메뉴 건너뛰기




Volumn 53, Issue 4, 2002, Pages 297-306

Mitochondria and apoptosis;Mitocondria y apoptosis

Author keywords

Apoptosis; Bcl 2; Heat shock proteins (HSP); Mitochondria; Programmed cell death

Indexed keywords

APOPTOSIS INDUCING FACTOR; APOPTOSIS INHIBITOR; CASPASE; CYTOCHROME C; HEAT SHOCK PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; PROTEIN BCL 2; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND;

EID: 0038067872     PISSN: 00015504     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (7)

References (92)
  • 1
    • 0028817287 scopus 로고
    • Apoptosis in unicellular eukaryote (Trypanosoma cruzi): Implications for the evolutionary origin and role of programmed cell death in the control of cell proliferation, differentiation and survival
    • Ameisen, J.C., Idziorek, T., Billaut-Mulot, O., Loyens, M., Tissier, J.P., Potentier, A. and Ouaissi, A. Apoptosis in unicellular eukaryote (Trypanosoma cruzi): implications for the evolutionary origin and role of programmed cell death in the control of cell proliferation, differentiation and survival. Cell Death Diff 2: 285-300, 1995.
    • (1995) Cell Death Diff. , vol.2 , pp. 285-300
    • Ameisen, J.C.1    Idziorek, T.2    Billaut-Mulot, O.3    Loyens, M.4    Tissier, J.P.5    Potentier, A.6    Ouaissi, A.7
  • 2
    • 0036311492 scopus 로고    scopus 로고
    • On the origin, evolution, and nature of programmed cell death: A timeline of four billion years
    • Ameisen, J.C. On the origin, evolution, and nature of programmed cell death: a timeline of four billion years. Cell Death Differ. 9: 367-393, 2002.
    • (2002) Cell Death Differ. , vol.9 , pp. 367-393
    • Ameisen, J.C.1
  • 4
    • 0024654435 scopus 로고
    • Nucleotide sequence organization and nature of the protein product of the carotenoid biosynthesis gene cluster of Rhodobaxter capsulatus
    • Armstrong, G.A., Alberti, M., Leach, F. and Hearst, J.E. Nucleotide sequence organization and nature of the protein product of the carotenoid biosynthesis gene cluster of Rhodobaxter capsulatus. Mol. Gen. Genet. 216: 254-268, 1989.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 254-268
    • Armstrong, G.A.1    Alberti, M.2    Leach, F.3    Hearst, J.E.4
  • 5
    • 0034107096 scopus 로고    scopus 로고
    • Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by direct cleaving BID
    • Barry, M., Heibein, J.A., Pinkoski, M.J., Lee, S.F., Moyer, R.W., Green, R.D. and Bleackley, R.C. Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by direct cleaving BID. Mol. Cell Biol. 20: 3781-3794, 2000.
    • (2000) 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, R.D.6    Bleackley, R.C.7
  • 6
    • 0034991311 scopus 로고    scopus 로고
    • Inactivation of multiple targets by nitric oxide in CD95-triggered apoptosis
    • Bernassola, F., Catani, M.V., Corazzari, M., Rossi, A. and Melino, G. Inactivation of multiple targets by nitric oxide in CD95-triggered apoptosis. J. Cell Biochem. 82: 123-133, 2001.
    • (2001) J. Cell Biochem. , vol.82 , pp. 123-133
    • Bernassola, F.1    Catani, M.V.2    Corazzari, M.3    Rossi, A.4    Melino, G.5
  • 7
    • 0031054167 scopus 로고    scopus 로고
    • La mort des bactéries: Provoquée ou programmée? Subie ou voulue?
    • Boutibonnes, P. La mort des bactéries: provoquée ou programmée? Subie ou voulue? Med/Sci 13: 73-80, 1997
    • (1997) Med./Sci. , vol.13 , pp. 73-80
    • Boutibonnes, P.1
  • 8
    • 0036244305 scopus 로고    scopus 로고
    • Nitric oxide and cell signaling pathways in mitochondrial-dependent apoptosis
    • Boyd, C.S. and Cadenas, E. Nitric oxide and cell signaling pathways in mitochondrial-dependent apoptosis. Biol. Chem. 383: 411-423, 2002.
