메뉴 건너뛰기




Volumn 20, Issue 2, 2015, Pages 136-150

The Bcl-2 family: Structures, interactions and targets for drug discovery

Author keywords

Apoptosis; Bcl 2; Cancer; Drug discovery; Virus

Indexed keywords

4 [4 (4' CHLORO 2 BIPHENYLYLMETHYL) 1 PIPERAZINYL] N [4 [3 DIMETHYLAMINO 1 (PHENYLTHIOMETHYL)PROPYLAMINO] 3 NITROBENZENESULFONYL]BENZAMIDE; BECLIN 1; BH3 PROTEIN; NAVITOCLAX; PROTEIN BCL 2; VENETOCLAX; VIRUS PROTEIN; ANTINEOPLASTIC AGENT;

EID: 84922076832     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-014-1051-7     Document Type: Article
Times cited : (139)

References (167)
  • 1
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • 1:CAS:528:DC%2BD2sXhsVKrsrrP 18097445
    • Youle RJ, Strasser A (2008) The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 9:47-59
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 2
    • 84860389354 scopus 로고    scopus 로고
    • Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases
    • 1:CAS:528:DC%2BC3MXhtVKit77M 3173800 21863020
    • Strasser A, Cory S, Adams JM (2011) Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases. EMBO J 30:3667-3683
    • (2011) EMBO J , vol.30 , pp. 3667-3683
    • Strasser, A.1    Cory, S.2    Adams, J.M.3
  • 3
    • 27944470616 scopus 로고    scopus 로고
    • Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators
    • 1:CAS:528:DC%2BD2MXht1KgtLnI 16093567
    • Aouacheria A, Brunet F, Gouy M (2005) Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators. Mol Biol Evol 22:2395-2416
    • (2005) Mol Biol Evol , vol.22 , pp. 2395-2416
    • Aouacheria, A.1    Brunet, F.2    Gouy, M.3
  • 7
    • 84889581765 scopus 로고    scopus 로고
    • Structural biology of the Bcl-2 family and its mimicry by viral proteins
    • 1:CAS:528:DC%2BC3sXhslCrtbzL 3847314 24201808
    • Kvansakul M, Hinds MG (2013) Structural biology of the Bcl-2 family and its mimicry by viral proteins. Cell Death Dis 4:e909
    • (2013) Cell Death Dis , vol.4 , pp. 909
    • Kvansakul, M.1    Hinds, M.G.2
  • 8
    • 45449083640 scopus 로고    scopus 로고
    • Living with death: The evolution of the mitochondrial pathway of apoptosis in animals
    • 1:CAS:528:DC%2BD1cXntFOltrw%3D 2612587 18451868
    • Oberst A, Bender C, Green DR (2008) Living with death: the evolution of the mitochondrial pathway of apoptosis in animals. Cell Death Differ 15:1139-1146
    • (2008) Cell Death Differ , vol.15 , pp. 1139-1146
    • Oberst, A.1    Bender, C.2    Green, D.R.3
  • 9
    • 0031731989 scopus 로고    scopus 로고
    • Genetics of programmed cell death in C. Elegans: Past, present and future
    • 1:CAS:528:DyaK1cXnt1ClsLg%3D 9820030
    • Metzstein MM, Stanfield GM, Horvitz HR (1998) Genetics of programmed cell death in C. elegans: past, present and future. Trends Genet 14:410-416
    • (1998) Trends Genet , vol.14 , pp. 410-416
    • Metzstein, M.M.1    Stanfield, G.M.2    Horvitz, H.R.3
  • 12
    • 0033578303 scopus 로고    scopus 로고
    • Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1
    • 1:CAS:528:DyaK1MXlsVymtr8%3D 22270 10449754
    • Moriishi K, Huang DC, Cory S, Adams JM (1999) Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1. Proc Natl Acad Sci U S A 96:9683-9688
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9683-9688
    • Moriishi, K.1    Huang, D.C.2    Cory, S.3    Adams, J.M.4
  • 13
    • 84902826904 scopus 로고    scopus 로고
    • Antiapoptotic potency of Bcl-2 proteins primarily relies on their stability, not binding selectivity
    • 1:CAS:528:DC%2BC2cXotV2ks7w%3D 24622325
    • Rooswinkel RW, van de Kooij B, de Vries E, Paauwe M, Braster R, Verheij M, Borst J (2014) Antiapoptotic potency of Bcl-2 proteins primarily relies on their stability, not binding selectivity. Blood 123:2806-2815
    • (2014) Blood , vol.123 , pp. 2806-2815
    • Rooswinkel, R.W.1    Van De Kooij, B.2    De Vries, E.3    Paauwe, M.4    Braster, R.5    Verheij, M.6    Borst, J.7
  • 14
    • 77952449083 scopus 로고    scopus 로고
    • Phylostratigraphic tracking of cancer genes suggests a link to the emergence of multicellularity in metazoa
    • 2880965 20492640
    • Domazet-Loso T, Tautz D (2010) Phylostratigraphic tracking of cancer genes suggests a link to the emergence of multicellularity in metazoa. BMC Biol 8:66
    • (2010) BMC Biol , vol.8 , pp. 66
    • Domazet-Loso, T.1    Tautz, D.2
  • 16
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • 1:CAS:528:DC%2BD3cXks1CktA%3D%3D 10647931
    • Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100:57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 17
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • 1:CAS:528:DC%2BC3MXjsFeqtrk%3D 21376230
    • Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144:646-674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 18
    • 84890909335 scopus 로고    scopus 로고
    • Control of apoptosis by the BCL-2 protein family: Implications for physiology and therapy
    • 1:CAS:528:DC%2BC3sXhvFOjsbvI 24355989
    • Czabotar PE, Lessene G, Strasser A, Adams JM (2014) Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nat Rev Mol Cell Biol 15:49-63
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 49-63
    • Czabotar, P.E.1    Lessene, G.2    Strasser, A.3    Adams, J.M.4
  • 19
    • 54949132875 scopus 로고    scopus 로고
    • Bcl-2 family proteins and cancer
    • 1:CAS:528:DC%2BD1cXht12ltLvO 18955968
    • Yip KW, Reed JC (2008) Bcl-2 family proteins and cancer. Oncogene 27:6398-6406
    • (2008) Oncogene , vol.27 , pp. 6398-6406
    • Yip, K.W.1    Reed, J.C.2
  • 20
    • 80051761743 scopus 로고    scopus 로고
    • The role of Bcl-2 and its pro-survival relatives in tumourigenesis and cancer therapy
    • 1:CAS:528:DC%2BC3MXhtVWnt7rJ 3149740 21415859
    • Kelly PN, Strasser A (2011) The role of Bcl-2 and its pro-survival relatives in tumourigenesis and cancer therapy. Cell Death Differ 18:1414-1424
    • (2011) Cell Death Differ , vol.18 , pp. 1414-1424
    • Kelly, P.N.1    Strasser, A.2
  • 21
    • 0021679848 scopus 로고
    • Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation
    • 1:CAS:528:DyaL2MXhvVyjug%3D%3D 6093263
    • Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM (1984) Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation. Science 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
  • 22
    • 0022379447 scopus 로고
    • The t(14;18) chromosome translocations involved in B-cell neoplasms result from mistakes in VDJ joining
    • 1:CAS:528:DyaL2MXlsFGhsrs%3D 3929382
    • Tsujimoto Y, Gorham J, Cossman J, Jaffe E, Croce CM (1985) The t(14;18) chromosome translocations involved in B-cell neoplasms result from mistakes in VDJ joining. Science 229:1390-1393
    • (1985) Science , vol.229 , pp. 1390-1393
    • Tsujimoto, Y.1    Gorham, J.2    Cossman, J.3    Jaffe, E.4    Croce, C.M.5
  • 23
    • 0022546957 scopus 로고
    • Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma
    • 1:CAS:528:DyaL28XltV2rs74%3D 323921 3523487
