메뉴 건너뛰기




Volumn 83, Issue 14, 2009, Pages 7085-7098

The fowlpox virus BCL-2 homologue, FPV039, interacts with activated Bax and a discrete subset of BH3-only proteins to inhibit apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN P24; GAMMA INTERFERON; LIPID A; OVALBUMIN; PROTEASOME;

EID: 67650453767     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00437-09     Document Type: Article
Times cited : (38)

References (90)
  • 2
    • 21844464054 scopus 로고    scopus 로고
    • Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis
    • Annis, M. G., E. L. Soucie, P. J. Dlugosz, J. A. Cruz-Aguado, L. Z. Penn, B. Leber, and D. W. Andrews. 2005. Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis. EMBO J. 24:2096-2103.
    • (2005) EMBO J , vol.24 , pp. 2096-2103
    • Annis, M.G.1    Soucie, E.L.2    Dlugosz, P.J.3    Cruz-Aguado, J.A.4    Penn, L.Z.5    Leber, B.6    Andrews, D.W.7
  • 3
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson, B., S. Montessuit, S. Lauper, R. Eskes, and J. C. Martinou. 2000. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345:271-278.
    • (2000) Biochem. J , vol.345 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 4
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson, B., S. Montessuit, B. Sanchez, and J. C. Martinou. 2001. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J. Biol. Chem. 276:11615- 11623.
    • (2001) J. Biol. Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 6
    • 35148886675 scopus 로고    scopus 로고
    • Fowlpox virus encodes a Bcl-2 homologue that protects cells from apoptotic death through interaction with the proapoptotic protein Bak
    • Banadyga, L., J. Gerig, T. Stewart, and M. Barry. 2007. Fowlpox virus encodes a Bcl-2 homologue that protects cells from apoptotic death through interaction with the proapoptotic protein Bak. J. Virol. 81:11032-11045.
    • (2007) J. Virol , vol.81 , pp. 11032-11045
    • Banadyga, L.1    Gerig, J.2    Stewart, T.3    Barry, M.4
  • 7
    • 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
    • Barry, M., J. A. Heibein, M. J. Pinkoski, S. F. Lee, R. W. Moyer, D. R. Green, and R. C. Bleackley. 2000. Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid. Mol. Cell. Biol. 20:3781-3794.
    • (2000) Bid. Mol. Cell. Biol , vol.20 , 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
  • 8
    • 33750304036 scopus 로고    scopus 로고
    • The potential role of fowlpox virus in rational vaccine design
    • Beukema, E. L., M. P. Brown, and J. D. Hayball. 2006. The potential role of fowlpox virus in rational vaccine design. Expert Rev. Vaccines 5:565-577.
    • (2006) Expert Rev. Vaccines , vol.5 , pp. 565-577
    • Beukema, E.L.1    Brown, M.P.2    Hayball, J.D.3
  • 10
    • 15444364107 scopus 로고    scopus 로고
    • Distinct domains control the addressing and the insertion of Bax into mitochondria
    • Cartron, P. F., H. Arokium, L. Oliver, K. Meflah, S. Manon, and F. M. Vallette. 2005. Distinct domains control the addressing and the insertion of Bax into mitochondria. J. Biol. Chem. 280:10587-10598.
    • (2005) J. Biol. Chem , vol.280 , pp. 10587-10598
    • Cartron, P.F.1    Arokium, H.2    Oliver, L.3    Meflah, K.4    Manon, S.5    Vallette, F.M.6
  • 11
    • 9744244990 scopus 로고    scopus 로고
    • The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA
    • Cartron, P. F., T. Gallenne, G. Bougras, F. Gautier, F. Manero, P. Vusio, K. Meflah, F. M. Vallette, and P. Juin. 2004. The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA. Mol. Cell 16:807-818.
    • (2004) Mol. Cell , vol.16 , pp. 807-818
    • Cartron, P.F.1    Gallenne, T.2    Bougras, G.3    Gautier, F.4    Manero, F.5    Vusio, P.6    Meflah, K.7    Vallette, F.M.8    Juin, P.9
  • 12
    • 33646354381 scopus 로고    scopus 로고
    • Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members
    • Certo, M., V. Del Gaizo Moore, M. Nishino, G. Wei, S. Korsmeyer, S. A. Armstrong, and A. Letai. 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 Moore, V.2    Nishino, M.3    Wei, G.4    Korsmeyer, S.5    Armstrong, S.A.6    Letai, A.7
  • 14
    • 0031017578 scopus 로고    scopus 로고
    • A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak
    • Cheng, E. H., J. Nicholas, D. S. Bellows, G. S. Hayward, H. G. Guo, M. S. Reitz, and J. M. Hardwick. 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. USA 94:690-694.
