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Volumn 5, Issue 3, 2003, Pages 291-305

Interactions of mitochondrial thiols with nitric oxide

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE PEROXIDASE; MITOCHONDRIAL PROTEIN; NITRIC OXIDE; PEROXIREDOXIN; PROTEIN; PROTEIN DISULFIDE ISOMERASE; THIOL DERIVATIVE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 0038236743     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/152308603322110878     Document Type: Review
Times cited : (69)

References (183)
  • 1
    • 0033582533 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells
    • Arai M, Imai H, Koumura T, Yoshida M, Emoto K, Umeda M, Chiba N, and Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells. J Biol Chem 274: 4924-4933, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 4924-4933
    • Arai, M.1    Imai, H.2    Koumura, T.3    Yoshida, M.4    Emoto, K.5    Umeda, M.6    Chiba, N.7    Nakagawa, Y.8
  • 2
    • 0028987969 scopus 로고
    • - donation by S-nitrosothiols: Implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
    • - donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch Biochem Biophys 318: 279-285, 1995.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 3
    • 0032980375 scopus 로고    scopus 로고
    • Function of thioredoxin reductase as a peroxynitrite reductase using selenocystine or ebselen
    • Arteel GE, Briviba K, and Sies H. Function of thioredoxin reductase as a peroxynitrite reductase using selenocystine or ebselen. Chem Res Toxicol 12: 264-269, 1999.
    • (1999) Chem Res Toxicol , vol.12 , pp. 264-269
    • Arteel, G.E.1    Briviba, K.2    Sies, H.3
  • 4
    • 0032980390 scopus 로고    scopus 로고
    • Protection against peroxynitrite
    • Arteel GE, Briviba K, and Sies H. Protection against peroxynitrite. FEBS Lett 445: 226-230, 1999.
    • (1999) FEBS Lett , vol.445 , pp. 226-230
    • Arteel, G.E.1    Briviba, K.2    Sies, H.3
  • 7
    • 0019323599 scopus 로고
    • General specificity of cytoplasmic thioltransferase (thiol:disulfide oxidoreductase) from rat liver for thiol and disulfide substrates
    • Axelsson K and Mannervik B. General specificity of cytoplasmic thioltransferase (thiol: disulfide oxidoreductase) from rat liver for thiol and disulfide substrates. Biochim BiophysActa 613: 324-336, 1980.
    • (1980) Biochim BiophysActa , vol.613 , pp. 324-336
    • Axelsson, K.1    Mannervik, B.2
  • 8
    • 0029962693 scopus 로고    scopus 로고
    • Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage
    • Barker JE, Bolanos JP, Land JM, Clark JB, and Heales SJR. Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage. Dev Neurosci 18: 391-396, 1996.
    • (1996) Dev Neurosci , vol.18 , pp. 391-396
    • Barker, J.E.1    Bolanos, J.P.2    Land, J.M.3    Clark, J.B.4    Heales, S.J.R.5
  • 9
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty JW, Hampton MB, and Winterbourn CC. Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2: 1261-1266, 2002.
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 11
    • 0028641246 scopus 로고
    • Peroxynitrite versus hydroxyl radical: The role of nitric oxide in superoxide-dependent cerebral injury
    • Beckman JS. Peroxynitrite versus hydroxyl radical: the role of nitric oxide in superoxide-dependent cerebral injury. Ann N Y Acad Sci 738: 69-75, 1994.
    • (1994) Ann N Y Acad Sci , vol.738 , pp. 69-75
    • Beckman, J.S.1
  • 12
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad and the ugly
    • Beckman JS and Koppenol WH. Nitric oxide, superoxide, and peroxynitrite: the good, the bad and the ugly. Am J Physiol 271: C1424-C1437, 1996.
    • (1996) Am J Physiol , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 13
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman JS, Beckman TW, Chen J, Marshall PA, and Freeman BA. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci U S A 87: 1620-1624, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 16
    • 0034687662 scopus 로고    scopus 로고
    • The effect of nitric oxide on cell respiration: A key to understanding its role in cell survival or death
    • Beltran B, Mathur A, Duchen MR, Erusalimsky JD, and Moncada S. The effect of nitric oxide on cell respiration: a key to understanding its role in cell survival or death. Proc Natl Acad Sci U S A 97: 14602-14607, 2000.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14602-14607
    • Beltran, B.1    Mathur, A.2    Duchen, M.R.3    Erusalimsky, J.D.4    Moncada, S.5
  • 17
    • 0035958044 scopus 로고    scopus 로고
    • Rat seminal vesicle FAD-dependent sulfhydryl oxidase. Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family
    • Benayoun B, Esnard-Feve A, Castella S, Courty Y, and Esnard F. Rat seminal vesicle FAD-dependent sulfhydryl oxidase. Biochemical characterization and molecular cloning of a member of the new sulfhydryl oxidase/quiescin Q6 gene family. J Biol Chem 276: 13830-13837, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 13830-13837
    • Benayoun, B.1    Esnard-Feve, A.2    Castella, S.3    Courty, Y.4    Esnard, F.5
  • 18
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi P, Broekmeier KM, and Pfeiffer DR. Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J Bioenerg Biomembr 26: 509-517, 1994.
    • (1994) J Bioenerg Biomembr , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekmeier, K.M.2    Pfeiffer, D.R.3
  • 19
    • 0034639911 scopus 로고    scopus 로고
    • Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties
    • Bizouarn T, Fjellstrom O, Meuller J, Axelsson M, Bergkvist A, Johansson C, Goran Karlsson B, and Rydstrom J. Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties. Biochim Biophys Acta 1457: 211-228, 2000.
    • (2000) Biochim Biophys Acta , vol.1457 , pp. 211-228
    • Bizouarn, T.1    Fjellstrom, O.2    Meuller, J.3    Axelsson, M.4    Bergkvist, A.5    Johansson, C.6    Goran Karlsson, B.7    Rydstrom, J.8
  • 20
    • 0038233014 scopus 로고    scopus 로고
    • Nitric oxide-mediated mitochondrial damage in the brain: Mechanisms and implications for neurodegenerative diseases
    • Bolanos JP, Almeida A, Stewart V, Peuchan S, Land JM, Clark JB, and Heales SJR. Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases. J Neurochem 68: 2227-2240, 1997.
    • (1997) J Neurochem , vol.68 , pp. 2227-2240
    • Bolanos, J.P.1    Almeida, A.2    Stewart, V.3    Peuchan, S.4    Land, J.M.5    Clark, J.B.6    Heales, S.J.R.7
  • 21
    • 0034663637 scopus 로고    scopus 로고
    • Reversal of nitric oxide-, peroxynitrite- and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex I activity by light and thiols
    • Borutaite V, Budriunaite A, and Brown GC. Reversal of nitric oxide-, peroxynitrite- and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex I activity by light and thiols. Biochim Biophys Acta 1459: 405-412, 2000.
