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Volumn 687, Issue , 2010, Pages 49-63

BH3-only proteins and their effects on cancer

Author keywords

[No Author keywords available]

Indexed keywords

BCL2 RELATED PROTEIN A1; BH3 PROTEIN; BIM PROTEIN; BORTEZOMIB; DOXORUBICIN; ETOPOSIDE; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FLUOROURACIL; GEFITINIB; GLUCOCORTICOID; HISTONE DEACETYLASE INHIBITOR; IMATINIB; PACLITAXEL; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BID; PROTEIN BNIP3; PROTEIN MCL 1; PROTEIN NOXA; PUMA PROTEIN; TUMOR NECROSIS FACTOR;

EID: 77958128601     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-6706-0_3     Document Type: Article
Times cited : (37)

References (124)
  • 1
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • DOI 10.1038/34112
    • Enari M, Sakahira H, Yokoyama H et al. A caspase-activated DNase that degrades DNA during apoptosis and its inhibitor ICAD. Nature 1998; 391(6662):43-50. (Pubitemid 28079208)
    • (1998) Nature , vol.391 , Issue.6662 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 2
  • 3
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y et al. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102(1):33-42.
    • (2000) Cell , vol.102 , Issue.1 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3
  • 4
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • DOI 10.1016/S0092-8674(00)80085-9
    • Liu X, Kim CN, Yang J et al. Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 1996; 86(1):147-157. (Pubitemid 26256586)
    • (1996) Cell , vol.86 , Issue.1 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 5
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev 2001; 15(22):2922-2933. (Pubitemid 33078942)
    • (2001) Genes and Development , vol.15 , Issue.22 , pp. 2922-2933
    • Wang, X.1
  • 6
    • 0034613302 scopus 로고    scopus 로고
    • Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1
    • Jiang X, Wang X. Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1. J Biol Chem 2000; 275(40):31199-31203.
    • (2000) J Biol Chem , vol.275 , Issue.40 , pp. 31199-31203
    • Jiang, X.1    Wang, X.2
  • 7
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • DOI 10.1101/gad.13.24.3179
    • Rodriguez J, Lazebnik Y. Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev 1999; 13(24):3179-3184. (Pubitemid 30030439)
    • (1999) Genes and Development , vol.13 , Issue.24 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 8
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H, Li Y, Liu X et al. An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J Biol Chem 1999; 274(17):11549-11556.
    • (1999) J Biol Chem , vol.274 , Issue.17 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3
  • 10
    • 33745933456 scopus 로고    scopus 로고
    • The Bax pore in liposomes, Biophysics
    • DOI 10.1038/sj.cdd.4401991, PII 4401991
    • Schlesinger PH, Saito M. The Bax pore in liposomes, Biophysics. Cell Death Differ 2006; 13(8):1403-1408. (Pubitemid 44057476)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.8 , pp. 1403-1408
    • Schlesinger, P.H.1    Saito, M.2
  • 14
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • DOI 10.1074/jbc.273.17.10777
    • Hsu YT, Youle RJ. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J Biol Chem 1998; 273(17):10777-10783. (Pubitemid 28227695)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.17 , pp. 10777-10783
    • Hsu, Y.-T.1    Youle, R.J.2
  • 16
    • 0030026865 scopus 로고    scopus 로고
    • Bax-independent inhibition of apoptosis by BCL-XL
    • Cheng EH, Levine B, Boise LH et al. Bax-independent inhibition of apoptosis by BCL-XL. Nature 1996; 379(6565):554-556.
    • (1996) Nature , vol.379 , Issue.6565 , pp. 554-556
    • Cheng, E.H.1    Levine, B.2    Boise, L.H.3
  • 17
    • 33646354381 scopus 로고    scopus 로고
    • Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members
    • DOI 10.1016/j.ccr.2006.03.027, PII S1535610806001139
    • Certo M, Del Gaizo Moore V, Nishino M et al. Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. Cancer Cell 2006; 9(5):351-365. (Pubitemid 43668734)
    • (2006) Cancer Cell , vol.9 , Issue.5 , pp. 351-365
    • Certo, M.1    Moore, V.D.G.2    Nishino, M.3    Wei, G.4    Korsmeyer, S.5    Armstrong, S.A.6    Letai, A.7
  • 20
    • 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 et al. Bad, a heterodimeric partner for BCL-XL and BCL-2, displaces Bax and promotes cell death. Cell 1995; 80(2):285-291.
    • (1995) Cell , vol.80 , Issue.2 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3
  • 21
    • 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 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(9):1921-1928.
