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Volumn 10, Issue 2, 2010, Pages 83-93

Gases in the mitochondria

Author keywords

Carbon monoxide; Gasomodulators; Hydrogen sulphide; Mitochondria; Nitric oxide

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARBON MONOXIDE; CYTOCHROME C OXIDASE; HYDROGEN SULFIDE; MITOCHONDRIAL DNA; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE;

EID: 76049130069     PISSN: 15677249     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mito.2009.12.142     Document Type: Review
Times cited : (52)

References (165)
  • 1
    • 49549098876 scopus 로고    scopus 로고
    • 2S-induced pancreatic acinar cell apoptosis is mediated via JNK and p38 MAP kinase
    • 2S-induced pancreatic acinar cell apoptosis is mediated via JNK and p38 MAP kinase. J. Cell Mol. Med. 12 (2008) 1374-1383
    • (2008) J. Cell Mol. Med. , vol.12 , pp. 1374-1383
    • Adhikari, S.1    Bhatia, M.2
  • 2
    • 0036023498 scopus 로고    scopus 로고
    • Toxicity of fire smoke
    • Alarie Y. Toxicity of fire smoke. Crit. Rev. Toxicol. 32 (2002) 259-289
    • (2002) Crit. Rev. Toxicol. , vol.32 , pp. 259-289
    • Alarie, Y.1
  • 3
    • 0035909948 scopus 로고    scopus 로고
    • Different responses of astrocytes and neurons to nitric oxide: the role of glycolytically generated ATP in astrocyte protection
    • Almeida A., Almeida J., Bolanos J.P., and Moncada S. Different responses of astrocytes and neurons to nitric oxide: the role of glycolytically generated ATP in astrocyte protection. Proc. Natl. Acad. Sci. USA 98 (2001) 15294-15299
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15294-15299
    • Almeida, A.1    Almeida, J.2    Bolanos, J.P.3    Moncada, S.4
  • 5
    • 0042736338 scopus 로고    scopus 로고
    • Carbon monoxide specifically inhibits cytochrome c oxidase of human mitochondrial respiratory chain
    • Alonso J.R., Cardellach F., Lopez S., Casademont J., and Miro O. Carbon monoxide specifically inhibits cytochrome c oxidase of human mitochondrial respiratory chain. Pharmacol. Toxicol. 93 (2003) 142-146
    • (2003) Pharmacol. Toxicol. , vol.93 , pp. 142-146
    • Alonso, J.R.1    Cardellach, F.2    Lopez, S.3    Casademont, J.4    Miro, O.5
  • 6
    • 0033822197 scopus 로고    scopus 로고
    • Nitric oxide-induced necrosis and apoptosis in PC12 cells mediated by mitochondria
    • Bal-Price A., and Brown G.C. Nitric oxide-induced necrosis and apoptosis in PC12 cells mediated by mitochondria. J. Neurochem. 75 (2000) 1455-1464
    • (2000) J. Neurochem. , vol.75 , pp. 1455-1464
    • Bal-Price, A.1    Brown, G.C.2
  • 7
    • 33845982557 scopus 로고    scopus 로고
    • Hydrogen sulphide-induces DNA damage and changes in apoptotic gene expression in human lung fibroblast cells
    • Baskar R., Li L., and Moore P.K. Hydrogen sulphide-induces DNA damage and changes in apoptotic gene expression in human lung fibroblast cells. FASEB J. 21 (2007) 247-255
    • (2007) FASEB J. , vol.21 , pp. 247-255
    • Baskar, R.1    Li, L.2    Moore, P.K.3
  • 8
    • 68049092062 scopus 로고    scopus 로고
    • Applying gases for microcirculatory and cellular oxygenation in sepsis: effects of nitric oxide, carbon monoxide and hydrogen sulphide
    • Baumgart K., Radermacher P., and Wagner F. Applying gases for microcirculatory and cellular oxygenation in sepsis: effects of nitric oxide, carbon monoxide and hydrogen sulphide. Curr. Opin. Anaesthesiol. 22 (2009) 168-176
    • (2009) Curr. Opin. Anaesthesiol. , vol.22 , pp. 168-176
    • Baumgart, K.1    Radermacher, P.2    Wagner, F.3
  • 9
    • 38449118776 scopus 로고    scopus 로고
    • Mitochondria and neurodegeneration
    • Beal M.F. Mitochondria and neurodegeneration. Novartis Found. Symp. 287 (2007) 183-192
    • (2007) Novartis Found. Symp. , vol.287 , pp. 183-192
    • Beal, M.F.1
  • 12
    • 33745872953 scopus 로고    scopus 로고
    • Modulation of astroglial energy metabolism by nitric oxide
    • Bolanos J.P., and Almeida A. Modulation of astroglial energy metabolism by nitric oxide. Antioxid. Redox Signal. 8 (2006) 955-965
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 955-965
    • Bolanos, J.P.1    Almeida, A.2
  • 13
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary culture
    • Bolanos J.P., Heales S.J., Land J.M., and Clark J.B. Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary culture. J. Neurochem. 64 (1995) 1965-1972
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.2    Land, J.M.3    Clark, J.B.4
  • 15
    • 0344012010 scopus 로고    scopus 로고
    • Nitric oxide induces apoptosis via hydrogen peroxide, but necrosis via energy and thiol depletion
    • Borutaite V., and Brown G.C. Nitric oxide induces apoptosis via hydrogen peroxide, but necrosis via energy and thiol depletion. Free Radical Biol. Med. 35 (2003) 1457-1468
    • (2003) Free Radical Biol. Med. , vol.35 , pp. 1457-1468
    • Borutaite, V.1    Brown, G.C.2
  • 16
    • 0034693134 scopus 로고    scopus 로고
    • Nitric oxide-inducible expression of heme oxygenase-1 in human cells. Translation independent stabilization of the mRNA and evidence for direct action of nitric oxide
    • Bouton C., and Demple B. Nitric oxide-inducible expression of heme oxygenase-1 in human cells. Translation independent stabilization of the mRNA and evidence for direct action of nitric oxide. J. Biol. Chem. 275 (2000) 32688-32693
    • (2000) J. Biol. Chem. , vol.275 , pp. 32688-32693
    • Bouton, C.1    Demple, B.2
  • 17
    • 0037124078 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumour necrosis factor-alpha-mediated apoptosis
    • Brouard S., Berberat P.O., Tobiash E., Seldon M.P., Bach F.H., and Soares M.P. Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumour necrosis factor-alpha-mediated apoptosis. J. Biol. Chem. 277 (2002) 17950-17961
    • (2002) J. Biol. Chem. , vol.277 , pp. 17950-17961
    • Brouard, S.1    Berberat, P.O.2    Tobiash, E.3    Seldon, M.P.4    Bach, F.H.5    Soares, M.P.6
  • 18
    • 0032947296 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial respiration
    • Brown G.C. Nitric oxide and mitochondrial respiration. Biochim. Biophys. Acta 1411 (1999) 351-369
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 351-369
    • Brown, G.C.1
  • 19
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols
    • Brown G.C., and Borutaite V. Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols. Biochim. Biophys. Acta 1658 (2004) 44-49
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2
  • 20
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown G.C., and Cooper C.E. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356 (1994) 295-298