    • (2000) Biochim Biophys Acta , vol.1459 , pp. 405-412
    • Borutaite, V.1    Budriunaite, A.2    Brown, G.C.3
  • 22
    • 0033980876 scopus 로고    scopus 로고
    • Nitric oxide donors, nitrosothiols and mitochondrial respiration inhibitors induce caspase activation by different mechanisms
    • Borutaite V, Morkuniene R, and Brown GC. Nitric oxide donors, nitrosothiols and mitochondrial respiration inhibitors induce caspase activation by different mechanisms. FEBS Lett 467: 155-159, 2000.
    • (2000) FEBS Lett , vol.467 , pp. 155-159
    • Borutaite, V.1    Morkuniene, R.2    Brown, G.C.3
  • 23
    • 0037082357 scopus 로고    scopus 로고
    • The mitochondrial NO signalling pathway and the transduction of nitrosative to oxidative cell signals
    • Brookes P and Darley-Usmar V. The mitochondrial NO signalling pathway and the transduction of nitrosative to oxidative cell signals. Free Radic Biol Med 32: 370-374, 2002.
    • (2002) Free Radic Biol Med , vol.32 , pp. 370-374
    • Brookes, P.1    Darley-Usmar, V.2
  • 24
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase
    • Brown GC. Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase. FEBS Lett 369: 136-139, 1995.
    • (1995) FEBS Lett , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 25
    • 0032947296 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial respiration
    • Brown GC. Nitric oxide and mitochondrial respiration. Biochim Biophys Acta 1411: 351-369, 1999.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 351-369
    • Brown, G.C.1
  • 26
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown GC and Cooper CE. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett 356: 295-298, 1994.
    • (1994) FEBS Lett , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 27
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R, Griffin P, and Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407: 211-215, 2000.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 28
    • 0031106373 scopus 로고    scopus 로고
    • Labeling of mitochondrial proteins in living cells by the thiol probe thiobutyltriphenylphosphonium bromide
    • Burns RJ and Murphy MP. Labeling of mitochondrial proteins in living cells by the thiol probe thiobutyltriphenylphosphonium bromide. Arch Biochem Biophys 339: 33-39, 1997.
    • (1997) Arch Biochem Biophys , vol.339 , pp. 33-39
    • Burns, R.J.1    Murphy, M.P.2
  • 29
    • 0029090125 scopus 로고
    • Synthesis and characterization of thiobutyltriphenylphosphonium bromide, a novel thiol reagent targeted to the mitochondrial matrix
    • Burns RJ, Smith RAJ, and Murphy MP. Synthesis and characterization of thiobutyltriphenylphosphonium bromide, a novel thiol reagent targeted to the mitochondrial matrix. Arch Biochem Biophys 322: 60-68, 1995.
    • (1995) Arch Biochem Biophys , vol.322 , pp. 60-68
    • Burns, R.J.1    Smith, R.A.J.2    Murphy, M.P.3
  • 30
    • 0028858786 scopus 로고
    • NO nitrosonium ions, nitroxide ions, nitrosothiols and iron nitrosyls in biology: A chemist's perspective
    • Butler AR, Flitney FW, and WIliams DLH. NO, nitrosonium ions, nitroxide ions, nitrosothiols and iron nitrosyls in biology: a chemist's perspective. Trends Pharmacol Sci 16: 18-22, 1995.
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 18-22
    • Butler, A.R.1    Flitney, F.W.2    WIliams, D.L.H.3
  • 31
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J and Jones DP. Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J Biol Chem 273: 11401-11404, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 33
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina A and Radi R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch Biochem Biophys 328: 309-316, 1996.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 34
    • 0033963540 scopus 로고    scopus 로고
    • Enrichment and functional reconstitution of glutathione transport activity from rabbit kidney mitochondria: Further evidence for the role of the dicarboxylate and 2-oxoglutarate carriers in mitochondrial glutathione transport
    • Chen Z, Putt DA, and Lash LH. Enrichment and functional reconstitution of glutathione transport activity from rabbit kidney mitochondria: further evidence for the role of the dicarboxylate and 2-oxoglutarate carriers in mitochondrial glutathione transport. Arch Biochem Biophys 373: 193-202, 2000.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 193-202
    • Chen, Z.1    Putt, D.A.2    Lash, L.H.3
  • 35
    • 0028287096 scopus 로고
    • Nitric oxide reacts with intracellular glutathione and activates the hexose monophosphate shunt in human neutrophils: Evidence for S-nitrosoglutathione as a bioactive intermediary
    • Clancy RM, Levartovsky D, Leszczynska-Piziak J, Yegudin J, and Abramson SB. Nitric oxide reacts with intracellular glutathione and activates the hexose monophosphate shunt in human neutrophils: evidence for S-nitrosoglutathione as a bioactive intermediary. Proc Natl Acad Sci U S A 91: 3680-3684, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3680-3684
    • Clancy, R.M.1    Levartovsky, D.2    Leszczynska-Piziak, J.3    Yegudin, J.4    Abramson, S.B.5
  • 36
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E, Brown GC, Feelisch M, and Moncada S. Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc Natl Acad Sci U S A 95: 7631-7636, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 37
    • 0031010596 scopus 로고    scopus 로고
    • Parkinson disease: A new link between monoamine oxidase and mitochondrial electron flow
    • Cohen G, Farooqui R, and Kesler N. Parkinson disease: a new link between monoamine oxidase and mitochondrial electron flow. Proc Natl Acad Sci U S A 94: 4890-4894, 1997.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 4890-4894
    • Cohen, G.1    Farooqui, R.2    Kesler, N.3
  • 38
    • 0036162636 scopus 로고    scopus 로고
    • Nitric oxide and cytochrome oxidase: Substrate, inhibitor or effector?
    • Cooper CE. Nitric oxide and cytochrome oxidase: substrate, inhibitor or effector? Trends Biochem Sci 27: 33-39, 2002.
    • (2002) Trends Biochem Sci , vol.27 , pp. 33-39
    • Cooper, C.E.1
  • 39
    • 0033953170 scopus 로고    scopus 로고
    • GSH extrusion and the mitochondrial pathway of apoptotic signalling
    • Coppola S and Ghibelli L. GSH extrusion and the mitochondrial pathway of apoptotic signalling. Biochem Soc Trans 28: 56-61, 2000.
    • (2000) Biochem Soc Trans , vol.28 , pp. 56-61
    • Coppola, S.1    Ghibelli, L.2
  • 40
    • 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 AS, Vieira HLA, Larochette N, de Pablo MA, Zamzami N, Susin SA, Brenner C, and 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: 307-314, 2000.
    • (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.A.5    Zamzami, N.6    Susin, S.A.7    Brenner, C.8    Kroemer, G.9
  • 41
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry - Glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation?
    • Cotgreave IA and Gerdes RG. Recent trends in glutathione biochemistry - glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem Biophys Res Commun 242: 1-9, 1998.
