메뉴 건너뛰기




Volumn 6, Issue 5, 2000, Pages 513-519

Mitochondrial control of cell death

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE KINASE; CYTOCHROME C; PROTEIN BAX; PROTEIN BCL 2; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0034068601     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/74994     Document Type: Review
Times cited : (2853)

References (81)
  • 1
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer, C., Dallaporta, B. & Resche-Rigon, M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu. Rev. Physiol. 60, 619-642 (1998).
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, C.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 2
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D.R. & Reed, J.C. Mitochondria and apoptosis. Science 281, 1309-1312 (1998).
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 3
    • 0033179760 scopus 로고    scopus 로고
    • Bcl-2 family members and the mitochondria in apoptosis
    • Cross, A., McDonnell, J.M. & Korsmeyer, S.J. Bcl-2 family members and the mitochondria in apoptosis. Genes Dev. 13, 1988-1911 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1988-11911
    • Cross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 4
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: Inhibitors of apoptosis or regulators of mitochondrial homeostasis?
    • Vander Heiden, M.G. & Thompson, C.B. Bcl-2 proteins: Inhibitors of apoptosis or regulators of mitochondrial homeostasis? Nature Cell Biol. 1, E209-E216 (1999).
    • (1999) Nature Cell Biol. , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 5
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin, S.A. et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 397, 441-446 (1999).
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1
  • 6
    • 0033605376 scopus 로고    scopus 로고
    • Mitochondrial depopolarization accompanies cytochrome c release during apoptosis in PC6 cells
    • Heiskanen, K.M., Bhat, M.B., Wang, H.W., Ma, J.J. & Nieminen, A.L. Mitochondrial depopolarization accompanies cytochrome c release during apoptosis in PC6 cells. J. Biol. Chem. 274, 5654-5658 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 5654-5658
    • Heiskanen, K.M.1    Bhat, M.B.2    Wang, H.W.3    Ma, J.J.4    Nieminen, A.L.5
  • 7
    • 0032823410 scopus 로고    scopus 로고
    • Ultrastructural and biochemical observations on the early changes in apoptotic epithelial cells of the rat prostate induced by castration
    • Kwong, J., Choi, H.L., Huang, Y. & Chan, F.L. Ultrastructural and biochemical observations on the early changes in apoptotic epithelial cells of the rat prostate induced by castration. Cell Tissue Res. 298, 123-136 (1999).
    • (1999) Cell Tissue Res. , vol.298 , pp. 123-136
    • Kwong, J.1    Choi, H.L.2    Huang, Y.3    Chan, F.L.4
  • 8
    • 0033568486 scopus 로고    scopus 로고
    • Mitochondria and cell death - Mechanistic aspects and methodological issues
    • Bernardi, P., Scorrano, L., Colonna, R., Petronilli, V. & Di Lisa, F. Mitochondria and cell death - Mechanistic aspects and methodological issues. Eur. J. Biochem. 264, 687-701 (1999).
    • (1999) Eur. J. Biochem. , vol.264 , pp. 687-701
    • Bernardi, P.1    Scorrano, L.2    Colonna, R.3    Petronilli, V.4    Di Lisa, F.5
  • 9
    • 0032504568 scopus 로고    scopus 로고
    • The mitochondrial permeability transition in cell death: A common mechanism in necrosis, apoptosis and autophagy
    • Lemasters, J.J. et al. The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochim. Biophys. Acta 1366, 177-196 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 177-196
    • Lemasters, J.J.1
  • 10
    • 0032574761 scopus 로고    scopus 로고
    • Bax directly induces release of cytochrome c from isolated mitochondria
    • Jürgensmeier, J.M. et al. Bax directly induces release of cytochrome c from isolated mitochondria. Proc. Natl. Acad. Sci. USA 95, 4997-5002 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4997-5002
    • Jürgensmeier, J.M.1
  • 11
    • 0032566649 scopus 로고    scopus 로고
    • Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis
    • Marzo, I. et al. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science 281, 2027-2031 (1998).