    • (1994) FEBS Lett. , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 21
    • 0026506763 scopus 로고
    • Recovery of energy metabolism in rat brain after carbon monoxide hypoxia
    • Brown S.D., and Piantadosi C.A. Recovery of energy metabolism in rat brain after carbon monoxide hypoxia. J. Clin. Invest. 89 (1992) 666-672
    • (1992) J. Clin. Invest. , vol.89 , pp. 666-672
    • Brown, S.D.1    Piantadosi, C.A.2
  • 25
    • 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 (1996) 309-316
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 26
    • 0028090219 scopus 로고
    • Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
    • Castro L., Rodriguez M., and Radi R. Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. J. Biol. Chem. 269 (1994) 29409-29415
    • (1994) J. Biol. Chem. , vol.269 , pp. 29409-29415
    • Castro, L.1    Rodriguez, M.2    Radi, R.3
  • 27
    • 0035900675 scopus 로고    scopus 로고
    • P38 MAP kinase mediates nitric oxide-induced apoptosis of neural progenitor cells
    • Cheng A., Chan S.L., Milhavet O., Wang S., and Mattson M.P. P38 MAP kinase mediates nitric oxide-induced apoptosis of neural progenitor cells. J. Biol. Chem. 276 (2001) 43320-43327
    • (2001) J. Biol. Chem. , vol.276 , pp. 43320-43327
    • Cheng, A.1    Chan, S.L.2    Milhavet, O.3    Wang, S.4    Mattson, M.P.5
  • 29
    • 10944237677 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiration by nitric oxide rapidly stimulates cytoprotective GLUT3-mediated glucose uptake through 5′-AMP-activated protein kinase
    • Cidad P., Almeida A., and Bolanos J.P. Inhibition of mitochondrial respiration by nitric oxide rapidly stimulates cytoprotective GLUT3-mediated glucose uptake through 5′-AMP-activated protein kinase. Biochem. J. 384 (2004) 629-636
    • (2004) Biochem. J. , vol.384 , pp. 629-636
    • Cidad, P.1    Almeida, A.2    Bolanos, J.P.3
  • 30
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • Cleeter M.W., Cooper J.M., Darley-Usmar V.M., Moncada S., and Schapira A.H. Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett. 345 (1994) 50-54
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 31
    • 26644471251 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial biogenesis: a key to long-term regulation of cellular metabolism
    • Clementi E., and Nisoli E. Nitric oxide and mitochondrial biogenesis: a key to long-term regulation of cellular metabolism. Comp. Biochem. Physiol. 142 (2005) 102-110
    • (2005) Comp. Biochem. Physiol. , vol.142 , pp. 102-110
    • Clementi, E.1    Nisoli, E.2
  • 32
    • 33845640469 scopus 로고    scopus 로고
    • HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism
    • Converso D.P., Taille C., Carreras M.C., Jaitovich A., Ponderoso J.J., and Boczkowski J. HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism. FASEB J. 20 (2006) 1236-1238
    • (2006) FASEB J. , vol.20 , pp. 1236-1238
    • Converso, D.P.1    Taille, C.2    Carreras, M.C.3    Jaitovich, A.4    Ponderoso, J.J.5    Boczkowski, J.6
  • 33
    • 57049151773 scopus 로고    scopus 로고
    • The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulphide: chemical mechanism and physiological significance
    • Cooper C.E., and Brown G.C. The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulphide: chemical mechanism and physiological significance. J. Bioenerg. Biomembr. 40 (2008) 533-539
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 533-539
    • Cooper, C.E.1    Brown, G.C.2
  • 34
    • 34447509483 scopus 로고    scopus 로고
    • Nitric oxide regulation of mitochondrial oxygen consumption II: molecular mechanism and tissue physiology
    • Cooper C.E., and Giulivi C. Nitric oxide regulation of mitochondrial oxygen consumption II: molecular mechanism and tissue physiology. Am. J. Physiol. Cell Physiol. 292 (2007) C1993-C2003
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Cooper, C.E.1    Giulivi, C.2
  • 35
    • 0031559913 scopus 로고    scopus 로고
    • Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidized copper: a general mechanism for the interaction of copper proteins with nitric oxide?
    • Cooper C.E., Torres J., Sharpe M.A., and Wilson M.T. Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidized copper: a general mechanism for the interaction of copper proteins with nitric oxide?. FEBS Lett. 414 (1997) 281-284
    • (1997) FEBS Lett. , vol.414 , pp. 281-284
    • Cooper, C.E.1    Torres, J.2    Sharpe, M.A.3    Wilson, M.T.4
  • 37
    • 33745486718 scopus 로고    scopus 로고
    • Inhibition of cellular respiration by endogenously produced carbon monoxide
    • D'Amico G., Lam F., Hagan T., and Moncada S. Inhibition of cellular respiration by endogenously produced carbon monoxide. J. Cell Sci. 119 (2006) 2291-2298
    • (2006) J. Cell Sci. , vol.119 , pp. 2291-2298
    • D'Amico, G.1    Lam, F.2    Hagan, T.3    Moncada, S.4
  • 38
    • 0032918830 scopus 로고    scopus 로고
    • Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells
    • Datta P.K., and Lianos E.A. Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells. Kidney Int. 55 (1999) 1734-1739
    • (1999) Kidney Int. , vol.55 , pp. 1734-1739
    • Datta, P.K.1    Lianos, E.A.2
  • 39
    • 0025051343 scopus 로고
    • The MSS51 gene product is required for the translation of the COX1 mRNA in yeast mitochondria
    • Decoster E., Simon M., Hatat D., and Faye G. The MSS51 gene product is required for the translation of the COX1 mRNA in yeast mitochondria. Mol. Gen. Genet. 224 (1990) 111-118
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 111-118
    • Decoster, E.1    Simon, M.2    Hatat, D.3    Faye, G.4
  • 40
    • 77954830445 scopus 로고    scopus 로고
    • Effects of exogenous carbon monoxide on neurocytes: experiment in vitro
    • Deng M., Zhao J.Y., and Fan D.S. Effects of exogenous carbon monoxide on neurocytes: experiment in vitro. Zhonghua Yi Xue Za Zhi 88 (2008) 3085-3089
    • (2008) Zhonghua Yi Xue Za Zhi , vol.88 , pp. 3085-3089
    • Deng, M.1    Zhao, J.Y.2    Fan, D.S.3
  • 41
    • 2442535969 scopus 로고    scopus 로고
    • Nitric oxide-induced transcriptional up-regulation of protective genes by Nrf2 via the antioxidant response element counteracts apoptosis of neuroblastoma cells
    • Dhakshinamoorthy S., and Porter A.G. Nitric oxide-induced transcriptional up-regulation of protective genes by Nrf2 via the antioxidant response element counteracts apoptosis of neuroblastoma cells. J. Biol. Chem. 279 (2004) 20096-20107
    • (2004) J. Biol. Chem. , vol.279 , pp. 20096-20107
    • Dhakshinamoorthy, S.1    Porter, A.G.2
  • 42
    • 62249115660 scopus 로고    scopus 로고
