고
    • Fas/Fas ligand-driven T cell apoptosis as a consequence of ineffective thyroid immunoprivilege in Hashimoto's thyroiditis
    • Stassi G, Todaro M, Bucchieri F, Stoppacciaro A, Farina F, Zummo G, Testi R, De Maria R. Fas/Fas ligand-driven T cell apoptosis as a consequence of ineffective thyroid immunoprivilege in Hashimoto's thyroiditis. J Immunol 1999; 162: 263-267.
    • (1999) J Immunol , vol.162 , pp. 263-267
    • Stassi, G.1    Todaro, M.2    Bucchieri, F.3    Stoppacciaro, A.4    Farina, F.5    Zummo, G.6    Testi, R.7    De Maria, R.8
  • 371
    • 0034043074 scopus 로고    scopus 로고
    • Expression of bcl-2. Bax and Fas in oxyphil cells of Hashimoto thyroiditis
    • Muller-Hocker, J. Expression of bcl-2. Bax and Fas in oxyphil cells of Hashimoto thyroiditis. Virchows Arch 2000; 436: 602-607.
    • (2000) Virchows Arch , vol.436 , pp. 602-607
    • Muller-Hocker, J.1
  • 372
    • 0031912361 scopus 로고    scopus 로고
    • Resistance of T-cells to apoptosis in autoimmune diabetic (NOD) mice is increased early in life and is associated with dysregulated expression of Bcl-x
    • Lamhamedi-Cherradi SE, Luan JJ, Eloy L, Fluteau G, Bach JF, Garchon HJ. Resistance of T-cells to apoptosis in autoimmune diabetic (NOD) mice is increased early in life and is associated with dysregulated expression of Bcl-x. Diabetologia 1998; 41: 178-184.
    • (1998) Diabetologia , vol.41 , pp. 178-184
    • Lamhamedi-Cherradi, S.E.1    Luan, J.J.2    Eloy, L.3    Fluteau, G.4    Bach, J.F.5    Garchon, H.J.6
  • 373
    • 0025165221 scopus 로고
    • Preferential linkage of bcl-2 to immunoglobulin light chain gene in chronic lymphocytic leukemia
    • Adachi ,M Tefferi A, Greipp PR, Kipps TJ, Tsujimoto Y. Preferential linkage of bcl-2 to immunoglobulin light chain gene in chronic lymphocytic leukemia. J Exp Med 1990; 171: 559-564.
    • (1990) J Exp Med , vol.171 , pp. 559-564
    • Adachi, M.1    Tefferi, A.2    Greipp, P.R.3    Kipps, T.J.4    Tsujimoto, Y.5
  • 374
    • 0028357022 scopus 로고
    • Loss of heterozygosity at the bcl-2 gene locus and expression of bcl-2 in human gastric and colorectal carcinomas
    • Ayhan A, Yasui W, Yokozaki H, Seto M, Ueda R, Tahara E. Loss of heterozygosity at the bcl-2 gene locus and expression of bcl-2 in human gastric and colorectal carcinomas. Jpn J Cancer Res 1994; 85: 584-591.
    • (1994) Jpn J Cancer Res , vol.85 , pp. 584-591
    • Ayhan, A.1    Yasui, W.2    Yokozaki, H.3    Seto, M.4    Ueda, R.5    Tahara, E.6
  • 376
    • 0029582891 scopus 로고
    • Bcl-2 protein expression in breast cancer in relation to established prognostic factors and other clinicopathological variables
    • Binder C, Marx D, Overhoff R, Binder L, Schauer A, Hiddemann W. Bcl-2 protein expression in breast cancer in relation to established prognostic factors and other clinicopathological variables. Ann Oncol 1995; 6: 1005-1010.
    • (1995) Ann Oncol , vol.6 , pp. 1005-1010
    • Binder, C.1    Marx, D.2    Overhoff, R.3    Binder, L.4    Schauer, A.5    Hiddemann, W.6
  • 377
    • 0028905806 scopus 로고
    • bcl-2 protein expression in melanocytic neoplasms of the skin
    • Ramsay JA, From L, Kahn HJ. bcl-2 protein expression in melanocytic neoplasms of the skin. Mod Pathol 1995; 8: 150-154.
    • (1995) Mod Pathol , vol.8 , pp. 150-154
    • Ramsay, J.A.1    From, L.2    Kahn, H.J.3
  • 380
    • 0029868847 scopus 로고    scopus 로고
    • Expression of Bcl-2 protein in hyperplastic polyps, adenomas, and carcinomas of the colon
    • Flohil CC, Janssen PA, Bosman FT. Expression of Bcl-2 protein in hyperplastic polyps, adenomas, and carcinomas of the colon. J Pathol 1996; 178: 393-397.
    • (1996) J Pathol , vol.178 , pp. 393-397
    • Flohil, C.C.1    Janssen, P.A.2    Bosman, F.T.3
  • 381
    • 0031868609 scopus 로고    scopus 로고
    • Immunohistochemical analysis of Ki-67 antigen and Bcl-2 protein expression in prostate cancer: Effect of neoadjuvant hormonal therapy
    • Tsuji M, Murakami Y, Kanayama H, Sano T, Kagawa S. Immunohistochemical analysis of Ki-67 antigen and Bcl-2 protein expression in prostate cancer: effect of neoadjuvant hormonal therapy. Br J Urol 1998; 81: 116-121.