    • (1997) Proc. Natl. Acad. Sci. USA , 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
  • 15
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk, J. E., and D. R. Green. 2008. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol. 18:157-164.
    • (2008) Trends Cell Biol , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 16
    • 0028986876 scopus 로고    scopus 로고
    • Chittenden, T., E. A. Harrington, R. O'Connor, C. Flemington, R. J. Lutz, G. I. Evan, and B. C. Guild. 1995. Induction of apoptosis by the Bcl-2 homologue Bak. Nature 374:733-736.
    • Chittenden, T., E. A. Harrington, R. O'Connor, C. Flemington, R. J. Lutz, G. I. Evan, and B. C. Guild. 1995. Induction of apoptosis by the Bcl-2 homologue Bak. Nature 374:733-736.
  • 18
    • 0036791781 scopus 로고    scopus 로고
    • Viral homologs of BCL-2: Role of apoptosis in the regulation of virus infection
    • Cuconati, A., and E. White. 2002. Viral homologs of BCL-2: role of apoptosis in the regulation of virus infection. Genes Dev. 16:2465-2478.
    • (2002) Genes Dev , vol.16 , pp. 2465-2478
    • Cuconati, A.1    White, E.2
  • 20
    • 4344600796 scopus 로고    scopus 로고
    • Poxvirus protein N1L targets the I-κB kinase complex, inhibits signaling to NF-κB by the tumor necrosis factor superfamily of receptors, and inhibits NF-κB and IRF3 signaling by toll-like receptors
    • DiPerna, G., J. Stack, A. G. Bowie, A. Boyd, G. Kotwal, Z. Zhang, S. Arvikar, E. Latz, K. A. Fitzgerald, and W. L. Marshall. 2004. Poxvirus protein N1L targets the I-κB kinase complex, inhibits signaling to NF-κB by the tumor necrosis factor superfamily of receptors, and inhibits NF-κB and IRF3 signaling by toll-like receptors. J. Biol. Chem. 279:36570-36578.
    • (2004) J. Biol. Chem , vol.279 , pp. 36570-36578
    • DiPerna, G.1    Stack, J.2    Bowie, A.G.3    Boyd, A.4    Kotwal, G.5    Zhang, Z.6    Arvikar, S.7    Latz, E.8    Fitzgerald, K.A.9    Marshall, W.L.10
  • 22
    • 33947727119 scopus 로고    scopus 로고
    • Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2
    • Douglas, A. E., K. D. Corbett, J. M. Berger, G. McFadden, and T. M. Handel. 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
  • 23
    • 85025432190 scopus 로고    scopus 로고
    • Earl, P. L., B. Moss, L. S. Wyatt, and M. W. Carroll. 1998. Generation of recombinant vaccinia viruses, p.16.17.1-16.17.19. In R. B. Frederick, M. Ausubel, Robert E. Kingston, David D. Moore, J. G. Seidman, John A. Smith, and Kevin Struhl (ed.), Current protocols in molecular biology. John Wiley and Sons, Inc., New York, NY.
    • Earl, P. L., B. Moss, L. S. Wyatt, and M. W. Carroll. 1998. Generation of recombinant vaccinia viruses, p.16.17.1-16.17.19. In R. B. Frederick, M. Ausubel, Robert E. Kingston, David D. Moore, J. G. Seidman, John A. Smith, and Kevin Struhl (ed.), Current protocols in molecular biology. John Wiley and Sons, Inc., New York, NY.
  • 24
    • 0023928504 scopus 로고
    • Membrane potential can be determined in individual cells from the Nernstian distribution of cationic dyes
    • Ehrenberg, B., V. Montana, M. D. Wei, J. P. Wuskell, and L. M. Loew. 1988. Membrane potential can be determined in individual cells from the Nernstian distribution of cationic dyes. Biophys. J. 53:785-794.
