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Volumn 115, Issue 7, 2005, Pages 1828-1838

Inhibition of adenine nucleotide translocator pore function and protection against apoptosis in vivo by an HIV protease inhibitor

(24)  Weaver, Joel G R a,b,c   Tarze, Agathe d   Moffat, Tia C e   Lebras, Morgane d   Deniaud, Aurelien d   Brenner, Catherine d   Bren, Gary D b   Morin, Mario Y e   Phenix, Barbara N c   Dong, Li a,c   Jiang, Susan X f   Sim, Valerie L g   Zurakowski, Bogdan f   Lallier, Jessica e   Hardin, Heather b   Wettstein, Peter b   Van Heeswijk, Rolf P G c   Douen, Andre c   Kroemer, Romano T h   Hou, Sheng T f   more..

h SANOFI   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; NELFINAVIR; PROTEIN SUBUNIT; PROTEINASE INHIBITOR; RITONAVIR; STAPHYLOCOCCUS ENTEROTOXIN B;

EID: 22144498421     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI22954     Document Type: Article
Times cited : (83)

References (66)
  • 1
    • 0036022394 scopus 로고    scopus 로고
    • Modulation of apoptosis by HIV protease inhibitors
    • Phenix, B.N., Cooper, C., Owen, C., and Badley, A.D. 2002. Modulation of apoptosis by HIV protease inhibitors. Apoptosis. 7:295-312.
    • (2002) Apoptosis , vol.7 , pp. 295-312
    • Phenix, B.N.1    Cooper, C.2    Owen, C.3    Badley, A.D.4
  • 2
    • 0036791645 scopus 로고    scopus 로고
    • HIV protease inhibitor ritonavir induces cytotoxicity of human endothelial cells
    • Zhong, D.S., et al. 2002. HIV protease inhibitor ritonavir induces cytotoxicity of human endothelial cells. Arterioscler. Thromb. Vasc. Biol. 22:1560-1566.
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 1560-1566
    • Zhong, D.S.1
  • 3
    • 0036896223 scopus 로고    scopus 로고
    • Antitumor effect of the human immunodeficiency virus protease inhibitor ritonavir: Induction of tumor-cell apoptosis associated with perturbation of proteasomal proteolysis
    • Gaedicke, S., et al. 2002. Antitumor effect of the human immunodeficiency virus protease inhibitor ritonavir: induction of tumor-cell apoptosis associated with perturbation of proteasomal proteolysis. Cancer Res. 62:6901-6908.
    • (2002) Cancer Res. , vol.62 , pp. 6901-6908
    • Gaedicke, S.1
  • 4
    • 0037105651 scopus 로고    scopus 로고
    • The human immunodeficiency virus (HIV)-1 protease inhibitor saquinavir inhibits proteasome function and causes apoptosis and radiosensitization in non-HIV-associated human cancer cells
    • Pajonk, F., Himmelsbach, J., Riess, K., Sommer, A., and McBride, W.H. 2002. The human immunodeficiency virus (HIV)-1 protease inhibitor saquinavir inhibits proteasome function and causes apoptosis and radiosensitization in non-HIV-associated human cancer cells. Cancer Res. 62:5230-5235.
    • (2002) Cancer Res. , vol.62 , pp. 5230-5235
    • Pajonk, F.1    Himmelsbach, J.2    Riess, K.3    Sommer, A.4    McBride, W.H.5
  • 5
    • 0036100575 scopus 로고    scopus 로고
    • Effects of antiretroviral drugs on human immunodeficiency virus type 1-induced CD4(+) T-cell death
    • Estaquier, J., et al. 2002. Effects of antiretroviral drugs on human immunodeficiency virus type 1-induced CD4(+) T-cell death. J. Virol. 76:5966-5973.