    • (1998) Science , vol.281 , pp. 2027-2031
    • Marzo, I.1
  • 12
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita, M. et al. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. USA 95, 14681-14686 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1
  • 13
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher, S. et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J. Cell Biol. 144, 891-901 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 891-901
    • Desagher, S.1
  • 14
    • 0033615649 scopus 로고    scopus 로고
    • Functional consequences of sustained or transient activation by Bax of the mitochondrial permeability transition pore
    • Pastorino, J.G. et al. Functional consequences of sustained or transient activation by Bax of the mitochondrial permeability transition pore. J. Biol. Chem. 274, 31734-31739 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31734-31739
    • Pastorino, J.G.1
  • 15
    • 0033535347 scopus 로고    scopus 로고
    • Cell damage-induced conformational changes of the proapoptotic protein bak in vivo precede the onset of apoptosis
    • Griffiths, G.J. et al. Cell damage-induced conformational changes of the proapoptotic protein bak in vivo precede the onset of apoptosis. J. Cell Biol. 144, 903-914 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 903-914
    • Griffiths, G.J.1
  • 16
    • 0033230611 scopus 로고    scopus 로고
    • Apoptotic cytosol facilitates Bax translocation to mitochondria that involves cytosolic factor regulated by Bcl-2
    • Nomura, M. et al. Apoptotic cytosol facilitates Bax translocation to mitochondria that involves cytosolic factor regulated by Bcl-2. Cancer Res 59, 5542-5548 (1999).
    • (1999) Cancer Res , vol.59 , pp. 5542-5548
    • Nomura, M.1
  • 17
    • 0033406781 scopus 로고    scopus 로고
    • Withdrawal of IL-7 induces Bax translocation from cytosol to mitochondria through a rise in intracellular pH
    • Khaled, A.R., Kim, K., Hofmeister, R., Muegge, K. & Durum, S.K. Withdrawal of IL-7 induces Bax translocation from cytosol to mitochondria through a rise in intracellular pH. Proc. Natl. Acad. Sci. USA 96, 14476-14481 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14476-14481
    • Khaled, A.R.1    Kim, K.2    Hofmeister, R.3    Muegge, K.4    Durum, S.K.5
  • 18
    • 0033104996 scopus 로고    scopus 로고
    • The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
    • Puthalalath, G., Huang, D.C.S., O'Reilly, L.A., King, S.M. & Strasser, A. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. Mol. Cell 3, 287-296 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 287-296
    • Puthalalath, G.1    Huang, D.C.S.2    O'Reilly, L.A.3    King, S.M.4    Strasser, A.5
  • 19
    • 0033120591 scopus 로고    scopus 로고
    • Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A
    • Harada, H. et al. Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A. Mol. Cell 3, 413-422 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 413-422
    • Harada, H.1
  • 20
    • 0033537768 scopus 로고    scopus 로고
    • Ca2+-induced apoptosis through calcineurin dephosphorylation of Bad
    • Wang, H.G. et al. Ca2+-induced apoptosis through calcineurin dephosphorylation of Bad. Science 284, 339-343 (1999).
    • (1999) Science , vol.284 , pp. 339-343
    • Wang, H.G.1
  • 21
    • 0033607006 scopus 로고    scopus 로고
    • Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis
    • Yin, X.-M. et al. Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis. Nature 400, 886-891 (1999).
    • (1999) Nature , vol.400 , pp. 886-891
    • Yin, X.-M.1
  • 22
    • 0033597785 scopus 로고    scopus 로고
    • Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c
    • Kirsch, D.G. et al. Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c. J. Biol. Chem. 274, 21155-21161 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 21155-21161
    • Kirsch, D.G.1
  • 23
    • 0034614658 scopus 로고    scopus 로고
    • Translocation of SAPK/JNK to mitochondria and interaction with Bel-XL in response to DNA damage
    • Kharbanda, S. et al. Translocation of SAPK/JNK to mitochondria and interaction with Bel-XL in response to DNA damage. J. Biol. Chem. 275, 322-327 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 322-327
    • Kharbanda, S.1
  • 24
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton, M. The mitochondrial permeability transition pore and its role in cell death Biochem, J. 341, 233-249 (1999).