    • Mitochondrial pathways for ROS formation, myocardial injury: the relevance of p66(Shc), monoamine oxidase
    • Di Lisa F., Kaludercic N., Carpi A., Menabo R., and Giorgio M. Mitochondrial pathways for ROS formation, myocardial injury: the relevance of p66(Shc), monoamine oxidase. Basic Res. Cardiol. 104 (2009) 131-139
    • (2009) Basic Res. Cardiol. , vol.104 , pp. 131-139
    • Di Lisa, F.1    Kaludercic, N.2    Carpi, A.3    Menabo, R.4    Giorgio, M.5
  • 43
    • 0036146130 scopus 로고    scopus 로고
    • Cytochrome oxidase inhibition induced by acute hydrogen sulphide inhalation: correlation with tissue sulphide concentrations in the rat brain, liver, lung and nasal epithelium
    • Dorman D.C., Moulin F.J.M., McManus B.E., Mahle K.C., James R.A., and Struve M.F. Cytochrome oxidase inhibition induced by acute hydrogen sulphide inhalation: correlation with tissue sulphide concentrations in the rat brain, liver, lung and nasal epithelium. Toxicol. Sci. 65 (2002) 18-25
    • (2002) Toxicol. Sci. , vol.65 , pp. 18-25
    • Dorman, D.C.1    Moulin, F.J.M.2    McManus, B.E.3    Mahle, K.C.4    James, R.A.5    Struve, M.F.6
  • 44
    • 0030961521 scopus 로고    scopus 로고
    • Nitric oxide induces heme oxygenase-1 gene expression and carbon monoxide production in vascular smooth muscle cells
    • Durante W., Kroll M.H., Christodoulides N., Peyton K.J., and Scahfer A.I. Nitric oxide induces heme oxygenase-1 gene expression and carbon monoxide production in vascular smooth muscle cells. Circ. Res. 80 (1997) 557-564
    • (1997) Circ. Res. , vol.80 , pp. 557-564
    • Durante, W.1    Kroll, M.H.2    Christodoulides, N.3    Peyton, K.J.4    Scahfer, A.I.5
  • 45
    • 4444237412 scopus 로고    scopus 로고
    • 2S cytotoxicity mechanism involves reactive oxygen species formation and mitochondrial depolarisation
    • 2S cytotoxicity mechanism involves reactive oxygen species formation and mitochondrial depolarisation. Toxicology 203 (2004) 69-76
    • (2004) Toxicology , vol.203 , pp. 69-76
    • Eghbal, M.A.1    Pennefather, P.S.2    O'Brien, P.J.3
  • 46
    • 0032878565 scopus 로고    scopus 로고
    • Heme oxygenase: recent advances in understanding its regulation and role
    • Elbirt K.K., and Bonkovsky H.L. Heme oxygenase: recent advances in understanding its regulation and role. Proc. Assoc. Am. Physicians 111 (1999) 438-447
    • (1999) Proc. Assoc. Am. Physicians , vol.111 , pp. 438-447
    • Elbirt, K.K.1    Bonkovsky, H.L.2
  • 47
    • 0037064058 scopus 로고    scopus 로고
    • Biochemistry of mitochondrial nitric-oxide synthase
    • Elfering S.L., Sarkela T.M., and Giulivi C. Biochemistry of mitochondrial nitric-oxide synthase. J. Biol. Chem. 277 (2002) 38079-38086
    • (2002) J. Biol. Chem. , vol.277 , pp. 38079-38086
    • Elfering, S.L.1    Sarkela, T.M.2    Giulivi, C.3
  • 48
    • 42649100331 scopus 로고    scopus 로고
    • Mitochondrial mechanisms of sepsis-induced organ failure
    • Exline M.C., and Crouser E.D. Mitochondrial mechanisms of sepsis-induced organ failure. Front Biosci. 13 (2008) 5030-5041
    • (2008) Front Biosci. , vol.13 , pp. 5030-5041
    • Exline, M.C.1    Crouser, E.D.2
  • 50
    • 13244285610 scopus 로고    scopus 로고
    • Generation of bile pigments by haem oxygenase: a refined cellular strategy in response to stressful insults
    • Foresti R., Green C.J., and Motterlini R. Generation of bile pigments by haem oxygenase: a refined cellular strategy in response to stressful insults. Biochem. Soc. Symp. 71 (2004) 177-192
    • (2004) Biochem. Soc. Symp. , vol.71 , pp. 177-192
    • Foresti, R.1    Green, C.J.2    Motterlini, R.3
  • 51
    • 0033846743 scopus 로고    scopus 로고
    • Role of heme oxygenase-1 in the regulation of manganese superoxide dismutase gene expression in oxidatively-challenged astroglia
    • Frankel D., Mehindate K., and Schipper H.M. Role of heme oxygenase-1 in the regulation of manganese superoxide dismutase gene expression in oxidatively-challenged astroglia. J. Cell Physiol. 185 (2000) 80-86
    • (2000) J. Cell Physiol. , vol.185 , pp. 80-86
    • Frankel, D.1    Mehindate, K.2    Schipper, H.M.3
  • 52
    • 36248940497 scopus 로고    scopus 로고
    • Interactive endogenous small molecule (gaseous) signalling: implications for teratogenesis
    • Fukuto J.M., and Collins M.D. Interactive endogenous small molecule (gaseous) signalling: implications for teratogenesis. Curr. Pharm. Des. 13 (2007) 2952-2978
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 2952-2978
    • Fukuto, J.M.1    Collins, M.D.2
  • 53
    • 0037428488 scopus 로고    scopus 로고
    • Peroxynitrite protects neurons against nitric oxide-mediated apoptosis. A key role for glucose-6-phosphate dehydrogenase activity in neuroprotection
    • Garcia-Nogales P., Almeida A., and Bolanos J.P. Peroxynitrite protects neurons against nitric oxide-mediated apoptosis. A key role for glucose-6-phosphate dehydrogenase activity in neuroprotection. J. Biol. Chem. 278 (2003) 864-874
    • (2003) J. Biol. Chem. , vol.278 , pp. 864-874
    • Garcia-Nogales, P.1    Almeida, A.2    Bolanos, J.P.3
  • 54
    • 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 (1997) 291-296
    • (1997) FEBS Lett. , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 55
    • 0032883191 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase regulates mitochondrial matrix pH
    • Ghafourifar P., and Richter C. Mitochondrial nitric oxide synthase regulates mitochondrial matrix pH. Biol. Chem. 380 (1999) 1025-1028
    • (1999) Biol. Chem. , vol.380 , pp. 1025-1028
    • Ghafourifar, P.1    Richter, C.2
  • 57
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi C., Poderoso J.J., and Boveris A. Production of nitric oxide by mitochondria. J. Biol. Chem. 273 (1998) 11038-11043
    • (1998) J. Biol. Chem. , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 59
    • 30644480616 scopus 로고    scopus 로고
    • Arabidopsis nitric oxide synthase1 is targeted to mitochondria and protects against oxidative damage and dark-induced senescence
    • Guo F.Q., and Crawford N.M. Arabidopsis nitric oxide synthase1 is targeted to mitochondria and protects against oxidative damage and dark-induced senescence. Plant Cell. 17 (2005) 3436-3450
    • (2005) Plant Cell. , vol.17 , pp. 3436-3450
    • Guo, F.Q.1    Crawford, N.M.2
  • 60
    • 0141531067 scopus 로고    scopus 로고
    • Identification of a plant nitric oxide synthase gene involved in hormonal signaling
    • Guo F.Q., Okamoto M., and Crawford N.M. Identification of a plant nitric oxide synthase gene involved in hormonal signaling. Science 302 (2003) 100-103
    • (2003) Science , vol.302 , pp. 100-103
    • Guo, F.Q.1    Okamoto, M.2    Crawford, N.M.3