    • (2002) J. Virol. , vol.76 , pp. 5966-5973
    • Estaquier, J.1
  • 6
    • 0031596167 scopus 로고    scopus 로고
    • Inhibition of interleukin-1beta-converting enzyme in human hematopoietic progenitor cells results in blockade of cytokine-mediated apoptosis and expansion of their proliferative potential
    • Sloand, E.M., Young, N.S., Sato, T., Kim, S., and Maciejewski, J.P. 1998. Inhibition of interleukin-1beta-converting enzyme in human hematopoietic progenitor cells results in blockade of cytokine-mediated apoptosis and expansion of their proliferative potential. Exp. Hematol. 26:1093-1099.
    • (1998) Exp. Hematol. , vol.26 , pp. 1093-1099
    • Sloand, E.M.1    Young, N.S.2    Sato, T.3    Kim, S.4    Maciejewski, J.P.5
  • 7
    • 0033504073 scopus 로고    scopus 로고
    • HIV-1 protease inhibitor ritonavir modulates susceptibility to apoptosis of uninfected T cells
    • Weichold, F.F., et al. 1999. HIV-1 protease inhibitor ritonavir modulates susceptibility to apoptosis of uninfected T cells. J. Hum. Virol. 2:261-269.
    • (1999) J. Hum. Virol. , vol.2 , pp. 261-269
    • Weichold, F.F.1
  • 8
    • 0033179343 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 protease inhibitor modulates activation of peripheral blood CD4(+) T cells and decreases their susceptibility to apoptosis in vitro and in vivo
    • Sloand, E.M., et al. 1999. Human immunodeficiency virus type 1 protease inhibitor modulates activation of peripheral blood CD4(+) T cells and decreases their susceptibility to apoptosis in vitro and in vivo. Blood. 94:1021-1027.
    • (1999) Blood , vol.94 , pp. 1021-1027
    • Sloand, E.M.1
  • 9
    • 0034667552 scopus 로고    scopus 로고
    • Protease inhibitors stimulate hematopoiesis and decrease apoptosis and ICE expression in CD34(+) cells
    • Sloand, E.M., et al. 2000. Protease inhibitors stimulate hematopoiesis and decrease apoptosis and ICE expression in CD34(+) cells. Blood. 96:2735-2739.
    • (2000) Blood , vol.96 , pp. 2735-2739
    • Sloand, E.M.1
  • 10
    • 0642345201 scopus 로고    scopus 로고
    • Anti-apoptotic effect of HIV protease inhibitors via direct inhibition of calpain
    • Ghibelli, L., et al. 2003. Anti-apoptotic effect of HIV protease inhibitors via direct inhibition of calpain. Biochem. Pharmacol. 66:1505-1512.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1505-1512
    • Ghibelli, L.1
  • 11
    • 0035883068 scopus 로고    scopus 로고
    • Anti-apoptotic mechanism of HIV protease inhibitors: Preventing mitochondrial transmembrane potential loss
    • Phenix, B.N., Lum, J.J., Nie, Z., Sanchez-Dardon, J., and Badley, A.D. 2001. Anti-apoptotic mechanism of HIV protease inhibitors: preventing mitochondrial transmembrane potential loss. Blood. 98:1078-1085.
    • (2001) Blood , vol.98 , pp. 1078-1085
    • Phenix, B.N.1    Lum, J.J.2    Nie, Z.3    Sanchez-Dardon, J.4    Badley, A.D.5
  • 12
    • 0038620230 scopus 로고    scopus 로고
    • Mitochondrial membrane hyperpolarization hijacks activated T lymphocytes toward the apoptotic-prone phenotype: Homeostatic mechanisms of HIV protease inhibitors
    • Matarrese, P., et al. 2003. Mitochondrial membrane hyperpolarization hijacks activated T lymphocytes toward the apoptotic-prone phenotype: homeostatic mechanisms of HIV protease inhibitors. J. Immunol. 170:6006-6015.
    • (2003) J. Immunol. , vol.170 , pp. 6006-6015
    • Matarrese, P.1
  • 13
    • 0037169169 scopus 로고    scopus 로고
    • Different degree of immune recovery using antiretroviral regimens with protease inhibitors or non-nucleosides
    • Barreiro, P., Soriano, V., Casas, E., and Gonzalez-Lahoz, J. 2002. Different degree of immune recovery using antiretroviral regimens with protease inhibitors or non-nucleosides. AIDS. 16:245-249.