    • (2002) Biol. Chem. , vol.383 , pp. 411-423
    • Boyd, C.S.1    Cadenas, E.2
  • 12
    • 0028176651 scopus 로고
    • Oxidative stress as a mediator of apoptosis
    • Buttke, T.M. and Sandstrom, P.A. Oxidative stress as a mediator of apoptosis. Immunology Today. 15: 7-10, 1994.
    • (1994) Immunology Today , vol.15 , pp. 7-10
    • Buttke, T.M.1    Sandstrom, P.A.2
  • 13
    • 0036478928 scopus 로고    scopus 로고
    • The Apaf-1 apoptosome: A large caspase-activating complex
    • Cain, K., Bratton, S.B. and Cohen, G.M. The Apaf-1 apoptosome: a large caspase-activating complex. Biochimie. 84: 203-214, 2002.
    • (2002) Biochimie , vol.84 , pp. 203-214
    • Cain, K.1    Bratton, S.B.2    Cohen, G.M.3
  • 14
    • 0036479012 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): A novel caspase-independent death effector released from mitochondria
    • Cande, C., Cohen, I., Daugas, E., Ravagnan, L., Larochette, N., Zamzami, N. and Kroemer, G. Apoptosis-inducing factor (AIF): a novel caspase-independent death effector released from mitochondria. Biochimie. 84: 215-222, 2002.
    • (2002) Biochimie , vol.84 , pp. 215-222
    • Cande, C.1    Cohen, I.2    Daugas, E.3    Ravagnan, L.4    Larochette, N.5    Zamzami, N.6    Kroemer, G.7
  • 15
    • 0024330729 scopus 로고
    • Nucleotide transport in Rhodobaxter capsulatus
    • Carmeli, C. and Lifshitz, Y. Nucleotide transport in Rhodobaxter capsulatus. J. Bacteriol. 171: 6521-6525, 1989.
    • (1989) J. Bacteriol. , vol.171 , pp. 6521-6525
    • Carmeli, C.1    Lifshitz, Y.2
  • 16
    • 0034725610 scopus 로고    scopus 로고
    • Mitochondria localization and dimerization are required for CIDE-B to induce apoptosis
    • Chen, Z., Guo, K., Toh, S.Y., Zhou, Z. and Li, P. Mitochondria localization and dimerization are required for CIDE-B to induce apoptosis. J. Biol. Chem. 275: 22619-22622, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22619-22622
    • Chen, Z.1    Guo, K.2    Toh, S.Y.3    Zhou, Z.4    Li, P.5
  • 18
    • 0028932673 scopus 로고
    • Limitations to in vivo import of hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesized apocytochrome b
    • Claros, M.G., Perea, J., Shu, Y., Samatey, F.A., Popot, J.L. and Jacq, C. Limitations to in vivo import of hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesized apocytochrome b. Eur. J. Biochem. 228: 762-771, 1995.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 762-771
    • Claros, M.G.1    Perea, J.2    Shu, Y.3    Samatey, F.A.4    Popot, J.L.5    Jacq, C.6
  • 22
    • 0034919499 scopus 로고    scopus 로고
    • Hydrogen peroxide induces apoptosis-like death in Leishmania donovani promastigotes
    • Das, M., Mukherjee, S.B. and Shaha, C. Hydrogen peroxide induces apoptosis-like death in Leishmania donovani promastigotes. J. Cell Sci. 114: 2461-2469, 2001.
    • (2001) J. Cell Sci. , vol.114 , pp. 2461-2469
    • Das, M.1    Mukherjee, S.B.2    Shaha, C.3
  • 23
    • 0034117177 scopus 로고    scopus 로고
    • Mitochondrio-nuclear redistribution of AIF in apoptosis and necrosis
    • Daugas, E., Susin, S.A. and Zamzami, N. Mitochondrio-nuclear redistribution of AIF in apoptosis and necrosis. FASEB J. 14: 729-739, 2000.
    • (2000) FASEB J. , vol.14 , pp. 729-739
    • Daugas, E.1    Susin, S.A.2    Zamzami, N.3
  • 24
    • 0032608038 scopus 로고    scopus 로고
    • Heat Shock Proteins: Facts, Thoughts and Dreams
    • De Maio, A. Heat Shock Proteins: Facts, Thoughts and Dreams. Shock. 11: 1-12, 1999.