    • (1998) Br J Urol , vol.81 , pp. 116-121
    • Tsuji, M.1    Murakami, Y.2    Kanayama, H.3    Sano, T.4    Kagawa, S.5
  • 382
    • 0031804606 scopus 로고    scopus 로고
    • Molecular comparison of human and mouse pulmonary adenocarcinomas
    • Malkinson AM. Molecular comparison of human and mouse pulmonary adenocarcinomas. Exp Lung Res 1998; 24: 541-555.
    • (1998) Exp Lung Res , vol.24 , pp. 541-555
    • Malkinson, A.M.1
  • 384
  • 385
    • 0036251711 scopus 로고    scopus 로고
    • Apoptosis and expression of Bcl-2, Bcl-XL, and Bax in renal cell carcinomas
    • Gobe G, Rubin M, Williams G, Sawczuk I, Buttyan R. Apoptosis and expression of Bcl-2, Bcl-XL, and Bax in renal cell carcinomas. Cancer Invest 2002; 20: 324-332.
    • (2002) Cancer Invest , vol.20 , pp. 324-332
    • Gobe, G.1    Rubin, M.2    Williams, G.3    Sawczuk, I.4    Buttyan, R.5
  • 388
    • 0027892521 scopus 로고
    • bcl-2 protein inhibits etoposide-induced apoptosis through its effects on events subsequent to topoisomerase II-induced DNA strand breaks and their repair
    • Kamesaki S, Kamesaki H, Jorgensen TJ, Tanizawa A, Pommier Y. Cossman J. bcl-2 protein inhibits etoposide-induced apoptosis through its effects on events subsequent to topoisomerase II-induced DNA strand breaks and their repair. Cancer Res 1993; 53: 4251-4256.
    • (1993) Cancer Res , vol.53 , pp. 4251-4256
    • Kamesaki, S.1    Kamesaki, H.2    Jorgensen, T.J.3    Tanizawa, A.4    Pommier, Y.5    Cossman, J.6
  • 390
    • 0031889769 scopus 로고    scopus 로고
    • High expression of bcl-2 mRNA as a determinant of poor prognosis in acute myeloid leukemia
    • Karakas T, Maurer U, Weidmann E, Miething CC, Hoelzer D, Bergmann L. High expression of bcl-2 mRNA as a determinant of poor prognosis in acute myeloid leukemia. Ann Oncol 1998; 9: 159-165.
    • (1998) Ann Oncol , vol.9 , pp. 159-165
    • Karakas, T.1    Maurer, U.2    Weidmann, E.3    Miething, C.C.4    Hoelzer, D.5    Bergmann, L.6
  • 391
    • 0032723350 scopus 로고    scopus 로고
    • Bcl-2, Bcl-X, Bax, and Bak expression in short-and long-lived patients with diffuse large B-cell lymphomas
    • Bairey O, Zimra Y, Shaklai M, Okon E, Rabizadeh E. Bcl-2, Bcl-X, Bax, and Bak expression in short-and long-lived patients with diffuse large B-cell lymphomas. Clin Cancer Res 1999; 5: 2860-2866.
    • (1999) Clin Cancer Res , vol.5 , pp. 2860-2866
    • Bairey, O.1    Zimra, Y.2    Shaklai, M.3    Okon, E.4    Rabizadeh, E.5
  • 392
    • 0036299715 scopus 로고    scopus 로고
    • High expression of Bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy
    • Tothova E, Fricova M, Stecova N, Kafkova A, Elbertova A. High expression of Bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy. Neoplasma 2002; 49: 141-144.
    • (2002) Neoplasma , vol.49 , pp. 141-144
    • Tothova, E.1    Fricova, M.2    Stecova, N.3    Kafkova, A.4    Elbertova, A.5
  • 394
    • 0030714175 scopus 로고    scopus 로고
    • Calphostin C synergistically induces apoptosis with VP-16 in lymphoma cells which express abundant phosphorylated Bcl-2 protein
    • Murata M, Nagai M, Fujita M, Ohmori M, TakaharaJ. Calphostin C synergistically induces apoptosis with VP-16 in lymphoma cells which express abundant phosphorylated Bcl-2 protein. Cell Mol Life Sci 1997; 53: 737-743.
    • (1997) Cell Mol Life Sci , vol.53 , pp. 737-743
    • Murata, M.1    Nagai, M.2    Fujita, M.3    Ohmori, M.4    Takahara, J.5
  • 395
    • 1842739136 scopus 로고    scopus 로고
    • Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance
    • Deng X, Kornblau SM, Ruvolo PP, May WSJr. Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance. J Natl Cancer Inst Monogr 2001; 28: 30-37.
    • (2001) J Natl Cancer Inst Monogr , vol.28 , pp. 30-37
    • Deng, X.1    Kornblau, S.M.2    Ruvolo, P.P.3    May Jr., W.S.4
  • 396
    • 0032544721 scopus 로고    scopus 로고
    • Okadaic acid-induced apoptosis of HL60 leukemia cells is preceded by destabilization of bcl-2 mRNA and downregulation of bcl-2 protein
    • Riordan FA, Foroni L, Hoffbrand AV, Mehta AB, Wickremasinghe RG. Okadaic acid-induced apoptosis of HL60 leukemia cells is preceded by destabilization of bcl-2 mRNA and downregulation of bcl-2 protein. FEBS Lett 1998; 435: 195-198.