    • (1988) Biophys. J , vol.53 , pp. 785-794
    • Ehrenberg, B.1    Montana, V.2    Wei, M.D.3    Wuskell, J.P.4    Loew, L.M.5
  • 25
    • 0034192298 scopus 로고    scopus 로고
    • M11L: A novel mitochondria-localized protein of myxoma virus that blocks apoptosis of infected leukocytes
    • Everett, H., M. Barry, S. F. Lee, X. Sun, K. Graham, J. Stone, R. C. Bleackley, and G. McFadden. 2000. M11L: a novel mitochondria-localized protein of myxoma virus that blocks apoptosis of infected leukocytes. J. Exp. Med. 191:1487-1498.
    • (2000) J. Exp. Med , vol.191 , pp. 1487-1498
    • Everett, H.1    Barry, M.2    Lee, S.F.3    Sun, X.4    Graham, K.5    Stone, J.6    Bleackley, R.C.7    McFadden, G.8
  • 27
    • 39449086762 scopus 로고    scopus 로고
    • BH3 domains define selective inhibitory interactions with BHRF-1 and KSHV BCL-2
    • Flanagan, A. M., and A. Letai. 2008. BH3 domains define selective inhibitory interactions with BHRF-1 and KSHV BCL-2. Cell Death Differ. 15:580-588.
    • (2008) Cell Death Differ , vol.15 , pp. 580-588
    • Flanagan, A.M.1    Letai, A.2
  • 28
    • 43249094403 scopus 로고    scopus 로고
    • A179L, a viral Bcl-2 homologue, targets the core Bcl-2 apoptotic machinery and its upstream BH3 activators with selective binding restrictions for Bid and Noxa
    • Galindo, I., B. Hernaez, G. Diaz-Gil, J. M. Escribano, and C. Alonso. 2008. A179L, a viral Bcl-2 homologue, targets the core Bcl-2 apoptotic machinery and its upstream BH3 activators with selective binding restrictions for Bid and Noxa. Virology 375:561-572.
    • (2008) Virology , vol.375 , pp. 561-572
    • Galindo, I.1    Hernaez, B.2    Diaz-Gil, G.3    Escribano, J.M.4    Alonso, C.5
  • 29
    • 44949151607 scopus 로고    scopus 로고
    • Galluzzi, L., C. Brenner, E. Morselli, Z. Touat, and G. Kroemer. 2008. Viral control of mitochondrial apoptosis. PLoS Pathog 4:e1000018.
    • Galluzzi, L., C. Brenner, E. Morselli, Z. Touat, and G. Kroemer. 2008. Viral control of mitochondrial apoptosis. PLoS Pathog 4:e1000018.
  • 31
    • 0042815099 scopus 로고    scopus 로고
    • Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway
    • Gillissen, B., F. Essmann, V. Graupner, L. Starck, S. Radetzki, B. Dorken, K. Schulze-Osthoff, and P. T. Daniel. 2003. Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway. EMBO J. 22:3580-3590.
    • (2003) EMBO J , vol.22 , pp. 3580-3590
    • Gillissen, B.1    Essmann, F.2    Graupner, V.3    Starck, L.4    Radetzki, S.5    Dorken, B.6    Schulze-Osthoff, K.7    Daniel, P.T.8
  • 33
    • 37049021087 scopus 로고    scopus 로고
    • Characterization of the BH3 protein Bmf in Gallus gallus: Identification of a novel chicken-specific isoform
    • Gomez-Esquer, F., M. A. Palomar, I. Rivas, J. Delcan, R. Linares, and G. Diaz-Gil. 2008. Characterization of the BH3 protein Bmf in Gallus gallus: identification of a novel chicken-specific isoform. Gene 407:21-29.
    • (2008) Gene , vol.407 , pp. 21-29
    • Gomez-Esquer, F.1    Palomar, M.A.2    Rivas, I.3    Delcan, J.4    Linares, R.5    Diaz-Gil, G.6
  • 35
    • 50849109845 scopus 로고    scopus 로고
    • Graham, S. C., M. W. Bahar, S. Cooray, R. A. Chen, D. M. Whalen, N. G. Abrescia, D. Alderton, R. J. Owens, D. I. Stuart, G. L. Smith, and J. M. Grimes. 2008. Vaccinia virus proteins A52 and B14 Share a Bcl-2-like fold but have evolved to inhibit NF-κB rather than apoptosis. PLoS Pathog 4:e1000128.