    • (1999) Biochem, J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 25
    • 0033570890 scopus 로고    scopus 로고
    • Apoptosis driven by IP3-linked mitochondrial calcium signals
    • Szalai, G., Krischnamurthy, R. & Hajnoczky, G. Apoptosis driven by IP3-linked mitochondrial calcium signals EMBO J. 18, 6349-6361 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6349-6361
    • Szalai, G.1    Krischnamurthy, R.2    Hajnoczky, G.3
  • 26
    • 0033575320 scopus 로고    scopus 로고
    • Ceramide induces Bcl-2 dephosphorylation via a mechanism involving mitochondrial PP2A
    • Ruvolo, P.R., Deng, X., Ito, T., Carr, B.K. & May, W.S. Ceramide induces Bcl-2 dephosphorylation via a mechanism involving mitochondrial PP2A. J. Biol. Chem. 274, 20296-20300 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 20296-20300
    • Ruvolo, P.R.1    Deng, X.2    Ito, T.3    Carr, B.K.4    May, W.S.5
  • 27
    • 0033529712 scopus 로고    scopus 로고
    • Commitment to apoptosis by CD3 ganglioside depends on opening of the mitochondrial permeability transition pore
    • Scorrano, L., Petronilli, V., Di Lisa, F. & Bernardi, P. Commitment to apoptosis by CD3 ganglioside depends on opening of the mitochondrial permeability transition pore. J. Biol. Chem. 274, 22581-22585 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22581-22585
    • Scorrano, L.1    Petronilli, V.2    Di Lisa, F.3    Bernardi, P.4
  • 28
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in mouse and man
    • Wallace, D.C. Mitochondrial diseases in mouse and man. Science 283, 1482-1488 (1999).
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 29
    • 0033615544 scopus 로고    scopus 로고
    • Mitochondrial nitrix-oxide synthase stimulation causes cytochrome c release from isolated mitochondrai -evidence for intramitochondrial peroxynitrite formation
    • Ghafourifar, P., Schenk, U., Klein, S.D. & Richter, C. Mitochondrial nitrix-oxide synthase stimulation causes cytochrome c release from isolated mitochondrai -Evidence for intramitochondrial peroxynitrite formation. J. Biol. Chem. 274, 31185-31188 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31185-31188
    • Ghafourifar, P.1    Schenk, U.2    Klein, S.D.3    Richter, C.4
  • 30
    • 0032587982 scopus 로고    scopus 로고
    • Bcl-XL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange
    • Van der Heiden, M., Chandel, N.S., Schumacker, P.T. & Thompson, C.B. Bcl-XL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. Mol. Cell 3, 159-167 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 159-167
    • Van Der Heiden, M.1    Chandel, N.S.2    Schumacker, P.T.3    Thompson, C.B.4
  • 31
    • 0034688175 scopus 로고    scopus 로고
    • Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator
    • Brenner, C. et al. Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator. Oncogene 19, 329-336 (2000).
    • (2000) Oncogene , vol.19 , pp. 329-336
    • Brenner, C.1
  • 32
    • 13044276250 scopus 로고    scopus 로고
    • A cytomegalovirus-encoded mitochondria-localized inhibitor of apoptosis structurally unrelated to Bcl-2
    • Goldmacher, V.S. et al. A cytomegalovirus-encoded mitochondria-localized inhibitor of apoptosis structurally unrelated to Bcl-2. Proc. Natl. Acad. Sci. USA 96, 12536-12541 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12536-12541
    • Goldmacher, V.S.1
  • 33
    • 0034598337 scopus 로고    scopus 로고
    • The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore
    • Jacotot, E. et al. The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore. J. Exp. Med. 191, 33-45 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 33-45
    • Jacotot, E.1
  • 34
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu, S., Narita, M. & Tsujimoto, Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399, 483-487 (1999).
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 35
    • 0032487583 scopus 로고    scopus 로고
    • Bax-induced cytochrome c release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions
    • Eskes, R. et al. Bax-induced cytochrome c release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions. J. Cell Biol. 143, 217-224 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 217-224
    • Eskes, R.1
  • 36
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes, R., Desagher, S., Antonsson, B. & Martinou, J.C. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol. Cell. Biol. 20, 929-935 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 37
    • 0032550363 scopus 로고    scopus 로고
    • The permeability transition pore complex: A target for apoptosis regulation by caspases and Bcl-2 related proteins
    • Marzo, I. et al. The permeability transition pore complex: a target for apoptosis regulation by caspases and Bcl-2 related proteins. J. Exp. Med. 187, 1261-1271 (1998).