    • (1998) Biochem Biophys Res Commun , vol.242 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 43
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum G. Lipids of mitochondria. Biochim Biophys Acta 822: 1-42, 1985.
    • (1985) Biochim Biophys Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 45
    • 0032584141 scopus 로고    scopus 로고
    • Diffusion of peroxynitrite across erythrocyte membranes
    • Denicola A, Souza JM, and Radi R. Diffusion of peroxynitrite across erythrocyte membranes. Proc Natl Acad Sci U S A 95: 3566-3571, 1998.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 3566-3571
    • Denicola, A.1    Souza, J.M.2    Radi, R.3
  • 47
    • 0037064058 scopus 로고    scopus 로고
    • Biochemistry of mitochondrial nitric-oxide synthase
    • Elfering SL, Sarkela TM, and Giulivi C. Biochemistry of mitochondrial nitric-oxide synthase. J Biol Chem 277: 38079-38086, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 38079-38086
    • Elfering, S.L.1    Sarkela, T.M.2    Giulivi, C.3
  • 50
    • 0025979356 scopus 로고
    • Impaired uptake of glutathione by hepatic mitochondria from chronic ethanol-fed rats. Tracer kinetic studies in vitro and in vivo and susceptibility to oxidant stress
    • Fernandez-Checa JC, Garcia-Ruiz C, Ookhtens M, and Kaplowitz N. Impaired uptake of glutathione by hepatic mitochondria from chronic ethanol-fed rats. Tracer kinetic studies in vitro and in vivo and susceptibility to oxidant stress. J Clin Invest 87: 397-405, 1991.
    • (1991) J Clin Invest , vol.87 , pp. 397-405
    • Fernandez-Checa, J.C.1    Garcia-Ruiz, C.2    Ookhtens, M.3    Kaplowitz, N.4
  • 52
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signalling
    • Finkel T. Oxygen radicals and signalling. Curr Opin Cell Biol 10: 248-253, 1998.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 248-253
    • Finkel, T.1
  • 53
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel T and Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature 408: 239-247, 2000.
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 54
    • 0030939089 scopus 로고    scopus 로고
    • On the virtual existence of superoxide anions in mitochondria: Thoughts regarding its role in pathophysiology
    • Forman HJ and Azzi A. On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology. FASEB J 11: 374-375, 1997.
    • (1997) FASEB J , vol.11 , pp. 374-375
    • Forman, H.J.1    Azzi, A.2
  • 56
    • 0028788763 scopus 로고
    • Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor nuclear factor-kappa B: Studies with isolated mitochondria and rat hepatocytes
    • Garcia-Ruiz C, Colell A, Morales A, Kaplowitz N, and Fernandez-Checa JC. Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor nuclear factor-kappa B: studies with isolated mitochondria and rat hepatocytes. Mol Pharmacol 48: 825-834, 1995.
    • (1995) Mol Pharmacol , vol.48 , pp. 825-834
    • Garcia-Ruiz, C.1    Colell, A.2    Morales, A.3    Kaplowitz, N.4    Fernandez-Checa, J.C.5
  • 57
    • 27244462713 scopus 로고    scopus 로고
    • Development of a peptide antibody specific to human glutathione S-transferase alpha 4-4 (hGSTA4-4) reveals preferential localization in human liver mitochondria
    • Gardner JL and Gallagher EP. Development of a peptide antibody specific to human glutathione S-transferase alpha 4-4 (hGSTA4-4) reveals preferential localization in human liver mitochondria. Arch Biochem Biophys 390: 19-27, 2001.
    • (2001) Arch Biochem Biophys , vol.390 , pp. 19-27
    • Gardner, J.L.1    Gallagher, E.P.2
  • 58
    • 0032898734 scopus 로고    scopus 로고
    • Cloning, sequencing and functional expression of a novel human thioredoxin reductase
    • Gasdaska PY, Berggren MM, Berry MJ, and Powis G. Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett 442: 105-111, 1999.
    • (1999) FEBS Lett , vol.442 , pp. 105-111
    • Gasdaska, P.Y.1    Berggren, M.M.2    Berry, M.J.3    Powis, G.4
  • 59
    • 0028335587 scopus 로고
    • Peroxynitrite-mediated oxidation of albumin to the protein-thiyl free radical
    • Gatti RM, Radi R, and Augusto O. Peroxynitrite-mediated oxidation of albumin to the protein-thiyl free radical. FEBS Lett 348: 287-290, 1994.
    • (1994) FEBS Lett , vol.348 , pp. 287-290
    • Gatti, R.M.1    Radi, R.2    Augusto, O.3
  • 60
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • Ghafourifar P and Richter C. Nitric oxide synthase activity in mitochondria. FEBS Lett 418: 291-296, 1997.
    • (1997) FEBS Lett , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 61
    • 0033615544 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase stimulation causes cytochrome c release from isolated mitochondria
    • Ghafourifar P, Schenk U, Klein SD, and Richter C. Mitochondrial nitric oxide synthase stimulation causes cytochrome c release from isolated mitochondria. 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
  • 62
  • 63
    • 0030724094 scopus 로고    scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • Gilbert HF. Protein disulfide isomerase and assisted protein folding. J Biol Chem 272: 29399-29402, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 29399-29402
    • Gilbert, H.F.1
  • 64
    • 0031260471 scopus 로고    scopus 로고
    • General methods to identify and enrich vicinal thiol proteins present in intact cells in the oxidised disulfide state
    • Gitler C, Zarmi B, and Kalef E. General methods to identify and enrich vicinal thiol proteins present in intact cells in the oxidised disulfide state. Anal Biochem 252: 48-55, 1997.
    • (1997) Anal Biochem , vol.252 , pp. 48-55
    • Gitler, C.1    Zarmi, B.2    Kalef, E.3
  • 66
    • 0028205403 scopus 로고
    • Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria
    • Godeas C, Sandri G, and Panfili E. Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria. Biochim Biophys Acta 1191: 147-150, 1994.