    • (1998) FEBS Lett , vol.435 , pp. 195-198
    • Riordan, F.A.1    Foroni, L.2    Hoffbrand, A.V.3    Mehta, A.B.4    Wickremasinghe, R.G.5
  • 397
    • 0033748335 scopus 로고    scopus 로고
    • Effects of Bcl-2 modulation with G3139 antisense oligonucleotide on human breast cancer cells are independent of inherent Bcl-2 protein expression
    • Chi KC, Wallis AE, Lee CH, De Menezes DL, Sartor J, Dragowska WH, Mayer LD. Effects of Bcl-2 modulation with G3139 antisense oligonucleotide on human breast cancer cells are independent of inherent Bcl-2 protein expression. Breast Cancer Res Treat 2000; 63: 199-212.
    • (2000) Breast Cancer Res Treat , vol.63 , pp. 199-212
    • Chi, K.C.1    Wallis, A.E.2    Lee, C.H.3    De Menezes, D.L.4    Sartor, J.5    Dragowska, W.H.6    Mayer, L.D.7
  • 398
    • 0034015672 scopus 로고    scopus 로고
    • Phase I clinical and pharmacokinetic study of bcl-2 antisense oligonucleotide therapy in patients with non-Hodgkin's lymphoma
    • Waters JS, Webb A, Cunningham D, Clarke PA, Raynaud F, di Stefano F, Cotter FE. Phase I clinical and pharmacokinetic study of bcl-2 antisense oligonucleotide therapy in patients with non-Hodgkin's lymphoma. J Clin Oncol 2000; 18: 1812-1823.
    • (2000) J Clin Oncol , vol.18 , pp. 1812-1823
    • Waters, J.S.1    Webb, A.2    Cunningham, D.3    Clarke, P.A.4    Raynaud, F.5    Di Stefano, F.6    Cotter, F.E.7
  • 401
    • 0242456160 scopus 로고    scopus 로고
    • The future of antisense therapy: Combination with anticancer treatments
    • Biroccio A, Leonetti C, Zupi G. The future of antisense therapy: combination with anticancer treatments. Oncogene 2003; 22: 6579-6588.
    • (2003) Oncogene , vol.22 , pp. 6579-6588
    • Biroccio, A.1    Leonetti, C.2    Zupi, G.3
  • 404
    • 0036251711 scopus 로고    scopus 로고
    • Apoptosis and expression of Bcl-2, Bcl-XL, and Bax in renal cell carcinomas
    • Gobe G, Rubin M, Williams G, Sawczuk I, Buttyan R. Apoptosis and expression of Bcl-2, Bcl-XL, and Bax in renal cell carcinomas. Cancer Invest 2002; 20: 324-332.
    • (2002) Cancer Invest , vol.20 , pp. 324-332
    • Gobe, G.1    Rubin, M.2    Williams, G.3    Sawczuk, I.4    Buttyan, R.5
  • 405
    • 0034235836 scopus 로고    scopus 로고
    • Bcl-X(L) is up-regulated by HTLV-I and HTLV-II in vitro and in ex vivo ATLL samples
    • Nicot C, Mahieux R, Takemoto S, Franchini G. Bcl-X(L) is up-regulated by HTLV-I and HTLV-II in vitro and in ex vivo ATLL samples. Blood 2000; 96: 275-281.
    • (2000) Blood , vol.96 , pp. 275-281
    • Nicot, C.1    Mahieux, R.2    Takemoto, S.3    Franchini, G.4
  • 407
    • 0029033619 scopus 로고
    • Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and activation of phospholipase A2 in breast carcinoma cells
    • Jaattela M, Benedict M, Tewari M, Shayman JA, Dixit VM. Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and activation of phospholipase A2 in breast carcinoma cells. Oncogene 1995; 10: 2297-2305.
    • (1995) Oncogene , vol.10 , pp. 2297-2305
    • Jaattela, M.1    Benedict, M.2    Tewari, M.3    Shayman, J.A.4    Dixit, V.M.5
  • 408
    • 0033799480 scopus 로고    scopus 로고
    • Heterodimerization of Bcl-2 and Bcl-X(L) with Bax and Bad in colorectal cancer
    • Hattori T, Ookawa N, Fujita R, Fukuchi K. Heterodimerization of Bcl-2 and Bcl-X(L) with Bax and Bad in colorectal cancer. Acta Oncol 2000; 39: 495-500.
    • (2000) Acta Oncol , vol.39 , pp. 495-500
    • Hattori, T.1    Ookawa, N.2    Fujita, R.3    Fukuchi, K.4
  • 410
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 1996; 87: 619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 413
    • 0042707655 scopus 로고    scopus 로고
    • Necrotic cell death in response to oxidant stress involves the activation of the apoptogenic caspase-8/bid pathway
    • Wang X, Ryter SW, Dai C, Tang ZL, Watkins SC, Yin XM, Song R, Choi AM. Necrotic cell death in response to oxidant stress involves the activation of the apoptogenic caspase-8/bid pathway. J Biol Chem 2003; 278: 29184-29191.