    • (1998) J. Exp. Med. , vol.187 , pp. 1261-1271
    • Marzo, I.1
  • 38
    • 0032831667 scopus 로고    scopus 로고
    • Calcium induced release of mitochondrial cytochrome c by different mechanisms selective for brain versus liver
    • Andreyev, A. & Fiskum, G. Calcium induced release of mitochondrial cytochrome c by different mechanisms selective for brain versus liver. Cell Death Differ 6, 825-832 (1999).
    • (1999) Cell Death Differ , vol.6 , pp. 825-832
    • Andreyev, A.1    Fiskum, G.2
  • 39
    • 0033579810 scopus 로고    scopus 로고
    • Mitochondrial release of caspases-2 and -9 during the apoptotic process
    • Susin, S.A. et al. Mitochondrial release of caspases-2 and -9 during the apoptotic process. J. Exp. Med. 189, 381-394 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 381-394
    • Susin, S.A.1
  • 40
    • 13044305983 scopus 로고    scopus 로고
    • Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia
    • Krajewski, S. et al. Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia. Proc. Natl. Acad. Sci. USA 96, 5752-5757 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5752-5757
    • Krajewski, S.1
  • 43
    • 0034016574 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins released from mitochondria undergoing permeability transition
    • Patterson, S. et al. Mass spectrometric identification of proteins released from mitochondria undergoing permeability transition. Cell Death Differ. 7, 137-144 (2000).
    • (2000) Cell Death Differ. , vol.7 , pp. 137-144
    • Patterson, S.1
  • 44
    • 0032860116 scopus 로고    scopus 로고
    • Cyclosporin A and its nonimmunosuppressive analogue N-Me-Val-4-cyclosporin A mitigate glucose/oxygen deprivation-induced damage to rat cultured hippocampal neurons
    • Khaspekov, L., Friberg, H., Halestrap, A., Viktorov, I. & Wieloch, T. Cyclosporin A and its nonimmunosuppressive analogue N-Me-Val-4-cyclosporin A mitigate glucose/oxygen deprivation-induced damage to rat cultured hippocampal neurons. Eur. J. Neurosci. 11, 3194-3198 (1999).
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 3194-3198
    • Khaspekov, L.1    Friberg, H.2    Halestrap, A.3    Viktorov, I.4    Wieloch, T.5
  • 45
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition and its role in reperfusion injury of the heart
    • Halestrup, A.P., Kerr, P.M., Javadov, S. & Woodfield, K.-Y. Elucidating the molecular mechanism of the permeability transition and its role in reperfusion injury of the heart. Biochim. Biohys. Acta 1366, 79-94 (1998).
    • (1998) Biochim. Biohys. Acta , vol.1366 , pp. 79-94
    • Halestrup, A.P.1    Kerr, P.M.2    Javadov, S.3    Woodfield, K.-Y.4
  • 46
    • 0032400374 scopus 로고    scopus 로고
    • Mitochondrial permeability transition during hypothermic to normothermic reperfusion in rat liver demonstrated by the protective effect of cyclosporin A
    • LeDucq, N. et al. Mitochondrial permeability transition during hypothermic to normothermic reperfusion in rat liver demonstrated by the protective effect of cyclosporin A. Biochem. J. 336, 501 -506 (1998).
    • (1998) Biochem. J. , vol.336 , pp. 501-506
    • LeDucq, N.1
  • 47
    • 0033612939 scopus 로고    scopus 로고
    • Posttreatment with the immunosuppressant cyclosporin A in transient focal ischemia
    • Yoshimoto, T. & Siesjo, B.K. Posttreatment with the immunosuppressant cyclosporin A in transient focal ischemia. Brain Res. 839, 283-291 (1999).
    • (1999) Brain Res. , vol.839 , pp. 283-291
    • Yoshimoto, T.1    Siesjo, B.K.2
  • 48
    • 0032906990 scopus 로고    scopus 로고
    • Mitochondrial permeability transition induced DNA-fragmentation in the rat hippocampus following hypoglycemia
    • Ferrand Drake, M., Friberg, H. & Wieloch, T. Mitochondrial permeability transition induced DNA-fragmentation in the rat hippocampus following hypoglycemia. Neuroscience 90, 1325-1338 (1999).
