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Volumn 29, Issue 10, 2000, Pages 1056-1058

How proapoptotic proteins can escape from mitochondria?

Author keywords

Apoptosis; Apoptosis inducing factor; Bax; Bid; Cytochrome c; Mitochondria

Indexed keywords

APOPTOSIS INDUCING FACTOR; CELL PROTEIN; CYTOCHROME C; PROCASPASE; UNCLASSIFIED DRUG;

EID: 0034669664     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(00)00291-4     Document Type: Letter
Times cited : (21)

References (16)
  • 2
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c.
    • X. Liu C. Naekyung J. Yang R. Jemmerson X. Wang Induction of apoptotic program in cell-free extracts requirement for dATP and cytochrome c . Cell 86 1996 147 157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Naekyung, C.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 3
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
    • R.M. Kluck E. Bossy-Wetzel D.R. Green D.D. Newmeyer The release of cytochrome c from mitochondria a primary site for Bcl-2 regulation of apoptosis Science 275 1997 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
  • 4
    • 0033230015 scopus 로고    scopus 로고
    • Bcl-2 and glutatione: alterations in cellular redox state that regulate apoptosis sensitivity
    • D.W. Voehringer Bcl-2 and glutatione alterations in cellular redox state that regulate apoptosis sensitivity Free Radic. Biol. Med. 27 1999 945 950
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 945-950
    • Voehringer, D.W.1
  • 5
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell
    • V.P. Skulachev Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell FEBS Lett. 397 1996 7 10
    • (1996) FEBS Lett. , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 6
    • 0033010612 scopus 로고    scopus 로고
    • Apoptosis inducing factor (AIF): a phylogenetically old, caspase-independent effector of cell death
    • H.K. Lorenzo S.A. Susin J. Pennenger G. Kroemer Apoptosis inducing factor (AIF) a phylogenetically old, caspase-independent effector of cell death Cell Death Diff. 6 1999 516 524
    • (1999) Cell Death Diff. , vol.6 , pp. 516-524
    • Lorenzo, H.K.1    Susin, S.A.2    Pennenger, J.3    Kroemer, G.4
  • 7
    • 85120121211 scopus 로고
    • V.P. Skulachev Membrane bioenergetics 1988 Springer-Verlag Berlin
    • (1988)
    • Skulachev, V.P.1
  • 8
    • 0032749848 scopus 로고    scopus 로고
    • Mitochondrial physiology and pathology; concepts of programmed death of organelles, cells and organisms
    • V.P. Skulachev Mitochondrial physiology and pathology; concepts of programmed death of organelles, cells and organisms Mol. Asp. Med. 20 1999 139 184
    • (1999) Mol. Asp. Med. , vol.20 , pp. 139-184
    • Skulachev, V.P.1
  • 9
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells
    • A. Samali J. Cai B. Zhivotovsky D.P. Jones S. Orrenius Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells EMBO J. 18 1999 2040 2048
    • (1999) EMBO J. , vol.18 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 12
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • S. Shimizu M. Narita Y. Tsujimoto Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC Nature 399 1999 483 487
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 14
    • 0034681110 scopus 로고    scopus 로고
    • Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity
    • S. Shimizu Y. Tsujimoto Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity Proc. Natl. Acad. Sci. USA 97 2000 577 582
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 577-582
    • Shimizu, S.1    Tsujimoto, Y.2
  • 15
    • 0033615649 scopus 로고    scopus 로고
    • Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore
    • J.G. Pastorino M. Tafani R.J. Rothman A. Marcineviciute J.B. Hoek J.L. Farber Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore J. Biol. Chem. 274 1999 31734 31739
    • (1999) J. Biol. Chem. , vol.274 , pp. 31734-31739
    • Pastorino, J.G.1    Tafani, M.2    Rothman, R.J.3    Marcineviciute, A.4    Hoek, J.B.5    Farber, J.L.6
  • 16
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • V.P. Skulachev Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants Quart. Rev. Biophys. 29 1996 169 202
    • (1996) Quart. Rev. Biophys. , vol.29 , pp. 169-202
    • Skulachev, V.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.