    • (2003) J Biol Chem , vol.278 , pp. 29184-29191
    • Wang, X.1    Ryter, S.W.2    Dai, C.3    Tang, Z.L.4    Watkins, S.C.5    Yin, X.M.6    Song, R.7    Choi, A.M.8
  • 414
    • 4544274785 scopus 로고    scopus 로고
    • Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway
    • Wagner KW, Engels IH, Deveraux QL. Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway. J Biol Chem 2004; 279: 35047-35052.
    • (2004) J Biol Chem , vol.279 , pp. 35047-35052
    • Wagner, K.W.1    Engels, I.H.2    Deveraux, Q.L.3
  • 415
    • 3142581992 scopus 로고    scopus 로고
    • Requirement for aspartate-cleaved bid in apoptosis signalling by DNA-damaging anti-cancer regimens
    • Werner AB, Tait SW, de Vries E, Eldering E, Borst J. Requirement for aspartate-cleaved bid in apoptosis signalling by DNA-damaging anti-cancer regimens. J Biol Chem 2004; 279: 28771-28780.
    • (2004) J Biol Chem , vol.279 , pp. 28771-28780
    • Werner, A.B.1    Tait, S.W.2    De Vries, E.3    Eldering, E.4    Borst, J.5
  • 417
    • 0032852636 scopus 로고    scopus 로고
    • Induction of apoptosis by the p53-273L (Arg → Leu) mutant in HSC3 cells without transactivation of p21Waf1/Cip1/Sdi1 and bax
    • Kaneuchi M, Yamashita T, Shindoh M, Segawa K, Takahashi S, Furuta I, Fujimoto S, Fujinaga K. Induction of apoptosis by the p53-273L (Arg → Leu) mutant in HSC3 cells without transactivation of p21Waf1/Cip1/Sdi1 and bax. Mol Carcinog 1999; 26: 44-52.
    • (1999) Mol Carcinog , vol.26 , pp. 44-52
    • Kaneuchi, M.1    Yamashita, T.2    Shindoh, M.3    Segawa, K.4    Takahashi, S.5    Furuta, I.6    Fujimoto, S.7    Fujinaga, K.8
  • 419
    • 0034518022 scopus 로고    scopus 로고
    • Abnormal intracellular localization of Bax with a normal membrane anchor domain in human lung cancer cell lines
    • Salah-eldin A, Inoue S, Tsuda M, Matsuura A. Abnormal intracellular localization of Bax with a normal membrane anchor domain in human lung cancer cell lines. Jpn J Cancer Res 2000; 91: 1269-1277.
    • (2000) Jpn J Cancer Res , vol.91 , pp. 1269-1277
    • Salah-eldin, A.1    Inoue, S.2    Tsuda, M.3    Matsuura, A.4
  • 420
    • 0033960641 scopus 로고    scopus 로고
    • Frequent microsatellite instability and BAX mutations in T cell acute lymphoblastic leukemia cell lines
    • Inoue K, Kohno T, Takakura S, Hayashi Y, Mizoguchi H, Yokota J. Frequent microsatellite instability and BAX mutations in T cell acute lymphoblastic leukemia cell lines. Leuk Res 2000; 24: 255-262.
    • (2000) Leuk Res , vol.24 , pp. 255-262
    • Inoue, K.1    Kohno, T.2    Takakura, S.3    Hayashi, Y.4    Mizoguchi, H.5    Yokota, J.6
  • 422
    • 0033135639 scopus 로고    scopus 로고
    • Impairment of the proapoptotic activity of Bax by missense mutations found in gastrointestinal cancers
    • Gil J, Yamamoto H, Zapata JM, Reed JC, Perucho M. Impairment of the proapoptotic activity of Bax by missense mutations found in gastrointestinal cancers. Cancer Res 1999; 59: 2034-2037.
    • (1999) Cancer Res , vol.59 , pp. 2034-2037
    • Gil, J.1    Yamamoto, H.2    Zapata, J.M.3    Reed, J.C.4    Perucho, M.5
  • 424
    • 0033182742 scopus 로고    scopus 로고
    • Apoptosis of human tumor cells by chemotherapeutic anthracyclines is enhanced by Bax overexpression
    • Lu Y, Yagi T. Apoptosis of human tumor cells by chemotherapeutic anthracyclines is enhanced by Bax overexpression. J Radiat Res (Tokyo) 1999; 40: 263-272.
    • (1999) J Radiat Res (Tokyo) , vol.40 , pp. 263-272
    • Lu, Y.1    Yagi, T.2
  • 425
    • 0034106050 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of bax with caspase-8 controlled by myelin basic protein promoter exerts an enhanced cytotoxic effect in gliomas
    • Shinoura N, Saito K, Yoshida Y, Hashimoto M, Asai A, Kirino T, Hamada H. Adenovirus-mediated transfer of bax with caspase-8 controlled by myelin basic protein promoter exerts an enhanced cytotoxic effect in gliomas. Cancer Gene Ther 2000; 7: 739-748.