    • (1995) Oncogene , vol.11 , Issue.9 , pp. 1921-1928
    • Boyd, J.M.1    Gallo, G.J.2    Elangovan, B.3
  • 23
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • DOI 10.1016/S1097-2765(01)00214-3
    • Nakano K, Vousden KH. PUMA, a novel proapoptotic gene, is induced by p53. Mol Cell 2001; 7(3):683-694. (Pubitemid 32706359)
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 24
    • 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)
    • DOI 10.1093/emboj/16.7.1686
    • Inohara N, Ding L, Chen S et al. 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(7):1686-1694. (Pubitemid 27151963)
    • (1997) EMBO Journal , vol.16 , Issue.7 , pp. 1686-1694
    • Inohara, N.1    Ding, L.2    Chen, S.3    Nunez, G.4
  • 25
  • 26
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • DOI 10.1016/j.cell.2005.06.009, PII S0092867405005568
    • Zhong Q, Gao W, Du F et al. Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 2005; 121(7):1085-1095. (Pubitemid 40884398)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 27
    • 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(4):2780-2785.
    • (2001) J Biol Chem , vol.276 , Issue.4 , pp. 2780-2785
    • Guo, B.1    Godzik, A.2    Reed, J.C.3
  • 28
    • 0032524656 scopus 로고    scopus 로고
    • Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence
    • DOI 10.1074/jbc.273.20.12415
    • Yasuda M, Theodorakis P, Subramanian T et al. Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence. J Biol Chem 1998; 273(20):12415-12421. (Pubitemid 28240613)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.20 , pp. 12415-12421
    • Yasuda, M.1    Theodorakisi, P.2    Subramanian, T.3    Chinnadurai, G.4
  • 29
    • 34249037565 scopus 로고    scopus 로고
    • L-beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein
    • DOI 10.1074/jbc.M700492200
    • Oberstein A, Jeffrey PD, Shi Y. Crystal structure of the BCL-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J Biol Chem 2007; 282(17):13123-13132. (Pubitemid 47100641)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 30
    • 13244252344 scopus 로고    scopus 로고
    • Apolipoprotein L6, a novel proapoptotic Bcl-2 homology 3-only protein, includes mitochondria-mediated apoptosis in cancer cells
    • Liu Z, Lu H, Jiang Z et al. Apolipoprotein l6, a novel proapoptotic BCL-2 homology 3-only protein, induces mitochondria-mediated apoptosis in cancer cells. Mol Cancer Res 2005; 3(1):21-31. (Pubitemid 40189593)
    • (2005) Molecular Cancer Research , vol.3 , Issue.1 , pp. 21-31
    • Liu, Z.1    Lu, H.2    Jiang, Z.3    Pastuszyn, A.4    Hu, C.-A.A.5
  • 32
    • 0037390872 scopus 로고    scopus 로고
    • Spike, a novel BH3-only protein, regulates apoptosis at the endoplasmic reticulum
    • Mund T, Gewies A, Schoenfeld N et al. Spike, a novel BH3-only protein, regulates apoptosis at the endoplasmic reticulum. FASEB J 2003; 17(6):696-698.
    • (2003) FASEB J , vol.17 , Issue.6 , pp. 696-698
    • Mund, T.1    Gewies, A.2    Schoenfeld, N.3
  • 33
    • 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 et al. 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(4):2802-2807.
    • (2001) J Biol Chem , vol.276 , Issue.4 , pp. 2802-2807
    • Tan, K.O.1    Tan, K.M.2    Chan, S.L.3
  • 34
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • DOI 10.1016/S1535-6108(02)00127-7
    • Letai A, Bassik MC, Walensky LD et al. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2002; 2(3):183-192. (Pubitemid 41043974)
    • (2002) Cancer Cell , vol.2 , Issue.3 , 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
  • 35
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • DOI 10.1101/gad.897601
    • Zong WX, Lindsten T, Ross AJ et al. BH3-only proteins that bind pro-survival BCL-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev 2001; 15(12):1481-1486. (Pubitemid 32552527)
    • (2001) Genes and Development , vol.15 , Issue.12 , pp. 1481-1486
    • Zong, W.-X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 37
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • Lovell JF, Billen LP, Bindner S et al. Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 2008; 135(6):1074-1084.
    • (2008) Cell , vol.135 , Issue.6 , pp. 1074-1084
    • Lovell, J.F.1    Billen, L.P.2    Bindner, S.3
  • 38
    • 54549114986 scopus 로고    scopus 로고
    • BAX activation is initiated at a novel interaction site
    • Gavathiotis E, Suzuki M, Davis ML et al. BAX activation is initiated at a novel interaction site. Nature 2008; 455(7216):1076-1081.