    • (1999) Shock , vol.11 , pp. 1-12
    • De Maio, A.1
  • 25
    • 0035161964 scopus 로고    scopus 로고
    • The heat shock paradox: Does NF-kappaB determine cell fate?
    • DeMeester, S.L., Buchman, T.G. and Cobb, J.P. The heat shock paradox: does NF-kappaB determine cell fate?. FASEB J. 15: 270-274, 2001.
    • (2001) FASEB J. , vol.15 , pp. 270-274
    • DeMeester, S.L.1    Buchman, T.G.2    Cobb, J.P.3
  • 26
    • 0028227969 scopus 로고
    • L'apoptose dérive-t-elle de la mort nucléaire programmée mise en oeuvre par les protistes?
    • Denis, H. and Mignotte, B. L'apoptose dérive-t-elle de la mort nucléaire programmée mise en oeuvre par les protistes?. Med/Sci. 10: 687-695, 1994.
    • (1994) Med./Sci. , vol.10 , pp. 687-695
    • Denis, H.1    Mignotte, B.2
  • 27
    • 0035026438 scopus 로고    scopus 로고
    • Antiapoptotic proteins. The Bcl-2 and inhibitor of apoptosis protein families
    • Deveraux, Q.L., Schendel, S.L. and Reed, J.C. Antiapoptotic proteins. The Bcl-2 and inhibitor of apoptosis protein families. Cardiol. Clin. 19: 57-74, 2001.
    • (2001) Cardiol. Clin. , vol.19 , pp. 57-74
    • Deveraux, Q.L.1    Schendel, S.L.2    Reed, J.C.3
  • 28
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L. and Wang, X. Smac, a mitochondrial protein that promotes cytochrome c dependent caspase activation by eliminating IAP inhibition. Cell. 102: 33-42, 2000.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 29
    • 0026051936 scopus 로고
    • Genes required for the engulfment of cell corps during programmed cell death in Caenorhabditis elegans
    • Ellis, R.E., Jacobson, D.M. and Horvitz, H.R. Genes required for the engulfment of cell corps during programmed cell death in Caenorhabditis elegans. Genetics. 129: 79-94, 1991.
    • (1991) Genetics , vol.129 , pp. 79-94
    • Ellis, R.E.1    Jacobson, D.M.2    Horvitz, H.R.3
  • 30
    • 0036478970 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species in cell death signaling
    • Fleury, C., Mignote, B. and Vayssiere, J.L. Mitochondrial reactive oxygen species in cell death signaling. Biochimie. 84: 131-141, 2002.
    • (2002) Biochimie , vol.84 , pp. 131-141
    • Fleury, C.1    Mignote, B.2    Vayssiere, J.L.3
  • 31
    • 0031239745 scopus 로고    scopus 로고
    • Origin of eukaryotic programmed cell death: A consequence of aerobic metabolism?
    • Frade, J.M. and Michaelidis, T.M. Origin of eukaryotic programmed cell death: a consequence of aerobic metabolism?. Bioessays. 19: 827-832, 1997.
    • (1997) Bioessays , vol.19 , pp. 827-832
    • Frade, J.M.1    Michaelidis, T.M.2
  • 32
    • 0029979079 scopus 로고    scopus 로고
    • Inconstant association between 27 kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells
    • Garrido, C., Mehlen, P., Fromentin, A., Hammann, A., Assem, M., Arrigo, A.P. and Chauffert, B. Inconstant association between 27 kDa heat-shock protein (Hsp27) content and doxorubicin resistance in human colon cancer cells. Eur. J. Biochem. 237: 653-659, 1996.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 653-659
    • Garrido, C.1    Mehlen, P.2    Fromentin, A.3    Hammann, A.4    Assem, M.5    Arrigo, A.P.6    Chauffert, B.7
  • 34
    • 0024444559 scopus 로고
    • The evolutionary origins of organelles
    • Gray, M.W. The evolutionary origins of organelles. Trends Genet. 5: 294-299, 1989.