    • (2000) Cancer Gene Ther , vol.7 , pp. 739-748
    • Shinoura, N.1    Saito, K.2    Yoshida, Y.3    Hashimoto, M.4    Asai, A.5    Kirino, T.6    Hamada, H.7
  • 427
    • 0035136282 scopus 로고    scopus 로고
    • Adenovirus-mediated Bax overexpression for the induction of therapeutic apoptosis in prostate cancer
    • Li X, Marani M, Yu J, Nan B, Roth JA, Kagawa S, Fang B, Denner L, Marcelli M. Adenovirus-mediated Bax overexpression for the induction of therapeutic apoptosis in prostate cancer. Cancer Res 2001; 61: 186-191.
    • (2001) Cancer Res , vol.61 , pp. 186-191
    • Li, X.1    Marani, M.2    Yu, J.3    Nan, B.4    Roth, J.A.5    Kagawa, S.6    Fang, B.7    Denner, L.8    Marcelli, M.9
  • 428
    • 2442651256 scopus 로고    scopus 로고
    • Reduced expression of Bax in ceramide-resistant HL-60 subline
    • Sawai H, Kawai S, Domae N. Reduced expression of Bax in ceramide-resistant HL-60 subline. Biochem Biophys Res Commun 2004; 319: 46-49.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 46-49
    • Sawai, H.1    Kawai, S.2    Domae, N.3
  • 429
    • 13144304342 scopus 로고    scopus 로고
    • BAK overexpression mediates p53-independent apoptosis inducing effects on human gastric cancer cells
    • Tong QS, Zheng LD, Wang L, Liu J, Qian W. BAK overexpression mediates p53-independent apoptosis inducing effects on human gastric cancer cells. BMC Cancer 2004; 4: 33.
    • (2004) BMC Cancer , vol.4 , pp. 33
    • Tong, Q.S.1    Zheng, L.D.2    Wang, L.3    Liu, J.4    Qian, W.5
  • 431
    • 0033637306 scopus 로고    scopus 로고
    • Role of Bak in UV-induced apoptosis in skin cancer and abrogation by HPV E6 proteins
    • Jackson S, Harwood C, Thomas M, Banks L, Storey A. Role of Bak in UV-induced apoptosis in skin cancer and abrogation by HPV E6 proteins. Genes Dev 2000; 14: 3065-3073.
    • (2000) Genes Dev , vol.14 , pp. 3065-3073
    • Jackson, S.1    Harwood, C.2    Thomas, M.3    Banks, L.4    Storey, A.5
  • 435
    • 0032781685 scopus 로고    scopus 로고
    • Decreased programmed cell death in the uterine cervix associated with high risk human papillomavirus infection
    • Nair P, Nair KM, Jayaprakash PG, Pillai MR. Decreased programmed cell death in the uterine cervix associated with high risk human papillomavirus infection. Pathol Oncol Res 1999; 5: 95-103.
    • (1999) Pathol Oncol Res , vol.5 , pp. 95-103
    • Nair, P.1    Nair, K.M.2    Jayaprakash, P.G.3    Pillai, M.R.4
  • 436
    • 0029990550 scopus 로고    scopus 로고
    • Immunohistochemical analysis of in vivo patterns of Bak expression, a proapoptotic member of the Bcl-2 protein family
    • Krajewski S, Krajewska M, Reed JC. Immunohistochemical analysis of in vivo patterns of Bak expression, a proapoptotic member of the Bcl-2 protein family. Cancer Res 1996; 56: 2849-2855.
    • (1996) Cancer Res , vol.56 , pp. 2849-2855
    • Krajewski, S.1    Krajewska, M.2    Reed, J.C.3
  • 438
    • 1342301477 scopus 로고    scopus 로고
    • IFNgamma sensitization to TRAIL-induced apoptosis in human thyroid carcinoma cells by upregulating Bak expression
    • Wang SH, Mezosi E, Wolf JM, Cao Z, Utsugi S, Gauger PG, Doherty GM, Baker JR Jr. IFNgamma sensitization to TRAIL-induced apoptosis in human thyroid carcinoma cells by upregulating Bak expression. Oncogene 2004; 23: 928-935.
    • (2004) Oncogene , vol.23 , pp. 928-935
    • Wang, S.H.1    Mezosi, E.2    Wolf, J.M.3    Cao, Z.4    Utsugi, S.5    Gauger, P.G.6    Doherty, G.M.7    Baker Jr., J.R.8
  • 441
    • 0037374302 scopus 로고    scopus 로고
    • Bcl-w is expressed in a majority of infiltrative gastric adenocarcinomas and suppresses the cancer cell death by blocking stress-activated protein kinase/c-Jun NH2-terminal kinase activation
    • Lee HW, Lee SS, Lee SJ, Um HD. Bcl-w is expressed in a majority of infiltrative gastric adenocarcinomas and suppresses the cancer cell death by blocking stress-activated protein kinase/c-Jun NH2-terminal kinase activation. Cancer Res 2003; 63: 1093-1100.
    • (2003) Cancer Res , vol.63 , pp. 1093-1100
    • Lee, H.W.1    Lee, S.S.2    Lee, S.J.3    Um, H.D.4
  • 442
    • 0034632668 scopus 로고    scopus 로고
    • Bcl-w is an important determinant of damage-induced apoptosis in epithelia of small and large intestine
    • Pritchard DM, Print C, O'Reilly L, Adams JM, Potten CS, Hickman JA. Bcl-w is an important determinant of damage-induced apoptosis in epithelia of small and large intestine. Oncogene 2000; 19: 3955-3959.