    • (2002) AIDS , vol.16 , pp. 245-249
    • Barreiro, P.1    Soriano, V.2    Casas, E.3    Gonzalez-Lahoz, J.4
  • 14
    • 0036932757 scopus 로고    scopus 로고
    • Differences in cellular activation and apoptosis in HIV-infected patients receiving protease inhibitors or nonnucleoside reverse transcriptase inhibitors
    • Benito, J.M., et al. 2002. Differences in cellular activation and apoptosis in HIV-infected patients receiving protease inhibitors or nonnucleoside reverse transcriptase inhibitors. AIDS Res. Hum. Retroviruses. 18:1379-1388.
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , pp. 1379-1388
    • Benito, J.M.1
  • 15
    • 0035050209 scopus 로고    scopus 로고
    • Comparative CD4 T-cell responses of reverse transcriptase inhibitor therapy with or without nelfinavit matched for viral exposure
    • Kravcik, S., et al. 2001. Comparative CD4 T-cell responses of reverse transcriptase inhibitor therapy with or without nelfinavit matched for viral exposure. HIV Clin. Trials. 2:160-170.
    • (2001) HIV Clin. Trials , vol.2 , pp. 160-170
    • Kravcik, S.1
  • 16
    • 10744229823 scopus 로고    scopus 로고
    • Immune reconstitution is comparable in antiretroviral-naive subjects after 1 year of successful therapy with a nucleoside reverse-transcriptase inhibitor- or protease inhibitor-containing antiretroviral regimen
    • Landay, A.L., et al. 2003. Immune reconstitution is comparable in antiretroviral-naive subjects after 1 year of successful therapy with a nucleoside reverse-transcriptase inhibitor- or protease inhibitor-containing antiretroviral regimen. J. Infect. Dis. 188:1444-1454.
    • (2003) J. Infect. Dis. , vol.188 , pp. 1444-1454
    • Landay, A.L.1
  • 17
    • 0346025675 scopus 로고    scopus 로고
    • Pharmacological and therapeutic properties of ritonavir-boosted protease inhibitor therapy in HIV-infected patients
    • Zeldin, R.K., and Petruschke, R.A. 2004. Pharmacological and therapeutic properties of ritonavir-boosted protease inhibitor therapy in HIV-infected patients. J. Antimicrob. Chemother. 53:4-9.
    • (2004) J. Antimicrob. Chemother. , vol.53 , pp. 4-9
    • Zeldin, R.K.1    Petruschke, R.A.2
  • 18
    • 0038610713 scopus 로고    scopus 로고
    • Caspase 8 small interfering RNA prevents acute liver failure in mice
    • Zender, L., et al. 2003. Caspase 8 small interfering RNA prevents acute liver failure in mice. Proc. Natl. Acad. Sci. U. S. A. 100:7797-7802.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7797-7802
    • Zender, L.1
  • 19
    • 0037348329 scopus 로고    scopus 로고
    • RNA interference targeting Fas protects mice from fulminant hepatitis
    • Song, E., et al. 2003. RNA interference targeting Fas protects mice from fulminant hepatitis. Nat. Med. 9:347-351.
    • (2003) Nat. Med. , vol.9 , pp. 347-351
    • Song, E.1
  • 20
    • 0035854780 scopus 로고    scopus 로고
    • Interleukin-6 protects against Fas-mediated death by establishing a critical level of anti-apoptotic hepatic proteins FLIP, Bcl-2, and Bcl-xL
    • Kovalovich, K., et al. 2001. Interleukin-6 protects against Fas-mediated death by establishing a critical level of anti-apoptotic hepatic proteins FLIP, Bcl-2, and Bcl-xL J. Biol. Chem. 276:26605-26613.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26605-26613
    • Kovalovich, K.1
  • 21
    • 0028943136 scopus 로고
    • Murine CD8+ T cells that specifically delete autologous CD4+ T cells expressing V beta 8 TCR: A role of the Qa-1 molecule
    • Jiang, H., et al. 1995. Murine CD8+ T cells that specifically delete autologous CD4+ T cells expressing V beta 8 TCR: a role of the Qa-1 molecule. Immunity. 2:185-194.
