메뉴 건너뛰기




Volumn 304, Issue 3, 2003, Pages 471-479

Redox regulation and signaling lipids in mitochondrial apoptosis

Author keywords

Apoptosis; Ceramide; Gangliosides; Glutathione; Necrosis; Reactive oxygen species

Indexed keywords

CHOLESTEROL; CYTOCHROME C; FAS LIGAND; GANGLIOSIDE GD3; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; GLYCOSPHINGOLIPID; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPID; MANGANESE SUPEROXIDE DISMUTASE; MITOCHONDRIAL PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN BAX; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STRESS ACTIVATED PROTEIN KINASE; THIOREDOXIN; THIOREDOXIN REDUCTASE; TRANSCRIPTION FACTOR; TRANSMEMBRANE CONDUCTANCE REGULATOR; TUMOR NECROSIS FACTOR; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0037427413     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00619-3     Document Type: Article
Times cited : (109)

References (85)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F.R., Willie A.H., Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Brit. J. Cancer. 26:1972;239-257.
    • (1972) Brit. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Willie, A.H.2    Currie, A.R.3
  • 2
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K.F., Kroemer G. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3:2001;E255-E263.
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 3
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 4
    • 0036308059 scopus 로고    scopus 로고
    • Mitochondria, the killer organelles and their weapons
    • Ravagnan L., Roumier T., Kroemer G. Mitochondria, the killer organelles and their weapons. J. Cell Physiol. 192:2002;131-137.
    • (2002) J. Cell Physiol. , vol.192 , pp. 131-137
    • Ravagnan, L.1    Roumier, T.2    Kroemer, G.3
  • 5
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X.S., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.S.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 6
    • 0037184910 scopus 로고    scopus 로고
    • Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis
    • Martín A.G., Fearnhead H.O. Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis. J. Biol. Chem. 277:2002;50834-50841.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50834-50841
    • Martín, A.G.1    Fearnhead, H.O.2
  • 7
    • 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., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 102:2000;33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 12
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic Dnase when released from mitochondria
    • Li L.Y., Luo X., Wang X. Endonuclease G is an apoptotic Dnase when released from mitochondria. Nature. 412:2001;95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 13
    • 0034682695 scopus 로고    scopus 로고
    • Apoptosis. Mitochondria - The death signal integrators
    • Brenner C., Kroemer G. Apoptosis. Mitochondria - the death signal integrators. Science. 289:2000;1150-1151.
    • (2000) Science , vol.289 , pp. 1150-1151
    • Brenner, C.1    Kroemer, G.2
  • 15
    • 0035229427 scopus 로고    scopus 로고
    • Mitochondria in apoptosis. How pandora's box opens
    • Zamzami N., Kroemer G. Mitochondria in apoptosis. How pandora's box opens. Nat. Rev. Mol. Cell Biol. 2:2001;67-71.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 18
    • 0037147199 scopus 로고    scopus 로고
    • Liver protection from apoptosis requires both blockade of initiator caspase activities and inhibition of ASK1/JNK pathway via GST regulation
    • Gilot D., Loyer P., Corlu A., Glaise D., Lagdic-Gossmann D., Atfi A., Morel F., Ichijo H., Guguen-Guillouzo C. Liver protection from apoptosis requires both blockade of initiator caspase activities and inhibition of ASK1/JNK pathway via GST regulation. J. Biol. Chem. 277:2002;49220-49229.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49220-49229
    • Gilot, D.1    Loyer, P.2    Corlu, A.3    Glaise, D.4    Lagdic-Gossmann, D.5    Atfi, A.6    Morel, F.7    Ichijo, H.8    Guguen-Guillouzo, C.9
  • 21
    • 0037205443 scopus 로고    scopus 로고
    • Diphenyleneiodonium triggers the efflux of glutathione from cultured cells
    • Pullar J.M., Hampton M.B. Diphenyleneiodonium triggers the efflux of glutathione from cultured cells. J. Biol. Chem. 277:2002;19402-19407.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19402-19407
    • Pullar, J.M.1    Hampton, M.B.2
  • 22
    • 0037424431 scopus 로고    scopus 로고
    • Role of reduced glutathione efflux in apoptosis of immortalized human keratinocytes induced by UVA
    • He Y.Y., Huang J.L., Ramírez D.C., Chignell C.F. Role of reduced glutathione efflux in apoptosis of immortalized human keratinocytes induced by UVA. J. Biol. Chem. 278:2003;8058-8064.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8058-8064
    • He, Y.Y.1    Huang, J.L.2    Ramírez, D.C.3    Chignell, C.F.4
  • 24
    • 0037008671 scopus 로고    scopus 로고
    • Glutathione levels and Bax activation during apoptosis due to oxidative stress in cells expressing wild type and mutant cystic fibrosis transmembrane conductance regulator
    • Jungas T., Motta I., Duffieux F., Fanan P., Stoven V., Ojcius D.M. Glutathione levels and Bax activation during apoptosis due to oxidative stress in cells expressing wild type and mutant cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277:2002;27912-27918.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27912-27918
    • Jungas, T.1    Motta, I.2    Duffieux, F.3    Fanan, P.4    Stoven, V.5    Ojcius, D.M.6
  • 25
    • 0036293621 scopus 로고    scopus 로고
    • Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-induced apoptosis in cultured mouse hepatocytes
    • Nagai H., Matsumura K., Feng G., Kaplowitz N. Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-induced apoptosis in cultured mouse hepatocytes. Hepatology. 36:2002;55-64.