    • (2000) Oncogene , vol.19 , pp. 3955-3959
    • Pritchard, D.M.1    Print, C.2    O'Reilly, L.3    Adams, J.M.4    Potten, C.S.5    Hickman, J.A.6
  • 443
    • 0036699925 scopus 로고    scopus 로고
    • Expression of the bcl-2 family of pro- and anti-apoptotic genes in multiple myeloma and normal plasma cells: Regulation during interleukin-6(IL-6)- induced growth and survival
    • Spets H, Stromberg T, Georgii-Hemming P, SiljasonJ, Nilsson K, Jernberg-Wiklund H. Expression of the bcl-2 family of pro- and anti-apoptotic genes in multiple myeloma and normal plasma cells: regulation during interleukin-6(IL-6)-induced growth and survival. Eur J Haematol 2002; 69: 76-89.
    • (2002) Eur J Haematol , vol.69 , pp. 76-89
    • Spets, H.1    Stromberg, T.2    Georgii-Hemming, P.3    Siljason, J.4    Nilsson, K.5    Jernberg-Wiklund, H.6
  • 445
    • 0042090228 scopus 로고    scopus 로고
    • Noxa in colorectal cancer: A study on DNA, mRNA and protein expression
    • Jansson AK, Emterling AM, Arbman G, Sun XF. Noxa in colorectal cancer: a study on DNA, mRNA and protein expression. Oncogene 2003; 22: 4675-4678.
    • (2003) Oncogene , vol.22 , pp. 4675-4678
    • Jansson, A.K.1    Emterling, A.M.2    Arbman, G.3    Sun, X.F.4
  • 446
  • 447
    • 16644395702 scopus 로고    scopus 로고
    • mRNA and protein expression of PUMA in sporadic colorectal cancer
    • Jansson A, Arbman G, Sun XF. mRNA and protein expression of PUMA in sporadic colorectal cancer. Oncol Rep 2004; 12: 1245-1249.
    • (2004) Oncol Rep , vol.12 , pp. 1245-1249
    • Jansson, A.1    Arbman, G.2    Sun, X.F.3
  • 448
    • 0033822959 scopus 로고    scopus 로고
    • Evaluation of two new urinary tumor markers: Bladder tumor fibronectin and cytokeratin 18 for the diagnosis of bladder cancer
    • Sanchez-Carbayo M, Urrutia M, Gonzalez de Buitrago JM, Navajo JA. Evaluation of two new urinary tumor markers: bladder tumor fibronectin and cytokeratin 18 for the diagnosis of bladder cancer. Clin Cancer Res 2000; 6: 3585-3594.
    • (2000) Clin Cancer Res , vol.6 , pp. 3585-3594
    • Sanchez-Carbayo, M.1    Urrutia, M.2    Gonzalez De Buitrago, J.M.3    Navajo, J.A.4
  • 449
    • 0035514046 scopus 로고    scopus 로고
    • Degenerative disorders caused by Bcl-2 deficiency prevented by loss of its BH3-only antagonist Bim
    • Bouillet P, Cory S, Zhang LC, Strasser A, Adams JM. Degenerative disorders caused by Bcl-2 deficiency prevented by loss of its BH3-only antagonist Bim. Dev Cell 2001; 1: 645-653.
    • (2001) Dev Cell , vol.1 , pp. 645-653
    • Bouillet, P.1    Cory, S.2    Zhang, L.C.3    Strasser, A.4    Adams, J.M.5
  • 450
  • 451
    • 1842457774 scopus 로고    scopus 로고
    • Lovastatin-induced up-regulation of the BH3-only protein, Bim, and cell death in glioblastoma cells
    • Jiang Z, Zheng X, Lytle RA, Higashikubo R, Rich KM. Lovastatin-induced up-regulation of the BH3-only protein, Bim, and cell death in glioblastoma cells. J Neurochem 2004; 89: 168-178.
    • (2004) J Neurochem , vol.89 , pp. 168-178
    • Jiang, Z.1    Zheng, X.2    Lytle, R.A.3    Higashikubo, R.4    Rich, K.M.5
  • 452
    • 0344629844 scopus 로고    scopus 로고
    • Gene expression profiling in clinically localised prostate cancer: A four-gene expression model predicts clinical behavior
    • Latil A, Bieche I, Chene L, Laurendeau I, Berthon P, Cussenot O, Vidaud M. Gene expression profiling in clinically localised prostate cancer: a four-gene expression model predicts clinical behavior. Clin Cancer Res 2003; 9: 5477-5485.
    • (2003) Clin Cancer Res , vol.9 , pp. 5477-5485
    • Latil, A.1    Bieche, I.2    Chene, L.3    Laurendeau, I.4    Berthon, P.5    Cussenot, O.6    Vidaud, M.7
  • 455
    • 2442617195 scopus 로고    scopus 로고
    • The Bcl-2 family member Bfl-1/A1 is strongly repressed in normal and malignant plasma cells but is a potent anti-apoptotic factor for myeloma cells
    • Tarte K, Jourdan M, Veyrune JL, Berberich I, Fiol G, Redal N, Shaughnessy J Jr, Klein B. The Bcl-2 family member Bfl-1/A1 is strongly repressed in normal and malignant plasma cells but is a potent anti-apoptotic factor for myeloma cells. Br J Haematol 2004; 125: 373-382.