    • Tsujimoto Y, Croce CM (1986) Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc Natl Acad Sci U S A 83:5214-5218
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 24
    • 0023786047 scopus 로고
    • Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
    • 1:CAS:528:DyaL1MXlt1alsA%3D%3D 3262202
    • Vaux DL, Cory S, Adams JM (1988) Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature 335:440-442
    • (1988) Nature , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 26
    • 28544443984 scopus 로고    scopus 로고
    • Promoting apoptosis as a strategy for cancer drug discovery
    • 1:CAS:528:DC%2BD2MXht1Witb7J 16239906
    • Fesik SW (2005) Promoting apoptosis as a strategy for cancer drug discovery. Nat Rev Cancer 5:876-885
    • (2005) Nat Rev Cancer , vol.5 , pp. 876-885
    • Fesik, S.W.1
  • 29
    • 0030822420 scopus 로고    scopus 로고
    • Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family
    • 1:CAS:528:DyaK2sXnt12lsbc%3D 9346936
    • Aritomi M, Kunishima N, Inohara N, Ishibashi Y, Ohta S, Morikawa K (1997) Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family. J Biol Chem 272:27886-27892
    • (1997) J Biol Chem , vol.272 , pp. 27886-27892
    • Aritomi, M.1    Kunishima, N.2    Inohara, N.3    Ishibashi, Y.4    Ohta, S.5    Morikawa, K.6
  • 30
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • 1:CAS:528:DC%2BD2MXhtVKlsLbK 16208361
    • Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y (2005) Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437:831-837
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1    Chai, J.2    Lee, E.S.3    Gu, L.4    Liu, Q.5    He, J.6    Wu, J.W.7    Kokel, D.8    Li, H.9    Hao, Q.10    Xue, D.11    Shi, Y.12
  • 32
    • 0041885229 scopus 로고    scopus 로고
    • Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2
    • 1:CAS:528:DC%2BD3sXnt1amsrs%3D 14499614
    • Huang Q, Petros AM, Virgin HW, Fesik SW, Olejniczak ET (2003) Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2. J Mol Biol 332:1123-1130
    • (2003) J Mol Biol , vol.332 , pp. 1123-1130
    • Huang, Q.1    Petros, A.M.2    Virgin, H.W.3    Fesik, S.W.4    Olejniczak, E.T.5
  • 34
    • 2942616796 scopus 로고    scopus 로고
    • Comparative genomics: The evolutionary history of the Bcl-2 family
    • 1:CAS:528:DC%2BD2cXksFOmtrw%3D 15177682
    • Lanave C, Santamaria M, Saccone C (2004) Comparative genomics: the evolutionary history of the Bcl-2 family. Gene 333:71-79
    • (2004) Gene , vol.333 , pp. 71-79
    • Lanave, C.1    Santamaria, M.2    Saccone, C.3
  • 35
    • 67649592467 scopus 로고    scopus 로고
    • BCL2DB: Moving 'helix-bundled' BCL-2 family members to their database
    • 19543976
    • Blaineau SV, Aouacheria A (2009) BCL2DB: moving 'helix-bundled' BCL-2 family members to their database. Apoptosis 14:923-925
    • (2009) Apoptosis , vol.14 , pp. 923-925
    • Blaineau, S.V.1    Aouacheria, A.2
  • 36
    • 84874250575 scopus 로고    scopus 로고
    • Evolution of Bcl-2 homology motifs: Homology versus homoplasy
    • 1:CAS:528:DC%2BC3sXitVGgu78%3D 3582728 23199982
    • Aouacheria A, Rech de Laval V, Combet C, Hardwick JM (2013) Evolution of Bcl-2 homology motifs: homology versus homoplasy. Trends Cell Biol 23:103-111
    • (2013) Trends Cell Biol , vol.23 , pp. 103-111
    • Aouacheria, A.1    Rech De Laval, V.2    Combet, C.3    Hardwick, J.M.4
  • 37
    • 84891756251 scopus 로고    scopus 로고
    • The BCL-2 database, Act 2: Moving beyond dualism to diversity and pleiotropy
    • 1:CAS:528:DC%2BC2cXis1Gguw%3D%3D 4040653 24384724
    • Aouacheria A (2014) The BCL-2 database, Act 2: moving beyond dualism to diversity and pleiotropy. Cell Death Dis 5:e981
    • (2014) Cell Death Dis , vol.5 , pp. 981
    • Aouacheria, A.1
  • 38
    • 52149113769 scopus 로고    scopus 로고
    • Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands
    • 1:CAS:528:DC%2BD1cXhtFWht7jM 18551131
    • Kvansakul M, Yang H, Fairlie WD, Czabotar PE, Fischer SF, Perugini MA, Huang DC, Colman PM (2008) Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands. Cell Death Differ 15:1564-1571
    • (2008) Cell Death Differ , vol.15 , pp. 1564-1571
    • Kvansakul, M.1    Yang, H.2    Fairlie, W.D.3    Czabotar, P.E.4    Fischer, S.F.5    Perugini, M.A.6    Huang, D.C.7    Colman, P.M.8
  • 39
    • 0036849273 scopus 로고    scopus 로고
    • Pro-apoptotic BH3-only Bcl-2 family members in vertebrate model organisms suitable for genetic experimentation
    • 1:CAS:528:DC%2BD38XotFOrsbg%3D 12404114
    • Coultas L, Huang DC, Adams JM, Strasser A (2002) Pro-apoptotic BH3-only Bcl-2 family members in vertebrate model organisms suitable for genetic experimentation. Cell Death Differ 9:1163-1166
    • (2002) Cell Death Differ , vol.9 , pp. 1163-1166
    • Coultas, L.1    Huang, D.C.2    Adams, J.M.3    Strasser, A.4
  • 40
    • 84861777075 scopus 로고    scopus 로고
    • Multipolar functions of BCL-2 proteins link energetics to apoptosis
    • 1:CAS:528:DC%2BC38XosVGltbg%3D 3499971 22560661
    • Hardwick JM, Chen YB, Jonas EA (2012) Multipolar functions of BCL-2 proteins link energetics to apoptosis. Trends Cell Biol 22:318-328
    • (2012) Trends Cell Biol , vol.22 , pp. 318-328
    • Hardwick, J.M.1    Chen, Y.B.2    Jonas, E.A.3
  • 41
    • 14244265108 scopus 로고    scopus 로고
    • Solution structure of prosurvival Mcl-1 and characterization of its binding by proapoptotic BH3-only ligands
    • 1:CAS:528:DC%2BD2MXhtVymtrk%3D 15550399
    • Day CL, Chen L, Richardson SJ, Harrison PJ, Huang DC, Hinds MG (2005) Solution structure of prosurvival Mcl-1 and characterization of its binding by proapoptotic BH3-only ligands. J Biol Chem 280:4738-4744
    • (2005) J Biol Chem , vol.280 , pp. 4738-4744
    • Day, C.L.1    Chen, L.2    Richardson, S.J.3    Harrison, P.J.4    Huang, D.C.5    Hinds, M.G.6
  • 42
    • 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
    • 1:CAS:528:DyaK28XhvFyks74%3D 8631771
    • Zha H, Aime-Sempe C, Sato T, Reed JC (1996) Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem 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
  • 43
    • 0033635733 scopus 로고    scopus 로고
    • BH3-Only proteins-essential initiators of apoptotic cell death
    • 1:CAS:528:DC%2BD3cXovFCjt7o%3D 11136969
    • Huang DC, Strasser A (2000) BH3-Only proteins-essential initiators of apoptotic cell death. Cell 103:839-842
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.1    Strasser, A.2
  • 44
    • 45849104776 scopus 로고    scopus 로고
    • Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1
    • 1:CAS:528:DC%2BD1cXotlCmsLY%3D 18589438
    • Day CL, Smits C, Fan FC, Lee EF, Fairlie WD, Hinds MG (2008) Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. J Mol Biol 380:958-971
    • (2008) J Mol Biol , vol.380 , pp. 958-971
    • Day, C.L.1    Smits, C.2    Fan, F.C.3    Lee, E.F.4    Fairlie, W.D.5    Hinds, M.G.6
  • 45
  • 47
    • 84055212651 scopus 로고    scopus 로고
    • Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: The next step forward or two steps back?