    • Graham, S. C., M. W. Bahar, S. Cooray, R. A. Chen, D. M. Whalen, N. G. Abrescia, D. Alderton, R. J. Owens, D. I. Stuart, G. L. Smith, and J. M. Grimes. 2008. Vaccinia virus proteins A52 and B14 Share a Bcl-2-like fold but have evolved to inhibit NF-κB rather than apoptosis. PLoS Pathog 4:e1000128.
  • 36
    • 0035891057 scopus 로고    scopus 로고
    • Griffiths, G. J., B. M. Corfe, P. Savory, S. Leech, M. D. Esposti, J. A. Hickman, and C. Dive. 2001. Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak. Oncogene 20:7668-7676.
    • Griffiths, G. J., B. M. Corfe, P. Savory, S. Leech, M. D. Esposti, J. A. Hickman, and C. Dive. 2001. Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak. Oncogene 20:7668-7676.
  • 37
    • 0033535347 scopus 로고    scopus 로고
    • Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis
    • Griffiths, G. J., L. Dubrez, C. P. Morgan, N. A. Jones, J. Whitehouse, B. M. Corfe, C. Dive, and J. A. Hickman. 1999. Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis. J. Cell Biol. 144:903-914.
    • (1999) J. Cell Biol , vol.144 , pp. 903-914
    • Griffiths, G.J.1    Dubrez, L.2    Morgan, C.P.3    Jones, N.A.4    Whitehouse, J.5    Corfe, B.M.6    Dive, C.7    Hickman, J.A.8
  • 38
    • 0029790857 scopus 로고    scopus 로고
    • Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K
    • Han, J., P. Sabbatini, and E. White. 1996. Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K. Mol. Cell. Biol. 16:5857-5864.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 5857-5864
    • Han, J.1    Sabbatini, P.2    White, E.3
  • 39
    • 7444243152 scopus 로고    scopus 로고
    • Survival factor-induced extracellular signal-regulated kinase phosphorylates BIM, inhibiting its association with BAX and proapoptotic activity
    • Harada, H., B. Quearry, A. Ruiz-Vela, and S. J. Korsmeyer. 2004. Survival factor-induced extracellular signal-regulated kinase phosphorylates BIM, inhibiting its association with BAX and proapoptotic activity. Proc. Natl. Acad. Sci. USA 101:15313-15317.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15313-15317
    • Harada, H.1    Quearry, B.2    Ruiz-Vela, A.3    Korsmeyer, S.J.4
  • 40
    • 0037276564 scopus 로고    scopus 로고
    • Viral versus cellular BCL-2 proteins
    • Hardwick, J. M., and D. S. Bellows. 2003. Viral versus cellular BCL-2 proteins. Cell Death Differ 10(Suppl. 1):S68-S76.
    • (2003) Cell Death Differ , vol.10 , Issue.SUPPL. 1
    • Hardwick, J.M.1    Bellows, D.S.2
  • 41
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-XL during apoptosis
    • Hsu, Y. T., K. G. Wolter, and R. J. Youle. 1997. Cytosol-to-membrane redistribution of Bax and Bcl-XL during apoptosis. Proc. Natl. Acad. Sci. USA 94:3668-3672.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 42
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu, Y. T., and R. J. Youle. 1998. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J. Biol. Chem. 273:10777-10783.
    • (1998) J. Biol. Chem , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 43
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu, Y. T., and R. J. Youle. 1997. Nonionic detergents induce dimerization among members of the Bcl-2 family. J. Biol. Chem. 272:13829-13834.
    • (1997) J. Biol. Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 44
    • 0041885229 scopus 로고    scopus 로고
    • Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2
    • Huang, Q., A. M. Petros, H. W. Virgin, S. W. Fesik, and E. T. Olejniczak. 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
  • 45
    • 56349162153 scopus 로고    scopus 로고
    • Vaccinia virus lacking the Bcl-2-like protein N1 induces a stronger natural killer cell response to infection
    • Jacobs, N., N. W. Bartlett, R. H. Clark, and G. L. Smith. 2008. Vaccinia virus lacking the Bcl-2-like protein N1 induces a stronger natural killer cell response to infection. J. Gen. Virol. 89:2877-2881.