    • (2004) Br J Haematol , vol.125 , pp. 373-382
    • Tarte, K.1    Jourdan, M.2    Veyrune, J.L.3    Berberich, I.4    Fiol, G.5    Redal, N.6    Shaughnessy Jr., J.7    Klein, B.8
  • 457
    • 0033916788 scopus 로고    scopus 로고
    • The bfl-1 gene is transcriptionally upregulated by the Epstein-Barr virus LMP1, and its expression promotes the survival of a Burkitt's lymphoma cell line
    • D'Souza B, Rowe M, Walls D. The bfl-1 gene is transcriptionally upregulated by the Epstein-Barr virus LMP1, and its expression promotes the survival of a Burkitt's lymphoma cell line. J Virol 2000; 74: 6652-6658.
    • (2000) J Virol , vol.74 , pp. 6652-6658
    • D'Souza, B.1    Rowe, M.2    Walls, D.3
  • 458
    • 0029815941 scopus 로고    scopus 로고
    • bfl-1, a bcl-2 homologue, suppresses p53-induced apoptosis and exhibits potent cooperative transforming activity
    • D'Sa-Eipper C, Subramanian T, Chimiadurai G. bfl-1, a bcl-2 homologue, suppresses p53-induced apoptosis and exhibits potent cooperative transforming activity. Cancer Res 1996; 56: 3879-3882.
    • (1996) Cancer Res , vol.56 , pp. 3879-3882
    • D'Sa-Eipper, C.1    Subramanian, T.2    Chimiadurai, G.3
  • 459
    • 0346256581 scopus 로고    scopus 로고
    • Bfl-1 gene expression in breast cancer: Its relationship with other prognostic factors
    • Yoon HS, Hong SH, Kang HJ, Ko BK, Ahn SH, Huh JR. Bfl-1 gene expression in breast cancer: its relationship with other prognostic factors. J Korean Med Sci 2003; 18: 225-230.
    • (2003) J Korean Med Sci , vol.18 , pp. 225-230
    • Yoon, H.S.1    Hong, S.H.2    Kang, H.J.3    Ko, B.K.4    Ahn, S.H.5    Huh, J.R.6
  • 460
  • 462
    • 1342347887 scopus 로고    scopus 로고
    • Cisplatin-induced apoptosis in HL-60 human promyelocytic leukemia cells: Differential expression of BCL2 and novel apoptosis-related gene BCL2L12
    • Floros KV, Thomadaki H, Lallas G, Katsaros N, Talieri M, Scorilas A. Cisplatin-induced apoptosis in HL-60 human promyelocytic leukemia cells: differential expression of BCL2 and novel apoptosis-related gene BCL2L12. Ann NY Acad Sci 2003; 1010: 153-158.
    • (2003) Ann NY Acad Sci , vol.1010 , pp. 153-158
    • Floros, K.V.1    Thomadaki, H.2    Lallas, G.3    Katsaros, N.4    Talieri, M.5    Scorilas, A.6
  • 463
    • 10044239114 scopus 로고    scopus 로고
    • mRNA expression analysis of a variety of apoptosis-related genes, including the novel gene of the BCL2-family, BCL2L12, in HL-60 leukemia cells after treatment with carboplatin and doxorubicin
    • Floros KV, Thomadaki H, Katsaros N, Talieri M, Scorilas A. mRNA expression analysis of a variety of apoptosis-related genes, including the novel gene of the BCL2-family, BCL2L12, in HL-60 leukemia cells after treatment with carboplatin and doxorubicin. Biol Chem 2004; 385: 1099-1103.
    • (2004) Biol Chem , vol.385 , pp. 1099-1103
    • Floros, K.V.1    Thomadaki, H.2    Katsaros, N.3    Talieri, M.4    Scorilas, A.5
  • 464
    • 0032835528 scopus 로고    scopus 로고
    • Mapping of a target region of allelic loss to a 0.5-cM interval on chromosome 22q13 in human colorectal cancer
    • Castells A, Ino Y, Louis DN, Ramesh V, Gusella JF, Rustgi AK. Mapping of a target region of allelic loss to a 0.5-cM interval on chromosome 22q13 in human colorectal cancer. Gastroenterology 1999; 117: 831-837.
    • (1999) Gastroenterology , vol.117 , pp. 831-837
    • Castells, A.1    Ino, Y.2    Louis, D.N.3    Ramesh, V.4    Gusella, J.F.5    Rustgi, A.K.6
  • 465
    • 0033179162 scopus 로고    scopus 로고
    • Expression of the death gene Bik/Nbk promotes sensitivity to drug-induced apoptosis in corticosteroid-resistant T-cell lymphoma and prevents tumor growth in severe combined immunodeficient mice
    • Daniel PT, Pun KT, Ritschel S, Sturm I, Holler J, Dorken B, Brown R. Expression of the death gene Bik/Nbk promotes sensitivity to drug-induced apoptosis in corticosteroid-resistant T-cell lymphoma and prevents tumor growth in severe combined immunodeficient mice. Blood 1999; 94: 1100-1107.