    • (1999) Neuroscience , vol.90 , pp. 1325-1338
    • Ferrand Drake, M.1    Friberg, H.2    Wieloch, T.3
  • 49
    • 0033525008 scopus 로고    scopus 로고
    • Cyclosporin A limits calcium-induced axonal damage following traumatic brain injury
    • Okonkwo, D.O., Buki, A., Siman, R. & Povlishock, J.T. Cyclosporin A limits calcium-induced axonal damage following traumatic brain injury. Neuroreport 10, 353-358 (1999).
    • (1999) Neuroreport , vol.10 , pp. 353-358
    • Okonkwo, D.O.1    Buki, A.2    Siman, R.3    Povlishock, J.T.4
  • 50
    • 0033199875 scopus 로고    scopus 로고
    • ATP-sensitive K+ channel openers prevent Ca2+ overload in rat cardiac mitochondria
    • Holmuhamedov, E.L., Wang, L.W. & Terzic, A. ATP-sensitive K+ channel openers prevent Ca2+ overload in rat cardiac mitochondria. J. Physiol. (London) 519, 347-360 (1999).
    • (1999) J. Physiol. (London) , vol.519 , pp. 347-360
    • Holmuhamedov, E.L.1    Wang, L.W.2    Terzic, A.3
  • 51
    • 0032951125 scopus 로고    scopus 로고
    • The parkinsonian neurotoxin MPP+ opens the mitochondrial permeability transition pore and releases cytochrome c in isolted mitochondria via an oxidative mechanism
    • Cassarino, D.S., Pars, J.K., Parker, W.D. & Bennett, J.P. The parkinsonian neurotoxin MPP+ opens the mitochondrial permeability transition pore and releases cytochrome c in isolted mitochondria via an oxidative mechanism. Biochim. Biophys. Acta 1453, 49-62 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1453 , pp. 49-62
    • Cassarino, D.S.1    Pars, J.K.2    Parker, W.D.3    Bennett, J.P.4
  • 52
    • 0032842038 scopus 로고    scopus 로고
    • Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: Implication for Parkinson's disease
    • Berman, S.B. & Hastings, T.G. Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: Implication for Parkinson's disease. J. Neurochem. 73, 1127-1137 (1999).
    • (1999) J. Neurochem. , vol.73 , pp. 1127-1137
    • Berman, S.B.1    Hastings, T.G.2
  • 53
    • 0032846812 scopus 로고    scopus 로고
    • Ursodeoxycholic acid prevents cytochrome c release in apoptosis by inhibiting mitochondrial membrane permeabilization and channel formation
    • Rodrigues, C.M.P. et al. Ursodeoxycholic acid prevents cytochrome c release in apoptosis by inhibiting mitochondrial membrane permeabilization and channel formation. Cell Death Differ. 6, 842-854 (1999).
    • (1999) Cell Death Differ. , vol.6 , pp. 842-854
    • Rodrigues, C.M.P.1
  • 54
    • 0032525819 scopus 로고    scopus 로고
    • A novel role for ursodeoxycholic acid in inhibiting apoptosis by modulating mitochondrial membrane perturbation
    • Rodrigues, C.M.P., Fan, G.S., Ma, X.M., Kren, B.T. & Steer, C.J. A novel role for ursodeoxycholic acid in inhibiting apoptosis by modulating mitochondrial membrane perturbation. J. Clin. Invest. 101, 2790-2799 (1998).
    • (1998) J. Clin. Invest. , vol.101 , pp. 2790-2799
    • Rodrigues, C.M.P.1    Fan, G.S.2    Ma, X.M.3    Kren, B.T.4    Steer, C.J.5
  • 55
    • 0032515108 scopus 로고    scopus 로고
    • Ursodeoxycholate protects against ethanol-induced liver mitochondrial injury
    • Tabouy, L. et al. Ursodeoxycholate protects against ethanol-induced liver mitochondrial injury. Life Sci. 63, 2259-2270 (1998).
    • (1998) Life Sci. , vol.63 , pp. 2259-2270
    • Tabouy, L.1
  • 56
    • 0033595684 scopus 로고    scopus 로고
    • Aging-dependent large accumulation of point mutations in the human mtDNA control region for replication
    • Michikawa, Y., Mazzucchelli, F., Bresolin, N., Scarlato, C. & Attardi, G. Aging-dependent large accumulation of point mutations in the human mtDNA control region for replication. Science 286, 774-779 (1999).