  • 61
    • 52649125410 scopus 로고    scopus 로고
    • Redox regulation of mitochondrial sulphide oxidation in the lugworm, Arenicola marina
    • Hildebrandt T.M., and Grieshaber M.K. Redox regulation of mitochondrial sulphide oxidation in the lugworm, Arenicola marina. J. Exp. Biol. 211 (2008) 2617-2623
    • (2008) J. Exp. Biol. , vol.211 , pp. 2617-2623
    • Hildebrandt, T.M.1    Grieshaber, M.K.2
  • 63
    • 58849151866 scopus 로고    scopus 로고
    • Hydrogen sulphide inhibits rotenone-induced apoptosis via preservation of mitochondrial function
    • Hu L.F., Lu M., Wu Z.Y., Wong P.T., and Bian J.S. Hydrogen sulphide inhibits rotenone-induced apoptosis via preservation of mitochondrial function. Mol. Pharmacol. 75 (2009) 27-34
    • (2009) Mol. Pharmacol. , vol.75 , pp. 27-34
    • Hu, L.F.1    Lu, M.2    Wu, Z.Y.3    Wong, P.T.4    Bian, J.S.5
  • 64
    • 0033605676 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide: implications for oxygen sensing and signalling
    • Huang L.E., Willmore W.G., Gu J., Goldberg M.A., and Bunn H.F. Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide: implications for oxygen sensing and signalling. J. Biol. Chem. 274 (1999) 9038-9044
    • (1999) J. Biol. Chem. , vol.274 , pp. 9038-9044
    • Huang, L.E.1    Willmore, W.G.2    Gu, J.3    Goldberg, M.A.4    Bunn, H.F.5
  • 65
    • 34548160965 scopus 로고    scopus 로고
    • Myocardial cytochrome oxidase activity is decreased following carbon monoxide exposure
    • Iheagwara K.N., Thom S.R., Deutschman C.S., and Levy R.J. Myocardial cytochrome oxidase activity is decreased following carbon monoxide exposure. Biochim. Biophys. Acta 1772 (2007) 1112-1116
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 1112-1116
    • Iheagwara, K.N.1    Thom, S.R.2    Deutschman, C.S.3    Levy, R.J.4
  • 68
    • 61749099621 scopus 로고    scopus 로고
    • Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex
    • Kapetanaki S.M., Silkstone G., Husu I., Liebl U., Wilson M.T., and Vos M.H. Interaction of carbon monoxide with the apoptosis-inducing cytochrome c-cardiolipin complex. Biochemistry 48 (2009) 1613-1619
    • (2009) Biochemistry , vol.48 , pp. 1613-1619
    • Kapetanaki, S.M.1    Silkstone, G.2    Husu, I.3    Liebl, U.4    Wilson, M.T.5    Vos, M.H.6
  • 69
    • 40949103593 scopus 로고    scopus 로고
    • Gasotransmitters in the gastrointestinal tract
    • Kasparek M.S., Linden D.R., Kreis M.E., and Sarr M.G. Gasotransmitters in the gastrointestinal tract. Surgery 143 (2007) 455-459
    • (2007) Surgery , vol.143 , pp. 455-459
    • Kasparek, M.S.1    Linden, D.R.2    Kreis, M.E.3    Sarr, M.G.4
  • 71
    • 33646185795 scopus 로고    scopus 로고
    • Carbon monoxide protects hepatocytes from TNF-alpha/actinomycin D by inhibition of the caspase-8-mediated apoptotic pathway
    • Kim H.S., Loughran P.A., Kim P.K., Billiar T.R., and Zuckerbraun B.S. Carbon monoxide protects hepatocytes from TNF-alpha/actinomycin D by inhibition of the caspase-8-mediated apoptotic pathway. Biochem. Biophys. Res. Commun. 344 (2006) 1172-1178
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 1172-1178
    • Kim, H.S.1    Loughran, P.A.2    Kim, P.K.3    Billiar, T.R.4    Zuckerbraun, B.S.5
  • 73
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulphide protects neurons from oxidative stress
    • Kimura Y., and Kimura H. Hydrogen sulphide protects neurons from oxidative stress. FASEB J. 18 (2004) 1165-1167
    • (2004) FASEB J. , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 74
    • 33646680757 scopus 로고    scopus 로고
    • Hydrogen sulphide protects HT22 neuronal cells from oxidative stress
    • Kimura Y., Dargusch R., Schubert D., and Kimura H. Hydrogen sulphide protects HT22 neuronal cells from oxidative stress. Antioxid. Redox Signal. 8 (2006) 661-670
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 661-670
    • Kimura, Y.1    Dargusch, R.2    Schubert, D.3    Kimura, H.4
  • 77
    • 0030716481 scopus 로고    scopus 로고
    • Kinetics of the inhibition of mitochondrial respiration by NO
    • Kovisto A., Matthias A., Bronnikov G., and Nedergaard J. Kinetics of the inhibition of mitochondrial respiration by NO. FEBS Lett. 417 (1997) 75-80
    • (1997) FEBS Lett. , vol.417 , pp. 75-80
    • Kovisto, A.1    Matthias, A.2    Bronnikov, G.3    Nedergaard, J.4
  • 79
    • 65649135789 scopus 로고    scopus 로고
    • Carbon monoxide rescues mice from lethal sepsis by supporting mitochondrial energetic metabolism and activating mitochondrial biogenesis
    • Lancel S., Hassoun S.M., Favory R., Decoster B., Motterlini R., and Neviere R. Carbon monoxide rescues mice from lethal sepsis by supporting mitochondrial energetic metabolism and activating mitochondrial biogenesis. J. Pharmacol. Exp. Ther. 329 (2009) 641-648
    • (2009) J. Pharmacol. Exp. Ther. , vol.329 , pp. 641-648
    • Lancel, S.1    Hassoun, S.M.2    Favory, R.3    Decoster, B.4    Motterlini, R.5    Neviere, R.6
  • 82
    • 36749002261 scopus 로고    scopus 로고
    • An overview of the biological significance of endogenous gases: new roles for old molecules
    • Li L., and Moore P.K. An overview of the biological significance of endogenous gases: new roles for old molecules. Biochem. Soc. Trans. 35 (2007) 1138-1141
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1138-1141
    • Li, L.1    Moore, P.K.2
  • 83
    • 33644618423 scopus 로고    scopus 로고
    • Carbon monoxide protects PC12 cells from peroxynitrite-induced apoptotic death by preventing the depolarization of mitochondrial transmembrane potential
    • Li M.H., Cha Y.N., and Surh Y.J. Carbon monoxide protects PC12 cells from peroxynitrite-induced apoptotic death by preventing the depolarization of mitochondrial transmembrane potential. Biochem. Biophys. Res. Commun. 342 (2006) 984-990
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 984-990
    • Li, M.H.1    Cha, Y.N.2    Surh, Y.J.3
  • 84
    • 34548224612 scopus 로고    scopus 로고
    • The regulatory effect of endogenous hydrogen sulphide on pulmonary vascular structure and gasotransmitters in rats with high pulmonary blood flow
    • Li X., Du J., Jin H., Tang X., Bu D., and Tang C. The regulatory effect of endogenous hydrogen sulphide on pulmonary vascular structure and gasotransmitters in rats with high pulmonary blood flow. Life Sci. 81 (2007) 841-849
    • (2007) Life Sci. , vol.81 , pp. 841-849
    • Li, X.1    Du, J.2    Jin, H.3    Tang, X.4    Bu, D.5    Tang, C.6
  • 85
    • 67849135882 scopus 로고    scopus 로고
    • Actions and interactions of nitric oxide, carbon monoxide and hydrogen sulphide in the cardiovascular system and in inflammation - a tale of three gases!