    • (2008) Nature , vol.455 , Issue.7216 , pp. 1076-1081
    • Gavathiotis, E.1    Suzuki, M.2    Davis, M.L.3
  • 39
    • 33846964621 scopus 로고    scopus 로고
    • Apoptosis initiated when BH3 ligands engage multiple BCL-2 homologs, not Bax or Bak
    • Willis SN, Fletcher JI, Kaufmann T et al. Apoptosis initiated when BH3 ligands engage multiple BCL-2 homologs, not Bax or Bak. Science 2007; 315(5813):856-859.
    • (2007) Science , vol.315 , Issue.5813 , pp. 856-859
    • Willis, S.N.1    Fletcher, J.I.2    Kaufmann, T.3
  • 40
    • 0842278331 scopus 로고    scopus 로고
    • Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
    • DOI 10.1126/science.1092734
    • Chipuk JE, Kuwana T, Bouchier-Hayes L et al. Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 2004; 303(5660):1010-1014. (Pubitemid 38209704)
    • (2004) Science , vol.303 , Issue.5660 , pp. 1010-1014
    • Chipuk, J.E.1    Kuwana, T.2    Bouchier-Hayes, L.3    Droin, N.M.4    Newmeyer, D.D.5    Schuler, M.6    Green, D.R.7
  • 46
    • 0036091728 scopus 로고    scopus 로고
    • Identification of novel isoforms of the BH3 domain protein bim which directly activate Bax to trigger apoptosis
    • DOI 10.1128/MCB.22.11.3577-3589.2002
    • Marani M, Tenev T, Hancock D et al. Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis. Mol Cell Biol 2002; 22(11):3577-3589. (Pubitemid 34527138)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.11 , pp. 3577-3589
    • Marani, M.1    Tenev, T.2    Hancock, D.3    Downward, J.4    Lemoine, N.R.5
  • 47
    • 13544253706 scopus 로고    scopus 로고
    • Nomenclature of dynein light chain-linked BH3-only protein Bim isoforms [1]
    • DOI 10.1038/sj.cdd.4401529
    • Adachi M, Zhao X, Imai K. Nomenclature of dynein light chain-linked BH3-only protein Bim isoforms. Cell Death Differ 2005; 12(2):192-193. (Pubitemid 40220650)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.2 , pp. 192-193
    • Adachi, M.1    Zhao, X.2    Imai, K.3
  • 48
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • DOI 10.1016/S1097-2765(00)80456-6
    • Puthalakath H, Huang DC, O'Reilly LA et al. The proapoptotic activity of the BCL-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 1999; 3(3):287-296. (Pubitemid 29290669)
    • (1999) Molecular Cell , vol.3 , Issue.3 , pp. 287-296
    • Puthalakath, H.1    Huang, D.C.S.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 49
    • 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 et al. Expression of the pro-apoptotic BCL-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. Curr Biol 2000; 10(19):1201-1204.
    • (2000) Curr Biol , vol.10 , Issue.19 , pp. 1201-1204
    • Dijkers, P.F.1    Medema, R.H.2    Lammers, J.W.3
  • 53
    • 0034107096 scopus 로고    scopus 로고
    • Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving bid
    • DOI 10.1128/MCB.20.11.3781-3794.2000
    • Barry M, Heibein JA, Pinkoski MJ et al. Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid. Mol Cell Biol 2000; 20(11):3781-3794. (Pubitemid 30314478)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.11 , pp. 3781-3794
    • Barry, M.1    Heibein, J.A.2    Pinkoski, M.J.3    Lee, S.-F.4    Moyer, R.W.5    Green, D.R.6    Bleackley, R.C.7
  • 54
    • 0034694091 scopus 로고    scopus 로고
    • Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation
    • Sutton VR, Davis JE, Cancilla M et al. Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation. J Exp Med 2000; 192(10):1403-1414.
    • (2000) J Exp Med , vol.192 , Issue.10 , pp. 1403-1414
    • Sutton, V.R.1    Davis, J.E.2    Cancilla, M.3
  • 55
    • 49649123891 scopus 로고    scopus 로고
    • Cysteine cathepsins trigger caspase-dependent cell death through cleavage of bid and antiapoptotic BCL-2 homologues
    • Droga-Mazovec G, Bojic L, Petelin A et al. Cysteine cathepsins trigger caspase-dependent cell death through cleavage of bid and antiapoptotic BCL-2 homologues. J Biol Chem 2008; 283(27):19140-19150.