    • (1994) Biochim Biophys Acta , vol.1191 , pp. 147-150
    • Godeas, C.1    Sandri, G.2    Panfili, E.3
  • 67
    • 0029090167 scopus 로고
    • Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity
    • Goossens V, Grooten J, De Vos K, and Fiers W. Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity. Proc Natl Acad Sci U S A 92: 8115-8119, 1995.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8115-8119
    • Goossens, V.1    Grooten, J.2    De Vos, K.3    Fiers, W.4
  • 68
    • 0031029150 scopus 로고    scopus 로고
    • A novel reaction mechanism for the formation of S-nitrosothiol in vivo
    • Gow AJ, Buerk DG, and Ischiropoulos H. A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J Biol Chem 272: 2841-2845, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 2841-2845
    • Gow, A.J.1    Buerk, D.G.2    Ischiropoulos, H.3
  • 69
    • 0037155791 scopus 로고    scopus 로고
    • Basal and stimulated protein S-nitrosylation in multiple cell types and tissues
    • Gow AJ, Chen Q, Hess DT, Day BJ, Ischiropoulos H, and Stamler JS. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J Biol Chem 277: 9637-9640, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 9637-9640
    • Gow, A.J.1    Chen, Q.2    Hess, D.T.3    Day, B.J.4    Ischiropoulos, H.5    Stamler, J.S.6
  • 70
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina SA and Mieyal JJ. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32: 3368-3376, 1993.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 71
    • 0001547757 scopus 로고
    • Origin and turnover of mitochondrial glutathione
    • Griffith OW and Meister A. Origin and turnover of mitochondrial glutathione. Proc Natl Acad Sci U S A 82: 4668-4672, 1985.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4668-4672
    • Griffith, O.W.1    Meister, A.2
  • 72
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • Haendeler J, Hoffmann J, Tischler V, Berk BC, Zeiher AM, and Dimmeler S. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol 4: 743-749, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 73
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury
    • Halestrap AP, Kerr PM, Javadov S, and Woodfield KY. Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury. Biochim Biophys Acta 1366: 79-94, 1998.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 79-94
    • Halestrap, A.P.1    Kerr, P.M.2    Javadov, S.3    Woodfield, K.Y.4
  • 75
    • 0029927487 scopus 로고    scopus 로고
    • The role of glutathione in the transport and catabolism of nitric oxide
    • Hogg N, Singh RJ, and Kalyanaraman B. The role of glutathione in the transport and catabolism of nitric oxide. FEBS Lett 382: 223-228, 1996.
    • (1996) FEBS Lett , vol.382 , pp. 223-228
    • Hogg, N.1    Singh, R.J.2    Kalyanaraman, B.3
  • 78
    • 0030296758 scopus 로고    scopus 로고
    • Seleno compounds and glutathione peroxidase catalyzed decomposition of S-nitrosothiols
    • Hou Y, Guo Z, Li J, and Wang PG. Seleno compounds and glutathione peroxidase catalyzed decomposition of S-nitrosothiols. Biochem Biophys Res Commun 228: 88-93, 1996.
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 88-93
    • Hou, Y.1    Guo, Z.2    Li, J.3    Wang, P.G.4
  • 82
    • 0034714346 scopus 로고    scopus 로고
    • Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease
    • Jha N, Jurma O, Lalli G, Liu Y, Pettus EH, Greenamyre JT, Liu RM, Forman HJ, and Andersen JK. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease. J Biol Chem 275: 26096-26101, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 26096-26101
    • Jha, N.1    Jurma, O.2    Lalli, G.3    Liu, Y.4    Pettus, E.H.5    Greenamyre, J.T.6    Liu, R.M.7    Forman, H.J.8    Andersen, J.K.9
  • 83
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • Jia L, Bonaventura C, Bonaventura J, and Stamler JS. S-Nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380: 221-226, 1996.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 85
    • 0016774398 scopus 로고
    • Some properties of mitochondrial glutathione
    • Jocelyn PC. Some properties of mitochondrial glutathione. Biochim Biophys Acta 396: 427-436, 1975.
    • (1975) Biochim Biophys Acta , vol.396 , pp. 427-436
    • Jocelyn, P.C.1
  • 86
    • 0030296409 scopus 로고    scopus 로고
    • S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione
    • Jung CH and Thomas JA. S-Glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione. Arch Biochem Biophys 335: 61-72, 1996.
    • (1996) Arch Biochem Biophys , vol.335 , pp. 61-72
    • Jung, C.H.1    Thomas, J.A.2
  • 88
    • 0029939154 scopus 로고    scopus 로고
    • Characterisation of sulfur-centred radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite
    • Karoui H, Hogg N, Frejaville C, Tordo P, and Kalyanaraman B. Characterisation of sulfur-centred radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite. J Biol Chem 271: 6000-6009, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 6000-6009
    • Karoui, H.1    Hogg, N.2    Frejaville, C.3    Tordo, P.4    Kalyanaraman, B.5
  • 89
    • 0034673552 scopus 로고    scopus 로고
    • Structural organization of the human glutathione reductase gene: Determination of correct cDNA sequence and identification of a mitochondrial leader sequence
    • Kelner MJ and Montoya MA. Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun 269: 366-368, 2000.
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 366-368
    • Kelner, M.J.1    Montoya, M.A.2
  • 90
    • 0028815563 scopus 로고
    • Nitric oxide: A new paradigm for second messengers
    • Kerwin JF, Lancaster JR, and Feldman PL. Nitric oxide: a new paradigm for second messengers. J Med Chem 38: 4343-4362, 1995.
    • (1995) J Med Chem , vol.38 , pp. 4343-4362
    • Kerwin, J.F.1    Lancaster, J.R.2    Feldman, P.L.3
  • 91
    • 0028803686 scopus 로고
    • Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen
    • Kharitonov VG, Sundquist AR, and Sharma VS. Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen. J Biol Chem 270: 28158-28164, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 28158-28164
    • Kharitonov, V.G.1    Sundquist, A.R.2    Sharma, V.S.3
  • 92
    • 0036023233 scopus 로고    scopus 로고
    • Accumulation of the mitochondrial form of the sulphydryl oxidase Erv1p/Alrp during the early stages of spermato genesis
    • Klissenbauer M, Winters S, Heinlein UA, and Lisowsky T. Accumulation of the mitochondrial form of the sulphydryl oxidase Erv1p/Alrp during the early stages of spermatogenesis. J Exp Biol 205: 1979-1986, 2002.
    • (2002) J Exp Biol , vol.205 , pp. 1979-1986
    • Klissenbauer, M.1    Winters, S.2    Heinlein, U.A.3    Lisowsky, T.4
  • 93
    • 0032557424 scopus 로고    scopus 로고
    • The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism
    • Kowaltowski AJ, Netto LE, and Vercesi AE. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism. J Biol Chem 273: 12766-12769, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12766-12769
    • Kowaltowski, A.J.1    Netto, L.E.2    Vercesi, A.E.3
  • 94
    • 0344936731 scopus 로고    scopus 로고
    • Nitric oxide: Cytotoxicity versus cytoprotection - How, why, when and where?
    • Kroncke KD, Fehsel K, and Kolb-Bachofen V. Nitric oxide: cytotoxicity versus cytoprotection - how, why, when and where? Nitric Oxide 1: 107-120, 1997.
    • (1997) Nitric Oxide , vol.1 , pp. 107-120
    • Kroncke, K.D.1    Fehsel, K.2    Kolb-Bachofen, V.3
  • 96
    • 0027992219 scopus 로고
    • Simulation of the diffusion and reaction of endogenously produced nitric oxide
    • Lancaster JR. Simulation of the diffusion and reaction of endogenously produced nitric oxide. Proc Natl Acad Sci U S A 91: 8137-8141, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8137-8141
    • Lancaster, J.R.1
  • 97
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Ervlp/ALR in the maturation of cytosolic Fe/S proteins
    • Lange H, Lisowsky T, Gerber J, Muhlenhoff U, Kispal G, and Lill R. An essential function of the mitochondrial sulfhydryl oxidase Ervlp/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep 2: 715-720, 2001.