    • (1989) Trends Genet. , vol.5 , pp. 294-299
    • Gray, M.W.1
  • 35
    • 0030052107 scopus 로고    scopus 로고
    • Role of mitochondria and C-terminal membrane anchor Bcl-2 in Bax induced growth arrest and mortality in Saccharomyces cerevisiae
    • Greenhalf, W., Stephan, C. and Chaudhuri, B. Role of mitochondria and C-terminal membrane anchor Bcl-2 in Bax induced growth arrest and mortality in Saccharomyces cerevisiae. FEBS Lett. 380: 169-175, 1996.
    • (1996) FEBS Lett. , vol.380 , pp. 169-175
    • Greenhalf, W.1    Stephan, C.2    Chaudhuri, B.3
  • 36
    • 0033609157 scopus 로고    scopus 로고
    • The proapoptotic function of Drosophila Hid is conserved in mammalian cells
    • Haining, W.N., Carboy-Newcomb, C., Wei, C.L. and Steller, H. The proapoptotic function of Drosophila Hid is conserved in mammalian cells. Proc. Natl. Acad. Sci. 96: 4936-4941, 1999.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 4936-4941
    • Haining, W.N.1    Carboy-Newcomb, C.2    Wei, C.L.3    Steller, H.4
  • 37
    • 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: 153-166, 2002.
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 38
    • 0028288277 scopus 로고
    • C.elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • Hengartner, M.O. and Horvitz, H.R. C.elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 76: 665-676, 1994.
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 39
    • 1842417077 scopus 로고    scopus 로고
    • Human Bak induces cell death in Schizosaccharomyces pombe with the morphological changes similar to those with apoptosis in mammalian cells
    • Ink, B., Zornig, M., Baum, B., Hajibagheri, N., James, C., Chittenden, T. and Evan, G. Human Bak induces cell death in Schizosaccharomyces pombe with the morphological changes similar to those with apoptosis in mammalian cells. Mol. Cell Biol. 17: 2468-2474, 1997.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2468-2474
    • Ink, B.1    Zornig, M.2    Baum, B.3    Hajibagheri, N.4    James, C.5    Chittenden, T.6    Evan, G.7
  • 40
    • 0035070581 scopus 로고    scopus 로고
    • Effects of schisandrin B pretreatment on tumor necrosis factor-alpha induced apoptosis and Hsp70 expression in mouse liver
    • Ip, S.P., Che, C.T., Kong, Y.C. and Ko, K.M. Effects of schisandrin B pretreatment on tumor necrosis factor-alpha induced apoptosis and Hsp70 expression in mouse liver. Cell Stress Chaperones. 6: 44-48, 2001.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 44-48
    • Ip, S.P.1    Che, C.T.2    Kong, Y.C.3    Ko, K.M.4
  • 41
    • 0025944612 scopus 로고
    • Structural similarities between a mitochondrially encoded polypeptide and a family of prokaryotic respiratory toxins involved in plasmid maintenance suggest a novel mechanism for the evolutionary maintenance of mitochondrial DNA
    • Jacobs, H.T. Structural similarities between a mitochondrially encoded polypeptide and a family of prokaryotic respiratory toxins involved in plasmid maintenance suggest a novel mechanism for the evolutionary maintenance of mitochondrial DNA. J. Mol. Evol. 32: 333-339, 1991.
    • (1991) J. Mol. Evol. , vol.32 , pp. 333-339
    • Jacobs, H.T.1
  • 43
    • 0031127578 scopus 로고    scopus 로고
    • CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9
    • James, C., Gschmeissner, S., Fraser, A. and Evan, G.I. CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9. Curr. Biol. 7: 246-252, 1997.
    • (1997) Curr. Biol. , vol.7 , pp. 246-252
    • James, C.1    Gschmeissner, S.2    Fraser, A.3    Evan, G.I.4
  • 45
    • 0036316720 scopus 로고    scopus 로고
    • Origin and evolution of eukaryotic apoptosis: The bacterial connection
    • Koonin, E.V. and Aranvid, L. Origin and evolution of eukaryotic apoptosis: the bacterial connection. Cell Death. Differ. 9:394-404, 2002.