    • (2008) J Biol Chem , vol.283 , Issue.27 , pp. 19140-19150
    • Droga-Mazovec, G.1    Bojic, L.2    Petelin, A.3
  • 56
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • DOI 10.1126/science.290.5497.1761
    • Zha J, Weiler S, Oh KJ et al. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 2000; 290(5497):1761-1765. (Pubitemid 32004806)
    • (2000) Science , vol.290 , Issue.5497 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 60
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell- intrinsic death machinery
    • DOI 10.1016/S0092-8674(00)80405-5
    • Datta SR, Dudek H, Tao X et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997; 91(2):231-241. (Pubitemid 27456390)
    • (1997) Cell , vol.91 , Issue.2 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Xu, T.3    Masters, S.4    Haian, F.5    Gotoh, Y.6    Greenberg, M.E.7
  • 61
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • DOI 10.1126/science.278.5338.687
    • del Peso L, Gonzalez-Garcia M, Page C et al. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 1997; 278(5338):687-689. (Pubitemid 27464966)
    • (1997) Science , vol.278 , Issue.5338 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 62
    • 0345498292 scopus 로고    scopus 로고
    • Bcl-2 targets the protein kinase Raf-1 to mitochondria
    • DOI 10.1016/S0092-8674(00)81383-5
    • Wang HG, Rapp UR, Reed JC. BCL-2 targets the protein kinase Raf-1 to mitochondria. Cell 1996; 87(4):629-638. (Pubitemid 26386937)
    • (1996) Cell , vol.87 , Issue.4 , pp. 629-638
    • Wang, H.-G.1    Rapp, U.R.2    Reed, J.C.3
  • 64
    • 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)
    • DOI 10.1016/S0092-8674(00)81382-3
    • Zha J, Harada H, Yang E et al. 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(4):619-628. (Pubitemid 26386936)
    • (1996) Cell , vol.87 , Issue.4 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 66
    • 0342657806 scopus 로고    scopus 로고
    • Protein phosphatase 1α is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis
    • Ayllon V, Martinez AC, Garcia A et al. Protein phosphatase 1alpha is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis. EMBO J 2000; 19(10):2237-2246. (Pubitemid 30259005)
    • (2000) EMBO Journal , vol.19 , Issue.10 , pp. 2237-2246
    • Ayllon, V.1    Martinez-A, C.2    Garcia, A.3    Cayla, X.4    Rebollo, A.5
  • 67
    • 0035283087 scopus 로고    scopus 로고
    • Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin-3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation
    • DOI 10.1182/blood.V97.5.1289
    • Chiang CW, Harris G, Ellig C et al. Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin-3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation. Blood 2001; 97(5):1289-1297. (Pubitemid 32183751)
    • (2001) Blood , vol.97 , Issue.5 , pp. 1289-1297
    • Chiang, C.-W.1    Harris, G.2    Ellig, C.3    Masters, S.C.4    Subramanian, R.5    Shenolikar, S.6    Wadzinski, B.E.7    Yang, E.8
  • 68
    • 85047699843 scopus 로고    scopus 로고
    • Induction and endoplasmic reticulum location of BIK/NBK in response to apoptotic signaling by E1A and p53
    • DOI 10.1038/sj/onc/1205340
    • Mathai JP, Germain M, Marcellus RC et al. Induction and endoplasmic reticulum location of BIK/ NBK in response to apoptotic signaling by E1A and p53. Oncogene 2002; 21(16):2534-2544. (Pubitemid 34438106)
    • (2002) Oncogene , vol.21 , Issue.16 , pp. 2534-2544
    • Mathai, J.P.1    Germain, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 69
    • 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(7):4671-4676.