    • (1999) Science , vol.286 , pp. 774-779
    • Michikawa, Y.1    Mazzucchelli, F.2    Bresolin, N.3    Scarlato, C.4    Attardi, G.5
  • 57
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse, and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova, H. et al. Studies of human, mouse, and yeast homologues indicate a mitochondrial function for frataxin. Nature Gen. 16, 345-351 (1997).
    • (1997) Nature Gen. , vol.16 , pp. 345-351
    • Koutnikova, H.1
  • 58
    • 0032511186 scopus 로고    scopus 로고
    • Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease
    • Casari, G. et al. Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93, 973-983 (1998).
    • (1998) Cell , vol.93 , pp. 973-983
    • Casari, G.1
  • 59
    • 0032851595 scopus 로고    scopus 로고
    • Increased apoptosis of Huntingon disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization
    • Sawa, A. et al. Increased apoptosis of Huntingon disease lymphoblasts associated with repeat length-dependent mitochondrial depolarization. Nature Med. 5, 1194-1198 (1999).
    • (1999) Nature Med. , vol.5 , pp. 1194-1198
    • Sawa, A.1
  • 60
    • 0032475979 scopus 로고    scopus 로고
    • A ubiquinone-binding site regulates the mitochondrial permeability transition pore
    • Fontaine, E., Ichas, F. & Bernardi, P. A ubiquinone-binding site regulates the mitochondrial permeability transition pore. J. Biol. Chem. 273, 25734-25740 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 25734-25740
    • Fontaine, E.1    Ichas, F.2    Bernardi, P.3
  • 61
    • 0030756459 scopus 로고    scopus 로고
    • Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Kostic, V., Jackson-Lewis, V., de Bilbao, F., Dubois-Dauphin, M. & Przedborski, S. Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis. Science 277, 559-562 (1997).
    • (1997) Science , vol.277 , pp. 559-562
    • Kostic, V.1    Jackson-Lewis, V.2    De Bilbao, F.3    Dubois-Dauphin, M.4    Przedborski, S.5
  • 62
    • 0032555066 scopus 로고    scopus 로고
    • Coenzyme Q(10) administration increase brain mitochondrial concentrations and exerts neuroprotective effects
    • Matthews, R.T., Yang, L.C., Browne, S., Baik, M. & Beal, M.F. Coenzyme Q(10) administration increase brain mitochondrial concentrations and exerts neuroprotective effects. Proc. Natl. Acad. Sci. USA 95, 8892-8897 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8892-8897
    • Matthews, R.T.1    Yang, L.C.2    Browne, S.3    Baik, M.4    Beal, M.F.5
  • 63
    • 0033051815 scopus 로고    scopus 로고
    • Neuroprotective effects of creatine in a transgenic animal model of amyotrophic lateral sclerosis
    • Klivenyi, P. et al. Neuroprotective effects of creatine in a transgenic animal model of amyotrophic lateral sclerosis. Nature Med. 5, 347-350 (1999).
    • (1999) Nature Med. , vol.5 , pp. 347-350
    • Klivenyi, P.1
  • 64
    • 0343412780 scopus 로고    scopus 로고
    • Characterization of a silencer element and purification of a silencer protein that negatively regulates the human adenine nucleotide translocator 2 promoter
    • Barrath, P., Albert-Fournier, B., Luciakova, K. & Nelson, B.D. Characterization of a silencer element and purification of a silencer protein that negatively regulates the human adenine nucleotide translocator 2 promoter. J. Biol. Chem. 274, 3378-3384 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3378-3384
    • Barrath, P.1    Albert-Fournier, B.2    Luciakova, K.3    Nelson, B.D.4
  • 65
    • 0033611057 scopus 로고    scopus 로고
    • Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis
    • Bauer, M.K.A., Schubert, A., Rocks, O. & Grimm, S. Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis. J. Cell Biol. 147, 1493-1501 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1493-1501
    • Bauer, M.K.A.1    Schubert, A.2    Rocks, O.3    Grimm, S.4
  • 66
    • 0033585463 scopus 로고    scopus 로고
    • Hexokinase type II: A novel tumor-specific promoter for gene-targeted therapy differentially expressed and regulated in human cancer cells
    • Katabi, M.M., Chan, H.L.B, Karp, S. & Batist, C. Hexokinase type II: A novel tumor-specific promoter for gene-targeted therapy differentially expressed and regulated in human cancer cells. Hum. Gene Ther. 10, 155-164 (1999).