    • 10.1016/j.pharmathera.2009.05.005
    • Li L., Hsu A., and Moore P.K. Actions and interactions of nitric oxide, carbon monoxide and hydrogen sulphide in the cardiovascular system and in inflammation - a tale of three gases!. Pharmacol. Ther. (2009) 10.1016/j.pharmathera.2009.05.005
    • (2009) Pharmacol. Ther.
    • Li, L.1    Hsu, A.2    Moore, P.K.3
  • 87
    • 76049089746 scopus 로고    scopus 로고
    • The mechanisms of carbon monoxide inhalation on the apoptosis of pulmonary cells in rats with acute lung injury induced by lipopolysaccharide
    • Liu S.H., Ma K., Xu B., and Xu X.R. The mechanisms of carbon monoxide inhalation on the apoptosis of pulmonary cells in rats with acute lung injury induced by lipopolysaccharide. Zhonghua Jie He He Hu Xi Za Zhi 29 (2006) 329-332
    • (2006) Zhonghua Jie He He Hu Xi Za Zhi , vol.29 , pp. 329-332
    • Liu, S.H.1    Ma, K.2    Xu, B.3    Xu, X.R.4
  • 88
    • 0029981670 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite exert distinct effects on mitochondrial respiration which are differentially blocked by glutathione or glucose
    • Lizasoain I., Moro M.A., Knowles R.G., Darley-Usmar 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 (1996) 877-880
    • (1996) Biochem. J. , vol.314 , pp. 877-880
    • Lizasoain, I.1    Moro, M.A.2    Knowles, R.G.3    Darley-Usmar, V.4    Moncada, S.5
  • 89
    • 27744498588 scopus 로고    scopus 로고
    • Identification of an inducible nitric oxide synthase in diaphragm mitochondria from septic mice: its relation with mitochondrial dysfunction and prevention by melatonin
    • Lopez L.C., Escames G., Tapias V., Utrilla P., Leon J., and Acuna-Castroviejo D. Identification of an inducible nitric oxide synthase in diaphragm mitochondria from septic mice: its relation with mitochondrial dysfunction and prevention by melatonin. Int. J. Biochem. Cell Biol. 38 (2006) 267-278
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 267-278
    • Lopez, L.C.1    Escames, G.2    Tapias, V.3    Utrilla, P.4    Leon, J.5    Acuna-Castroviejo, D.6
  • 90
    • 34047142764 scopus 로고    scopus 로고
    • 2S): the third gas of interest for pharmacologists
    • 2S): the third gas of interest for pharmacologists. Pharmacol. Rep. 59 (2007) 4-24
    • (2007) Pharmacol. Rep. , vol.59 , pp. 4-24
    • Lowicka, E.1    Beltowski, J.2
  • 91
    • 0028984035 scopus 로고
    • The product of the nuclear gene PET309 is required for translation of mature mRNA and stability or production of intron-containing RNAs derived from the mitochondrial COX1 locus of Saccharomyces cerevisiae
    • Manthey G.M., and McEwen J.E. The product of the nuclear gene PET309 is required for translation of mature mRNA and stability or production of intron-containing RNAs derived from the mitochondrial COX1 locus of Saccharomyces cerevisiae. EMBO J. 14 (1995) 4031-4043
    • (1995) EMBO J. , vol.14 , pp. 4031-4043
    • Manthey, G.M.1    McEwen, J.E.2
  • 92
    • 0015935274 scopus 로고
    • Cytochrome c oxidase from bakers' yeast. II. Site of translation of the protein components
    • Mason T.L., and Schatz G. Cytochrome c oxidase from bakers' yeast. II. Site of translation of the protein components. J. Biol. Chem. 248 (1973) 1355-1360
    • (1973) J. Biol. Chem. , vol.248 , pp. 1355-1360
    • Mason, T.L.1    Schatz, G.2
  • 93
    • 31444433077 scopus 로고    scopus 로고
    • Nitric oxide inhibition of respiration involves both competitive (heme) and non-competitive (copper) binding to cytochrome c oxidase
    • Mason M.G., Nicholls P., Wilson M.T., and Cooper C.E. Nitric oxide inhibition of respiration involves both competitive (heme) and non-competitive (copper) binding to cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 103 (2006) 708-713
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 708-713
    • Mason, M.G.1    Nicholls, P.2    Wilson, M.T.3    Cooper, C.E.4
  • 96
    • 0031941816 scopus 로고    scopus 로고
    • The role of nitric oxide in neurodegeneration. Potential for pharmacological intervention
    • Molina J.A., Jimenez-Jimenez F.J., Orti-Pareja M., and Navarro J.A. The role of nitric oxide in neurodegeneration. Potential for pharmacological intervention. Drugs Aging 12 (1998) 251-259
    • (1998) Drugs Aging , vol.12 , pp. 251-259
    • Molina, J.A.1    Jimenez-Jimenez, F.J.2    Orti-Pareja, M.3    Navarro, J.A.4
  • 97
    • 0345118939 scopus 로고    scopus 로고
    • Hydrogen sulphide: from the smell of the past to the mediator of the future?