    • (2001) J Biol Chem , vol.276 , Issue.7 , pp. 4671-4676
    • Verma, S.1    Zhao, L.J.2    Chinnadurai, G.3
  • 70
    • 33750054426 scopus 로고    scopus 로고
    • Transcriptional activation of the proapoptotic bik gene by E2F proteins in cancer cells
    • DOI 10.1016/j.febslet.2006.08.088, PII S0014579306011665
    • Real PJ, Sanz C, Gutierrez O et al. Transcriptional activation of the proapoptotic bik gene by E2F proteins in cancer cells. FEBS Lett 2006; 580(25):5905-5909. (Pubitemid 44584291)
    • (2006) FEBS Letters , vol.580 , Issue.25 , pp. 5905-5909
    • Real, P.J.1    Sanz, C.2    Gutierrez, O.3    Pipaon, C.4    Zubiaga, A.M.5    Fernandez-Luna, J.L.6
  • 75
  • 76
    • 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 et al. Specific and rapid induction of the proapoptotic protein Hrk after growth factor withdrawal in hematopoietic progenitor cells. Blood 2000; 95(9):2742-2747. (Pubitemid 30235877)
    • (2000) Blood , vol.95 , Issue.9 , pp. 2742-2747
    • Sanz, C.1    Benito, A.2    Inohara, N.3    Ekhterae, D.4    Nunez, G.5    Fernandez-Luna, J.L.6
  • 77
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100(1):57-70. (Pubitemid 30046295)
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 78
    • 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 et al. Proapoptotic BCL-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis and to preclude autoimmunity. Science 1999; 286(5445):1735-1738. (Pubitemid 129515880)
    • (1999) Science , vol.286 , Issue.5445 , pp. 1735-1738
    • Bouillet, P.1    Metcalf, D.2    Huang, D.C.S.3    Tarlinton, D.M.4    Kay, T.W.H.5    Kontgen, F.6    Adams, J.M.7    Strasser, A.8
  • 83
    • 2442674336 scopus 로고    scopus 로고
    • Microarray analysis of epigenetic silencing of gene expression in the KAS-6/1 multiple myeloma cell line
    • DOI 10.1158/0008-5472.CAN-03-3970
    • Pompeia C, Hodge DR, Plass C et al. Microarray analysis of epigenetic silencing of gene expression in the KAS-6/1 multiple myeloma cell line. Cancer Res 2004; 64(10):3465-3473. (Pubitemid 38657919)
    • (2004) Cancer Research , vol.64 , Issue.10 , pp. 3465-3473
    • Pompeia, C.1    Hodge, D.R.2    Plass, C.3    Wu, Y.-Z.4    Marquez, V.E.5    Kelley, J.A.6    Farrar, W.L.7
  • 84
    • 33644954099 scopus 로고    scopus 로고
    • Loss of the tissue-specific proapoptotic BH3-only protein Nbk/ Bik is a unifying feature of renal cell carcinoma
    • Sturm I, Stephan C, Gillissen B et al. Loss of the tissue-specific proapoptotic BH3-only protein Nbk/ Bik is a unifying feature of renal cell carcinoma. Cell Death Differ 2006; 13(4):619-627.
    • (2006) Cell Death Differ , vol.13 , Issue.4 , pp. 619-627
    • Sturm, I.1    Stephan, C.2    Gillissen, B.3
  • 87
    • 13944263967 scopus 로고    scopus 로고
    • PUMA expression is significantly reduced in human cutaneous melanomas
    • DOI 10.1038/sj.onc.1208374
    • Karst AM, Dai DL, Martinka M et al. PUMA expression is significantly reduced in human cutaneous melanomas. Oncogene 2005; 24(6):1111-1116. (Pubitemid 40313889)
    • (2005) Oncogene , vol.24 , Issue.6 , pp. 1111-1116
    • Karst, A.M.1    Dai, D.L.2    Martinka, M.3    Li, G.4
  • 88
    • 0032533594 scopus 로고    scopus 로고
    • Malignant melanoma: Modern black plague and genetic black box
    • Chin L, Merlino G, DePinho RA. Malignant melanoma: Modern black plague and genetic black box. Genes Dev 1998; 12(22):3467-3481. (Pubitemid 28553239)
    • (1998) Genes and Development , vol.12 , Issue.22 , pp. 3467-3481
    • Chin, L.1    Merlino, G.2    DePinho, R.A.3
  • 93
    • 0037097701 scopus 로고    scopus 로고
    • Complementary functions of the antiapoptotic protein A1 and serine/threonine kinase pim-1 in the BCR/ABL-mediated leukemogenesis
    • DOI 10.1182/blood.V99.12.4531
    • Nieborowska-Skorska M, Hoser G, Kossev P et al. Complementary functions of the antiapoptotic protein A1 and serine/threonine kinase pim-1 in the BCR/ABL-mediated leukemogenesis. Blood 2002; 99(12):4531-4539. (Pubitemid 34627224)
    • (2002) Blood , vol.99 , Issue.12 , pp. 4531-4539
    • Nieborowska-Skorska, M.1    Hoser, G.2    Kossev, P.3    Wasik, M.A.4    Skorski, T.5
  • 95
    • 0035877981 scopus 로고    scopus 로고
    • MCL1 transgenic mice exhibit a high incidence of B-cell lymphoma manifested as a spectrum of histologic subtypes
    • Zhou P, Levy NB, Xie H et al. MCL1 transgenic mice exhibit a high incidence of B-cell lymphoma manifested as a spectrum of histologic subtypes. Blood 2001; 97(12):3902-3909.