    • 1:CAS:528:DC%2BC3MXhs1Cgt7jP 21898539
    • Beverly LJ (2012) Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: the next step forward or two steps back? J Cell Biochem 113:3-12
    • (2012) J Cell Biochem , vol.113 , pp. 3-12
    • Beverly, L.J.1
  • 48
    • 84903397360 scopus 로고    scopus 로고
    • Genome-wide prediction and validation of peptides that bind human prosurvival bcl-2 proteins
    • 4072508 24967846
    • DeBartolo J, Taipale M, Keating AE (2014) Genome-wide prediction and validation of peptides that bind human prosurvival bcl-2 proteins. PLoS Comput Biol 10:e1003693
    • (2014) PLoS Comput Biol , vol.10 , pp. 1003693
    • Debartolo, J.1    Taipale, M.2    Keating, A.E.3
  • 50
    • 0033947233 scopus 로고    scopus 로고
    • Molecular evolution of apoptotic pathways: Cloning of key domains from sponges (Bcl-2 homology domains and death domains) and their phylogenetic relationships
    • 1:CAS:528:DC%2BD3cXksFWnu74%3D 10835482
    • Wiens M, Krasko A, Muller CI, Muller WE (2000) Molecular evolution of apoptotic pathways: cloning of key domains from sponges (Bcl-2 homology domains and death domains) and their phylogenetic relationships. J Mol Evol 50:520-531
    • (2000) J Mol Evol , vol.50 , pp. 520-531
    • Wiens, M.1    Krasko, A.2    Muller, C.I.3    Muller, W.E.4
  • 51
    • 84871235883 scopus 로고    scopus 로고
    • The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist
    • 1:STN:280:DC%2BC3s3hsFeitg%3D%3D 3542614 23235460
    • Rautureau GJ, Yabal M, Yang H, Huang DC, Kvansakul M, Hinds MG (2012) The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist. Cell Death Dis 3:e443
    • (2012) Cell Death Dis , vol.3 , pp. 443
    • Rautureau, G.J.1    Yabal, M.2    Yang, H.3    Huang, D.C.4    Kvansakul, M.5    Hinds, M.G.6
  • 52
    • 77953569619 scopus 로고    scopus 로고
    • The structure of Boo/Diva reveals a divergent Bcl-2 protein
    • 1:CAS:528:DC%2BC3cXlslegt7w%3D 20455273
    • Rautureau GJ, Day CL, Hinds MG (2010) The structure of Boo/Diva reveals a divergent Bcl-2 protein. Proteins 78:2181-2186
    • (2010) Proteins , vol.78 , pp. 2181-2186
    • Rautureau, G.J.1    Day, C.L.2    Hinds, M.G.3
  • 53
    • 42049103183 scopus 로고    scopus 로고
    • Regulation of Bcl-2 family proteins by posttranslational modifications
    • 1:CAS:528:DC%2BD1cXktlWgsLg%3D 18336291
    • Kutuk O, Letai A (2008) Regulation of Bcl-2 family proteins by posttranslational modifications. Curr Mol Med 8:102-118
    • (2008) Curr Mol Med , vol.8 , pp. 102-118
    • Kutuk, O.1    Letai, A.2
  • 54
    • 77951883210 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in bcl-2 regulated apoptosis
    • 1:CAS:528:DC%2BC3cXlt1yku7w%3D 2871139 20480043
    • Rautureau GJ, Day CL, Hinds MG (2010) Intrinsically disordered proteins in bcl-2 regulated apoptosis. Int J Mol Sci 11:1808-1824
    • (2010) Int J Mol Sci , vol.11 , pp. 1808-1824
    • Rautureau, G.J.1    Day, C.L.2    Hinds, M.G.3
  • 55
    • 0026773471 scopus 로고
    • The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor alpha
    • 1:CAS:528:DyaK38XksVKgsb0%3D 364450 1317006
    • White E, Sabbatini P, Debbas M, Wold WS, Kusher DI, Gooding LR (1992) The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by tumor necrosis factor alpha. Mol Cell Biol 12:2570-2580
    • (1992) Mol Cell Biol , vol.12 , pp. 2570-2580
    • White, E.1    Sabbatini, P.2    Debbas, M.3    Wold, W.S.4    Kusher, D.I.5    Gooding, L.R.6
  • 56
    • 33845920705 scopus 로고    scopus 로고
    • Vaccinia virus N1L protein resembles a B cell lymphoma-2 (Bcl-2) family protein
    • 1:CAS:528:DC%2BD2sXmsF2gtQ%3D%3D 2222835 17123957
    • Aoyagi M, Zhai D, Jin C, Aleshin AE, Stec B, Reed JC, Liddington RC (2007) Vaccinia virus N1L protein resembles a B cell lymphoma-2 (Bcl-2) family protein. Protein Sci 16:118-124
    • (2007) Protein Sci , vol.16 , pp. 118-124
    • Aoyagi, M.1    Zhai, D.2    Jin, C.3    Aleshin, A.E.4    Stec, B.5    Reed, J.C.6    Liddington, R.C.7
  • 57
    • 34249787896 scopus 로고    scopus 로고
    • Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein
    • 1:CAS:528:DC%2BD2sXmsFSgtr0%3D 2885619 17485524
    • Cooray S, Bahar MW, Abrescia NG, McVey CE, Bartlett NW, Chen RA, Stuart DI, Grimes JM, Smith GL (2007) Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein. J Gen Virol 88:1656-1666
    • (2007) J Gen Virol , vol.88 , pp. 1656-1666
    • Cooray, S.1    Bahar, M.W.2    Abrescia, N.G.3    McVey, C.E.4    Bartlett, N.W.5    Chen, R.A.6    Stuart, D.I.7    Grimes, J.M.8    Smith, G.L.9
  • 58
    • 33947304650 scopus 로고    scopus 로고
    • A structural viral mimic of prosurvival Bcl-2: A pivotal role for sequestering proapoptotic Bax and Bak
    • 1:CAS:528:DC%2BD2sXktFCgtr8%3D 17386268
    • Kvansakul M, van Delft MF, Lee EF, Gulbis JM, Fairlie WD, Huang DC, Colman PM (2007) A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak. Mol Cell 25:933-942
    • (2007) Mol Cell , vol.25 , pp. 933-942
    • Kvansakul, M.1    Van Delft, M.F.2    Lee, E.F.3    Gulbis, J.M.4    Fairlie, W.D.5    Huang, D.C.6    Colman, P.M.7
  • 59
    • 33947727119 scopus 로고    scopus 로고
    • Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2
    • 1:CAS:528:DC%2BD2sXktVOmt7w%3D 2203349 17384234
    • Douglas AE, Corbett KD, Berger JM, McFadden G, Handel TM (2007) Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2. Protein Sci 16:695-703
    • (2007) Protein Sci , vol.16 , pp. 695-703
    • Douglas, A.E.1    Corbett, K.D.2    Berger, J.M.3    McFadden, G.4    Handel, T.M.5
  • 61
    • 0027260656 scopus 로고
    • Epstein-Barr virus-coded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death
    • 1:CAS:528:DyaK2cXivVClsQ%3D%3D 47380 8397406
    • Henderson S, Huen D, Rowe M, Dawson C, Johnson G, Rickinson A (1993) Epstein-Barr virus-coded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death. Proc Natl Acad Sci U S A 90:8479-8483
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8479-8483
    • Henderson, S.1    Huen, D.2    Rowe, M.3    Dawson, C.4    Johnson, G.5    Rickinson, A.6
  • 62
    • 0031017578 scopus 로고    scopus 로고