    • (1999) Hum. Gene Ther. , vol.10 , pp. 155-164
    • Katabi, M.M.1    Chan, H.L.B.2    Karp, S.3    Batist, C.4
  • 67
    • 0032729633 scopus 로고    scopus 로고
    • Mitochondrial gene mutation, but not large-scale deletion, is a feature of colorectal carcinomas with mitochondrial microsatellite instability
    • Habano, W., Sugai, T., Yoshida, T. & Nakamura, S. Mitochondrial gene mutation, but not large-scale deletion, is a feature of colorectal carcinomas with mitochondrial microsatellite instability. Int. J. Cancer 83, 625-629 (1999).
    • (1999) Int. J. Cancer , vol.83 , pp. 625-629
    • Habano, W.1    Sugai, T.2    Yoshida, T.3    Nakamura, S.4
  • 68
    • 0033198390 scopus 로고    scopus 로고
    • Apoptosis induction by a novel anti-prostate cancer compound, BMD188 (a fatty acid-containing hydroxamic acid), requires the mitochondrial respiratory chain
    • Joshi, B. et al. Apoptosis induction by a novel anti-prostate cancer compound, BMD188 (a fatty acid-containing hydroxamic acid), requires the mitochondrial respiratory chain. Cancer Res. 59, 4343-4355 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 4343-4355
    • Joshi, B.1
  • 69
    • 0032545386 scopus 로고    scopus 로고
    • Activation of mitochondria and release of mitochondrial apoptogenic factors by betulinic acid
    • Fulda, S. et al. Activation of mitochondria and release of mitochondrial apoptogenic factors by betulinic acid. J. Biol. Chem. 273, 33942-33948 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33942-33948
    • Fulda, S.1
  • 70
    • 0033594404 scopus 로고    scopus 로고
    • Lonidamine triggers apoptosis via a direct, Bcl-2-inhibited effect on the mitochondrial permeability transition pore
    • Ravagnan, L. et al. Lonidamine triggers apoptosis via a direct, Bcl-2-inhibited effect on the mitochondrial permeability transition pore. Oncogene 18, 2537-2546 (1999).
    • (1999) Oncogene , vol.18 , pp. 2537-2546
    • Ravagnan, L.1
  • 71
    • 17144448793 scopus 로고    scopus 로고
    • The novel retinoid 6-[3-(1-adamantyl)-4-hydroxyphenyl]-2-naphtalene carboxylic acid can trigger apoptosis through a mitochondrial pathway independent of the nucleus
    • Marchetti, P. et al. The novel retinoid 6-[3-(1-adamantyl)-4-hydroxyphenyl]-2-naphtalene carboxylic acid can trigger apoptosis through a mitochondrial pathway independent of the nucleus. Cancer Res. 54, 6257-6275 (1999).
    • (1999) Cancer Res. , vol.54 , pp. 6257-6275
    • Marchetti, P.1
  • 72
    • 0032773849 scopus 로고    scopus 로고
    • Early release of mitochondrial cytochrome c and expression of mitochondrial epitope 7A6 with a porphyrin-derived photosensitizer: Bcl-2 and Bcl-XL overexpression do not prevent early mitochondrial events but still depress caspase activity
    • Carthy, C.M. et al. Early release of mitochondrial cytochrome c and expression of mitochondrial epitope 7A6 with a porphyrin-derived photosensitizer: Bcl-2 and Bcl-XL overexpression do not prevent early mitochondrial events but still depress caspase activity. Lab. Invest. 79, 953-965 (1999).
    • (1999) Lab. Invest. , vol.79 , pp. 953-965
    • Carthy, C.M.1
  • 73
    • 0032535579 scopus 로고    scopus 로고
    • Light-induced photoactivation of hypericin affects the energy metabolism of human glioma cells by inhibiting hexokinase bound to mitochondria
    • Miccoli, L. et al. Light-induced photoactivation of hypericin affects the energy metabolism of human glioma cells by inhibiting hexokinase bound to mitochondria. Cancer Res. 58, 5777-5786 (1998).