    • (2001) Blood , vol.97 , Issue.12 , pp. 3902-3909
    • Zhou, P.1    Levy, N.B.2    Xie, H.3
  • 96
    • 53249088373 scopus 로고    scopus 로고
    • Prognostic impact of bim, puma and noxa expression in human colon carcinomas
    • Sinicrope FA, Rego RL, Okumura K et al. Prognostic impact of bim, puma and noxa expression in human colon carcinomas. Clin Cancer Res 2008; 14(18):5810-5818.
    • (2008) Clin Cancer Res , vol.14 , Issue.18 , pp. 5810-5818
    • Sinicrope, F.A.1    Rego, R.L.2    Okumura, K.3
  • 97
    • 48249116801 scopus 로고    scopus 로고
    • Proapoptotic Bad and Bid protein expression predict survival in stages II and III colon cancers
    • Sinicrope FA, Rego RL, Foster NR et al. Proapoptotic Bad and Bid protein expression predict survival in stages II and III colon cancers. Clin Cancer Res 2008; 14(13):4128-4133.
    • (2008) Clin Cancer Res , vol.14 , Issue.13 , pp. 4128-4133
    • Sinicrope, F.A.1    Rego, R.L.2    Foster, N.R.3
  • 100
    • 50949091476 scopus 로고    scopus 로고
    • Bid participates in genotoxic drug-induced apoptosis of HeLa cells and is essential for death receptor ligands' apoptotic and synergistic effects
    • Kohler B, Anguissola S, Concannon CG et al. Bid participates in genotoxic drug-induced apoptosis of HeLa cells and is essential for death receptor ligands' apoptotic and synergistic effects. PLoS ONE 2008; 3(7):e2844.
    • (2008) PLoS ONE , vol.3 , Issue.7
    • Kohler, B.1    Anguissola, S.2    Concannon, C.G.3
  • 101
    • 39749136204 scopus 로고    scopus 로고
    • BCL-2 family regulation by the 20S proteasome inhibitor bortezomib
    • DOI 10.1038/sj.onc.1210744, PII 1210744
    • Fennell DA, Chacko A, Mutti L. BCL-2 family regulation by the 20S proteasome inhibitor bortezomib. Oncogene 2008; 27(9):1189-1197. (Pubitemid 351294694)
    • (2008) Oncogene , vol.27 , Issue.9 , pp. 1189-1197
    • Fennell, D.A.1    Chacko, A.2    Mutti, L.3
  • 102
    • 66449121337 scopus 로고    scopus 로고
    • Cleavage of bid by executioner caspases mediates feed forward amplification of mitochondrial outer membrane permeabilization during genotoxic stress-induced apoptosis in jurkat cells
    • Shelton SN, Shawgo ME, Robertson JD. Cleavage of bid by executioner caspases mediates feed forward amplification of mitochondrial outer membrane permeabilization during genotoxic stress-induced apoptosis in jurkat cells. J Biol Chem 2009.
    • (2009) J Biol Chem
    • Shelton, S.N.1    Shawgo, M.E.2    Robertson, J.D.3
  • 103
    • 42149143430 scopus 로고    scopus 로고
    • Bid exhibits S phase checkpoint activation and plays a pro-apoptotic role in response to etoposide-induced DNA damage in hepatocellular carcinoma cells
    • Song G, Chen GG, Chau DK et al. Bid exhibits S phase checkpoint activation and plays a pro-apoptotic role in response to etoposide-induced DNA damage in hepatocellular carcinoma cells. Apoptosis 2008; 13(5):693-701.
    • (2008) Apoptosis , vol.13 , Issue.5 , pp. 693-701
    • Song, G.1    Chen, G.G.2    Chau, D.K.3
  • 104
    • 35648953299 scopus 로고    scopus 로고
    • Gefitinib-induced killing of NSCLC cell lines expressing mutant EGFR requires BIM and can be enhanced by BH3 mimetics
    • discussion 1690
    • Cragg MS, Kuroda J, Puthalakath H et al. Gefitinib-induced killing of NSCLC cell lines expressing mutant EGFR requires BIM and can be enhanced by BH3 mimetics. PLoS Med 2007; 4(10):1681-1689; discussion 1690.