    • (2002) Cell Death Differ. , vol.9 , pp. 394-404
    • Koonin, E.V.1    Aranvid, L.2
  • 46
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer, G. and Reed, J.C. Mitochondrial control of cell death. Nat. Med. 6: 513-519, 2000.
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 47
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene bcl-2 and its role in regulating apoptosis
    • Kroemer, G. The proto-oncogene bcl-2 and its role in regulating apoptosis. Nature Medicine. 3: 614-620, 1997.
    • (1997) Nature Medicine , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 50
    • 0034640102 scopus 로고    scopus 로고
    • Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis
    • Li, K., Li, Y., Shelton, J.M., Richardson, J.A., Spencer, E., Chen, Z.J., Wang, X. and Williams, R.S. Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis. Cell. 101: 389-399, 2000.
    • (2000) Cell , vol.101 , pp. 389-399
    • Li, K.1    Li, Y.2    Shelton, J.M.3    Richardson, J.A.4    Spencer, E.5    Chen, Z.J.6    Wang, X.7    Williams, R.S.8
  • 51
    • 0030069729 scopus 로고    scopus 로고
    • Mechanism of protein import across the mitochondrial outer membrane
    • Lill, R. and Neupert, W. Mechanism of protein import across the mitochondrial outer membrane: Trends Cell Biol. 6: 56-61, 1996.
    • (1996) Trends Cell Biol. , vol.6 , pp. 56-61
    • Lill, R.1    Neupert, W.2
  • 52
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • Lin, K.M., Lin, B., Lian, I.Y., Mestril, R., Scheffler, I.E. and Dillmann, W.H. Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation. 103: 1787-1792, 2001.
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 53
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting tBid to mitochondria
    • Lutter, M., Fang, M., Luo, X., Nishijima, M., Xie, X.S. and Wang, X. Cardiolipin provides specificity for targeting tBid to mitochondria. Nat. Cell Biol. 2; 754-761, 2000.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 754-761
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.S.5    Wang, X.6
  • 55
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling
    • Marchenko, N.D., Zaika, A. and Moll, U.M. Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J. Biol. Chem. 275: 16202-16212, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 56
    • 0030035039 scopus 로고    scopus 로고
    • Archaeal-eubacterial mergers in the origin of Eukarya: Phylogenetic classification of life
    • Margulis, L. Archaeal-eubacterial mergers in the origin of Eukarya: phylogenetic classification of life: Proc. Natl. Acad. Sci. 93: 1071-1076, 1996.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 1071-1076
    • Margulis, L.1
  • 58
    • 0036513249 scopus 로고    scopus 로고
    • Does nitric oxide modulate mitochondrial energy generation and apoptosis?
    • Moncada, S. and Erusalimsky, J.D. Does nitric oxide modulate mitochondrial energy generation and apoptosis?. Nat. Rev. Mol. Cell Biol. 3: 214-220, 2002.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 214-220
    • Moncada, S.1    Erusalimsky, J.D.2
  • 59
    • 0029919619 scopus 로고    scopus 로고
    • Heat shock induction of apoptosis in promastigotes of the unicellular organism Leishmania (Leishmania) amazonensis
    • Moreira, M.E., Portillo, H.A., Milder, R.V., Balanco, J.M. and Barcinski, M.A. Heat shock induction of apoptosis in promastigotes of the unicellular organism Leishmania (Leishmania) amazonensis. J. Cell. Physiol. 167: 305-313, 1996.
    • (1996) J. Cell. Physiol. , vol.167 , pp. 305-313
    • Moreira, M.E.1    Portillo, H.A.2    Milder, R.V.3    Balanco, J.M.4    Barcinski, M.A.5
  • 60
    • 0036510606 scopus 로고    scopus 로고
    • Mitochondrial protein import: Molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44
    • Moro, F., Okamoto, K., Donzeau, M., Neupert, W. and Brunner, M. Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44. J. Biol. Chem. 277: 6874-6880, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6874-6880
    • Moro, F.1    Okamoto, K.2    Donzeau, M.3    Neupert, W.4    Brunner, M.5
  • 62
    • 0034973710 scopus 로고    scopus 로고
    • Cytokine-induced cell death in immortalized Schwann cells: Roles of nitric oxide and cyclic AMP
    • Nagano, S., Takeda, M., Ma, L. and Soliven B. Cytokine-induced cell death in immortalized Schwann cells: roles of nitric oxide and cyclic AMP. J. Neurochem. 77: 1486-1495, 2001.
