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Volumn 6, Issue 4, 2011, Pages

The anti-apoptotic Bcl-xl protein, a new piece in the puzzle of cytochrome c interactome

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; PROTEIN BAK; PROTEIN BCL XL; PROTEIN BCL X;

EID: 79955146862     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018329     Document Type: Article
Times cited : (41)

References (39)
  • 2
    • 31544467296 scopus 로고    scopus 로고
    • Cytochrome c: occurrence and functions
    • Bertini I, Cavallaro G, Rosato A, (2006) Cytochrome c: occurrence and functions. Chem Rev 106: 90-115.
    • (2006) Chem Rev , vol.106 , pp. 90-115
    • Bertini, I.1    Cavallaro, G.2    Rosato, A.3
  • 3
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X, (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell (Cambridge,Mass) 86: 147-157.
    • (1996) Cell (Cambridge,Mass) , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 4
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, et al. (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell (Cambridge,Mass) 91: 479-489.
    • (1997) Cell (Cambridge,Mass) , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5
  • 6
    • 1042302135 scopus 로고    scopus 로고
    • The cardiolipin-cytochrome c interaction and the mitochondrial regulation of apoptosis
    • Iverson SL, Orrenius S, (2004) The cardiolipin-cytochrome c interaction and the mitochondrial regulation of apoptosis. Arch Biochem Biophys 423: 37-46.
    • (2004) Arch Biochem Biophys , vol.423 , pp. 37-46
    • Iverson, S.L.1    Orrenius, S.2
  • 7
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: arbiters of cell survival
    • Adams JM, Cory S, (1998) The Bcl-2 protein family: arbiters of cell survival. Science 281: 1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 8
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl-2 family: regulators of the cellular life-or-death switch
    • Cory S, Adams JM, (2002) The Bcl-2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2: 647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 9
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: roles in cell survival and oncogenesis
    • Cory S, Huang DCS, Adams JM, (2003) The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 22: 8590-8607.
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.S.2    Adams, J.M.3
  • 10
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-xL during apoptosis
    • Hsu Y-T, Wolter KG, Youle RJ, (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
  • 11
    • 77957141008 scopus 로고    scopus 로고
    • Still embedded together binding to membranes regulates Bcl-2 protein interactions
    • Leber B, Lin J, Andrews DW, (2010) Still embedded together binding to membranes regulates Bcl-2 protein interactions. Oncogene 29: 5221-5230.
    • (2010) Oncogene , vol.29 , pp. 5221-5230
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 13
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-xL, and Apaf-1 form a ternary complex
    • Pan G, O'Rourke K, Dixit VM, (1998) Caspase-9, Bcl-xL, and Apaf-1 form a ternary complex. J Biol Chem 273: 5841-5845.
    • (1998) J Biol Chem , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 14
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-xL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu Y, Benedict MA, Wu W, Inohara N, Nunez J, (1998) Bcl-xL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Natl Acad Sci USA 95: 4386-4391.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, W.3    Inohara, N.4    Nunez, J.5
  • 15
    • 36249007399 scopus 로고    scopus 로고
    • High affinity binding of Bcl-xL to cytochrome c: possible relevance for interception of translocated cytochrome c in apoptosis
    • Yadaiah M, Rao PN, Harish P, Bhuyan AK, (2007) High affinity binding of Bcl-xL to cytochrome c: possible relevance for interception of translocated cytochrome c in apoptosis. Biochim Biophys Acta 1774: 1370-1379.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1370-1379
    • Yadaiah, M.1    Rao, P.N.2    Harish, P.3    Bhuyan, A.K.4
  • 16
    • 0346365095 scopus 로고    scopus 로고
    • Mapping the binding interface of the cytochrome b5-cytochrome c complex by nuclear magnetic resonance
    • Shao W, Im SC, Zuiderweg ER, Waskell L, (2003) Mapping the binding interface of the cytochrome b5-cytochrome c complex by nuclear magnetic resonance. Biochemistry 42: 14774-14784.
    • (2003) Biochemistry , vol.42 , pp. 14774-14784
    • Shao, W.1    Im, S.C.2    Zuiderweg, E.R.3    Waskell, L.4
  • 17
    • 14144250394 scopus 로고    scopus 로고
    • The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK
    • Volkov AN, Ferrari D, Worrall JA, Bonvin AM, Ubbink M, (2005) The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK. Protein Science 14: 799-811.
    • (2005) Protein Science , vol.14 , pp. 799-811
    • Volkov, A.N.1    Ferrari, D.2    Worrall, J.A.3    Bonvin, A.M.4    Ubbink, M.5
  • 19
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking
    • de Vries SJ, van Dijk M, Bonvin AM, (2010) The HADDOCK web server for data-driven biomolecular docking. Nat Protoc 5: 883-897.
    • (2010) Nat Protoc , vol.5 , pp. 883-897
    • de Vries, S.J.1    van Dijk, M.2    Bonvin, A.M.3
  • 20
    • 27944460932 scopus 로고    scopus 로고
    • A structural model for the adduct between cytochrome c and cytochrome c oxidase