    • (2007) PLoS Med , vol.4 , Issue.10 , pp. 1681-1689
    • Cragg, M.S.1    Kuroda, J.2    Puthalakath, H.3
  • 106
    • 11244305855 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid-induced apoptosis by targeting the major splice variants of BIM mRNA with small interfering RNA and short hairpin RNA
    • DOI 10.1074/jbc.M411767200
    • Abrams MT, Robertson NM, Yoon K et al. Inhibition of glucocorticoid- induced apoptosis by targeting the major splice variants of BIM mRNA with small interfering RNA and short hairpin RNA. J Biol Chem 2004; 279(53):55809-55817. (Pubitemid 40066588)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55809-55817
    • Abrams, M.T.1    Robertson, N.M.2    Yoon, K.3    Wickstrom, E.4
  • 107
    • 28844472952 scopus 로고    scopus 로고
    • BH3-only proteins Puma and Bim are rate-limiting for γ-radiation- and glucocorticoid-induced apoptosis of lymphoid cells in vivo
    • DOI 10.1182/blood-2005-04-1595
    • Erlacher M, Michalak EM, Kelly PN et al. BH3-only proteins Puma and Bim are rate-limiting for gamma-radiation- and glucocorticoid-induced apoptosis of lymphoid cells in vivo. Blood 2005; 106(13):4131-4138. (Pubitemid 41775918)
    • (2005) Blood , vol.106 , Issue.13 , pp. 4131-4138
    • Erlacher, M.1    Michalak, E.M.2    Kelly, P.N.3    Labi, V.4    Niederegger, H.5    Coultas, L.6    Adams, J.M.7    Strasser, A.8    Villunger, A.9
  • 108
    • 2442682766 scopus 로고    scopus 로고
    • The pro-apoptotic protein Bim is a convergence point for cAMP/protein kinase A- and glucocorticoid-promoted apoptosis of lymphoid cells
    • DOI 10.1074/jbc.M310643200
    • Zhang L, Insel PA. The pro-apoptotic protein Bim is a convergence point for cAMP/protein kinase A- and glucocorticoid-promoted apoptosis of lymphoid cells. J Biol Chem 2004; 279(20):20858-20865. (Pubitemid 38656482)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 20858-20865
    • Zhang, L.1    Insel, P.A.2
  • 109
    • 33845352223 scopus 로고    scopus 로고
    • Bim plays a crucial role in synergistic induction of apoptosis by the histone deacetylase inhibitor SBHA and TRAIL in melanoma cells
    • DOI 10.1007/s10495-006-0283-6
    • Gillespie S, Borrow J, Zhang XD et al. Bim plays a crucial role in synergistic induction of apoptosis by the histone deacetylase inhibitor SBHA and TRAIL in melanoma cells. Apoptosis 2006; 11(12):2251-2265. (Pubitemid 44885400)
    • (2006) Apoptosis , vol.11 , Issue.12 , pp. 2251-2265
    • Gillespie, S.1    Borrow, J.2    Zhang, X.D.3    Hersey, P.4
  • 110
    • 31544466465 scopus 로고    scopus 로고
    • Bmf is a possible mediator in histone deacetylase inhibitors FK228 and CBHA-induced apoptosis
    • Zhang Y, Adachi M, Kawamura R et al. Bmf is a possible mediator in histone deacetylase inhibitors FK228 and CBHA-induced apoptosis. Cell Death Differ 2006; 13(1):129-140.
    • (2006) Cell Death Differ , vol.13 , Issue.1 , pp. 129-140
    • Zhang, Y.1    Adachi, M.2    Kawamura, R.3
  • 112
    • 51549095216 scopus 로고    scopus 로고
    • A critical role for the proapoptotic protein bid in ultraviolet- induced immune suppression and cutaneous apoptosis
    • Pradhan S, Kim HK, Thrash CJ et al. A critical role for the proapoptotic protein bid in ultraviolet- induced immune suppression and cutaneous apoptosis. J Immunol 2008; 181(5):3077-3088.
    • (2008) J Immunol , vol.181 , Issue.5 , pp. 3077-3088
    • Pradhan, S.1    Kim, H.K.2    Thrash, C.J.3
  • 113
    • 62449193810 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase inhibition induces translocation of Bmf to promote apoptosis in melanoma
    • VanBrocklin MW, Verhaegen M, Soengas MS et al. Mitogen-activated protein kinase inhibition induces translocation of Bmf to promote apoptosis in melanoma. Cancer Res 2009; 69(5):1985-1994.