    • (2001) J. Neurochem. , vol.77 , pp. 1486-1495
    • Nagano, S.1    Takeda, M.2    Ma, L.3    Soliven, B.4
  • 64
    • 0035295778 scopus 로고    scopus 로고
    • Mitochondria in apoptosis and human disease
    • Olson, M. and Kornbluth, S. Mitochondria in apoptosis and human disease. Curr. Mol. Med. 1: 91-122,2001.
    • (2001) Curr. Mol. Med. , vol.1 , pp. 91-122
    • Olson, M.1    Kornbluth, S.2
  • 65
    • 0036479004 scopus 로고    scopus 로고
    • Mitochondria: Regulating the inevitable
    • Parone, P.A., James, D. and Martinou, J.C. Mitochondria: regulating the inevitable Biochimie. 84: 105-111, 2002.
    • (2002) Biochimie , vol.84 , pp. 105-111
    • Parone, P.A.1    James, D.2    Martinou, J.C.3
  • 66
    • 0035853721 scopus 로고    scopus 로고
    • The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ
    • Petronilli, V., Penzo, D., Scorrano, L., Bernardi, P. and Di Lisa, F. The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ. J. Biol. Chem. 276: 12030-12034, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12030-12034
    • Petronilli, V.1    Penzo, D.2    Scorrano, L.3    Bernardi, P.4    Di Lisa, F.5
  • 67
    • 0036479048 scopus 로고    scopus 로고
    • Influence of mitochondrial control of apoptosis on the pathogenesis, complications and treatment of HIV infection
    • Phenix, B.N. and Badley, A.D. Influence of mitochondrial control of apoptosis on the pathogenesis, complications and treatment of HIV infection. Biochimie. 84: 251-264, 2002.
    • (2002) Biochimie , vol.84 , pp. 251-264
    • Phenix, B.N.1    Badley, A.D.2
  • 68
    • 0035097710 scopus 로고    scopus 로고
    • Overexpression of inducible heat shock protein 70 in Cos-1 cells fails to protect from cytotoxicity of oxidized Idls
    • Pirillo, A., Norata, G.D., Zanelli, T. and Catapano, A.L. Overexpression of inducible heat shock protein 70 in Cos-1 cells fails to protect from cytotoxicity of oxidized Idls. Arterioscler Thromb. Vasc. Biol. 21: 348-354, 2001.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 348-354
    • Pirillo, A.1    Norata, G.D.2    Zanelli, T.3    Catapano, A.L.4
  • 70
    • 0342905085 scopus 로고    scopus 로고
    • Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel HVDAC3, and alters its transmembrane potential
    • Rahmani, Z., Huh, K.W., Lasher, R. and Siddiqui, A. Hepatitis B virus X protein colocalizes to mitochondria with a human voltage-dependent anion channel HVDAC3, and alters its transmembrane potential. J. Virol. 74: 2840-2846, 2000.
    • (2000) J. Virol. , vol.74 , pp. 2840-2846
    • Rahmani, Z.1    Huh, K.W.2    Lasher, R.3    Siddiqui, A.4
  • 73
    • 0030041936 scopus 로고    scopus 로고
    • Heat shock proteins increase resistance to apoptosis
    • Samali, A. and Cotter, T.G. Heat shock proteins increase resistance to apoptosis. Exp. Cell Res. 223: 163-170, 1996.
    • (1996) Exp. Cell Res. , vol.223 , pp. 163-170
    • Samali, A.1    Cotter, T.G.2
  • 74
    • 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
    • Samali, A., Cai, J., Zhivotovsky, B., Jones, D.P. and Orrenius, S. Presence of a pre-apoptotic complex of pro-caspase-3, HSP60 and HSP10 in the mitochondrial fraction of Jurkat cells. EMBO J. 18: 2040-2048, 1999.