    • (2002) Hepatology , vol.36 , pp. 55-64
    • Nagai, H.1    Matsumura, K.2    Feng, G.3    Kaplowitz, N.4
  • 27
    • 0037085261 scopus 로고    scopus 로고
    • Glutathione dependence of caspase-8 activation at the death-inducing signaling complex
    • Hentze H., Schmitz I., Latta M., Krueger A., Krammer P.H., Wendel A. Glutathione dependence of caspase-8 activation at the death-inducing signaling complex. J. Biol. Chem. 277:2002;5588-5595.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5588-5595
    • Hentze, H.1    Schmitz, I.2    Latta, M.3    Krueger, A.4    Krammer, P.H.5    Wendel, A.6
  • 28
    • 0033901357 scopus 로고    scopus 로고
    • Depletion of hepatic glutathione prevents death receptor-dependent apoptotic and necrotic liver injury in mice
    • Hentze H., Gantner F., Kolb S.A., Wendel A. Depletion of hepatic glutathione prevents death receptor-dependent apoptotic and necrotic liver injury in mice. Am. J. Pathol. 156:2000;2045-2056.
    • (2000) Am. J. Pathol. , vol.156 , pp. 2045-2056
    • Hentze, H.1    Gantner, F.2    Kolb, S.A.3    Wendel, A.4
  • 29
  • 30
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential consitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami N., Marchetti P., Castedo M., Zanin C., Vayssiere J.L., Petit P.X., Kroemer G. Reduction in mitochondrial potential consitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181:1995;1661-1672.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssiere, J.L.5    Petit, P.X.6    Kroemer, G.7
  • 31
    • 0032526940 scopus 로고    scopus 로고
    • The regulation of reactive oxygen species production during programmed cell death
    • Tan A.S., Sagara Y., Liu Y., Maher P., Schubert D. The regulation of reactive oxygen species production during programmed cell death. J. Cell Biol. 141:1998;1423-1432.
    • (1998) J. Cell Biol. , vol.141 , pp. 1423-1432
    • Tan, A.S.1    Sagara, Y.2    Liu, Y.3    Maher, P.4    Schubert, D.5
  • 32
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu Y., Fiskum G., Schubert D. Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 80:2002;780-787.
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 33
    • 0037421221 scopus 로고    scopus 로고
    • Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
    • Ricci J.E., Gottlieb R.A., Green D.R. Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis. J. Cell Biol. 160:2003;65-75.
    • (2003) J. Cell Biol. , vol.160 , pp. 65-75
    • Ricci, J.E.1    Gottlieb, R.A.2    Green, D.R.3
  • 34
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • Boveris A., Cadenas E., Stoppani A. Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 156:1976;435-444.
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.3
  • 35
    • 0028788763 scopus 로고
    • Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial GSH status in loss of mitochondrial function and activation of transcription factor NF-κB: Studies in isolated mitochondria and rat hepatocytes
    • Garcia-Ruiz C., Colell A., Morales A., Kaplowitz N., Fernández-Checa J.C. Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial GSH status in loss of mitochondrial function and activation of transcription factor NF-κB: studies in isolated mitochondria and rat hepatocytes. Mol. Pharmacol. 48:1995;825-834.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 825-834
    • Garcia-Ruiz, C.1    Colell, A.2    Morales, A.3    Kaplowitz, N.4    Fernández-Checa, J.C.5
  • 38
    • 0028868238 scopus 로고
    • Feeding S-adenosyl-L-methionine attenuates both ethanol-induced depletion of mitochondrial glutathione and mitochondrial dysfunction in periportal and perivenous rat hepatocytes
    • Garcia-Ruiz C., Morales A., Colell A., Ballesta A., Rodes J., Kaplowitz N., Fernandez-Checa J.C. Feeding S-adenosyl-L-methionine attenuates both ethanol-induced depletion of mitochondrial glutathione and mitochondrial dysfunction in periportal and perivenous rat hepatocytes. Hepatology. 21:1995;207-214.