    • (1998) Cancer Res. , vol.58 , pp. 5777-5786
    • Miccoli, L.1
  • 74
    • 0032819838 scopus 로고    scopus 로고
    • Anti-cancer activity of targeted pro-apoptotic peptides
    • Ellerby, H.M. et al. Anti-cancer activity of targeted pro-apoptotic peptides. Nature Med. 5, 1032-1038 (1999).
    • (1999) Nature Med. , vol.5 , pp. 1032-1038
    • Ellerby, H.M.1
  • 75
    • 0033531926 scopus 로고    scopus 로고
    • Bak BH3 peptides antagonize Bel-XL function and induce apoptosis through cytochrome c-independent activation of caspases
    • Holinger, E.P., Chittenden, T. & Lutz, R.J. Bak BH3 peptides antagonize Bel-XL function and induce apoptosis through cytochrome c-independent activation of caspases. J. Biol. Chem. 274, 13298-13304 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 13298-13304
    • Holinger, E.P.1    Chittenden, T.2    Lutz, R.J.3
  • 76
    • 0030803457 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegeneration
    • Cooper, J.M. & Schapira, A.H.V. Mitochondrial dysfunction in neurodegeneration. J. Bioenerg. Biomembr. 29, 175-183 (1997).
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 175-183
    • Cooper, J.M.1    Schapira, A.H.V.2
  • 77
    • 0031559896 scopus 로고    scopus 로고
    • Expression of Cu, Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells
    • Carri, M.T. et al. Expression of Cu, Zn Superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells. FEBS Lett. 414, 365-368 (1997).
    • (1997) FEBS Lett. , vol.414 , pp. 365-368
    • Carri, M.T.1
  • 78
    • 0031017696 scopus 로고    scopus 로고
    • Altered calcium homeostasis in cell transformed by mitochondria from individuals with Parkinson disease
    • Sheehan, J.P. et al. Altered calcium homeostasis in cell transformed by mitochondria from individuals with Parkinson disease. J. Neurochem. 68, 1221-1233 (1997).
    • (1997) J. Neurochem. , vol.68 , pp. 1221-1233
    • Sheehan, J.P.1
  • 79
    • 0032499885 scopus 로고    scopus 로고
    • Cyclosporin A increases resting mitochondrial membrane potential in SY5Y cells and reverses the depressed mitochondrial membrane potential of Alzheimer's disease cybrids
    • Cassarino, D.S., Swerdlow, R.H., Parks, J.K., Parker, W.D. & Bennett, J.P. Cyclosporin A increases resting mitochondrial membrane potential in SY5Y cells and reverses the depressed mitochondrial membrane potential of Alzheimer's disease cybrids. Biochem. Biophys. Res. Comm. 248, 168-173 (1998).
    • (1998) Biochem. Biophys. Res. Comm. , vol.248 , pp. 168-173
    • Cassarino, D.S.1    Swerdlow, R.H.2    Parks, J.K.3    Parker, W.D.4    Bennett, J.P.5
  • 80
    • 0033153450 scopus 로고    scopus 로고
    • Superoxide mediates the cell-death-enhancing action of presenilin-1 mutations
    • Guo, Q., Fu, W.M., Holtsberg, F.W., Steiner, S.M. & Mattson, M.P. Superoxide mediates the cell-death-enhancing action of presenilin-1 mutations. J. Neurosci. Res. 56, 457-470 (1999).
    • (1999) J. Neurosci. Res. , vol.56 , pp. 457-470
    • Guo, Q.1    Fu, W.M.2    Holtsberg, F.W.3    Steiner, S.M.4    Mattson, M.P.5
  • 81
    • 0033588019 scopus 로고    scopus 로고
    • Interaction of Alzheimer's presenilin-1 and presenilin-2 with Bcl-XL-A potential role in modulating the threshold of cell death
    • Passer, B.J., Pellegrini, L., Vito, P., Ganjei, J.K. & D'Adamio, L. Interaction of Alzheimer's presenilin-1 and presenilin-2 with Bcl-XL-A potential role in modulating the threshold of cell death. J. Biol. Chem. 274, 24007-24013 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24007-24013
    • Passer, B.J.1    Pellegrini, L.2    Vito, P.3    Ganjei, J.K.4    D'Adamio, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.