메뉴 건너뛰기




Volumn 20, Issue 3, 2000, Pages 929-935

Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CYTOCHROME C OXIDASE; PROTEIN BAX; PROTEIN BCL 2;

EID: 0033981577     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.3.929-935.2000     Document Type: Article
Times cited : (1039)

References (46)
  • 1
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams, J. M., and S. Cory. 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
  • 3
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel, E., D. D. Newmeyer, and D. R. Green. 1998. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J. 17:37-49.
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of Bid, An intracellular amplifier of apoptotic signaling
    • Chou, J. J., L. Honglin, G. S. Salvesen, J. Yuan, and G. Wagner. 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    Honglin, L.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 7
  • 10
    • 0031032105 scopus 로고    scopus 로고
    • Bcl-2 prevents activation of CPP32 cysteine protease and cleavage of poly (ADP-ribose) polymerase and U1-70 kD proteins in staurosporine-mediated apoptosis
    • Estoppey, S., I. Rodriguez, R. Sadoul, and J.-C. Martinou. 1997. Bcl-2 prevents activation of CPP32 cysteine protease and cleavage of poly (ADP-ribose) polymerase and U1-70 kD proteins in staurosporine-mediated apoptosis. Cell Death Differ. 4:34-38.
    • (1997) Cell Death Differ. , vol.4 , pp. 34-38
    • Estoppey, S.1    Rodriguez, I.2    Sadoul, R.3    Martinou, J.-C.4
  • 12
  • 13
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross, A., J. Jockel, M. C. Wei, and S. J. Korsmeyer. 1998. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17:3878-3885.
    • (1998) EMBO J. , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 16
    • 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
  • 17
    • 0031148667 scopus 로고    scopus 로고
    • Bcl-2-related proteins get connected
    • Jacobson, M. D. 1997. Bcl-2-related proteins get connected. Curr. Biol. 7:R277-R281.
    • (1997) Curr. Biol. , vol.7
    • Jacobson, M.D.1
  • 18
    • 0027666247 scopus 로고
    • Apoptosis and pleomorphic micromitochondriosis in the sinus nodes surgically excised from five patients with the long QT syndrome
    • James, T. N., F. Terasaki, E. R. Pavlovich, and A. M. Vikhert. 1993. Apoptosis and pleomorphic micromitochondriosis in the sinus nodes surgically excised from five patients with the long QT syndrome. J. Lab. Clin. Med. 122:309-323.
    • (1993) J. Lab. Clin. Med. , vol.122 , pp. 309-323
    • James, T.N.1    Terasaki, F.2    Pavlovich, E.R.3    Vikhert, A.M.4
  • 20
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: The role of the BH3 domain in apoptosis
    • Kelekar, A., and C. B. Thompson. 1998. Bcl-2-family proteins: the role of the BH3 domain in apoptosis. Trends Cell Biol. 8:324-330.
    • (1998) Trends Cell Biol. , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 21
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R. M., E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer. 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275:1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 22
    • 0030861571 scopus 로고    scopus 로고
    • Bcl-2 and Bax function independently to regulate cell death
    • Knudson, C. M., and S. J. Korsmeyer. 1997. Bcl-2 and Bax function independently to regulate cell death. Nat. Genet. 16:358-363.
    • (1997) Nat. Genet. , vol.16 , pp. 358-363
    • Knudson, C.M.1    Korsmeyer, S.J.2
  • 23
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer, G., B. Dallaporta, and M. Resche-Rigon. 1998. The mitochondrial death/life regulator in apoptosis and necrosis. Annu. Rev. Physiol. 60:619-642.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 25
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer, G. C. 1997. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat. Med. 3:614-620.
    • (1997) Nat. Med. , vol.3 , pp. 614-620
    • Kroemer, G.C.1