    • (1995) Hepatology , vol.21 , pp. 207-214
    • Garcia-Ruiz, C.1    Morales, A.2    Colell, A.3    Ballesta, A.4    Rodes, J.5    Kaplowitz, N.6    Fernandez-Checa, J.C.7
  • 39
    • 0036673665 scopus 로고    scopus 로고
    • Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in HL60 cells that overexpress Bcl-2
    • Armstrong J.S., Jones D.P. Glutathione depletion enforces the mitochondrial permeability transition and causes cell death in HL60 cells that overexpress Bcl-2. FASEB J. 16:2002;1263-1265.
    • (2002) FASEB J. , vol.16 , pp. 1263-1265
    • Armstrong, J.S.1    Jones, D.P.2
  • 40
    • 0036279279 scopus 로고    scopus 로고
    • E2F1 and c-Myc potentiate apoptosis through inhibition of NF-kB activity that facilitates Mn-SOD mediated ROS elimination
    • Tanaka H., Matsumura I., Ezoe S., Satoh Y., Sakamaki T., Albanese C., Machii T., Pestell R.G., Kanakura Y. E2F1 and c-Myc potentiate apoptosis through inhibition of NF-kB activity that facilitates Mn-SOD mediated ROS elimination. Mol. Cell. 9:2002;1017-1029.
    • (2002) Mol. Cell , vol.9 , pp. 1017-1029
    • Tanaka, H.1    Matsumura, I.2    Ezoe, S.3    Satoh, Y.4    Sakamaki, T.5    Albanese, C.6    Machii, T.7    Pestell, R.G.8    Kanakura, Y.9
  • 43
    • 0034642510 scopus 로고    scopus 로고
    • Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis
    • Costantini P., Belzacq A.S., Vieira H.L.A., Larochette N., de Pablo M., Zamzami N., Susin S.A., Brenner C., Kroemer G. Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene. 19:2000;307-314.
    • (2000) Oncogene , vol.19 , pp. 307-314
    • Costantini, P.1    Belzacq, A.S.2    Vieira, H.L.A.3    Larochette, N.4    De Pablo, M.5    Zamzami, N.6    Susin, S.A.7    Brenner, C.8    Kroemer, G.9
  • 44
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • Madesh M., Hajnoczky G. VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. J. Cell Biol. 155:2001;1003-1015.
    • (2001) J. Cell Biol. , vol.155 , pp. 1003-1015
    • Madesh, M.1    Hajnoczky, G.2
  • 47
    • 0034015563 scopus 로고    scopus 로고
    • Ethanol potentiates tumor necrosis factor cytotoxicity in hepatoma cells and primary rat hepatocytes by promoting induction of the mitochondrial permeability transition
    • Pastorino J., Hoek J.B. Ethanol potentiates tumor necrosis factor cytotoxicity in hepatoma cells and primary rat hepatocytes by promoting induction of the mitochondrial permeability transition. Hepatology. 31:2000;1141-1152.
    • (2000) Hepatology , vol.31 , pp. 1141-1152
    • Pastorino, J.1    Hoek, J.B.2
  • 48
    • 0034761961 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid protects hepatocytes from ethanol-fed rats against tumor necrosis factor-induced cell death by replenishing mitochondrial glutathione
    • Colell A., Coll O., García-Ruiz C., Paris R., Tiribelli C., Kaplowitz N., Fernández-Checa J.C. Tauroursodeoxycholic acid protects hepatocytes from ethanol-fed rats against tumor necrosis factor-induced cell death by replenishing mitochondrial glutathione. Hepatology. 34:2001;964-971.