    • (2001) EMBO Rep , vol.2 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Muhlenhoff, U.4    Kispal, G.5    Lill, R.6
  • 98
    • 0021847071 scopus 로고
    • Crucial role of sulfhydryl groups in the mitochondrial inner membrane structure
    • Le-Quoc K and Le-Quoc D. Crucial role of sulfhydryl groups in the mitochondrial inner membrane structure. J Biol Chem 260: 7422-7428, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 7422-7428
    • Le-Quoc, K.1    Le-Quoc, D.2
  • 99
    • 0019891860 scopus 로고
    • Evidence for the existence of two classes of sulfhydryl groups essential for membrane-bound succinate dehydrogenase activity
    • Le-Quoc K, Le-Quoc D, and Gaudemer Y. Evidence for the existence of two classes of sulfhydryl groups essential for membrane-bound succinate dehydrogenase activity. Biochemistry 20: 1705-1710, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1705-1710
    • Le-Quoc, K.1    Le-Quoc, D.2    Gaudemer, Y.3
  • 100
    • 0034647976 scopus 로고    scopus 로고
    • Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase
    • Lee J, Hofhaus G, and Lisowsky T. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett 477: 62-66, 2000.
    • (2000) FEBS Lett , vol.477 , pp. 62-66
    • Lee, J.1    Hofhaus, G.2    Lisowsky, T.3
  • 101
    • 0033582515 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver
    • Lee SR, Kim JR, Kwon KS, Yoon HW, Levine RL, Ginsburg A, and Rhee SG. Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. J Biol Chem 274: 4722-4734, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 4722-4734
    • Lee, S.R.1    Kim, J.R.2    Kwon, K.S.3    Yoon, H.W.4    Levine, R.L.5    Ginsburg, A.6    Rhee, S.G.7
  • 102
    • 0018095252 scopus 로고
    • 2+ release from mitochondria by the oxidation-reduction state of pyridine nucleotides
    • 2+ release from mitochondria by the oxidation-reduction state of pyridine nucleotides. Proc Natl Acad Sci U S A 75: 1690-1694, 1978.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 1690-1694
    • Lehninger, A.L.1    Vercesi, A.2    Bababunmi, E.A.3
  • 104
    • 0026683301 scopus 로고
    • Ca-sensitive reduction of 5,5′-dithiobis-(2-nitrobenzoic acid) by rat liver mitochondria
    • Lenartowicz E. Ca-sensitive reduction of 5,5′-dithiobis-(2-nitrobenzoic acid) by rat liver mitochondria. Biochem Biophys Res Commun 184: 1088-1093, 1992.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1088-1093
    • Lenartowicz, E.1
  • 105
    • 0035793599 scopus 로고    scopus 로고
    • Glutathiolation of proteins by glutathione disulfide S-oxide derived from S-nitrosoglutathione. Modifications of rat brain neurogranin/ RC3 and neuromodulin/GAP-43
    • Li J, Huang FL, and Huang KP. Glutathiolation of proteins by glutathione disulfide S-oxide derived from S-nitrosoglutathione. Modifications of rat brain neurogranin/ RC3 and neuromodulin/GAP-43. J Biol Chem 276: 3098-3105, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 3098-3105
    • Li, J.1    Huang, F.L.2    Huang, K.P.3
  • 107
    • 0032478104 scopus 로고    scopus 로고
    • Accelerated reaction of nitric oxide with oxygen within the hydrophobic interior of biological membranes
    • Liu X, Miller MJS, Joshi MS, Thomas DD, and Lancaster JR. Accelerated reaction of nitric oxide with oxygen within the hydrophobic interior of biological membranes. Proc Natl A cad Sci U S A 95: 2175-2179, 1998.
    • (1998) Proc Natl A Cad Sci U S A , vol.95 , pp. 2175-2179
    • Liu, X.1    Miller, M.J.S.2    Joshi, M.S.3    Thomas, D.D.4    Lancaster, J.R.5
  • 108
    • 0029981670 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite exert distinct effects on mitochondrial respiration which are differentially blocked by glutathione or glucose
    • Lizasoian I, Moro MA, Knowles RG, Darley-Usmer V, and Moncada S. Nitric oxide and peroxynitrite exert distinct effects on mitochondrial respiration which are differentially blocked by glutathione or glucose. Biochem J 314: 877-880, 1996.
    • (1996) Biochem J , vol.314 , pp. 877-880
    • Lizasoian, I.1    Moro, M.A.2    Knowles, R.G.3    Darley-Usmer, V.4    Moncada, S.5
  • 110
    • 0029862502 scopus 로고    scopus 로고
    • Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
    • MacMillan-Crow LA, Crow JP, Kerby JD, Beckman JS, and Thompson JA. Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts. Proc Natl Acad Sci U S A 93: 11853-11858, 1996.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11853-11858
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Kerby, J.D.3    Beckman, J.S.4    Thompson, J.A.5
  • 112
    • 0025049139 scopus 로고
    • High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function
    • Martensson J, Lai JCK, and Meister A. High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function. Proc Natl Acad Sci U S A 87: 7185-7189, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7185-7189
    • Martensson, J.1    Lai, J.C.K.2    Meister, A.3
  • 113
    • 0025820957 scopus 로고
    • Uptake of glutathione by renal cortical mitochondria
    • McKernan TB, Woods EB, and Lash LH. Uptake of glutathione by renal cortical mitochondria. Arch Biochem Biophys 288: 653-663, 1991.
    • (1991) Arch Biochem Biophys , vol.288 , pp. 653-663
    • McKernan, T.B.1    Woods, E.B.2    Lash, L.H.3
  • 114
    • 0029033862 scopus 로고
    • Mitochondrial changes associated with glutathione deficiency
    • Meister A. Mitochondrial changes associated with glutathione deficiency. Biochim Biophys Acta 1271: 35-42, 1995.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 35-42
    • Meister, A.1
  • 115
    • 0020478933 scopus 로고
    • Status of the mitochondrial pool of glutathione in the isolated hepatocyte
    • Meredith MJ and Reed DJ. Status of the mitochondrial pool of glutathione in the isolated hepatocyte. J Biol Chem 257: 3747-3753, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 3747-3753
    • Meredith, M.J.1    Reed, D.J.2
  • 116
    • 0028308730 scopus 로고
    • Kinetics and equilibria of S-nitrosothiol-thiol exchange between glutathione, cysteine, penicillamines and serum albumin
    • Meyer DJ, Kramer H, Ozer N, Coles B, and Ketterer B. Kinetics and equilibria of S-nitrosothiol-thiol exchange between glutathione, cysteine, penicillamines and serum albumin. FEBS Lett 345: 177-180, 1994.