    • Moore P.K., Bhatia M., and Moochhala S. Hydrogen sulphide: from the smell of the past to the mediator of the future?. Trends Pharmacol. Sci. 24 (2003) 609-611
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 609-611
    • Moore, P.K.1    Bhatia, M.2    Moochhala, S.3
  • 98
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy M.P. How mitochondria produce reactive oxygen species. Biochem. J. 417 (2009) 1-13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 99
    • 0020149565 scopus 로고
    • Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system
    • Nicholls P., and Kim J.K. Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system. Can. J. Biochem. 60 (1982) 613-623
    • (1982) Can. J. Biochem. , vol.60 , pp. 613-623
    • Nicholls, P.1    Kim, J.K.2
  • 102
    • 33745115862 scopus 로고    scopus 로고
    • Hydrogen sulphide inhibits nitric oxide production and nuclear factor-kappa B via heme oxygenase-1 expression in RAW264.7 macrophages stimulated with lipopolysaccharide
    • Oh G.S., Pae H.O., Lee B.S., Kim B.N., Kim J.M., Kim H.R., Jeon S.B., Jeon W.K., Chae H.J., and Chung H.T. Hydrogen sulphide inhibits nitric oxide production and nuclear factor-kappa B via heme oxygenase-1 expression in RAW264.7 macrophages stimulated with lipopolysaccharide. Free Radical Biol. Med. 41 (2006) 106-119
    • (2006) Free Radical Biol. Med. , vol.41 , pp. 106-119
    • Oh, G.S.1    Pae, H.O.2    Lee, B.S.3    Kim, B.N.4    Kim, J.M.5    Kim, H.R.6    Jeon, S.B.7    Jeon, W.K.8    Chae, H.J.9    Chung, H.T.10
  • 104
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer R.M., Ferrige A.G., and Moncada S. Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 327 (1987) 524-526
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.1    Ferrige, A.G.2    Moncada, S.3
  • 105
    • 0021749064 scopus 로고
    • Effect of carbon monoxide exposure on heart cytochrome c oxidase activity of rats
    • Pankow D., and Ponsold W. Effect of carbon monoxide exposure on heart cytochrome c oxidase activity of rats. Biomed. Biochim. Acta 43 (1984) 1185-1189
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 1185-1189
    • Pankow, D.1    Ponsold, W.2
  • 106
    • 0346101794 scopus 로고    scopus 로고
    • Reversal of cyanide inhibition of cytochrome c oxidase by the auxiliary substrate nitric oxide
    • Pearce L.L., Bominaar E.L., Hill B.C., and Peterson J. Reversal of cyanide inhibition of cytochrome c oxidase by the auxiliary substrate nitric oxide. J. Biol. Chem. 278 (2003) 52139-52145
    • (2003) J. Biol. Chem. , vol.278 , pp. 52139-52145
    • Pearce, L.L.1    Bominaar, E.L.2    Hill, B.C.3    Peterson, J.4
  • 107
    • 57449091270 scopus 로고    scopus 로고
    • Antagonism of nitric oxide toward the inhibition of cytochrome c oxidase by carbon monoxide and cyanide
    • Pearce L.L., Lopez M.E., Martinez-Bosch S., and Peterson J. Antagonism of nitric oxide toward the inhibition of cytochrome c oxidase by carbon monoxide and cyanide. Chem. Res. Toxicol. 21 (2008) 2073-2081
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 2073-2081
    • Pearce, L.L.1    Lopez, M.E.2    Martinez-Bosch, S.3    Peterson, J.4
  • 110
    • 0017353388 scopus 로고
    • The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase
    • Petersen L.C. The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase. Biochim. Biophys. Acta 460 (1977) 299-307
    • (1977) Biochim. Biophys. Acta , vol.460 , pp. 299-307
    • Petersen, L.C.1
  • 111
    • 0036090811 scopus 로고    scopus 로고
    • Biological chemistry of carbon monoxide
    • Piantadosi C.A. Biological chemistry of carbon monoxide. Antioxid. Redox Signal. 4 (2002) 259-270
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 259-270
    • Piantadosi, C.A.1
  • 112
    • 48549090696 scopus 로고    scopus 로고
    • Carbon monoxide, reactive oxygen signalling and oxidative stress
    • Piantadosi C.A. Carbon monoxide, reactive oxygen signalling and oxidative stress. Free Radical Biol. Med. 45 (2008) 562-569
    • (2008) Free Radical Biol. Med. , vol.45 , pp. 562-569
    • Piantadosi, C.A.1
  • 113
    • 0023742503 scopus 로고
    • Direct effects of CO on cerebral energy metabolism in bloodless rats
    • Piantadosi C.A., Lee P.A., and Sylvia A.L. Direct effects of CO on cerebral energy metabolism in bloodless rats. J. Appl. Physiol. 65 (1988) 878-887
    • (1988) J. Appl. Physiol. , vol.65 , pp. 878-887
    • Piantadosi, C.A.1    Lee, P.A.2    Sylvia, A.L.3
  • 114
    • 0028964043 scopus 로고
    • Hydroxyl radical production in the brain after CO hypoxia in rats
    • Piantadosi C.A., Tatro L., and Zhang J. Hydroxyl radical production in the brain after CO hypoxia in rats. Free Radical Biol. Med. 18 (1995) 603-609
    • (1995) Free Radical Biol. Med. , vol.18 , pp. 603-609
    • Piantadosi, C.A.1    Tatro, L.2    Zhang, J.3
  • 115
    • 0031238801 scopus 로고    scopus 로고
    • Apoptosis and delayed neuronal damage after carbon monoxide poisoning in the rat
    • Piantadosi C.A., Zhang J., Levin E.D., Folz R.J., and Schmechel D.E. Apoptosis and delayed neuronal damage after carbon monoxide poisoning in the rat. Exp. Neurol. 147 (1997) 103-114
    • (1997) Exp. Neurol. , vol.147 , pp. 103-114
    • Piantadosi, C.A.1    Zhang, J.2    Levin, E.D.3    Folz, R.J.4    Schmechel, D.E.5
  • 116
    • 33646019300 scopus 로고    scopus 로고
    • Carbon monoxide, oxidative stress, and mitochondrial permeability pore transition
    • Piantadosi C.A., Carraway M.S., and Suliman H.B. Carbon monoxide, oxidative stress, and mitochondrial permeability pore transition. Free Radical Biol. Med. 40 (2006) 1332-1339
    • (2006) Free Radical Biol. Med. , vol.40 , pp. 1332-1339
    • Piantadosi, C.A.1    Carraway, M.S.2    Suliman, H.B.3
  • 117
    • 58149328569 scopus 로고    scopus 로고
    • Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via Nrf2-mediated transcriptional control of nuclear respiratory factor-1
    • Piantadosi C.A., Carraway M.S., Babikr A., and Suliman H.B. Heme oxygenase-1 regulates cardiac mitochondrial biogenesis via Nrf2-mediated transcriptional control of nuclear respiratory factor-1. Circ. Res. 103 (2008) 1232-1240
    • (2008) Circ. Res. , vol.103 , pp. 1232-1240
    • Piantadosi, C.A.1    Carraway, M.S.2    Babikr, A.3    Suliman, H.B.4
  • 118
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Ponderoso J.J., Carreras M.C., 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 (1996) 85-92
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 85-92
    • Ponderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobo, N.4    Schopfer, F.5    Boveris, A.6
  • 119
    • 66549128367 scopus 로고    scopus 로고
    • Interactions of the gaseous neuromodulators nitric oxide, carbon monoxide, and hydrogen sulphide in the salamander retina
    • 10.1002/jnr.22042
    • Pong W.W., and Eldred W.D. Interactions of the gaseous neuromodulators nitric oxide, carbon monoxide, and hydrogen sulphide in the salamander retina. J. Neurosci. Res. (2009) 10.1002/jnr.22042
    • (2009) J. Neurosci. Res.