    • A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak
    • 1:CAS:528:DyaK2sXnvVeqsg%3D%3D 19575 9012846
    • Cheng EH, Nicholas J, Bellows DS, Hayward GS, Guo HG, Reitz MS, Hardwick JM (1997) A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak. Proc Natl Acad Sci U S A 94:690-694
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 690-694
    • Cheng, E.H.1    Nicholas, J.2    Bellows, D.S.3    Hayward, G.S.4    Guo, H.G.5    Reitz, M.S.6    Hardwick, J.M.7
  • 63
    • 0031575535 scopus 로고    scopus 로고
    • Inhibition of apoptosis by the African swine fever virus Bcl-2 homologue: Role of the BH1 domain
    • 1:CAS:528:DyaK2sXhsFehsb0%3D 9123849
    • Revilla Y, Cebrian A, Baixeras E, Martinez C, Vinuela E, Salas ML (1997) Inhibition of apoptosis by the African swine fever virus Bcl-2 homologue: role of the BH1 domain. Virology 228:400-404
    • (1997) Virology , vol.228 , pp. 400-404
    • Revilla, Y.1    Cebrian, A.2    Baixeras, E.3    Martinez, C.4    Vinuela, E.5    Salas, M.L.6
  • 64
    • 84873574038 scopus 로고    scopus 로고
    • A survey of host range genes in poxvirus genomes
    • 1:CAS:528:DC%2BC3sXjt1Sjurg%3D 4080715 23268114
    • Bratke KA, McLysaght A, Rothenburg S (2013) A survey of host range genes in poxvirus genomes. Infect Genet Evol 14:406-425
    • (2013) Infect Genet Evol , vol.14 , pp. 406-425
    • Bratke, K.A.1    McLysaght, A.2    Rothenburg, S.3
  • 68
    • 0030893693 scopus 로고    scopus 로고
    • Herpesvirus saimiri encodes a functional homolog of the human bcl-2 oncogene
    • 1:CAS:528:DyaK2sXisFWnsLg%3D 191568 9094693
    • Nava VE, Cheng EH, Veliuona M, Zou S, Clem RJ, Mayer ML, Hardwick JM (1997) Herpesvirus saimiri encodes a functional homolog of the human bcl-2 oncogene. J Virol 71:4118-4122
    • (1997) J Virol , vol.71 , pp. 4118-4122
    • Nava, V.E.1    Cheng, E.H.2    Veliuona, M.3    Zou, S.4    Clem, R.J.5    Mayer, M.L.6    Hardwick, J.M.7
  • 69
    • 0028965636 scopus 로고
    • A Bcl-2-related gene is activated in avian cells transformed by the Rous sarcoma virus
    • 1:CAS:528:DyaK2MXlsFShsr8%3D 398222 7729415
    • Gillet G, Guerin M, Trembleau A, Brun G (1995) A Bcl-2-related gene is activated in avian cells transformed by the Rous sarcoma virus. EMBO J 14:1372-1381
    • (1995) EMBO J , vol.14 , pp. 1372-1381
    • Gillet, G.1    Guerin, M.2    Trembleau, A.3    Brun, G.4
  • 70
    • 84887528665 scopus 로고    scopus 로고
    • Poxviruses and the evolution of host range and virulence
    • 1:CAS:528:DC%2BC2cXisFeks7w%3D 24161410
    • Haller SL, Peng C, McFadden G, Rothenburg S (2014) Poxviruses and the evolution of host range and virulence. Infect Genet Evol 21:15-40
    • (2014) Infect Genet Evol , vol.21 , pp. 15-40
    • Haller, S.L.1    Peng, C.2    McFadden, G.3    Rothenburg, S.4
  • 71
    • 34250897851 scopus 로고    scopus 로고
    • A novel Bcl-2-like inhibitor of apoptosis is encoded by the parapoxvirus ORF virus
    • 1:CAS:528:DC%2BD2sXntVOitrY%3D 1933275 17475653
    • Westphal D, Ledgerwood EC, Hibma MH, Fleming SB, Whelan EM, Mercer AA (2007) A novel Bcl-2-like inhibitor of apoptosis is encoded by the parapoxvirus ORF virus. J Virol 81:7178-7188
    • (2007) J Virol , vol.81 , pp. 7178-7188
    • Westphal, D.1    Ledgerwood, E.C.2    Hibma, M.H.3    Fleming, S.B.4    Whelan, E.M.5    Mercer, A.A.6
  • 72
    • 79551716137 scopus 로고    scopus 로고
    • Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and Bax
    • 1:CAS:528:DC%2BC3MXhtVWlt7nN 3067780 21159883
    • Banadyga L, Lam SC, Okamoto T, Kvansakul M, Huang DC, Barry M (2011) Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and Bax. J Virol 85:1922-1934
    • (2011) J Virol , vol.85 , pp. 1922-1934
    • Banadyga, L.1    Lam, S.C.2    Okamoto, T.3    Kvansakul, M.4    Huang, D.C.5    Barry, M.6
  • 73
    • 84869071184 scopus 로고    scopus 로고
    • Sheeppox virus SPPV14 encodes a Bcl-2-like cell death inhibitor that counters a distinct set of mammalian proapoptotic proteins
    • 1:CAS:528:DC%2BC38XhsFCmur7K 3486325 22896610
    • Okamoto T, Campbell S, Mehta N, Thibault J, Colman PM, Barry M, Huang DC, Kvansakul M (2012) Sheeppox virus SPPV14 encodes a Bcl-2-like cell death inhibitor that counters a distinct set of mammalian proapoptotic proteins. J Virol 86:11501-11511
    • (2012) J Virol , vol.86 , pp. 11501-11511
    • Okamoto, T.1    Campbell, S.2    Mehta, N.3    Thibault, J.4    Colman, P.M.5    Barry, M.6    Huang, D.C.7    Kvansakul, M.8
  • 75
    • 43249095547 scopus 로고    scopus 로고
    • Murine cytomegalovirus m38.5 protein inhibits Bax-mediated cell death
    • 1:CAS:528:DC%2BD1cXlvVKis7c%3D 2346748 18321965
    • Jurak I, Schumacher U, Simic H, Voigt S, Brune W (2008) Murine cytomegalovirus m38.5 protein inhibits Bax-mediated cell death. J Virol 82:4812-4822
    • (2008) J Virol , vol.82 , pp. 4812-4822
    • Jurak, I.1    Schumacher, U.2    Simic, H.3    Voigt, S.4    Brune, W.5
  • 77
    • 27944497377 scopus 로고    scopus 로고
    • Regulation of apoptosis: Uncovering the binding determinants
    • 1:CAS:528:DC%2BD2MXht1GnsrzP 16263267
    • Hinds MG, Day CL (2005) Regulation of apoptosis: uncovering the binding determinants. Curr Opin Struct Biol 15:690-699
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 690-699
    • Hinds, M.G.1    Day, C.L.2
  • 78
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • 1:CAS:528:DC%2BD3cXot1Gnu7c%3D 11106734
    • Suzuki M, Youle RJ, Tjandra N (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103:645-654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 79
    • 0344608883 scopus 로고    scopus 로고
    • The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
    • 1:CAS:528:DC%2BD3sXisFeqsbo%3D 152889 12660157
    • Hinds MG, Lackmann M, Skea GL, Harrison PJ, Huang DC, Day CL (2003) The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. EMBO J 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
  • 80
    • 0027480450 scopus 로고
    • MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2
    • 1:CAS:528:DyaK3sXks1CmtL8%3D 46331 7682708
    • Kozopas KM, Yang T, Buchan HL, Zhou P, Craig RW (1993) MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2. Proc Natl Acad Sci U S A 90:3516-3520