    • (2001) Hepatology , vol.34 , pp. 964-971
    • Colell, A.1    Coll, O.2    García-Ruiz, C.3    Paris, R.4    Tiribelli, C.5    Kaplowitz, N.6    Fernández-Checa, J.C.7
  • 49
    • 0036827706 scopus 로고    scopus 로고
    • Protection of NRK-52E cells, a rat renal proximal tubular cell line, from chemical-induced apoptosis by overexpression of a mitochondrial glutathione transporter
    • Lash L.H., Putt D.A., Matherly Protection of NRK-52E cells, a rat renal proximal tubular cell line, from chemical-induced apoptosis by overexpression of a mitochondrial glutathione transporter. J. Pharm. Exp. Ther. 303:2002;476-486.
    • (2002) J. Pharm. Exp. Ther. , vol.303 , pp. 476-486
    • Lash, L.H.1    Putt, D.A.2    Matherly3
  • 50
    • 0037033039 scopus 로고    scopus 로고
    • Superoxide activates mitochondrial uncoupling protein 2 from the matrix side: Studies using targeted antioxidants
    • Echtay K.S., Murphy M.P., Smith R.A.J., Talbot D.A., Brand M.D. Superoxide activates mitochondrial uncoupling protein 2 from the matrix side: studies using targeted antioxidants. J. Biol. Chem. 277:2002;47129-47135.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47129-47135
    • Echtay, K.S.1    Murphy, M.P.2    Smith, R.A.J.3    Talbot, D.A.4    Brand, M.D.5
  • 52
    • 18744374204 scopus 로고    scopus 로고
    • The proapoptotic Bcl2 family member tBid localizes to mitochondrial contact sites
    • M. Lutter, G.A. Perkins, X. Wang, The proapoptotic Bcl2 family member tBid localizes to mitochondrial contact sites. BMC Cell Biol. Available from http://www.biomedcentral.com/1471-2121/2/22, 2002.
    • (2002) BMC Cell Biol
    • Lutter, M.1    Perkins, G.A.2    Wang, X.3
  • 54
    • 0028229899 scopus 로고
    • Effect of chronic ethanol feeding on glutathione and functional integrity of mitochondria in periportal and perivenous rat hepatocytes
    • García-Ruiz C., Morales A., Ballesta A., Rodés J., Kaplowitz N., Fernández-Checa J.C. Effect of chronic ethanol feeding on glutathione and functional integrity of mitochondria in periportal and perivenous rat hepatocytes. J. Clin Invest. 94:1994;193-201.
    • (1994) J. Clin Invest. , vol.94 , pp. 193-201
    • García-Ruiz, C.1    Morales, A.2    Ballesta, A.3    Rodés, J.4    Kaplowitz, N.5    Fernández-Checa, J.C.6
  • 55
    • 0030819482 scopus 로고    scopus 로고
    • Transport of reduced glutathione in hepatic mitochondria and mitoplasts from ethanol-fed rats: Effect of membrane physical properties and S-adenosyl-L-methionine
    • Colell A., García-Ruiz C., Morales A., Ballesta A., Ookhtens M., Rodés J., Kaplowitz N., Fernández-Checa J.C. Transport of reduced glutathione in hepatic mitochondria and mitoplasts from ethanol-fed rats: effect of membrane physical properties and S-adenosyl-L-methionine. Hepatology. 26:1997;699-708.
    • (1997) Hepatology , vol.26 , pp. 699-708
    • Colell, A.1    García-Ruiz, C.2    Morales, A.3    Ballesta, A.4    Ookhtens, M.5    Rodés, J.6    Kaplowitz, N.7    Fernández-Checa, J.C.8
  • 57
    • 0036891947 scopus 로고    scopus 로고
    • Effects of ethanol dose and ethanol withdrawal on rat liver mitochondrial glutathione: Implication of potentiated acetaminophen toxicity in alcoholics
    • Zhao P., Slattery J.T. Effects of ethanol dose and ethanol withdrawal on rat liver mitochondrial glutathione: implication of potentiated acetaminophen toxicity in alcoholics. Drug Met. Disp. 30:2002;1413-1417.
    • (2002) Drug Met. Disp. , vol.30 , pp. 1413-1417
    • Zhao, P.1    Slattery, J.T.2
  • 58
    • 0036024260 scopus 로고    scopus 로고
    • S-Adenosyl-L-methionine and mitochondrial reduced glutathione depletion in alcoholic liver disease
    • Fernandez-Checa J.C., Colell A., Garcia-Ruiz C. S-Adenosyl-L-methionine and mitochondrial reduced glutathione depletion in alcoholic liver disease. Alcohol. 27:2002;179-183.