    • (1999) EMBO J. , vol.18 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 75
    • 0030220261 scopus 로고    scopus 로고
    • Porins: General to specific, native to engineered passive pores
    • Schulz, G.E. Porins: general to specific, native to engineered passive pores. Curr. Opin. Struct. Biol. 6: 485-490, 1996.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 485-490
    • Schulz, G.E.1
  • 76
    • 0034681110 scopus 로고    scopus 로고
    • Proapoptic 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
    • Shimizu, S. and Tsujimoto, Y. Proapoptic 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. 97: 577-582, 2000.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 577-582
    • Shimizu, S.1    Tsujimoto, Y.2
  • 80
    • 0036479052 scopus 로고    scopus 로고
    • Mitochondrial disappearance froms cells: A clue to the role of autophagy in programmed cell death and disease?
    • Tolkovsky, A.M., Xue, L., Fletcher, G.C. and Borutaite, V. Mitochondrial disappearance froms cells: a clue to the role of autophagy in programmed cell death and disease?. Biochimie. 84: 233-240, 2002.
    • (2002) Biochimie , vol.84 , pp. 233-240
    • Tolkovsky, A.M.1    Xue, L.2    Fletcher, G.C.3    Borutaite, V.4
  • 81
    • 0036479053 scopus 로고    scopus 로고
    • Mitochondria as sensors of sphingolipids
    • Tomassini, B. and Testi, R. Mitochondria as sensors of sphingolipids Biochimie. 84: 123-129, 2002.
    • (2002) Biochimie , vol.84 , pp. 123-129
    • Tomassini, B.1    Testi, R.2
  • 82
    • 0021679848 scopus 로고
    • Cloning of the chromosome breakpoint of neoplastic B cells with the t (14;18) chromosome translocation
    • Tsujimoto, Y., Finger, L.R., Yunis, J., Nowell, P.C. and Croce, C.M. Cloning of the chromosome breakpoint of neoplastic B cells with the t (14;18) chromosome translocation. Science. 226: 1097-1099, 1984.
    • (1984) Science , vol.226 , pp. 1097-1099
    • Tsujimoto, Y.1    Finger, L.R.2    Yunis, J.3    Nowell, P.C.4    Croce, C.M.5
  • 85
    • 0034520113 scopus 로고    scopus 로고
    • Permeabilization of the mitochondrial inner membrane during apoptosis: Impact of the adenine nucleotide translocator
    • Vieira, H.L., Haouzi, D., El Hamel, C., Jacotot, E., Belzacq, AS., Brenner, C. and Kroemer, G. Permeabilization of the mitochondrial inner membrane during apoptosis: impact of the adenine nucleotide translocator. Cell Death Differ. 7: 1146-1154, 2000.
    • (2000) Cell Death Differ. , vol.7 , pp. 1146-1154
    • Vieira, H.L.1    Haouzi, D.2    El Hamel, C.3    Jacotot, E.4    Belzacq, A.S.5    Brenner, C.6    Kroemer, G.7
  • 86
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev. 15: 2922-2933, 2001.
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 87
    • 0036479001 scopus 로고    scopus 로고
    • And all of a sudden it's over: Mitochondrial outer-membrane permeabilization in apoptosis
    • Waterhouse, N.J., Ricci, J.E. and Green, D.R. and all of a sudden it's over: mitochondrial outer-membrane permeabilization in apoptosis Biochimie. 84: 113-121, 2002.
    • (2002) Biochimie , vol.84 , pp. 113-121
    • Waterhouse, N.J.1    Ricci, J.E.2    Green, D.R.3
  • 91
    • 22644448368 scopus 로고    scopus 로고
    • AIF: Un nouvel agent double mitochondrial
    • Zamzani, N., Susin, S. and Kroemer, G. AIF: un nouvel agent double mitochondrial. Médicine/Science. 15: 436-437, 1999.
    • (1999) Médicine/Science , vol.15 , pp. 436-437
    • Zamzani, N.1    Susin, S.2    Kroemer, G.3
  • 92
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-A. a human protein homologous to C. elegans ced-4 participates in cytochrome c dependent activation of caspase-3
    • Zhou, H., Henzel, W.J., Liu, X., Lutschg, A. and Wang, X. Apaf-A. a human protein homologous to C. elegans ced-4 participates in cytochrome c dependent activation of caspase-3. Cell. 90: 405-413, 1997.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zhou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.