    • (2008) J. Gen. Virol , vol.89 , pp. 2877-2881
    • Jacobs, N.1    Bartlett, N.W.2    Clark, R.H.3    Smith, G.L.4
  • 46
    • 9844226204 scopus 로고    scopus 로고
    • Caspase-dependent apoptosis of COS-7 cells induced by Bax overexpression: Differential effects of Bcl-2 and Bcl-xL on Bax-induced caspase activation and apoptosis
    • Kitanaka, C., T. Namiki, K. Noguchi, T. Mochizuki, S. Kagaya, S. Chi, A. Hayashi, A. Asai, Y. Tsujimoto, and Y. Kuchino. 1997. Caspase-dependent apoptosis of COS-7 cells induced by Bax overexpression: differential effects of Bcl-2 and Bcl-xL on Bax-induced caspase activation and apoptosis. Oncogene 15:1763-1772.
    • (1997) Oncogene , vol.15 , pp. 1763-1772
    • Kitanaka, C.1    Namiki, T.2    Noguchi, K.3    Mochizuki, T.4    Kagaya, S.5    Chi, S.6    Hayashi, A.7    Asai, A.8    Tsujimoto, Y.9    Kuchino, Y.10
  • 47
    • 0021717580 scopus 로고
    • Establishment of monoclonal anti-Nk-1.1 antibody
    • Koo, G. C., and J. R. Peppard. 1984. Establishment of monoclonal anti-Nk-1.1 antibody. Hybridoma 3:301-303.
    • (1984) Hybridoma , vol.3 , pp. 301-303
    • Koo, G.C.1    Peppard, J.R.2
  • 48
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana, T., L. Bouchier-Hayes, J. E. Chipuk, C. Bonzon, B. A. Sullivan, D. R. Green, and D. D. Newmeyer. 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
  • 49
    • 33947304650 scopus 로고    scopus 로고
    • A structural viral mimic of prosurvival bcl-2: A pivotal role for sequestering proapoptotic bax and bak
    • Kvansakul, M., M. F. van Delft, E. F. Lee, J. M. Gulbis, W. D. Fairlie, D. C. Huang, and P. M. Colman. 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
  • 50
    • 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
    • Kvansakul, M., H. Yang, W. D. Fairlie, P. E. Czabotar, S. F. Fischer, M. A. Perugini, D. C. Huang, and P. M. Colman. 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
  • 52
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
    • Leber, B., J. Lin, and D. W. Andrews. 2007. Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes. Apoptosis 12:897-911.
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 54
    • 57149135309 scopus 로고    scopus 로고
    • Lovell, J. F., L. P. Billen, S. Bindner, A. Shamas-Din, C. Fradin, B. Leber, and D. W. Andrews. 2008. Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 135:1074-1084.
    • Lovell, J. F., L. P. Billen, S. Bindner, A. Shamas-Din, C. Fradin, B. Leber, and D. W. Andrews. 2008. Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 135:1074-1084.
  • 55
    • 0032052217 scopus 로고    scopus 로고
    • Metivier, D., B. Dallaporta, N. Zamzami, N. Larochette, S. A. Susin, I. Marzo, and G. Kroemer. 1998. Cytofluorometric detection of mitochondrial alterations in early CD95/Fas/APO-1-triggered apoptosis of Jurkat T lymphoma cells. Comparison of seven mitochondrion-specific fluorochromes. Immunol. Lett. 61:157-163.
    • Metivier, D., B. Dallaporta, N. Zamzami, N. Larochette, S. A. Susin, I. Marzo, and G. Kroemer. 1998. Cytofluorometric detection of mitochondrial alterations in early CD95/Fas/APO-1-triggered apoptosis of Jurkat T lymphoma cells. Comparison of seven mitochondrion-specific fluorochromes. Immunol. Lett. 61:157-163.
  • 56
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan, A., C. L. Smith, Y. T. Hsu, and R. J. Youle. 1999. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 18:2330-2341.
    • (1999) EMBO J , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 57
    • 0032518787 scopus 로고    scopus 로고
    • O'Connor, L., A. Strasser, L. A. O'Reilly, G. Hausmann, J. M. Adams, S. Cory, and D. C. Huang. 1998. Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J. 17:384-395.