    • (1995) Immunity , vol.2 , pp. 185-194
    • Jiang, H.1
  • 22
    • 0026596020 scopus 로고
    • T cell-mediated lethal shock triggered in mice by the superantigen staphylococcal enterotoxin B: Critical role of tumor necrosis factor
    • Miethke, T., et al. 1992. T cell-mediated lethal shock triggered in mice by the superantigen staphylococcal enterotoxin B: critical role of tumor necrosis factor. J. Exp. Med. 175:91-98.
    • (1992) J. Exp. Med. , vol.175 , pp. 91-98
    • Miethke, T.1
  • 23
    • 0029112465 scopus 로고
    • Protective effect of granulocyte colony-stimulating factor against T-cell-meditated lethal shock triggered by superantigens
    • Aoki, Y., et al. 1995. Protective effect of granulocyte colony-stimulating factor against T-cell-meditated lethal shock triggered by superantigens. Blood. 86:1420-1427.
    • (1995) Blood , vol.86 , pp. 1420-1427
    • Aoki, Y.1
  • 24
    • 0026697724 scopus 로고
    • NeuN, a neuronal specific nuclear protein in vertebrates
    • Mullen, R.J., Buck, C.R., and Smith, A.M. 1992. NeuN, a neuronal specific nuclear protein in vertebrates. Development. 116:201-211.
    • (1992) Development , vol.116 , pp. 201-211
    • Mullen, R.J.1    Buck, C.R.2    Smith, A.M.3
  • 25
    • 0034724791 scopus 로고    scopus 로고
    • Neurological impairment in rats after transient middle cerebral artery occlusion: A comparative study under various treatment paradigms
    • Zausinger, S., Hungerhuber, E., Baethmann, A., Reulen, H., and Schmid-Elsaesser, R. 2000. Neurological impairment in rats after transient middle cerebral artery occlusion: a comparative study under various treatment paradigms. Brain Res. 863:94-105.
    • (2000) Brain Res. , vol.863 , pp. 94-105
    • Zausinger, S.1    Hungerhuber, E.2    Baethmann, A.3    Reulen, H.4    Schmid-Elsaesser, R.5
  • 26
    • 0346366987 scopus 로고    scopus 로고
    • Nasal vaccination with myelin oligodendrocyte glycoprotein reduces stroke size by inducing IL-10-producing CD4+ T cells
    • Frenkel, D., et al. 2003. Nasal vaccination with myelin oligodendrocyte glycoprotein reduces stroke size by inducing IL-10-producing CD4+ T cells. J. Immunol. 171:6549-6555.
    • (2003) J. Immunol. , vol.171 , pp. 6549-6555
    • Frenkel, D.1
  • 28
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami, N., and Kroemer, G. 2001. The mitochondrion in apoptosis: how Pandora's box opens. Nat. Rev. Mol. Cell Biol. 2:67-71.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 29
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou, H., Hanzel, W.J., Liu, X., Lutschg, A., and Wang, X. 1997. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell. 90:405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Hanzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 30
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou, H., Li, Y., Liu, X., and Wang, X. 1999. An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274:11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 31
  • 32
    • 0034520113 scopus 로고    scopus 로고
    • Permeabilization of the mitochondrial inner membrane during apoptosis: Impact of the adenine nucleotide translocator
    • Vieira, H.L.A., et al. 2000. Permeabilization of the mitochondrial inner membrane during apoptosis: impact of the adenine nucleotide translocator. Cell Death Differ. 7:1146-1154.
    • (2000) Cell Death Differ. , vol.7 , pp. 1146-1154
    • Vieira, H.L.A.1
  • 33
    • 0035910754 scopus 로고    scopus 로고
    • Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein rR and Bcl-2
    • Jacotot, E., et al. 2001. Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein rR and Bcl-2. J. Exp. Med. 193:509-519.