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3516-3520
    • Kozopas, K.M.1    Yang, T.2    Buchan, H.L.3    Zhou, P.4    Craig, R.W.5
  • 81
    • 81855168361 scopus 로고    scopus 로고
    • Characterization of unique signature sequences in the divergent maternal protein Bcl2l10
    • 1:CAS:528:DC%2BC3MXhsFSktrbN 21705382
    • Guillemin Y, Cornut-Thibaut A, Gillet G, Penin F, Aouacheria A (2011) Characterization of unique signature sequences in the divergent maternal protein Bcl2l10. Mol Biol Evol 28:3271-3283
    • (2011) Mol Biol Evol , vol.28 , pp. 3271-3283
    • Guillemin, Y.1    Cornut-Thibaut, A.2    Gillet, G.3    Penin, F.4    Aouacheria, A.5
  • 83
    • 84903460450 scopus 로고    scopus 로고
    • The Structural Biology of BH3-Only Proteins
    • 1:CAS:528:DC%2BC2cXhs1GntrvL 24974286
    • Kvansakul M, Hinds MG (2014) The Structural Biology of BH3-Only Proteins. Methods Enzymol 544:49-74
    • (2014) Methods Enzymol , vol.544 , pp. 49-74
    • Kvansakul, M.1    Hinds, M.G.2
  • 84
    • 33751544565 scopus 로고    scopus 로고
    • The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site
    • 1:CAS:528:DC%2BD28XhtlCns7zM 17157251
    • Moldoveanu T, Liu Q, Tocilj A, Watson M, Shore G, Gehring K (2006) The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell 24:677-688
    • (2006) Mol Cell , vol.24 , pp. 677-688
    • Moldoveanu, T.1    Liu, Q.2    Tocilj, A.3    Watson, M.4    Shore, G.5    Gehring, K.6
  • 85
    • 79954419930 scopus 로고    scopus 로고
    • Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX
    • 1:CAS:528:DC%2BC3MXksVCgsbk%3D 3343310 21060336
    • Ku B, Liang C, Jung JU, Oh BH (2011) Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX. Cell Res 21:627-641
    • (2011) Cell Res , vol.21 , pp. 627-641
    • Ku, B.1    Liang, C.2    Jung, J.U.3    Oh, B.H.4
  • 86
    • 0036220239 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes
    • 11751312
    • Martinez-Senac Mdel M, Corbalan-Garcia S, Gomez-Fernandez JC (2002) The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes. Biophys J 82:233-243
    • (2002) Biophys J , vol.82 , pp. 233-243
    • Martinez-Senac Mdel, M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 89
    • 84869434589 scopus 로고    scopus 로고
    • Molecular basis for membrane pore formation by Bax protein carboxyl terminus
    • 1:CAS:528:DC%2BC38XhsFymsb7M 23110300
    • Tatulian SA, Garg P, Nemec KN, Chen B, Khaled AR (2012) Molecular basis for membrane pore formation by Bax protein carboxyl terminus. Biochemistry 51:9406-9419
    • (2012) Biochemistry , vol.51 , pp. 9406-9419
    • Tatulian, S.A.1    Garg, P.2    Nemec, K.N.3    Chen, B.4    Khaled, A.R.5
  • 90
    • 84870314860 scopus 로고    scopus 로고
    • Transmembrane pore formation by the carboxyl terminus of Bax protein
    • 1:CAS:528:DC%2BC3sXhtFSmug%3D%3D 22906710
    • Garg P, Nemec KN, Khaled AR, Tatulian SA (2013) Transmembrane pore formation by the carboxyl terminus of Bax protein. Biochim Biophys Acta 1828:732-742
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 732-742
    • Garg, P.1    Nemec, K.N.2    Khaled, A.R.3    Tatulian, S.A.4
  • 93
    • 84872298568 scopus 로고    scopus 로고
    • The C-terminal helix of Bcl-x(L) mediates Bax retrotranslocation from the mitochondria
    • 1:CAS:528:DC%2BC3sXosVynsQ%3D%3D 3554327 23079612
    • Todt F, Cakir Z, Reichenbach F, Youle RJ, Edlich F (2013) The C-terminal helix of Bcl-x(L) mediates Bax retrotranslocation from the mitochondria. Cell Death Differ 20:333-342
    • (2013) Cell Death Differ , vol.20 , pp. 333-342
    • Todt, F.1    Cakir, Z.2    Reichenbach, F.3    Youle, R.J.4    Edlich, F.5
  • 95
    • 65249149086 scopus 로고    scopus 로고
    • The Epstein-Barr virus Bcl-2 homolog, BHRF1, blocks apoptosis by binding to a limited amount of Bim
    • 1:CAS:528:DC%2BD1MXkvFGhuro%3D 2657086 19293378
    • Desbien AL, Kappler JW, Marrack P (2009) The Epstein-Barr virus Bcl-2 homolog, BHRF1, blocks apoptosis by binding to a limited amount of Bim. Proc Natl Acad Sci U S A 106:5663-5668
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5663-5668
    • Desbien, A.L.1    Kappler, J.W.2    Marrack, P.3
  • 96
    • 84903878807 scopus 로고    scopus 로고
    • Structural Insight into BH3 Domain Binding of Vaccinia Virus Antiapoptotic F1L
    • 1:CAS:528:DC%2BC2cXhsFegsr7I 24850748
    • Campbell S, Thibault J, Mehta N, Colman PM, Barry M, Kvansakul M (2014) Structural Insight into BH3 Domain Binding of Vaccinia Virus Antiapoptotic F1L. J Virol 88:8667-8677
    • (2014) J Virol , vol.88 , pp. 8667-8677
    • Campbell, S.1    Thibault, J.2    Mehta, N.3    Colman, P.M.4    Barry, M.5    Kvansakul, M.6
  • 97
    • 34249037565 scopus 로고    scopus 로고
    • Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein
    • 1:CAS:528:DC%2BD2sXksVShsLk%3D 17337444
    • Oberstein A, Jeffrey PD, Shi Y (2007) Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J Biol Chem 282:13123-13132
    • (2007) J Biol Chem , vol.282 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 98
    • 40449127353 scopus 로고    scopus 로고
    • Structural and biochemical bases for the inhibition of autophagy and apoptosis by viral BCL-2 of murine gamma-herpesvirus 68
    • Ku B, Woo JS, Liang C, Lee KH, Hong HS, E X, Kim KS, Jung JU, Oh BH (2008) Structural and biochemical bases for the inhibition of autophagy and apoptosis by viral BCL-2 of murine gamma-herpesvirus 68. PLoS Pathog 4:e25
    • (2008) PLoS Pathog , vol.4 , pp. e25
    • Ku, B.1    Woo, J.S.2    Liang, C.3    Lee, K.H.4    Hong, H.S.X.E.5    Kim, K.S.6    Jung, J.U.7    Oh, B.H.8
  • 100
    • 84855272569 scopus 로고    scopus 로고
    • The E1B19K oncoprotein complexes with Beclin 1 to regulate autophagy in adenovirus-infected cells
    • 1:CAS:528:DC%2BC38Xms1Ojtw%3D%3D 3248451 22242123
    • Piya S, White EJ, Klein SR, Jiang H, McDonnell TJ, Gomez-Manzano C, Fueyo J (2011) The E1B19K oncoprotein complexes with Beclin 1 to regulate autophagy in adenovirus-infected cells. PLoS ONE 6:e29467
    • (2011) PLoS ONE , vol.6 , pp. 29467