    • O'Connor, L., A. Strasser, L. A. O'Reilly, G. Hausmann, J. M. Adams, S. Cory, and D. C. Huang. 1998. Bim: a novel member of the Bcl-2 family that promotes apoptosis. EMBO J. 17:384-395.
  • 58
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai, Z. N., C. L. Milliman, and S. J. Korsmeyer. 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
  • 61
    • 33745961009 scopus 로고    scopus 로고
    • Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis
    • Postigo, A., J. R. Cross, J. Downward, and M. Way. 2006. Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis. Cell Death Differ. 13:1651-1662.
    • (2006) Cell Death Differ , vol.13 , pp. 1651-1662
    • Postigo, A.1    Cross, J.R.2    Downward, J.3    Way, M.4
  • 63
    • 0013770208 scopus 로고
    • Reactions of N-ethylmaleimide with peptides and amino acids
    • Smyth, D. G., O. O. Blumenfeld, and W. Konigsberg. 1964. Reactions of N-ethylmaleimide with peptides and amino acids. Biochem. J. 91:589-595.
    • (1964) Biochem. J , vol.91 , pp. 589-595
    • Smyth, D.G.1    Blumenfeld, O.O.2    Konigsberg, W.3
  • 64
    • 0025961008 scopus 로고
    • The target DNA sequence for resolution of poxvirus replicative intermediates is an active late promoter
    • Stuart, D., K. Graham, M. Schreiber, C. Macaulay, and G. McFadden. 1991. The target DNA sequence for resolution of poxvirus replicative intermediates is an active late promoter. J. Virol. 65:61-70.
    • (1991) J. Virol , vol.65 , pp. 61-70
    • Stuart, D.1    Graham, K.2    Schreiber, M.3    Macaulay, C.4    McFadden, G.5
  • 65
    • 31144454896 scopus 로고    scopus 로고
    • Myxoma virus M11L blocks apoptosis through inhibition of conformational activation of Bax at the mitochondria
    • Su, J., G. Wang, J. W. Barrett, T. S. Irvine, X. Gao, and G. McFadden. 2006. Myxoma virus M11L blocks apoptosis through inhibition of conformational activation of Bax at the mitochondria. J. Virol. 80:1140-1151.
    • (2006) J. Virol , vol.80 , pp. 1140-1151
    • Su, J.1    Wang, G.2    Barrett, J.W.3    Irvine, T.S.4    Gao, X.5    McFadden, G.6
  • 66
    • 0035976902 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K
    • Sundararajan, R., A. Cuconati, D. Nelson, and E. White. 2001. Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K. J. Biol. Chem. 276:45120-45127.
    • (2001) J. Biol. Chem , vol.276 , pp. 45120-45127
    • Sundararajan, R.1    Cuconati, A.2    Nelson, D.3    White, E.4
  • 67
    • 0034905003 scopus 로고    scopus 로고
    • E1B 19K blocks Bax oligomerization and tumor necrosis factor alpha-mediated apoptosis
    • Sundararajan, R., and E. White. 2001. E1B 19K blocks Bax oligomerization and tumor necrosis factor alpha-mediated apoptosis. J. Virol. 75:7506-7516.
    • (2001) J. Virol , vol.75 , pp. 7506-7516
    • Sundararajan, R.1    White, E.2
  • 69
    • 29144495592 scopus 로고    scopus 로고
    • Near death experiences: Poxvirus regulation of apoptotic death
    • Taylor, J. M., and M. Barry. 2006. Near death experiences: poxvirus regulation of apoptotic death. Virology 344:139-150.
    • (2006) Virology , vol.344 , pp. 139-150
    • Taylor, J.M.1    Barry, M.2
  • 70
    • 33845972661 scopus 로고    scopus 로고
    • The vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein Bax
    • Taylor, J. M., D. Quilty, L. Banadyga, and M. Barry. 2006. The vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein Bax. J. Biol. Chem. 281:39728-39739.
    • (2006) J. Biol. Chem , vol.281 , pp. 39728-39739
    • Taylor, J.M.1    Quilty, D.2    Banadyga, L.3    Barry, M.4
  • 74
    • 27644535708 scopus 로고    scopus 로고
    • The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation
    • Wasilenko, S. T., L. Banadyga, D. Bond, and M. Barry. 2005. The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation. J. Virol. 79:14031-14043.