    • (2001) J. Exp. Med. , vol.193 , pp. 509-519
    • Jacotot, E.1
  • 34
    • 0041810128 scopus 로고    scopus 로고
    • The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death
    • Halestrap, A.P., and Brenner, C. 2003. The adenine nucleotide translocase: a central component of the mitochondrial permeability transition pore and key player in cell death. Curr. Med. Chem. 10:1507-1525.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1507-1525
    • Halestrap, A.P.1    Brenner, C.2
  • 35
    • 7944225778 scopus 로고    scopus 로고
    • Dynamic evolution of the adenine nucleotide translocase interactome during chemotherapy-induced apoptosis
    • Verrier, F., et al. 2004. Dynamic evolution of the adenine nucleotide translocase interactome during chemotherapy-induced apoptosis. Oncogene. 23:8049-8064.
    • (2004) Oncogene , vol.23 , pp. 8049-8064
    • Verrier, F.1
  • 36
    • 1642464737 scopus 로고    scopus 로고
    • Oxidative stress underlies the mechanisms for Ca2+-induced permeability transition of mitochondria
    • Kanno, T., et al. 2004. Oxidative stress underlies the mechanisms for Ca2+-induced permeability transition of mitochondria. Free Radic. Res. 38:27-35.
    • (2004) Free Radic. Res. , vol.38 , pp. 27-35
    • Kanno, T.1
  • 37
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • Halestrap, A.P., Woodfield, K.Y., and Connern, C.P. 1997. Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J. Biol. Chem. 272:3346-3354.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 38
    • 2342523174 scopus 로고    scopus 로고
    • Initiation of apoptotic signal by the peroxidation of cardiolipin of mitochondria
    • Nakagawa, Y. 2004. Initiation of apoptotic signal by the peroxidation of cardiolipin of mitochondria. Ann. N. Y. Acad. Sci. 1011:177-184.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1011 , pp. 177-184
    • Nakagawa, Y.1
  • 39
    • 0036494315 scopus 로고    scopus 로고
    • Peripheral benzodiazepine receptor ligands reverse apoptosis resistance of cancer cells in vitro and in vivo
    • Decaudin, D., et al. 2002. Peripheral benzodiazepine receptor ligands reverse apoptosis resistance of cancer cells in vitro and in vivo. Cancer Res. 62:1388-1393.
    • (2002) Cancer Res. , vol.62 , pp. 1388-1393
    • Decaudin, D.1
  • 40
    • 0032526746 scopus 로고    scopus 로고
    • PK11195, a ligand of the mitochondrial benzodiazepine receptor, facilitates the induction of apoptosis and reverses Bcl-2-mediated cytoprotection
    • Hirsch, T., et al. 1998. PK11195, a ligand of the mitochondrial benzodiazepine receptor, facilitates the induction of apoptosis and reverses Bcl-2-mediated cytoprotection. Exp. Cell Res. 241:426-434.
    • (1998) Exp. Cell Res. , vol.241 , pp. 426-434
    • Hirsch, T.1
  • 41
    • 0036792660 scopus 로고    scopus 로고
    • Mitochondrial permeability transition as a novel principle of hepatorenal toxicity in vivo
    • Haouzi, D., et al. 2002. Mitochondrial permeability transition as a novel principle of hepatorenal toxicity in vivo. Apoptosis. 7:395-405.
    • (2002) Apoptosis , vol.7 , pp. 395-405
    • Haouzi, D.1
  • 42
    • 0037428463 scopus 로고    scopus 로고
    • Mitochondrial outer membrane permeability change and hypersensitivity to digitonin early in staurosporine-induced apoptosis
    • Duan, S., et al. 2003. Mitochondrial outer membrane permeability change and hypersensitivity to digitonin early in staurosporine-induced apoptosis. J. Biol. Chem. 278:1346-1353.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1346-1353
    • Duan, S.1
  • 44
    • 0033927708 scopus 로고    scopus 로고
    • Purification and liposomal reconstitution of permeability transition pore complex
    • Brenner, C., Marzo, I., de Araujo Vieira, H.L., and Kroemer, G. 2000. Purification and liposomal reconstitution of permeability transition pore complex. Methods Enzymol. 322:243-252.