    • Piya, S.1    White, E.J.2    Klein, S.R.3    Jiang, H.4    McDonnell, T.J.5    Gomez-Manzano, C.6    Fueyo, J.7
  • 102
    • 33845486323 scopus 로고    scopus 로고
    • Bim, Bad and Bmf: Intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets
    • 1:CAS:528:DC%2BD28XhtlSqur7O 16645638
    • Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL (2007) Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death Differ 14:128-136
    • (2007) Cell Death Differ , vol.14 , pp. 128-136
    • Hinds, M.G.1    Smits, C.2    Fredericks-Short, R.3    Risk, J.M.4    Bailey, M.5    Huang, D.C.6    Day, C.L.7
  • 103
    • 84882279043 scopus 로고    scopus 로고
    • Resilience of death: Intrinsic disorder in proteins involved in the programmed cell death
    • 1:CAS:528:DC%2BC3sXht1OisLvK 3741502 23764774
    • Peng Z, Xue B, Kurgan L, Uversky VN (2013) Resilience of death: intrinsic disorder in proteins involved in the programmed cell death. Cell Death Differ 20:1257-1267
    • (2013) Cell Death Differ , vol.20 , pp. 1257-1267
    • Peng, Z.1    Xue, B.2    Kurgan, L.3    Uversky, V.N.4
  • 105
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • 1:CAS:528:DC%2BD1cXhsVagt7vI 2803065 19039133
    • Gsponer J, Futschik ME, Teichmann SA, Babu MM (2008) Tight regulation of unstructured proteins: from transcript synthesis to protein degradation. Science 322:1365-1368
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 107
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • 1:CAS:528:DyaK1MXit1Oms7k%3D 10198631
    • Puthalakath H, Huang DC, O'Reilly LA, King SM, Strasser A (1999) The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol Cell 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
  • 108
    • 84864311086 scopus 로고    scopus 로고
    • Linear motifs: Lost in (pre)translation
    • 1:CAS:528:DC%2BC38XoslKis7c%3D 22705166
    • Weatheritt RJ, Gibson TJ (2012) Linear motifs: lost in (pre)translation. Trends Biochem Sci 37:333-341
    • (2012) Trends Biochem Sci , vol.37 , pp. 333-341
    • Weatheritt, R.J.1    Gibson, T.J.2
  • 109
    • 84897970680 scopus 로고    scopus 로고
    • Coupled folding and binding of the disordered protein PUMA does not require particular residual structure
    • 1:CAS:528:DC%2BC2cXkslaksrw%3D 4017604 24654952
    • Rogers JM, Wong CT, Clarke J (2014) Coupled folding and binding of the disordered protein PUMA does not require particular residual structure. J Am Chem Soc 136:5197-5200
    • (2014) J Am Chem Soc , vol.136 , pp. 5197-5200
    • Rogers, J.M.1    Wong, C.T.2    Clarke, J.3
  • 110
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists
    • 1:CAS:528:DyaK1MXitVChsrs%3D 10089878
    • McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D (1999) Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. Cell 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
  • 111
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signaling
    • 1:CAS:528:DyaK1MXitVChsro%3D 10089877
    • Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G (1999) Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell 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
  • 112
    • 70149111283 scopus 로고    scopus 로고
    • Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL
    • 1:CAS:528:DC%2BD1MXhtVWku7rP 2762941 19670908
    • Yao Y, Bobkov AA, Plesniak LA, Marassi FM (2009) Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL. Biochemistry 48:8704-8711
    • (2009) Biochemistry , vol.48 , pp. 8704-8711
    • Yao, Y.1    Bobkov, A.A.2    Plesniak, L.A.3    Marassi, F.M.4
  • 113
    • 84890375541 scopus 로고    scopus 로고
    • Structural insights of tBid, the caspase-8-activated Bid, and its BH3 domain
    • 1:CAS:528:DC%2BC3sXhvFarur%2FK 3861634 24158446
    • Wang Y, Tjandra N (2013) Structural insights of tBid, the caspase-8-activated Bid, and its BH3 domain. J Biol Chem 288:35840-35851
    • (2013) J Biol Chem , vol.288 , pp. 35840-35851
    • Wang, Y.1    Tjandra, N.2
  • 114
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • 1:CAS:528:DC%2BD2MXit12rt7c%3D 15721256
    • Kuwana T, Bouchier-Hayes L, Chipuk JE, Bonzon C, Sullivan BA, Green DR, Newmeyer DD (2005) BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol Cell 17:525-535
    • (2005) Mol Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 115
    • 33646354381 scopus 로고    scopus 로고
    • Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members
    • 1:CAS:528:DC%2BD28XltF2nsLo%3D 16697956
    • Certo M, Del Gaizo Moore V, Nishino M, Wei G, Korsmeyer S, Armstrong SA, Letai A (2006) Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. Cancer Cell 9:351-365
    • (2006) Cancer Cell , vol.9 , pp. 351-365
    • Certo, M.1    Del Gaizo, M.V.2    Nishino, M.3    Wei, G.4    Korsmeyer, S.5    Armstrong, S.A.6    Letai, A.7
  • 118
    • 84863726664 scopus 로고    scopus 로고
    • BH3-only proteins are tail-anchored in the outer mitochondrial membrane and can initiate the activation of Bax
    • 1:CAS:528:DC%2BC38XhtVSqt77O 3392640 22343714
    • Wilfling F, Weber A, Potthoff S, Vogtle FN, Meisinger C, Paschen SA, Hacker G (2012) BH3-only proteins are tail-anchored in the outer mitochondrial membrane and can initiate the activation of Bax. Cell Death Differ 19:1328-1336
    • (2012) Cell Death Differ , vol.19 , pp. 1328-1336
    • Wilfling, F.1    Weber, A.2    Potthoff, S.3    Vogtle, F.N.4    Meisinger, C.5    Paschen, S.A.6    Hacker, G.7
  • 120
    • 84883690023 scopus 로고    scopus 로고
    • Assembly of the Bak apoptotic pore: A critical role for the Bak protein alpha6 helix in the multimerization of homodimers during apoptosis
    • 1:CAS:528:DC%2BC3sXhsVWrurbK 3764807 23893415
    • Ma S, Hockings C, Anwari K, Kratina T, Fennell S, Lazarou M, Ryan MT, Kluck RM, Dewson G (2013) Assembly of the Bak apoptotic pore: a critical role for the Bak protein alpha6 helix in the multimerization of homodimers during apoptosis. J Biol Chem 288:26027-26038
    • (2013) J Biol Chem , vol.288 , pp. 26027-26038
    • Ma, S.1    Hockings, C.2    Anwari, K.3    Kratina, T.4    Fennell, S.5    Lazarou, M.6    Ryan, M.T.7    Kluck, R.M.8    Dewson, G.9
  • 121