    • (1994) FEBS Lett , vol.345 , pp. 177-180
    • Meyer, D.J.1    Kramer, H.2    Ozer, N.3    Coles, B.4    Ketterer, B.5
  • 118
    • 0028175539 scopus 로고
    • Mechanism of covalent modification of glyceraldehyde-3-phosphate dehydrogenase at its active site thiol by nitric oxide, peroxynitrite and related nitrosating agents
    • Mohr S, Stamler JS, and Brune B. Mechanism of covalent modification of glyceraldehyde-3-phosphate dehydrogenase at its active site thiol by nitric oxide, peroxynitrite and related nitrosating agents. FEBS Lett 348: 223-227, 1994.
    • (1994) FEBS Lett , vol.348 , pp. 223-227
    • Mohr, S.1    Stamler, J.S.2    Brune, B.3
  • 119
    • 0026453106 scopus 로고
    • Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation
    • Molina y Vedia L, McDonald B, Reep B, Brune B, Di Silvio M, Billiar TR, and Lapetina E G. Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation. J Biol Chem 267: 24929-24932, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 24929-24932
    • Molina y Vedia, L.1    McDonald, B.2    Reep, B.3    Brune, B.4    Di Silvio, M.5    Billiar, T.R.6    Lapetina, E.G.7
  • 120
    • 0036513249 scopus 로고    scopus 로고
    • Does nitric oxide modulate mitochondrial energy generation and apoptosis?
    • Moncada S and Erusalimsky JD. 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
  • 121
    • 0030872907 scopus 로고    scopus 로고
    • Targeting bioactive compounds to mitochondria
    • Murphy MP. Targeting bioactive compounds to mitochondria. Trends Biotechnol 15: 326-330, 1997.
    • (1997) Trends Biotechnol , vol.15 , pp. 326-330
    • Murphy, M.P.1
  • 122
    • 0032898838 scopus 로고    scopus 로고
    • Nitric oxide and cell death
    • Murphy MP. Nitric oxide and cell death. Biochim Biophys Acta 1411: 401-414, 1999.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 401-414
    • Murphy, M.P.1
  • 123
    • 0343986284 scopus 로고    scopus 로고
    • Drug delivery to mitochondria: The key to mitochondrial medicine
    • Murphy MP and Smith RAJ. Drug delivery to mitochondria: the key to mitochondrial medicine. Adv Drug Deliv Rev 41: 235-250, 2000.
    • (2000) Adv Drug Deliv Rev , vol.41 , pp. 235-250
    • Murphy, M.P.1    Smith, R.A.J.2
  • 125
    • 0029764601 scopus 로고    scopus 로고
    • S-nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide
    • Nikitovic D and Holmgren A. S-Nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide. J Biol Chem 271: 19180-19185, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 19180-19185
    • Nikitovic, D.1    Holmgren, A.2
  • 126
    • 0034306791 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis
    • Nomura K, Imai H, Koumura T, Kobayashi T, and Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis. Biochem J 351: 183-193, 2000.
    • (2000) Biochem J , vol.351 , pp. 183-193
    • Nomura, K.1    Imai, H.2    Koumura, T.3    Kobayashi, T.4    Nakagawa, Y.5
  • 127
    • 0034124460 scopus 로고    scopus 로고
    • Attenuation of hyperoxia-induced growth inhibition in H 441 cells by gene transfer of mitochondrially targeted glutathione reductase
    • O'Donovan DJ, Katkin JP, Tamura T, Smith CV, and Welty SE. Attenuation of hyperoxia-induced growth inhibition in H441 cells by gene transfer of mitochondrially targeted glutathione reductase. Am J Respir Cell Mol Biol 22: 732-738, 2000
    • (2000) Am J Respir Cell Mol Biol , vol.22 , pp. 732-738
    • O'Donovan, D.J.1    Katkin, J.P.2    Tamura, T.3    Smith, C.V.4    Welty, S.E.5
  • 128
    • 0023846096 scopus 로고
    • Retention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment
    • Olafsdottir K and Reed DJ. Retention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment. Biochim Biophys Acta 964: 377-382, 1988.
    • (1988) Biochim Biophys Acta , vol.964 , pp. 377-382
    • Olafsdottir, K.1    Reed, D.J.2
  • 129
    • 0028306269 scopus 로고
    • Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A
    • Packer MA and Murphy ME Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A. FEBS Lett 345: 237-240, 1994.
    • (1994) FEBS Lett , vol.345 , pp. 237-240
    • Packer, M.A.1    Murphy, M.E.2
  • 130
    • 0028790583 scopus 로고
    • Peroxynitrite formed by simultaneous nitric oxide and superoxide generation causes cyclosporin A-sensitive calcium efflux from mitochondria
    • Packer MA and Murphy MP. Peroxynitrite formed by simultaneous nitric oxide and superoxide generation causes cyclosporin A-sensitive calcium efflux from mitochondria. Eur J Biochem 234: 231-239, 1995.
    • (1995) Eur J Biochem , vol.234 , pp. 231-239
    • Packer, M.A.1    Murphy, M.P.2
  • 131
    • 0029857135 scopus 로고    scopus 로고
    • Mitochondrial superoxide production in the presence of nitric oxide leads to the formation of peroxynitrite
    • Packer MA, Porteous CM, and Murphy MP. Mitochondrial superoxide production in the presence of nitric oxide leads to the formation of peroxynitrite. Biochem Mol Biol Int 40: 527-534, 1996.
    • (1996) Biochem Mol Biol Int , vol.40 , pp. 527-534
    • Packer, M.A.1    Porteous, C.M.2    Murphy, M.P.3
  • 132
    • 0025886108 scopus 로고
    • Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria
    • Panfili E, Sandri G, and Ernster L. Distribution of glutathione peroxidases and glutathione reductase in rat brain mitochondria. FEBS Lett 290: 35-37, 1991.
    • (1991) FEBS Lett , vol.290 , pp. 35-37
    • Panfili, E.1    Sandri, G.2    Ernster, L.3
  • 133
    • 0024324316 scopus 로고
    • Reduction of protein mixed disulfides (dethiolation) by E. coli thioredoxin: A study with glycogen phosphorylase b and creatine kinase
    • Park EM and Thomas JA. Reduction of protein mixed disulfides (dethiolation) by E. coli thioredoxin: a study with glycogen phosphorylase b and creatine kinase. Arch Biochem Biophys 272: 25-31, 1989.
    • (1989) Arch Biochem Biophys , vol.272 , pp. 25-31
    • Park, E.M.1    Thomas, J.A.2
  • 134
    • 0029854518 scopus 로고    scopus 로고
    • Glutathione S-transferase class Kappa: Characterization by the cloning of rat mitochondrial GST and identification of a human homologue
    • Pemble SE, Wardle AF, and Taylor JB. Glutathione S-transferase class Kappa: characterization by the cloning of rat mitochondrial GST and identification of a human homologue. Biochem J 319: 749-754, 1996.