    • (2002) Alcohol , vol.27 , pp. 179-183
    • Fernandez-Checa, J.C.1    Colell, A.2    Garcia-Ruiz, C.3
  • 59
    • 0037370152 scopus 로고    scopus 로고
    • Acetaldehyde impairs the mitochondrial glutathione transport in HepG2 cells through endoplasmic reticulum stress
    • Lluis J.M., Colell A., García-Ruiz C., Kaplowitz N., Fernández-Checa J.C. Acetaldehyde impairs the mitochondrial glutathione transport in HepG2 cells through endoplasmic reticulum stress. Gastroenterology. 124:2003;708-724.
    • (2003) Gastroenterology , vol.124 , pp. 708-724
    • Lluis, J.M.1    Colell, A.2    García-Ruiz, C.3    Kaplowitz, N.4    Fernández-Checa, J.C.5
  • 60
    • 0036312001 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization
    • Boya P., Cohen I., Zamzami N., Vieira H.L., Kroemer G. Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization. Cell Death Differ. 9:2002;465-467.
    • (2002) Cell Death Differ , vol.9 , pp. 465-467
    • Boya, P.1    Cohen, I.2    Zamzami, N.3    Vieira, H.L.4    Kroemer, G.5
  • 61
    • 0034091417 scopus 로고    scopus 로고
    • StARTint to understand cholesterol transfer
    • Stocco D.M. StARTint to understand cholesterol transfer. Nat. Struct. Biol. 7:2000;445-447.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 445-447
    • Stocco, D.M.1
  • 63
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition
    • Li H., Yao Z., Degenhardt B., Teper G., Papadopoulos V. Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition. Proc. Natl. Acad. Sci. USA. 98:2001;1267-1272.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1267-1272
    • Li, H.1    Yao, Z.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 64
    • 0033974782 scopus 로고    scopus 로고
    • Ceramide in the eukaryotic stress response
    • Hannun Y.A., Luberto C. Ceramide in the eukaryotic stress response. Trends Cell Biol. 10:2000;73-80.
    • (2000) Trends Cell Biol. , vol.10 , pp. 73-80
    • Hannun, Y.A.1    Luberto, C.2
  • 65
    • 0034708455 scopus 로고    scopus 로고
    • CD95 (Fas/APO-1) signals ceramide generation independent of the effector stage of apoptosis
    • Grullich C., Sullards M.C., Fucks Z., Merrill A.H. Jr., Kolesnick R. CD95 (Fas/APO-1) signals ceramide generation independent of the effector stage of apoptosis. J. Biol. Chem. 275:2000;8650-8656.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8650-8656
    • Grullich, C.1    Sullards, M.C.2    Fucks, Z.3    Merrill A.H., Jr.4    Kolesnick, R.5
  • 66
    • 1842330849 scopus 로고    scopus 로고
    • Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione
    • Garcia-Ruiz C., Colell A., Mari M., Morales M., Fernández-Checa J.C. Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione. J. Biol. Chem. 272:1997;11369-11377.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11369-11377
    • Garcia-Ruiz, C.1    Colell, A.2    Mari, M.3    Morales, M.4    Fernández-Checa, J.C.5
  • 67
    • 0030856714 scopus 로고    scopus 로고
    • Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide
    • Gudz T.I., Tserng K.Y., Hoppel C.L. Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide. J. Biol. Chem. 272:1997;24154-24158.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24154-24158
    • Gudz, T.I.1    Tserng, K.Y.2    Hoppel, C.L.3
  • 68
    • 1842375100 scopus 로고    scopus 로고
    • Implications of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis
    • Quillet-Mary A. Implications of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J. Biol. Chem. 272:1997;21388-21395.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21388-21395
    • Quillet-Mary, A.1
  • 69
    • 0033525685 scopus 로고    scopus 로고
    • Ceramide induces cytochrome c release from isolated mitochondria. Importance of mitochondrial redox state
    • Gharourifar P. Ceramide induces cytochrome c release from isolated mitochondria. Importance of mitochondrial redox state. J. Biol. Chem. 274:1999;6080-6084.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6080-6084
    • Gharourifar, P.1
  • 70
    • 0031919157 scopus 로고    scopus 로고
    • Regulation of ceramide production and apoptosis
    • Kolesnick R.N., Kronke M. Regulation of ceramide production and apoptosis. Annu. Rev. Physiol. 60:1998;643-665.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 643-665
    • Kolesnick, R.N.1    Kronke, M.2
  • 71
    • 0037201936 scopus 로고    scopus 로고
    • Role of sphingomyelinase and ceramide in modulating rafts: Do biophysical properties determine biologic outcome?