    • (2000) Methods Enzymol. , vol.322 , pp. 243-252
    • Brenner, C.1    Marzo, I.2    De Araujo Vieira, H.L.3    Kroemer, G.4
  • 45
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • Kokoszka, J.E., et al. 2004. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature. 427:461-465.
    • (2004) Nature , vol.427 , pp. 461-465
    • Kokoszka, J.E.1
  • 46
    • 4344707798 scopus 로고    scopus 로고
    • Mitochondrial permeability: Dual role for the ADP/ATP translocator?
    • Halestrap, A.P. 2004. Mitochondrial permeability: dual role for the ADP/ATP translocator? Nature. 430:984.
    • (2004) Nature , vol.430 , pp. 984
    • Halestrap, A.P.1
  • 47
    • 0036167816 scopus 로고    scopus 로고
    • International interlaboratory quality control program for measurement of antiretroviral drugs in plasma
    • Aarnoutse, R.E., et al. 2002. International interlaboratory quality control program for measurement of antiretroviral drugs in plasma. Antimicrob. Agents Chemother. 46:884-886.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 884-886
    • Aarnoutse, R.E.1
  • 48
    • 0034490822 scopus 로고    scopus 로고
    • Safety, tolerability, and antiretroviral effects of ritonavir- nelfinavir combination therapy administered for 48 weeks
    • Raines, C.P., et al. 2000. Safety, tolerability, and antiretroviral effects of ritonavir- nelfinavir combination therapy administered for 48 weeks. J. Acquir. Immune Defic. Syndr. 25:322-328.
    • (2000) J. Acquir. Immune Defic. Syndr. , vol.25 , pp. 322-328
    • Raines, C.P.1
  • 49
    • 0041335286 scopus 로고    scopus 로고
    • Absence of the transcription factor E2F1 attenuates brain injury and improves behavior after focal ischemia in mice
    • MacManus, J.P., et al. 2003. Absence of the transcription factor E2F1 attenuates brain injury and improves behavior after focal ischemia in mice. J. Cereb. Blood Flow Metab. 23:1020-1028.
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 1020-1028
    • MacManus, J.P.1
  • 50
    • 0033991698 scopus 로고    scopus 로고
    • Spectrophotometric measurement of experimental brain injury
    • Preston, E., and Webster, J. 2000. Spectrophotometric measurement of experimental brain injury. J. Neurosci. Methods. 94:187-192.
    • (2000) J. Neurosci. Methods , vol.94 , pp. 187-192
    • Preston, E.1    Webster, J.2
  • 51
    • 0037338153 scopus 로고    scopus 로고
    • Oligodendrocyte progenitor enrichment in the connexin32 null-mutant mouse
    • Melanson-Drapeau, L., et al. 2003. Oligodendrocyte progenitor enrichment in the connexin32 null-mutant mouse. J. Neurosci. 23:1759-1768.
    • (2003) J. Neurosci. , vol.23 , pp. 1759-1768
    • Melanson-Drapeau, L.1
  • 52
    • 0037385609 scopus 로고    scopus 로고
    • Ku70 suppresses the apoptotic translocation of Bax to mitochondria
    • Sawada, M., et al. 2003. Ku70 suppresses the apoptotic translocation of Bax to mitochondria. Nat. Cell Biol. 5:320-329.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 320-329
    • Sawada, M.1
  • 53
    • 0035853158 scopus 로고    scopus 로고
    • The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation
    • Forcet, C., et al. 2001. The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation. Proc. Natl. Acad. Sci. U. S. A. 98:3416-3421.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3416-3421
    • Forcet, C.1
  • 54
    • 0141669117 scopus 로고    scopus 로고
    • Protein kinase Calpha (PKCalpha) acts upstream of PKCtheta to activate IkappaB kinase and NF-kappaB in T lymphocytes
    • Trushin, S.A., et al. 2003. Protein kinase Calpha (PKCalpha) acts upstream of PKCtheta to activate IkappaB kinase and NF-kappaB in T lymphocytes. Mol. Cell. Biol. 23:7068-7081.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7068-7081
    • Trushin, S.A.1
  • 55
    • 0017101039 scopus 로고
    • Preparation of isolated rat liver cells
    • Seglen, P.O. 1976. Preparation of isolated rat liver cells. Methods Cell Biol. 13:29-83.