    • (1996) Biochem J , vol.319 , pp. 749-754
    • Pemble, S.E.1    Wardle, A.F.2    Taylor, J.B.3
  • 135
    • 0028239794 scopus 로고
    • The voltage sensor of the mitochondrial permeability transition is tuned by the oxidation-reduction state of vicinal thiols
    • Petronilli V, Costantini P, Scorrano L, Colonna R, Passamonti S, and Bernardi P. The voltage sensor of the mitochondrial permeability transition is tuned by the oxidation-reduction state of vicinal thiols. J Biol Chem 269: 16638-16642, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 16638-16642
    • Petronilli, V.1    Costantini, P.2    Scorrano, L.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 136
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso JJ, Carreras MC, Lisdero C, Riobo N, Schopfer F, and Boveris A. Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch Biochem Biophys 328: 85-92, 1996.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobo, N.4    Schopfer, F.5    Boveris, A.6
  • 139
    • 0028275459 scopus 로고
    • Inhibition of mitochondrial electron transport by peroxynitrite
    • Radi R, Rodriguez M, Castro L, and Telleri R. Inhibition of mitochondrial electron transport by peroxynitrite. Arch Biochem Biophys 308: 89-95, 1994.
    • (1994) Arch Biochem Biophys , vol.308 , pp. 89-95
    • Radi, R.1    Rodriguez, M.2    Castro, L.3    Telleri, R.4
  • 140
    • 0036244508 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite interactions with mitochondria
    • Radi R, Cassina A, and Hodara R. Nitric oxide and peroxynitrite interactions with mitochondria. Biol Chem 383: 401-409, 2002.
    • (2002) Biol Chem , vol.383 , pp. 401-409
    • Radi, R.1    Cassina, A.2    Hodara, R.3
  • 141
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S and Robinson BH. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem 25: 502-508, 2000.
    • (2000) Trends Biochem , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 142
    • 0025298423 scopus 로고
    • Glutathione depletion and formation of glutathione-protein mixed disulfide following exposure of brain mitochondria to oxidative stress
    • Ravindrath V and Reed DJ. Glutathione depletion and formation of glutathione-protein mixed disulfide following exposure of brain mitochondria to oxidative stress. Biochem Biophys Res Commun 169: 1075-1079, 1990.
    • (1990) Biochem Biophys Res Commun , vol.169 , pp. 1075-1079
    • Ravindrath, V.1    Reed, D.J.2
  • 143
    • 0025317268 scopus 로고
    • Glutathione: Toxicological implications
    • Reed D. Glutathione: toxicological implications. Annu Rev Pharmacol Toxicol 30: 603-631, 1990.
    • (1990) Annu Rev Pharmacol Toxicol , vol.30 , pp. 603-631
    • Reed, D.1
  • 145
    • 0031984162 scopus 로고    scopus 로고
    • Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability
    • Rigobello MP, Callegaro MT, Barzon E, Benetti M, and Bindoli A. Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability. Free Radic Biol Med 24: 370-376, 1998.
    • (1998) Free Radic Biol Med , vol.24 , pp. 370-376
    • Rigobello, M.P.1    Callegaro, M.T.2    Barzon, E.3    Benetti, M.4    Bindoli, A.5
  • 146
    • 0033980206 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of a rat liver mitochondrial protein disulfide isomerase
    • Rigobello MP, Donella-Deana A, Cesaro L, and Bindoli A. Isolation, purification, and characterization of a rat liver mitochondrial protein disulfide isomerase. Free Radic Biol Med 28: 266-272, 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 266-272
    • Rigobello, M.P.1    Donella-Deana, A.2    Cesaro, L.3    Bindoli, A.4
  • 147
    • 0035367291 scopus 로고    scopus 로고
    • Distribution of protein disulphide isomerase in rat liver mitochondria
    • Rigobello MP, Donella-Deana A, Cesaro L, and Bindoli A. Distribution of protein disulphide isomerase in rat liver mitochondria. Biochem J 356: 567-570, 2001.
    • (2001) Biochem J , vol.356 , pp. 567-570
    • Rigobello, M.P.1    Donella-Deana, A.2    Cesaro, L.3    Bindoli, A.4
  • 148
    • 0000597427 scopus 로고
    • Changes in sulfhydryl groups of rat liver mitochondria during swelling and contraction
    • Riley MV and Lehninger AL. Changes in sulfhydryl groups of rat liver mitochondria during swelling and contraction. J Biol Chem 239: 2083-2089, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 2083-2089
    • Riley, M.V.1    Lehninger, A.L.2
  • 149
    • 0342275186 scopus 로고    scopus 로고
    • Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A
    • Ruoppolo M, Lundstrom-Ljung J, Talamo F, Pucci P, and Marino G. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A. Biochemistry 36: 12259-12267, 1997.
    • (1997) Biochemistry , vol.36 , pp. 12259-12267
    • Ruoppolo, M.1    Lundstrom-Ljung, J.2    Talamo, F.3    Pucci, P.4    Marino, G.5
  • 150
    • 0035831466 scopus 로고    scopus 로고
    • The modulation of oxygen radical production by nitric oxide in mitochondria
    • Sarkela TM, Berthiaume J, Elfering S, Gybina AA, and Giulivi C. The modulation of oxygen radical production by nitric oxide in mitochondria. J Biol Chem 276: 6945-6949, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 6945-6949
    • Sarkela, T.M.1    Berthiaume, J.2    Elfering, S.3    Gybina, A.A.4    Giulivi, C.5
  • 151
    • 0028100230 scopus 로고
    • Release of mitochondrial glutathione and calcium by a cyclosporin A-sensitive mechanism occurs without large amplitude swelling
    • Savage MK and Reed DJ. Release of mitochondrial glutathione and calcium by a cyclosporin A-sensitive mechanism occurs without large amplitude swelling. Arch Biochem Biophys 315: 142-152, 1994.
    • (1994) Arch Biochem Biophys , vol.315 , pp. 142-152
    • Savage, M.K.1    Reed, D.J.2
  • 152
    • 0030580086 scopus 로고    scopus 로고
    • Alterations to glutathione and nicotinamide nucleotides during the mitochondrial permeability transition induced by peroxymitrite
    • Scarlett JL, Packer MA, Porteous CM, and Murphy MP. Alterations to glutathione and nicotinamide nucleotides during the mitochondrial permeability transition induced by peroxymitrite. Biochem Pharmacol 52: 1047-1055, 1996.
    • (1996) Biochem Pharmacol , vol.52 , pp. 1047-1055
    • Scarlett, J.L.1    Packer, M.A.2    Porteous, C.M.3    Murphy, M.P.4
  • 153
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ and Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30: 1191-1212, 2002.