    • Cremesti A.E., Goñi F.M., Kolesnick R.N. Role of sphingomyelinase and ceramide in modulating rafts: do biophysical properties determine biologic outcome? FEBS Lett. 531:2002;47-53.
    • (2002) FEBS Lett. , vol.531 , pp. 47-53
    • Cremesti, A.E.1    Goñi, F.M.2    Kolesnick, R.N.3
  • 72
    • 0035199418 scopus 로고    scopus 로고
    • Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis
    • Birbes H., Bawab S.E., Hannun Y.A., Obeid L.M. Selective hydrolysis of a mitochondrial pool of sphingomyelin induces apoptosis. FASEB J. 14:2001;2669-2679.
    • (2001) FASEB J. , vol.14 , pp. 2669-2679
    • Birbes, H.1    Bawab, S.E.2    Hannun, Y.A.3    Obeid, L.M.4
  • 74
    • 0037135518 scopus 로고    scopus 로고
    • Sphingolipid transport: Rafts and translocators
    • van Meer G., Lisman Q. Sphingolipid transport: rafts and translocators. J. Biol. Chem. 277:2002;25855-25858.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25855-25858
    • Van Meer, G.1    Lisman, Q.2
  • 75
    • 0036816141 scopus 로고    scopus 로고
    • Lubricating cell signaling pathways with gangliosides
    • Allende M.L., Proia R.L. Lubricating cell signaling pathways with gangliosides. Curr. Opin. Struct. Biol. 12:2002;587-592.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 587-592
    • Allende, M.L.1    Proia, R.L.2
  • 76
    • 0033529712 scopus 로고    scopus 로고
    • Commitment to apoptosis by GD3 ganglioside depends on opening of the mitochondrial permeability transition pore
    • Scorrano L., Petronilli P., DiLisa F., Bernardi P. Commitment to apoptosis by GD3 ganglioside depends on opening of the mitochondrial permeability transition pore. J. Biol. Chem. 274:1999;22581-22585.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22581-22585
    • Scorrano, L.1    Petronilli, P.2    DiLisa, F.3    Bernardi, P.4
  • 78
    • 0343883506 scopus 로고    scopus 로고
    • Direct interaction of GD3 ganglioside with mitochondria generates reactive oxygen species followed by mitochondrial permeability transition, cytochrome c release and caspase activation
    • García-Ruiz C., Colell A., París R., Fernández-Checa J.C. Direct interaction of GD3 ganglioside with mitochondria generates reactive oxygen species followed by mitochondrial permeability transition, cytochrome c release and caspase activation. FASEB J. 14:2000;847-858.
    • (2000) FASEB J. , vol.14 , pp. 847-858
    • García-Ruiz, C.1    Colell, A.2    París, R.3    Fernández-Checa, J.C.4
  • 81
    • 0037189948 scopus 로고    scopus 로고
    • Ceramide generated by acidic sphingomyelinase contributes to tumor necrosis factor-mediated apoptosis in HT-29 cells through glycosphingolipid generation. Possible role of ganglioside GD3
    • Colell A., Morales A., Fernandez-Checa J.C., Garcia-Ruiz C. Ceramide generated by acidic sphingomyelinase contributes to tumor necrosis factor-mediated apoptosis in HT-29 cells through glycosphingolipid generation. Possible role of ganglioside GD3. FEBS Lett. 526:2002;135-141.
    • (2002) FEBS Lett. , vol.526 , pp. 135-141
    • Colell, A.1    Morales, A.2    Fernandez-Checa, J.C.3    Garcia-Ruiz, C.4
  • 84
    • 0035319268 scopus 로고    scopus 로고
    • Ganglioside GD3 enhances apoptosis by suppressing the nuclear factor-kappaB-dependent survival pathway
    • Colell A., Garcia-Ruiz C., Roman J., Ballesta A., Fernandez-Checa J.C. Ganglioside GD3 enhances apoptosis by suppressing the nuclear factor-kappaB-dependent survival pathway. FASEB J. 15:2001;1068-1070.
    • (2001) FASEB J. , vol.15 , pp. 1068-1070
    • Colell, A.1    Garcia-Ruiz, C.2    Roman, J.3    Ballesta, A.4    Fernandez-Checa, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.