    • (1976) Methods Cell Biol. , vol.13 , pp. 29-83
    • Seglen, P.O.1
  • 56
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami, N., et al. 1995. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181:1661-1672.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1
  • 57
    • 0036848194 scopus 로고    scopus 로고
    • HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation
    • Nie, Z., et al. 2002. HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation. Cell Death Differ. 9:1172-1184.
    • (2002) Cell Death Differ. , vol.9 , pp. 1172-1184
    • Nie, Z.1
  • 59
    • 0027389308 scopus 로고
    • Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel
    • Blachly-Dyson, E., et al. 1993. Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel. J. Biol. Chem. 268:1835-1841.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1835-1841
    • Blachly-Dyson, E.1
  • 60
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson, E., Song, J., Wolfgang, W.J., Colombini, M., and Forte, M. 1997. Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein. Mol. Cell. Biol. 17:5727-5738.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5727-5738
    • Blachly-Dyson, E.1    Song, J.2    Wolfgang, W.J.3    Colombini, M.4    Forte, M.5
  • 61
    • 0025915949 scopus 로고
    • ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae
    • Drgon, T., Sabova, L., Nelson, N., and Kolarov, J. 1991. ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae. FEBS Lett. 289:159-162.
    • (1991) FEBS Lett. , vol.289 , pp. 159-162
    • Drgon, T.1    Sabova, L.2    Nelson, N.3    Kolarov, J.4
  • 62
    • 0029880071 scopus 로고    scopus 로고
    • Extracellular addition of a domain of HIV-1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death
    • Macreadie, I.G., Arunagiri, C.K., Hewish, D.R., White, J.F., and Azad, A.A. 1996. Extracellular addition of a domain of HIV-1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death. Mol. Microbiol. 19:1185-1192.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1185-1192
    • Macreadie, I.G.1    Arunagiri, C.K.2    Hewish, D.R.3    White, J.F.4    Azad, A.A.5
  • 63
    • 0032127416 scopus 로고    scopus 로고
    • The central role of the mitochondrial megachannel in apoptosis: Evidence obtained with intact cells, isolated mitochondria, and purified protein complexes
    • Marzo, I., Brenner, C., and Kroemer, G. 1998. The central role of the mitochondrial megachannel in apoptosis: evidence obtained with intact cells, isolated mitochondria, and purified protein complexes. Biomed. Pharmacother. 52:248-251.
    • (1998) Biomed. Pharmacother. , vol.52 , pp. 248-251
    • Marzo, I.1    Brenner, C.2    Kroemer, G.3
  • 64
    • 0037439801 scopus 로고    scopus 로고
    • Bcl-2 and Bax modulate adenine nucleotide translocase activity
    • Belzacq, A.S., et al. 2003. Bcl-2 and Bax modulate adenine nucleotide translocase activity. Cancer Res. 63:541-546.
    • (2003) Cancer Res. , vol.63 , pp. 541-546
    • Belzacq, A.S.1
  • 65
    • 0031181346 scopus 로고    scopus 로고
    • QXP: Powerful, rapid computer algorithms for structure-based drug design
    • McMartin, C., and Bohacek, R.S. 1997. QXP: powerful, rapid computer algorithms for structure-based drug design. J. Comput. Aided Mol. Des. 11:333-344.
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 333-344
    • McMartin, C.1    Bohacek, R.S.2
  • 66
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
    • Pebay-Peyroula, E., et al. 2003. Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature. 426:39-44.
    • (2003) Nature , vol.426 , pp. 39-44
    • Pebay-Peyroula, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.