    • 84891698320 scopus 로고    scopus 로고
    • Evaluation of the BH3-only protein Puma as a direct Bak activator
    • 1:CAS:528:DC%2BC2cXit1CqtA%3D%3D 3879582 24265320
    • Dai H, Pang YP, Ramirez-Alvarado M, Kaufmann SH (2014) Evaluation of the BH3-only protein Puma as a direct Bak activator. J Biol Chem 289:89-99
    • (2014) J Biol Chem , vol.289 , pp. 89-99
    • Dai, H.1    Pang, Y.P.2    Ramirez-Alvarado, M.3    Kaufmann, S.H.4
  • 123
    • 78650941519 scopus 로고    scopus 로고
    • BH3 domains other than Bim and Bid can directly activate Bax/Bak
    • 1:CAS:528:DC%2BC3MXmvVah 3013008 21041309
    • Du H, Wolf J, Schafer B, Moldoveanu T, Chipuk JE, Kuwana T (2011) BH3 domains other than Bim and Bid can directly activate Bax/Bak. J Biol Chem 286:491-501
    • (2011) J Biol Chem , vol.286 , pp. 491-501
    • Du, H.1    Wolf, J.2    Schafer, B.3    Moldoveanu, T.4    Chipuk, J.E.5    Kuwana, T.6
  • 124
    • 79960235245 scopus 로고    scopus 로고
    • Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization
    • 1:CAS:528:DC%2BC3MXptFKntL4%3D 3135403 21727192
    • Dai H, Smith A, Meng XW, Schneider PA, Pang YP, Kaufmann SH (2011) Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization. J Cell Biol 194:39-48
    • (2011) J Cell Biol , vol.194 , pp. 39-48
    • Dai, H.1    Smith, A.2    Meng, X.W.3    Schneider, P.A.4    Pang, Y.P.5    Kaufmann, S.H.6
  • 125
    • 84892412571 scopus 로고    scopus 로고
    • Building blocks of the apoptotic pore: How Bax and Bak are activated and oligomerize during apoptosis
    • 1:CAS:528:DC%2BC3sXhs1OltbnE 24162660
    • Westphal D, Kluck RM, Dewson G (2014) Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis. Cell Death Differ 21:196-205
    • (2014) Cell Death Differ , vol.21 , pp. 196-205
    • Westphal, D.1    Kluck, R.M.2    Dewson, G.3
  • 126
    • 0036328156 scopus 로고    scopus 로고
    • The vaccinia virus N1L protein is an intracellular homodimer that promotes virulence
    • 1:CAS:528:DC%2BD38XlvVCrs7g%3D 12124460
    • Bartlett N, Symons JA, Tscharke DC, Smith GL (2002) The vaccinia virus N1L protein is an intracellular homodimer that promotes virulence. J Gen Virol 83:1965-1976
    • (2002) J Gen Virol , vol.83 , pp. 1965-1976
    • Bartlett, N.1    Symons, J.A.2    Tscharke, D.C.3    Smith, G.L.4
  • 128
    • 79957987060 scopus 로고    scopus 로고
    • Mapping the IkappaB kinase beta (IKKbeta)-binding interface of the B14 protein, a vaccinia virus inhibitor of IKKbeta-mediated activation of nuclear factor kappaB
    • 1:CAS:528:DC%2BC3MXmvFCgtbc%3D 3121528 21474453
    • Benfield CT, Mansur DS, McCoy LE, Ferguson BJ, Bahar MW, Oldring AP, Grimes JM, Stuart DI, Graham SC, Smith GL (2011) Mapping the IkappaB kinase beta (IKKbeta)-binding interface of the B14 protein, a vaccinia virus inhibitor of IKKbeta-mediated activation of nuclear factor kappaB. J Biol Chem 286:20727-20735
    • (2011) J Biol Chem , vol.286 , pp. 20727-20735
    • Benfield, C.T.1    Mansur, D.S.2    McCoy, L.E.3    Ferguson, B.J.4    Bahar, M.W.5    Oldring, A.P.6    Grimes, J.M.7    Stuart, D.I.8    Graham, S.C.9    Smith, G.L.10
  • 129
    • 58149107158 scopus 로고    scopus 로고
    • Poxvirus K7 protein adopts a Bcl-2 fold: Biochemical mapping of its interactions with human DEAD box RNA helicase DDX3
    • 1:CAS:528:DC%2BD1MXkt1Skug%3D%3D 18845156
    • Kalverda AP, Thompson GS, Vogel A, Schroder M, Bowie AG, Khan AR, Homans SW (2009) Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3. J Mol Biol 385:843-853
    • (2009) J Mol Biol , vol.385 , pp. 843-853
    • Kalverda, A.P.1    Thompson, G.S.2    Vogel, A.3    Schroder, M.4    Bowie, A.G.5    Khan, A.R.6    Homans, S.W.7
  • 130
    • 70350738244 scopus 로고    scopus 로고
    • Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7
    • 1:CAS:528:DC%2BD1MXhsVajsrnK 19913487
    • Oda S, Schroder M, Khan AR (2009) Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7. Structure 17:1528-1537
    • (2009) Structure , vol.17 , pp. 1528-1537
    • Oda, S.1    Schroder, M.2    Khan, A.R.3
  • 134
    • 0031018674 scopus 로고    scopus 로고
    • Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
    • 1:CAS:528:DyaK2sXht1Cksrk%3D 9020077
    • Rampino N, Yamamoto H, Ionov Y, Li Y, Sawai H, Reed JC, Perucho M (1997) Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. Science 275:967-969
    • (1997) Science , vol.275 , pp. 967-969
    • Rampino, N.1    Yamamoto, H.2    Ionov, Y.3    Li, Y.4    Sawai, H.5    Reed, J.C.6    Perucho, M.7
  • 140
    • 1442310957 scopus 로고    scopus 로고
    • Structural biology of the Bcl-2 family of proteins
    • 1:CAS:528:DC%2BD2cXhslWgu7o%3D 14996493
    • Petros AM, Olejniczak ET, Fesik SW (2004) Structural biology of the Bcl-2 family of proteins. Biochim Biophys Acta 1644:83-94
    • (2004) Biochim Biophys Acta , vol.1644 , pp. 83-94
    • Petros, A.M.1    Olejniczak, E.T.2    Fesik, S.W.3
  • 141
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • 1:CAS:528:DyaK28Xnt1ansLs%3D 8929414
    • Shuker SB, Hajduk PJ, Meadows RP, Fesik SW (1996) Discovering high-affinity ligands for proteins: SAR by NMR. Science 274:1531-1534
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 143
    • 34548047900 scopus 로고    scopus 로고
    • Crystal structure of ABT-737 complexed with Bcl-xL: Implications for selectivity of antagonists of the Bcl-2 family
    • 1:CAS:528:DC%2BD2sXptFymur4%3D 17572662
    • Lee EF, Czabotar PE, Smith BJ, Deshayes K, Zobel K, Colman PM, Fairlie WD (2007) Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family. Cell Death Differ 14:1711-1713
    • (2007) Cell Death Differ , vol.14 , pp. 1711-1713
    • Lee, E.F.1    Czabotar, P.E.2    Smith, B.J.3    Deshayes, K.4    Zobel, K.5    Colman, P.M.6    Fairlie, W.D.7
  • 145
    • 77955891885 scopus 로고    scopus 로고
    • The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
    • 1:CAS:528:DC%2BC3cXns1Gis7c%3D 3033224 20562877
    • Stewart ML, Fire E, Keating AE, Walensky LD (2010) The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer. Nat Chem Biol 6:595-601
    • (2010) Nat Chem Biol , vol.6 , pp. 595-601
    • Stewart, M.L.1    Fire, E.2    Keating, A.E.3    Walensky, L.D.4