  • 26
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., D. Nijhawan, I. Budihardjo, S. M. Srinivasula, M. Ahmad, E. S. Alnemri, and X. Wang. 1997. Cytochrome c and dATP dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 27
    • 0030608832 scopus 로고    scopus 로고
    • Mitochondrial ultracondensation, but not swelling, is involved in TNF alpha-induced apoptosis in human T-lymphoblastic leukaemic cells
    • Lia, J., R. R. Dourmashkin, A. C. Newland, and S. M. Kelsey. 1997. Mitochondrial ultracondensation, but not swelling, is involved in TNF alpha-induced apoptosis in human T-lymphoblastic leukaemic cells. Leuk. Res. 21:973-983.
    • (1997) Leuk. Res. , vol.21 , pp. 973-983
    • Lia, J.1    Dourmashkin, R.R.2    Newland, A.C.3    Kelsey, S.M.4
  • 28
    • 0030792850 scopus 로고    scopus 로고
    • Mitochondrial proliferation and paradoxical membrane depolarization during terminal differenciation and apoptosis in a human colon carcinoma cell line
    • Mancini, M., B. O. Anderson, E. Caldwell, M. Sedghinasab, P. B. Paty, and D. M. Hockenbery. 1997. Mitochondrial proliferation and paradoxical membrane depolarization during terminal differenciation and apoptosis in a human colon carcinoma cell line. J. Cell Biol. 138:449-469.
    • (1997) J. Cell Biol. , vol.138 , pp. 449-469
    • Mancini, M.1    Anderson, B.O.2    Caldwell, E.3    Sedghinasab, M.4    Paty, P.B.5    Hockenbery, D.M.6
  • 29
    • 0033535345 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event
    • Martinou, I., S. Desagher, R. Eskes, B. Antonsson, E. André, S. Fakan, and J.-C. Martinou. 1999. The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event. J. Cell Biol. 144:883-889.
    • (1999) J. Cell Biol. , vol.144 , pp. 883-889
    • Martinou, I.1    Desagher, S.2    Eskes, R.3    Antonsson, B.4    André, E.5    Fakan, S.6    Martinou, J.-C.7
  • 31
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule bid: A structural basis for apoptotic agonists and antagonists
    • McDonnell, J. M., D. Fushman, C. L. Milliman, S. J. Korsmeyer, and D. Cowburn. 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
  • 32
    • 0030797727 scopus 로고    scopus 로고
    • Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death
    • Miller, T. M., K. L. Moulder, C. M. Knudson, D. J. Creedon, M. Deshmukh, S. J. Korsmeyer, and E. M. J. Johnson. 1997. Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death. J. Cell Biol. 139:205-217.
    • (1997) J. Cell Biol. , vol.139 , pp. 205-217
    • Miller, T.M.1    Moulder, K.L.2    Knudson, C.M.3    Creedon, D.J.4    Deshmukh, M.5    Korsmeyer, S.J.6    Johnson, E.M.J.7
  • 35
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the prermeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita, M., S. Shimizu, T. Ito, T. Chittenden, R. Lutz, H. Matsuda, and Y. Tsujimoto. 1998. Bax interacts with the prermeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. USA 95:14681-14686.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.5    Matsuda, H.6    Tsujimoto, Y.7
  • 36
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed, J. C. 1997. Double identity for proteins of the Bcl-2 family. Nature 387:773-776.
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.C.1
  • 44
    • 0029899181 scopus 로고    scopus 로고
    • Molecular thanatopsis: A discourse on the BCL2 family and cell death
    • Yang, E., and S. J. Korsmeyer. 1996. Molecular thanatopsis: a discourse on the BCL2 family and cell death. Blood 88:386-401.
    • (1996) Blood , vol.88 , pp. 386-401
    • Yang, E.1    Korsmeyer, S.J.2
  • 46
    • 0031795088 scopus 로고    scopus 로고
    • Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential
    • Zhuang, J., D. Dinsdale, and G. M. Cohen. 1998. Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential. Cell Death Differ. 5:953-962.
    • (1998) Cell Death Differ. , vol.5 , pp. 953-962
    • Zhuang, J.1    Dinsdale, D.2    Cohen, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.