    • (2002) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 154
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation
    • Schulze-Osthoff K, Bakker AC, Vanhaesebroeck B, Beyaert R, Jacob WA, and Fiers W. Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J Biol Chem 267: 5317-5323, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jacob, W.A.5    Fiers, W.6
  • 155
    • 0030057750 scopus 로고    scopus 로고
    • Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress
    • Seres T, Ravichandran V, Moriguchi T, Rokutan K, Thomas JA, and Johnston RB Jr. Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress. J Immunol 156: 1973-1980, 1996.
    • (1996) J Immunol , vol.156 , pp. 1973-1980
    • Seres, T.1    Ravichandran, V.2    Moriguchi, T.3    Rokutan, K.4    Thomas, J.A.5    Johnston R.B., Jr.6
  • 156
    • 0035912784 scopus 로고    scopus 로고
    • Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase
    • Shiva S, Brookes PS, Patel RP, Anderson PG, and Darley-Usmar VM. Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase. Proc Natl Acad Sci U S A 98: 7212-7217, 2001.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 7212-7217
    • Shiva, S.1    Brookes, P.S.2    Patel, R.P.3    Anderson, P.G.4    Darley-Usmar, V.M.5
  • 157
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev VP. Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q Rev Biophys 29: 169-202, 1996.
    • (1996) Q Rev Biophys , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 158
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis?
    • Skulachev VP. Why are mitochondria involved in apoptosis? FEBS Lett 397: 7-10, 1996.
    • (1996) FEBS Lett , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 160
    • 0028132836 scopus 로고
    • Redox signalling: Nitrosylation and related target interactions of nitric oxide
    • Stamler JS. Redox signalling: nitrosylation and related target interactions of nitric oxide. Cell 78: 931-936, 1994.
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 161
    • 0031971053 scopus 로고    scopus 로고
    • Oxidative modifications in nitrosative stress
    • Stamler JS and Hausladen A. Oxidative modifications in nitrosative stress. Nat Struct Biol 5: 247-249, 1998.
    • (1998) Nat Struct Biol , vol.5 , pp. 247-249
    • Stamler, J.S.1    Hausladen, A.2
  • 163
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox activated forms
    • Stamler JS, Singel DJ, and Loscalzo J. Biochemistry of nitric oxide and its redox activated forms. Science 258: 1898-1902, 1992.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 165
    • 0028146764 scopus 로고
    • Modulation of AP-1 activity by nitric oxide in vitro
    • Tabuchi A, Sano K, Oh E, Tsuchiya T, and Tsuda M. Modulation of AP-1 activity by nitric oxide in vitro. FEBS Lett 351: 123-127, 1994.
    • (1994) FEBS Lett , vol.351 , pp. 123-127
    • Tabuchi, A.1    Sano, K.2    Oh, E.3    Tsuchiya, T.4    Tsuda, M.5
  • 166
  • 167
    • 0031577469 scopus 로고    scopus 로고
    • Gene structure for mouse glutathione reductase, including a putative mitochondrial targeting signal
    • Tamura T, McMicken HW, Smith CV, and Hansen TN. Gene structure for mouse glutathione reductase, including a putative mitochondrial targeting signal. Biochem Biophys Res Commun 237: 419-422, 1997.
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 419-422
    • Tamura, T.1    McMicken, H.W.2    Smith, C.V.3    Hansen, T.N.4
  • 169
    • 0032079851 scopus 로고    scopus 로고
    • Purification and characterization of a nitric-oxide synthase from rat liver mitochondria
    • Tatoyan A and Giulivi C. Purification and characterization of a nitric-oxide synthase from rat liver mitochondria. J Biol Chem 273: 11044-11048, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 11044-11048
    • Tatoyan, A.1    Giulivi, C.2
  • 170
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas JA, Poland B, and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 319: 1-9, 1995.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 171
    • 0027436057 scopus 로고
    • The participation of reactive oxygen species and protein thiols in the mechanism of mitochondrial inner membrane permeabilisation by calcium plus prooxidants
    • Valle VGR, Fagian MM, Paretoni LS, Meinecke AR, and Vercesi AE. The participation of reactive oxygen species and protein thiols in the mechanism of mitochondrial inner membrane permeabilisation by calcium plus prooxidants. Arch Biochem Biophys 307: 1-7, 1993.
    • (1993) Arch Biochem Biophys , vol.307 , pp. 1-7
    • Valle, V.G.R.1    Fagian, M.M.2    Paretoni, L.S.3    Meinecke, A.R.4    Vercesi, A.E.5
  • 173
    • 15144349362 scopus 로고    scopus 로고
    • Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide
    • van der Vliet A, Hoen PA, Wong PS, Bast A, and Cross CE. Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide. J Biol Chem 273: 30255-30262, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 30255-30262
    • Van der Vliet, A.1    Hoen, P.A.2    Wong, P.S.3    Bast, A.4    Cross, C.E.5
  • 174
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace DC. Mitochondrial diseases in man and mouse. Science 283: 1482-1488, 1999.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 175
    • 0032432034 scopus 로고    scopus 로고
    • Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone
    • Wang CC. Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone. Ann N Y Acad Sci 864: 9-13, 1998.
    • (1998) Ann N Y Acad Sci , vol.864 , pp. 9-13
    • Wang, C.C.1
  • 177
    • 0029128399 scopus 로고
    • Nitric oxide reactions important to biological systems: A survey of some kinetics investigations
    • Wink DA and Ford PC. Nitric oxide reactions important to biological systems: a survey of some kinetics investigations. Methods 7: 14-20, 1995.
    • (1995) Methods , vol.7 , pp. 14-20
    • Wink, D.A.1    Ford, P.C.2
  • 178
    • 0027390329 scopus 로고
    • Superoxide as an intra cellular radical sink
    • Winterbourn CC. Superoxide as an intracellular radical sink. Free Radic Biol Med 14: 85-90, 1993.
    • (1993) Free Radic Biol Med , vol.14 , pp. 85-90
    • Winterbourn, C.C.1
  • 180
    • 0028157433 scopus 로고
    • On the protective mechanism of the thiol-specific antioxidant enzyme against the oxidative damage of biomacromolecules
    • Yim MB, Chae HZ, Rhee SG, Chock PB, and Stadtman ER. On the protective mechanism of the thiol-specific antioxidant enzyme against the oxidative damage of biomacromolecules. J Biol Chem 269: 1621-1626, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 1621-1626
    • Yim, M.B.1    Chae, H.Z.2    Rhee, S.G.3    Chock, P.B.4    Stadtman, E.R.5
  • 181
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide
    • Zai A, Rudd MA, Scribner AW, and Loscalzo J. Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J Clin Invest 103: 393-399, 1999.
    • (1999) J Clin Invest , vol.103 , pp. 393-399
    • Zai, A.1    Rudd, M.A.2    Scribner, A.W.3    Loscalzo, J.4
  • 182
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler DM. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu Rev Biochem 54: 305-329, 1985.
    • (1985) Annu Rev Biochem , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 183
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M and Zabo I. The mitochondrial permeability transition. Biochim Biophys Acta 1241: 139-176, 1995.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Zabo, I.2


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