    • (2009) Cancer Res , vol.69 , Issue.5 , pp. 1985-1994
    • VanBrocklin, M.W.1    Verhaegen, M.2    Soengas, M.S.3
  • 115
    • 14944349359 scopus 로고    scopus 로고
    • Apoptosis of non-small-cell lung cancer cell lines after paclitaxel treatment involves the BH3-only proapoptotic protein Bim
    • DOI 10.1038/sj.cdd.4401554
    • Li R, Moudgil T, Ross HJ et al. Apoptosis of nonsmall-cell lung cancer cell lines after paclitaxel treatment involves the BH3-only proapoptotic protein Bim. Cell Death Differ 2005; 12(3):292-303. (Pubitemid 40360952)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.3 , pp. 292-303
    • Li, R.1    Moudgil, T.2    Ross, H.J.3    Hu, H.-M.4
  • 116
    • 36348971785 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 deficiency prevents apoptosis in a Bax-controlled pathway and promotes clonogenic survival during paclitaxel treatment
    • DOI 10.1182/blood-2007-02-073213
    • Janssen K, Pohlmann S, Janicke RU et al. Apaf-1 and caspase-9 deficiency prevents apoptosis in a Bax-controlled pathway and promotes clonogenic survival during paclitaxel treatment. Blood 2007; 110(10):3662-3672. (Pubitemid 350159635)
    • (2007) Blood , vol.110 , Issue.10 , pp. 3662-3672
    • Janssen, K.1    Pohlmann, S.2    Janicke, R.U.3    Schulze-Osthoff, K.4    Fischer, U.5
  • 119
    • 33845994359 scopus 로고    scopus 로고
    • Chronic lymphocytic leukemia requires BCL2 to sequester prodeath BIM, explaining sensitivity to BCL2 antagonist ABT-737
    • DOI 10.1172/JCI28281
    • Del Gaizo Moore V, Brown JR, Certo M et al. Chronic lymphocytic leukemia requires BCL2 to sequester prodeath BIM, explaining sensitivity to BCL2 antagonist ABT-737. J Clin Invest 2007; 117(1):112-121. (Pubitemid 46048458)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.1 , pp. 112-121
    • Moore, V.D.G.1    Brown, J.R.2    Certo, M.3    Love, T.M.4    Novina, C.D.5    Letai, A.6
  • 120
    • 44049083639 scopus 로고    scopus 로고
    • Targeting the Bcl-2-regulated apoptosis pathway by BH3 mimetics: A breakthrough in anticancer therapy?
    • DOI 10.1038/cdd.2008.37, PII CDD200837
    • Labi V, Grespi F, Baumgartner F et al. Targeting the BCL-2-regulated apoptosis pathway by BH3 mimetics: A breakthrough in anticancer therapy? Cell Death Differ 2008; 15(6):977-987. (Pubitemid 351712602)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.6 , pp. 977-987
    • Labi, V.1    Grespi, F.2    Baumgartner, F.3    Villunger, A.4
  • 121
    • 34548814971 scopus 로고    scopus 로고
    • Activity of vincristine, L-ASP, and dexamethasone against acute lymphoblastic leukemia is enhanced by the BH3-mimetic ABT-737 in vitro and in vivo
    • DOI 10.1182/blood-2007-03-080325
    • Kang MH, Kang YH, Szymanska B et al. Activity of vincristine, L-ASP and dexamethasone against acute lymphoblastic leukemia is enhanced by the BH3-mimetic ABT-737 in vitro and in vivo. Blood 2007; 110(6):2057-2066. (Pubitemid 47443923)
    • (2007) Blood , vol.110 , Issue.6 , pp. 2057-2066
    • Kang, M.H.1    Kang, H.K.2    Szymanska, B.3    Wilczynska-Kalak, U.4    Sheard, M.A.5    Harned, T.M.6    Lock, R.B.7    Reynolds, C.P.8
  • 122
    • 34547603628 scopus 로고    scopus 로고
    • BH3 Profiling Identifies Three Distinct Classes of Apoptotic Blocks to Predict Response to ABT-737 and Conventional Chemotherapeutic Agents
    • DOI 10.1016/j.ccr.2007.07.001, PII S1535610807002000
    • Deng J, Carlson N, Takeyama K et al. BH3 profiling identifies three distinct classes of apoptotic blocks to predict response to ABT-737 and conventional chemotherapeutic agents. Cancer Cell 2007; 12(2):171-185. (Pubitemid 47199122)
    • (2007) Cancer Cell , vol.12 , Issue.2 , pp. 171-185
    • Deng, J.1    Carlson, N.2    Takeyama, K.3    Dal Cin, P.4    Shipp, M.5    Letai, A.6


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