    • Bertini I, Cavallaro G, Rosato A, (2005) A structural model for the adduct between cytochrome c and cytochrome c oxidase. J Biol Inorg Chem 10: 613-624.
    • (2005) J Biol Inorg Chem , vol.10 , pp. 613-624
    • Bertini, I.1    Cavallaro, G.2    Rosato, A.3
  • 21
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
    • Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, et al. (1996) X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature 381: 335-341.
    • (1996) Nature , vol.381 , pp. 335-341
    • Muchmore, S.W.1    Sattler, M.2    Liang, H.3    Meadows, R.P.4    Harlan, J.E.5
  • 22
    • 0030614915 scopus 로고    scopus 로고
    • Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
    • Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE, et al. (1997) Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 275: 983-986.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3    Meadows, R.P.4    Harlan, J.E.5
  • 23
    • 0000837519 scopus 로고    scopus 로고
    • Structural studies of eukariotic cytochromes c
    • In: Scott RA, Mauk AG, editors, Sausalito, California, University Science Books
    • Brayer GD, Murphy MEP, (1996) Structural studies of eukariotic cytochromes c. In: Scott RA, Mauk AG, editors. Cytochrome c. A multidisciplinary approach Sausalito, California University Science Books pp. 103-166.
    • (1996) Cytochrome C. A Multidisciplinary Approach , pp. 103-166
    • Brayer, G.D.1    Murphy, M.E.P.2
  • 25
    • 0036963585 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human cytochrome c in E. coli
    • Jeng WY, Chen CY, Chang HC, Chuang WJ, (2002) Expression and characterization of recombinant human cytochrome c in E. coli. J Bioenerg Biomembr 34: 423-431.
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 423-431
    • Jeng, W.Y.1    Chen, C.Y.2    Chang, H.C.3    Chuang, W.J.4
  • 26
    • 41349097770 scopus 로고    scopus 로고
    • A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia
    • Morison IM, Cramer Bordè EM, Cheesman EJ, Cheong PL, Holyoake AJ, et al. (2008) A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia. Nat Genet 40: 387-389.
    • (2008) Nat Genet , vol.40 , pp. 387-389
    • Morison, I.M.1    Cramer Bordè, E.M.2    Cheesman, E.J.3    Cheong, P.L.4    Holyoake, A.J.5
  • 28
    • 0035918306 scopus 로고    scopus 로고
    • A mutational epitope for cytochrome c binding to the apoptosis protease activation factor-1
    • Yu T, Wang X, Purring-Koch C, Wei Y, McLendon GL, (2001) A mutational epitope for cytochrome c binding to the apoptosis protease activation factor-1. J Biol Chem 276: 13034-13038.
    • (2001) J Biol Chem , vol.276 , pp. 13034-13038
    • Yu, T.1    Wang, X.2    Purring-Koch, C.3    Wei, Y.4    McLendon, G.L.5
  • 29
    • 77952652352 scopus 로고    scopus 로고
    • Structure of an apoptosome-procaspase-9 CARD complex
    • Yuan S, Yu X, Topf M, Ludtke SJ, Wang X, et al. (2010)of an apoptosome-procaspase-9 CARD complex. Structure 18: 571-583.
    • (2010) Structure , vol.18 , pp. 571-583
    • Yuan, S.1    Yu, X.2    Topf, M.3    Ludtke, S.J.4    Wang, X.5
  • 30
    • 78651241652 scopus 로고    scopus 로고
    • Structure of the Drosophila apoptosome at 6.9 Å resolution
    • Yuan S, Yu X, Topf M, Dorstyn L, Kumar S, et al. (2011) Structure of the Drosophila apoptosome at 6.9 Å resolution. Structure 19: 128-140.
    • (2011) Structure , vol.19 , pp. 128-140
    • Yuan, S.1    Yu, X.2    Topf, M.3    Dorstyn, L.4    Kumar, S.5
  • 31
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren IMA, Thornton JM, (2003) Diversity of protein-protein interactions. Embo Journal 22: 3486-3492.
    • (2003) Embo Journal , vol.22 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 32
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren IMA, Thornton JM, (2003) Structural characterisation and functional significance of transient protein-protein interactions. Journal of Molecular Biology 325: 991-1018.
    • (2003) Journal of Molecular Biology , vol.325 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 33
    • 0037022594 scopus 로고    scopus 로고
    • Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c
    • Lange C, Hunte C, (2002) Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c. Proc Natl Acad Sci USA 99: 2800-2805.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2800-2805
    • Lange, C.1    Hunte, C.2
  • 34
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c
    • Pelletier H, Kraut J, (1992) Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science 258: 1748-1755.
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 38
    • 24344460866 scopus 로고    scopus 로고
    • 1H, 13C and 15N resonance assignments of a Bcl-xL/Bad peptide complex
    • Petros AM, Fesik SW, Olejniczak ET, (2005) 1H, 13C and 15N resonance assignments of a Bcl-xL/Bad peptide complex. J Biomol NMR 32: 260.
    • (2005) J Biomol NMR , vol.32 , pp. 260
    • Petros, A.M.1    Fesik, S.W.2    Olejniczak, E.T.3
  • 39
    • 0030936560 scopus 로고    scopus 로고
    • Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system
    • Garrett DS, Seok YJ, Peterkofsky A, Clore GM, Gronenborn AM, (1997) Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system. Biochemistry 36: 4393-4398.
    • (1997) Biochemistry , vol.36 , pp. 4393-4398
    • Garrett, D.S.1    Seok, Y.J.2    Peterkofsky, A.3    Clore, G.M.4    Gronenborn, A.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.