    • (1999) Blood , vol.94 , pp. 1100-1107
    • Daniel, P.T.1    Pun, K.T.2    Ritschel, S.3    Sturm, I.4    Holler, J.5    Dorken, B.6    Brown, R.7
  • 472
    • 21644433994 scopus 로고    scopus 로고
    • Gene expression associated with the decrease in malignant phenotype of human liver cancer cells following stimulation with a histone deacetylase inhibitor
    • Wakabayashi K, Saito H, Kaneko F, Nakamoto N, Tada S, Hibi T. Gene expression associated with the decrease in malignant phenotype of human liver cancer cells following stimulation with a histone deacetylase inhibitor. Int J Oncol 2005; 26: 233-239.
    • (2005) Int J Oncol , vol.26 , pp. 233-239
    • Wakabayashi, K.1    Saito, H.2    Kaneko, F.3    Nakamoto, N.4    Tada, S.5    Hibi, T.6
  • 473
    • 12344276322 scopus 로고    scopus 로고
    • Mcl-1 expression in gestational trophoblastic disease correlates with clinical outcome: A differential expression study
    • Fong PY, Xue WC, Ngan HY, Chan KY, Khoo US, Tsao SW, Chiu PM, Man LS, Cheung AN. Mcl-1 expression in gestational trophoblastic disease correlates with clinical outcome: a differential expression study. Cancer 2005; 103: 268-276.
    • (2005) Cancer , vol.103 , pp. 268-276
    • Fong, P.Y.1    Xue, W.C.2    Ngan, H.Y.3    Chan, K.Y.4    Khoo, U.S.5    Tsao, S.W.6    Chiu, P.M.7    Man, L.S.8    Cheung, A.N.9
  • 475
    • 0036699925 scopus 로고    scopus 로고
    • Expression of the bcl-2 family of pro- and anti-apoptotic genes in multiple myeloma and normal plasma cells: Regulation during interleukin-6(IL-6)- induced growth and survival
    • Spets H, Stromberg T, Georgii-Hemming P, Siljason J, Nilsson K, Jernberg-Wiklund H. Expression of the bcl-2 family of pro- and anti-apoptotic genes in multiple myeloma and normal plasma cells: regulation during interleukin-6(IL-6)-induced growth and survival. Eur J Haematol 2002; 69: 76-89.
    • (2002) Eur J Haematol , vol.69 , pp. 76-89
    • Spets, H.1    Stromberg, T.2    Georgii-Hemming, P.3    Siljason, J.4    Nilsson, K.5    Jernberg-Wiklund, H.6
  • 476
    • 0038754616 scopus 로고    scopus 로고
    • Flavopiridol-induced apoptosis is mediated through up-regulation of E2F1 and repression of Mcl-1
    • Ma Y, Cress WD, Haura EB. Flavopiridol-induced apoptosis is mediated through up-regulation of E2F1 and repression of Mcl-1. Mol Cancer Ther 2003; 2: 73-81.
    • (2003) Mol Cancer Ther , vol.2 , pp. 73-81
    • Ma, Y.1    Cress, W.D.2    Haura, E.B.3
  • 477
    • 0026556434 scopus 로고
    • Bioregulation of kinins: Kallikreins, kininogens, and kininases
    • Bhoola KD, Figueroa CD, Worthy K. Bioregulation of kinins: kallikreins, kininogens, and kininases. Pharmacol Rev 1992; 44: 1-80.
    • (1992) Pharmacol Rev , vol.44 , pp. 1-80
    • Bhoola, K.D.1    Figueroa, C.D.2    Worthy, K.3
  • 481
    • 0032907690 scopus 로고    scopus 로고
    • Predictive value of c-erbB-2 and cathepsin-D for Greek breast cancer patients using univariate and multivariate analysis
    • Scorilas A, Yotis J, Pateras C, Trangas T, Talieri M. Predictive value of c-erbB-2 and cathepsin-D for Greek breast cancer patients using univariate and multivariate analysis. Clin Cancer Res 1999; 5: 815-821.
    • (1999) Clin Cancer Res , vol.5 , pp. 815-821
    • Scorilas, A.1    Yotis, J.2    Pateras, C.3    Trangas, T.4    Talieri, M.5
  • 482
    • 0032739089 scopus 로고    scopus 로고
    • Determination of c-myc amplification and overexpression in breast cancer patients: Evaluation of its prognostic value against c-erbB-2, cathepsin-D and clinicopathological characteristics using univariate and multivariate analysis
    • Scorilas A, Trangas T, Yotis J, Pateras C, Talieri M. Determination of c-myc amplification and overexpression in breast cancer patients: evaluation of its prognostic value against c-erbB-2, cathepsin-D and clinicopathological characteristics using univariate and multivariate analysis. Br J Cancer 1999; 81: 1385-1391.
    • (1999) Br J Cancer , vol.81 , pp. 1385-1391
    • Scorilas, A.1    Trangas, T.2    Yotis, J.3    Pateras, C.4    Talieri, M.5


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