    • (2005) J. Virol , vol.79 , pp. 14031-14043
    • Wasilenko, S.T.1    Banadyga, L.2    Bond, D.3    Barry, M.4
  • 75
    • 0344198504 scopus 로고    scopus 로고
    • Vaccinia virus encodes a previously uncharacterized mitochondrial-associated inhibitor of apoptosis
    • Wasilenko, S. T., T. L. Stewart, A. F. Meyers, and M. Barry. 2003. Vaccinia virus encodes a previously uncharacterized mitochondrial-associated inhibitor of apoptosis. Proc. Natl. Acad. Sci. USA 100:14345-14350.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14345-14350
    • Wasilenko, S.T.1    Stewart, T.L.2    Meyers, A.F.3    Barry, M.4
  • 78
    • 34250897851 scopus 로고    scopus 로고
    • A novel Bcl-2-like inhibitor of apoptosis is encoded by the parapoxvirus ORF virus
    • Westphal, D., E. C. Ledgerwood, M. H. Hibma, S. B. Fleming, E. M. Whelan, and A. A. Mercer. 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
  • 79
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: How BH3-only proteins induce apoptosis
    • Willis, S. N., and J. M. Adams. 2005. Life in the balance: how BH3-only proteins induce apoptosis. Curr. Opin. Cell Biol. 17:617-625.
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 80
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis, S. N., L. Chen, G. Dewson, A. Wei, E. Naik, J. I. Fletcher, J. M. Adams, and D. C. Huang. 2005. Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 19:1294-1305.
    • (2005) Genes Dev , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, L.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.8
  • 81
    • 33846964621 scopus 로고    scopus 로고
    • Willis, S. N., J. I. Fletcher, T. Kaufmann, M. F. van Delft, L. Chen, P. E. Czabotar, H. Ierino, E. F. Lee, W. D. Fairlie, P. Bouillet, A. Strasser, R. M. Kluck, J. M. Adams, and D. C. Huang. 2007. Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 315:856-859.
    • Willis, S. N., J. I. Fletcher, T. Kaufmann, M. F. van Delft, L. Chen, P. E. Czabotar, H. Ierino, E. F. Lee, W. D. Fairlie, P. Bouillet, A. Strasser, R. M. Kluck, J. M. Adams, and D. C. Huang. 2007. Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 315:856-859.
  • 82
    • 41649100863 scopus 로고    scopus 로고
    • Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases
    • Wilton, B. A., S. Campbell, N. Van Buuren, R. Garneau, M. Furukawa, Y. Xiong, and M. Barry. 2008. Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases. Virology 374:82-99.
    • (2008) Virology , vol.374 , pp. 82-99
    • Wilton, B.A.1    Campbell, S.2    Van Buuren, N.3    Garneau, R.4    Furukawa, M.5    Xiong, Y.6    Barry, M.7
  • 84
    • 0029906828 scopus 로고    scopus 로고
    • BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases
    • Xiang, J., D. T. Chao, and S. J. Korsmeyer. 1996. BAX-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases. Proc. Natl. Acad. Sci. USA 93:14559-14563.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 85
    • 0032524656 scopus 로고    scopus 로고
    • Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence
    • Yasuda, M., P. Theodorakis, T. Subramanian, and G. Chinnadurai. 1998. Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence. J. Biol. Chem. 273:12415-12421.
    • (1998) J. Biol. Chem , vol.273 , pp. 12415-12421
    • Yasuda, M.1    Theodorakis, P.2    Subramanian, T.3    Chinnadurai, G.4
  • 86
    • 0028206341 scopus 로고    scopus 로고
    • Yin, X. M., Z. N. Oltvai, and S. J. Korsmeyer. 1994. BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature 369:321-323.
    • Yin, X. M., Z. N. Oltvai, and S. J. Korsmeyer. 1994. BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature 369:321-323.
  • 87
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle, R. J., and A. Strasser. 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
  • 88
    • 0029917541 scopus 로고    scopus 로고
    • Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
    • Zha, H., C. Aime-Sempe, T. Sato, and J. C. Reed. 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
  • 90
    • 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
    • Zong, W. X., T. Lindsten, A. J. Ross, G. R. MacGregor, and C. B. Thompson. 2001. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15:1481-1486.
    • (2001) Genes Dev , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.