    • Pong, W.W.1    Eldred, W.D.2
  • 120
    • 34548595561 scopus 로고    scopus 로고
    • Carbon monoxide intoxication: an updated review
    • Prockop L.D., and Chichkova R.I. Carbon monoxide intoxication: an updated review. J. Neurol. Sci. 262 (2007) 122-130
    • (2007) J. Neurol. Sci. , vol.262 , pp. 122-130
    • Prockop, L.D.1    Chichkova, R.I.2
  • 121
  • 123
    • 0035831466 scopus 로고    scopus 로고
    • The modulation of oxygen radical production by nitric oxide in mitochondria
    • Sarkela T.M., Berthiaume J., Elfering S., Gybina A.A., and Giulivi C. The modulation of oxygen radical production by nitric oxide in mitochondria. J. Biol. Chem. 276 (2001) 6945-6949
    • (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
  • 125
    • 0037116605 scopus 로고    scopus 로고
    • Participation of the mitochondrial permeability transition pore in nitric oxide-induced plant cell death
    • Saviani E.E., Orsi C.H., Oliveira J.F., Pinto-Maglio C.A., and Salgado I. Participation of the mitochondrial permeability transition pore in nitric oxide-induced plant cell death. FEBS Lett. 510 (2002) 136-140
    • (2002) FEBS Lett. , vol.510 , pp. 136-140
    • Saviani, E.E.1    Orsi, C.H.2    Oliveira, J.F.3    Pinto-Maglio, C.A.4    Salgado, I.5
  • 126
    • 54049113885 scopus 로고    scopus 로고
    • 2+ channels via redox modulation of key cysteine residues by mitochondrial reactive oxygen species J
    • 2+ channels via redox modulation of key cysteine residues by mitochondrial reactive oxygen species J. Biol. Chem. 283 (2008) 24412-24419
    • (2008) Biol. Chem. , vol.283 , pp. 24412-24419
    • Scragg, J.L.1    Dallas, M.L.2    Wilkinson, J.A.3    Varadi, G.4    Peers, C.5
  • 127
    • 33746215182 scopus 로고    scopus 로고
    • The antiapoptotic effect of heme oxygenase-1 in endothelial cells involves the degradation of p38 alpha MAPK isoform
    • Silva G., Cunha A., Gregoire I.P., Seldon M.P., and Soares M.P. The antiapoptotic effect of heme oxygenase-1 in endothelial cells involves the degradation of p38 alpha MAPK isoform. J. Immunol. 177 (2006) 1894-1903
    • (2006) J. Immunol. , vol.177 , pp. 1894-1903
    • Silva, G.1    Cunha, A.2    Gregoire, I.P.3    Seldon, M.P.4    Soares, M.P.5
  • 129
    • 0020315396 scopus 로고
    • Effect of different conditions of acute exposure to carbon monoxide on the cerebral high-energy phosphates and ultrastructure of brain mitochondria in rats
    • Sokal J.A., Opacka J., Gorny R., and Kolakowski J. Effect of different conditions of acute exposure to carbon monoxide on the cerebral high-energy phosphates and ultrastructure of brain mitochondria in rats. Toxicol. Lett. 11 (1982) 213-219
    • (1982) Toxicol. Lett. , vol.11 , pp. 213-219
    • Sokal, J.A.1    Opacka, J.2    Gorny, R.3    Kolakowski, J.4
  • 130
    • 29144519820 scopus 로고    scopus 로고
    • CO from enhanced HO activity or from CORM-2 inhibits both O2- and NO production and downregulates HO-1 expression in LPS-stimulated macrophages
    • Srisook K., Han S.S., Choi H.S., Li M.H., Ueda H., Kim C., and Cha Y.N. CO from enhanced HO activity or from CORM-2 inhibits both O2- and NO production and downregulates HO-1 expression in LPS-stimulated macrophages. Biochem. Pharmacol. 71 (2006) 307-318
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 307-318
    • Srisook, K.1    Han, S.S.2    Choi, H.S.3    Li, M.H.4    Ueda, H.5    Kim, C.6    Cha, Y.N.7
  • 133
    • 0020483746 scopus 로고
    • Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat
    • Stipanuk M.H., and Beck P.W. Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat. Biochem. J. 206 (1982) 267-277
    • (1982) Biochem. J. , vol.206 , pp. 267-277
    • Stipanuk, M.H.1    Beck, P.W.2
  • 134
    • 33846993042 scopus 로고    scopus 로고
    • A new activating role for CO in cardiac mitochondrial biogenesis
    • Suliman H.B., Carraway M.S., Tatro L.G., and Piantadosi C.A. A new activating role for CO in cardiac mitochondrial biogenesis. J. Cell Sci. 120 (2007) 299-308
    • (2007) J. Cell Sci. , vol.120 , pp. 299-308
    • Suliman, H.B.1    Carraway, M.S.2    Tatro, L.G.3    Piantadosi, C.A.4
  • 135
    • 0035893841 scopus 로고    scopus 로고
    • Characterization of NO binding to human cystathionine beta synthase: possible implications of the effects of CO and NO binding to the human enzyme
    • Taoka S., and Banerjee R. Characterization of NO binding to human cystathionine beta synthase: possible implications of the effects of CO and NO binding to the human enzyme. J. Inorg. Biochem. 87 (2001) 245-251
    • (2001) J. Inorg. Biochem. , vol.87 , pp. 245-251
    • Taoka, S.1    Banerjee, R.2
  • 136
    • 35348823035 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress in female and male rat brain after ex vivo carbon monoxide treatment
    • Taskiran D., Nesil T., and Alkan K. Mitochondrial oxidative stress in female and male rat brain after ex vivo carbon monoxide treatment. Toxicology 26 (2007) 645-651
    • (2007) Toxicology , vol.26 , pp. 645-651
    • Taskiran, D.1    Nesil, T.2    Alkan, K.3
  • 137
    • 40349111259 scopus 로고    scopus 로고
    • Sulfide:quinone oxidoreductase (SQR) from the lugworm Arenicola marina shows cyanide- and thioredoxin-dependent activity
    • Theissen U., and Martin W. Sulfide:quinone oxidoreductase (SQR) from the lugworm Arenicola marina shows cyanide- and thioredoxin-dependent activity. FEBS J. 275 (2008) 1131-1139
    • (2008) FEBS J. , vol.275 , pp. 1131-1139
    • Theissen, U.1    Martin, W.2
  • 138
    • 33751393197 scopus 로고    scopus 로고
    • Oxidative stress and damages to biomolecules (lipids, proteins, DNA)
    • Therond P. Oxidative stress and damages to biomolecules (lipids, proteins, DNA). Ann. Pharm. Fr. 64 (2006) 383-389
    • (2006) Ann. Pharm. Fr. , vol.64 , pp. 383-389
    • Therond, P.1
  • 140
  • 141
    • 25144524703 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocytes
    • Tsui T.Y., Siu Y.T., Scholitt H.J., and Fan S.T. Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocytes. Biochem. Biophys. Res. Commun. 336 (2005) 898-902
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 898-902
    • Tsui, T.Y.1    Siu, Y.T.2    Scholitt, H.J.3    Fan, S.T.4
  • 144
    • 0033120803 scopus 로고    scopus 로고
    • Nitric oxide-induced apoptosis in human leukemic lines requires mitochondrial lipid degradation and cytochrome c release
    • Ushmorov A., Ratter F., Lehmann V., Droge W., Schirrmacher V., and Umansky V. Nitric oxide-induced apoptosis in human leukemic lines requires mitochondrial lipid degradation and cytochrome c release. Blood 93 (1999) 2342-2352
    • (1999) Blood , vol.93 , pp. 2342-2352
    • Ushmorov, A.1    Ratter, F.2    Lehmann, V.3    Droge, W.4    Schirrmacher, V.5    Umansky, V.6
  • 146
  • 147
    • 53149154867 scopus 로고    scopus 로고
    • Pre-conditioning induced by carbon monoxide provides neuronal protection against apoptosis
    • Vieira H.L., Queiroga C.S., and Alves P.M. Pre-conditioning induced by carbon monoxide provides neuronal protection against apoptosis. J. Neurochem. 107 (2008) 375-384
    • (2008) J. Neurochem. , vol.107 , pp. 375-384
    • Vieira, H.L.1    Queiroga, C.S.2    Alves, P.M.3
  • 149
    • 0030068577 scopus 로고    scopus 로고
    • Mitochondrial sulphide oxidation in Arenicola marina. Evidence for alternative electron pathways
    • Volkel S., and Grieshaber M.K. Mitochondrial sulphide oxidation in Arenicola marina. Evidence for alternative electron pathways. Eur. J. Biochem. 235 (1996) 231-237
    • (1996) Eur. J. Biochem. , vol.235 , pp. 231-237
    • Volkel, S.1    Grieshaber, M.K.2
  • 150
    • 0036845556 scopus 로고    scopus 로고
    • 2S be the third endogenous gaseous transmitter?
