메뉴 건너뛰기




Volumn 1757, Issue 9-10, 2006, Pages 1297-1300

Mitochondrial membrane permeability transition and cell death

Author keywords

Cell death; Mitochondria; Permeability transition

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; ANION CHANNEL; CIS TRANS ISOMERASE; CYCLIN D; CYCLOPHILIN; CYCLOSPORIN A; PROTEIN BCL 2; PROTEIN BCL XL;

EID: 33748961353     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.03.017     Document Type: Review
Times cited : (161)

References (30)
  • 1
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green D.R., and Evan G.I. A matter of life and death. Cancer Cell 1 (2002) 19-30
    • (2002) Cancer Cell , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 2
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev. 15 (2001) 2922-2933
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 3
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S., and Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10 (2000) 369-377
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 4
    • 0037401562 scopus 로고    scopus 로고
    • Cell death regulation by the Bcl-2 protein family in the mitochondria
    • Tsujimoto Y. Cell death regulation by the Bcl-2 protein family in the mitochondria. J. Cell. Physiol. 195 (2003) 158-167
    • (2003) J. Cell. Physiol. , vol.195 , pp. 158-167
    • Tsujimoto, Y.1
  • 5
    • 0035146929 scopus 로고    scopus 로고
    • Life-or-death decisions by the Bcl-2 protein family
    • Adams J.M., and Cory S. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem. Sci. 26 (2001) 61-66
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 61-66
    • Adams, J.M.1    Cory, S.2
  • 7
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M., and Szabo I. The mitochondrial permeability transition. Biochim. Biophys. Acta 1241 (1995) 139-176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 8
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: another view
    • Halestrap A.P., McStay G.P., and Clarke S.J. The permeability transition pore complex: another view. Biochimie 84 (2002) 153-166
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 9
    • 0042526700 scopus 로고    scopus 로고
    • On the involvement of mitochondrial intermembrane junctional complexes in apoptosis
    • Crompton M. On the involvement of mitochondrial intermembrane junctional complexes in apoptosis. Curr. Med. Chem. 10 (2003) 1473-1484
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1473-1484
    • Crompton, M.1
  • 10
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: how Pandora's box opens
    • Zamzami N., and Kroemer G. The mitochondrion in apoptosis: how Pandora's box opens. Nat. Rev. Mol. Cell Biol. 2 (2001) 67-71
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 12
    • 0024360271 scopus 로고
    • Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria
    • Broekemeier K.M., Dempsey M.E., and Pfeiffer D.R. Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J. Biol. Chem. 264 (1989) 7826-7830
    • (1989) J. Biol. Chem. , vol.264 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 13
    • 0037070178 scopus 로고    scopus 로고
    • Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function?
    • He L., and Lemasters J.J. Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function?. FEBS Lett. 512 (2002) 1-7
    • (2002) FEBS Lett. , vol.512 , pp. 1-7
    • He, L.1    Lemasters, J.J.2
  • 14
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 17
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., and Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112 (2003) 481-490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 18
    • 0035931765 scopus 로고    scopus 로고
    • Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells
    • Shimizu S., Matsuoka Y., Shinohara Y., Yoneda Y., and Tsujimoto Y. Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells. J. Cell Biol. 152 (2001) 237-250
    • (2001) J. Cell Biol. , vol.152 , pp. 237-250
    • Shimizu, S.1    Matsuoka, Y.2    Shinohara, Y.3    Yoneda, Y.4    Tsujimoto, Y.5
  • 19
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton M., Virji S., and Ward J.M. Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur. J. Biochem. 258 (1998) 729-735
    • (1998) Eur. J. Biochem. , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 20
    • 0032387842 scopus 로고    scopus 로고
    • Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
    • Woodfield K., Ruck A., Brdiczka D., and Halestrap A.P. Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Biochem. J. 336 (1998) 287-290
    • (1998) Biochem. J. , vol.336 , pp. 287-290
    • Woodfield, K.1    Ruck, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 24
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • Basso E., Fante L., Fowlkes J., Petronilli V., Forte M.A., and Bernardi P. Properties of the permeability transition pore in mitochondria devoid of cyclophilin D. J. Biol. Chem. 280 (2005) 18558-18561
    • (2005) J. Biol. Chem. , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 26
    • 0037163117 scopus 로고    scopus 로고
    • Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization
    • Lin D.T., and Lechleiter J.D. Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. J. Biol. Chem. 277 (2002) 31134-31141
    • (2002) J. Biol. Chem. , vol.277 , pp. 31134-31141
    • Lin, D.T.1    Lechleiter, J.D.2
  • 27
    • 1542332908 scopus 로고    scopus 로고
    • Cyclophilin D, a component of the permeability transition pore, is an apoptosis repressor
    • Schubert A., and Grimm S. Cyclophilin D, a component of the permeability transition pore, is an apoptosis repressor. Cancer Res. 64 (2004) 85-93
    • (2004) Cancer Res. , vol.64 , pp. 85-93
    • Schubert, A.1    Grimm, S.2
  • 29
    • 0032550363 scopus 로고    scopus 로고
    • The permeability transition pore complex: a target for apoptosis regulation by caspases and Bcl-2-related proteins
    • Reed J.C., and Kroemer G. The permeability transition pore complex: a target for apoptosis regulation by caspases and Bcl-2-related proteins. J. Exp. Med. 187 (1998) 1261-1271
    • (1998) J. Exp. Med. , vol.187 , pp. 1261-1271
    • Reed, J.C.1    Kroemer, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.