  • 150
    • 84896088630 scopus 로고    scopus 로고
    • Human viral oncogenesis: A cancer hallmarks analysis
    • 1:CAS:528:DC%2BC2cXks1Ons7o%3D 24629334
    • Mesri EA, Feitelson MA, Munger K (2014) Human viral oncogenesis: a cancer hallmarks analysis. Cell Host Microbe 15:266-282
    • (2014) Cell Host Microbe , vol.15 , pp. 266-282
    • Mesri, E.A.1    Feitelson, M.A.2    Munger, K.3
  • 151
    • 1042301963 scopus 로고    scopus 로고
    • Epstein-Barr virus and cancer
    • 1:CAS:528:DC%2BD2cXhtFCnsrY%3D 14871955
    • Thompson MP, Kurzrock R (2004) Epstein-Barr virus and cancer. Clin Cancer Res 10:803-821
    • (2004) Clin Cancer Res , vol.10 , pp. 803-821
    • Thompson, M.P.1    Kurzrock, R.2
  • 152
    • 33646413672 scopus 로고    scopus 로고
    • The global health burden of infection-associated cancers in the year 2002
    • 1:CAS:528:DC%2BD28XksVKlurY%3D 16404738
    • Parkin DM (2006) The global health burden of infection-associated cancers in the year 2002. Int J Cancer 118:3030-3044
    • (2006) Int J Cancer , vol.118 , pp. 3030-3044
    • Parkin, D.M.1
  • 153
    • 63449086437 scopus 로고    scopus 로고
    • An Epstein-Barr virus anti-apoptotic protein constitutively expressed in transformed cells and implicated in burkitt lymphomagenesis: The Wp/BHRF1 link
    • 2652661 19283066
    • Kelly GL, Long HM, Stylianou J, Thomas WA, Leese A, Bell AI, Bornkamm GW, Mautner J, Rickinson AB, Rowe M (2009) An Epstein-Barr virus anti-apoptotic protein constitutively expressed in transformed cells and implicated in burkitt lymphomagenesis: the Wp/BHRF1 link. PLoS Pathog 5:e1000341
    • (2009) PLoS Pathog , vol.5 , pp. 1000341
    • Kelly, G.L.1    Long, H.M.2    Stylianou, J.3    Thomas, W.A.4    Leese, A.5    Bell, A.I.6    Bornkamm, G.W.7    Mautner, J.8    Rickinson, A.B.9    Rowe, M.10
  • 155
    • 84870933938 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray characterization of Epstein-Barr virus BHRF1 in complex with a benzoylurea peptidomimetic
    • 1:CAS:528:DC%2BC38XhslCgtL3L
    • Caria S, Chugh S, Nhu D, Lessene G, Kvansakul M (2012) Crystallization and preliminary X-ray characterization of Epstein-Barr virus BHRF1 in complex with a benzoylurea peptidomimetic. Acta Crystallogr, Sect F: Struct Biol Cryst Commun 68:1521-1524
    • (2012) Acta Crystallogr, Sect F: Struct Biol Cryst Commun , vol.68 , pp. 1521-1524
    • Caria, S.1    Chugh, S.2    Nhu, D.3    Lessene, G.4    Kvansakul, M.5
  • 157
    • 84897009724 scopus 로고    scopus 로고
    • Targeting gamma-herpesvirus 68 Bcl-2-mediated down-regulation of autophagy
    • 1:CAS:528:DC%2BC2cXks1Oqsbo%3D 24443581
    • Su M, Mei Y, Sanishvili R, Levine B, Colbert CL, Sinha S (2014) Targeting gamma-herpesvirus 68 Bcl-2-mediated down-regulation of autophagy. J Biol Chem 289:8029-8040
    • (2014) J Biol Chem , vol.289 , pp. 8029-8040
    • Su, M.1    Mei, Y.2    Sanishvili, R.3    Levine, B.4    Colbert, C.L.5    Sinha, S.6
  • 159
    • 34247356153 scopus 로고    scopus 로고
    • Molecular determinants of the subcellular localization of the Drosophila Bcl-2 homologues DEBCL and BUFFY
    • 1:CAS:528:DC%2BD2sXktlOitrs%3D 17205077
    • Doumanis J, Dorstyn L, Kumar S (2007) Molecular determinants of the subcellular localization of the Drosophila Bcl-2 homologues DEBCL and BUFFY. Cell Death Differ 14:907-915
    • (2007) Cell Death Differ , vol.14 , pp. 907-915
    • Doumanis, J.1    Dorstyn, L.2    Kumar, S.3
  • 160
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • 1:CAS:528:DyaK3sXms1eqtbs%3D 8358790
    • Oltvai ZN, Milliman CL, Korsmeyer SJ (1993) Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74:609-619
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 161
    • 70449941949 scopus 로고    scopus 로고
    • Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices
    • 1:CAS:528:DC%2BC3cXksFWmtg%3D%3D 19941828
    • Dewson G, Kratina T, Czabotar P, Day CL, Adams JM, Kluck RM (2009) Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices. Mol Cell 36:696-703
    • (2009) Mol Cell , vol.36 , pp. 696-703
    • Dewson, G.1    Kratina, T.2    Czabotar, P.3    Day, C.L.4    Adams, J.M.5    Kluck, R.M.6
  • 162
    • 43049105074 scopus 로고    scopus 로고
    • To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions
    • 1:CAS:528:DC%2BD1cXmtFaktLY%3D 18471982
    • Dewson G, Kratina T, Sim HW, Puthalakath H, Adams JM, Colman PM, Kluck RM (2008) To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions. Mol Cell 30:369-380
    • (2008) Mol Cell , vol.30 , pp. 369-380
    • Dewson, G.1    Kratina, T.2    Sim, H.W.3    Puthalakath, H.4    Adams, J.M.5    Colman, P.M.6    Kluck, R.M.7
  • 163
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • 1:CAS:528:DyaK28XktlGnsbY%3D 8689682
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 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
  • 164
    • 0042220409 scopus 로고    scopus 로고
    • The structure of a Bcl-xL/Bim fragment complex: Implications for Bim function
    • 1:CAS:528:DC%2BD3sXnsl2jt7s%3D 14499110
    • Liu X, Dai S, Zhu Y, Marrack P, Kappler JW (2003) The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity 19:341-352
    • (2003) Immunity , vol.19 , pp. 341-352
    • Liu, X.1    Dai, S.2    Zhu, Y.3    Marrack, P.4    Kappler, J.W.5
  • 165
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • 1:CAS:528:DC%2BD1MXnt1Giu7w%3D 19481444
    • Hasegawa H, Holm L (2009) Advances and pitfalls of protein structural alignment. Curr Opin Struct Biol 19:341-348
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 166
    • 0346121671 scopus 로고    scopus 로고
    • Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions
    • 1:CAS:528:DC%2BD3sXptVCktL0%3D 12894216
    • Woo JS, Jung JS, Ha NC, Shin J, Kim KH, Lee W, Oh BH (2003) Unique structural features of a BCL-2 family protein CED-9 and biophysical characterization of CED-9/EGL-1 interactions. Cell Death Differ 10:1310-1319
    • (2003) Cell Death Differ , vol.10 , pp. 1310-1319
    • Woo, J.S.1    Jung, J.S.2    Ha, N.C.3    Shin, J.4    Kim, K.H.5    Lee, W.6    Oh, B.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.