    • 2S be the third endogenous gaseous transmitter?. FASEB J. 16 (2002) 1792-1798
    • (2002) FASEB J. , vol.16 , pp. 1792-1798
    • Wang, R.1
  • 151
    • 0025261953 scopus 로고
    • The pathophysiology of carbon monoxide poisoning and acute respiratory failure in a sheep model with smoke inhalation injury
    • Wang C.Z., Li A., and Yang Z.C. The pathophysiology of carbon monoxide poisoning and acute respiratory failure in a sheep model with smoke inhalation injury. Chest 97 (1990) 736-742
    • (1990) Chest , vol.97 , pp. 736-742
    • Wang, C.Z.1    Li, A.2    Yang, Z.C.3
  • 152
    • 44749095105 scopus 로고    scopus 로고
    • Role of gasotransmitters in the pathogenesis of pulmonary hypertension
    • Wang Y.F., Jin H.F., Tang C.S., and Du J.B. Role of gasotransmitters in the pathogenesis of pulmonary hypertension. Beijing Da Xue Xue Bao 38 (2006) 326-330
    • (2006) Beijing Da Xue Xue Bao , vol.38 , pp. 326-330
    • Wang, Y.F.1    Jin, H.F.2    Tang, C.S.3    Du, J.B.4
  • 153
    • 0024504354 scopus 로고
    • Acute hydrogen sulphide poisoning. Demonstration of selective uptake of sulphide by the brainstem by measurement of brain sulphide levels
    • Warenycia M.W., Goodwin L.R., Benishin C.G., Reiffenstein R.J., Francom D.M., Taylor J.D., and Dieken F.P. Acute hydrogen sulphide poisoning. Demonstration of selective uptake of sulphide by the brainstem by measurement of brain sulphide levels. Biochem. Pharmacol. 38 (1989) 973-981
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 973-981
    • Warenycia, M.W.1    Goodwin, L.R.2    Benishin, C.G.3    Reiffenstein, R.J.4    Francom, D.M.5    Taylor, J.D.6    Dieken, F.P.7
  • 154
    • 0034693251 scopus 로고    scopus 로고
    • Nitric oxide induces oxidative stress and apoptosis in neuronal cells
    • Wei T., Chen C., Hou J., Xin W., and Mori A. Nitric oxide induces oxidative stress and apoptosis in neuronal cells. Biochim. Biophys. Acta 1498 (2000) 72-79
    • (2000) Biochim. Biophys. Acta , vol.1498 , pp. 72-79
    • Wei, T.1    Chen, C.2    Hou, J.3    Xin, W.4    Mori, A.5
  • 155
    • 0030200037 scopus 로고    scopus 로고
    • The effects of nitric oxide on electron transport complexes
    • Welter R., Yu L., and Yu C.A. The effects of nitric oxide on electron transport complexes. Arch. Biochem. Biophys. 331 (1996) 9-14
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 9-14
    • Welter, R.1    Yu, L.2    Yu, C.A.3
  • 156
    • 0016852751 scopus 로고
    • Biochemical and biophysical studies on cytochrome c oxidase. XX. Reaction with sulphide
    • Wever R., van Gelder B.F., and Dervartanian D.V. Biochemical and biophysical studies on cytochrome c oxidase. XX. Reaction with sulphide. Biochim. Biophys. Acta 387 (1975) 189-193
    • (1975) Biochim. Biophys. Acta , vol.387 , pp. 189-193
    • Wever, R.1    van Gelder, B.F.2    Dervartanian, D.V.3
  • 157
    • 29844442868 scopus 로고    scopus 로고
    • Carbon monoxide: endogenous production, physiological functions, and pharmacological applications
    • Wu L., and Wang R. Carbon monoxide: endogenous production, physiological functions, and pharmacological applications. Pharmacol. Rev. 57 (2005) 585-630
    • (2005) Pharmacol. Rev. , vol.57 , pp. 585-630
    • Wu, L.1    Wang, R.2
  • 158
    • 19644368345 scopus 로고    scopus 로고
    • Nitric oxide: orchestrating hypoxia regulation through mitochondrial respiration and the endoplasmic reticulum stress response
    • Xu W., Charles I.G., and Moncada S. Nitric oxide: orchestrating hypoxia regulation through mitochondrial respiration and the endoplasmic reticulum stress response. Cell Res. 15 (2005) 63-65
    • (2005) Cell Res. , vol.15 , pp. 63-65
    • Xu, W.1    Charles, I.G.2    Moncada, S.3
  • 159
    • 0016275767 scopus 로고
    • Sequence of the reaction of heme catabolism catalysed by the microsomal heme oxygenase system
    • Yoshida T., and Kikuchi G. Sequence of the reaction of heme catabolism catalysed by the microsomal heme oxygenase system. FEBS Lett. 48 (1974) 256-261
    • (1974) FEBS Lett. , vol.48 , pp. 256-261
    • Yoshida, T.1    Kikuchi, G.2
  • 160
    • 33745312091 scopus 로고    scopus 로고
    • Nitric oxide/cGMP signalling pathway protects RAW264 cells against nitric oxide-induced apoptosis by inhibiting the activation of p38 mitogen-activated protein kinase
    • Yoshioka Y., Yamamuro A., and Maeda S. Nitric oxide/cGMP signalling pathway protects RAW264 cells against nitric oxide-induced apoptosis by inhibiting the activation of p38 mitogen-activated protein kinase. J. Pharmacol. Sci. 101 (2006) 126-134
    • (2006) J. Pharmacol. Sci. , vol.101 , pp. 126-134
    • Yoshioka, Y.1    Yamamuro, A.2    Maeda, S.3
  • 161
    • 0022452030 scopus 로고
    • Oxygenation of carbon monoxide by bovine heart cytochrome c oxidase
    • Young L.J., and Caughey W.S. Oxygenation of carbon monoxide by bovine heart cytochrome c oxidase. Biochemistry 25 (1986) 152-161
    • (1986) Biochemistry , vol.25 , pp. 152-161
    • Young, L.J.1    Caughey, W.S.2
  • 163
    • 15744378615 scopus 로고    scopus 로고
    • Carbon monoxide differentially modulates STAT1 and STAT3 and inhibits apoptosis via a phosphatidylinositol 3-kinase/Akt and p38 kinase-dependent STAT3 pathway during anoxia-reoxygenation injury
    • Zhang X., Shan P., Alam J., Fu X.Y., and Lee P.J. Carbon monoxide differentially modulates STAT1 and STAT3 and inhibits apoptosis via a phosphatidylinositol 3-kinase/Akt and p38 kinase-dependent STAT3 pathway during anoxia-reoxygenation injury. J. Biol. Chem. 280 (2005) 8714-8721
    • (2005) J. Biol. Chem. , vol.280 , pp. 8714-8721
    • Zhang, X.1    Shan, P.2    Alam, J.3    Fu, X.Y.4    Lee, P.J.5
  • 165
    • 33947628672 scopus 로고    scopus 로고
    • Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species
    • Zuckerbraun B.S., Chin B.Y., Bilban M., Costa d'Avila J., Rao J., Billiar T.R., and Ottebein L.E. Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species. FASEB J. 21 (2007) 1099-1106
    • (2007) FASEB J. , vol.21 , pp. 1099-1106
    • Zuckerbraun, B.S.1    Chin, B.Y.2    Bilban, M.3    Costa d'Avila, J.4    Rao, J.5    Billiar, T.R.6    Ottebein, L.E.7


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