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Volumn 26, Issue 1-2 SPEC. ISS., 2005, Pages 67-96

Nitric oxide and neurological disorders

Author keywords

Alzheimer's; Astrocyte; Mitochondria; Neurodegeneration; Nitric oxide (NO); Parkinson's

Indexed keywords

ENDOTHELIAL NITRIC OXIDE SYNTHASE; GLUTATHIONE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; INDUCIBLE NITRIC OXIDE SYNTHASE; NEURONAL NITRIC OXIDE SYNTHASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NITRIC OXIDE; NUCLEIC ACID; REACTIVE OXYGEN METABOLITE; UBIQUINONE;

EID: 13844292636     PISSN: 00982997     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mam.2004.09.004     Document Type: Review
Times cited : (164)

References (168)
  • 1
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • W.K. Alderton, C.E. Cooper, and R.G. Knowles Nitric oxide synthases: structure, function and inhibition Biochem. J. 357 2001 593 615
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 2
    • 1342310736 scopus 로고    scopus 로고
    • Nitric oxide switches on glycolysis through the AMP protein kinase and 6-phosphofructo-2-kinase pathway
    • A. Almeida, S. Moncada, and J.P. Bolaños Nitric oxide switches on glycolysis through the AMP protein kinase and 6-phosphofructo-2-kinase pathway Nat. Cell Biol. 6 2004 45 51
    • (2004) Nat. Cell Biol. , vol.6 , pp. 45-51
    • Almeida, A.1    Moncada, S.2    Bolaños, J.P.3
  • 3
    • 0024460992 scopus 로고
    • Endogenous oxidative DNA damage, aging, and cancer
    • B.N. Ames Endogenous oxidative DNA damage, aging, and cancer Free Radical Res. Commun. 7 1989 121 128
    • (1989) Free Radical Res. Commun. , vol.7 , pp. 121-128
    • Ames, B.N.1
  • 4
    • 0029003966 scopus 로고
    • Activity-dependant long-term enhancement of transmitter release by presynaptic 3′,5′-cyclic GMP in cultured hippocampal neurons
    • O. Arancio, E.R. Kander, and R.D. Hawkins Activity-dependant long-term enhancement of transmitter release by presynaptic 3′,5′-cyclic GMP in cultured hippocampal neurons Nat. Lond. 376 1995 74 80
    • (1995) Nat. Lond. , vol.376 , pp. 74-80
    • Arancio, O.1    Kander, E.R.2    Hawkins, R.D.3
  • 5
    • 0030582674 scopus 로고    scopus 로고
    • Nitric oxide acts directly in the presynaptic neuron in cultured hippocampal neurons
    • O. Arancio, M. Kieber, C.J. Lee, V. Lev-Ram, R.Y. Tsien, E.R. Kander, and R.D. Hawkins Nitric oxide acts directly in the presynaptic neuron in cultured hippocampal neurons Cell 87 1996 1025 1035
    • (1996) Cell , vol.87 , pp. 1025-1035
    • Arancio, O.1    Kieber, M.2    Lee, C.J.3    Lev-Ram, V.4    Tsien, R.Y.5    Kander, E.R.6    Hawkins, R.D.7
  • 7
    • 0030941354 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition by nitric oxide
    • M.Y. Balakirev, V.V. Khramtsov, and G. Zimmer Modulation of the mitochondrial permeability transition by nitric oxide Eur. J. Biochem. 246 1997 710 718
    • (1997) Eur. J. Biochem. , vol.246 , pp. 710-718
    • Balakirev, M.Y.1    Khramtsov, V.V.2    Zimmer, G.3
  • 8
    • 0035449358 scopus 로고    scopus 로고
    • Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitoxicity
    • A. Bal-Price, and G.C. Brown Inflammatory neurodegeneration mediated by nitric oxide from activated glia-inhibiting neuronal respiration, causing glutamate release and excitoxicity J. Neurosci. 21 2001 6480 6491
    • (2001) J. Neurosci. , vol.21 , pp. 6480-6491
    • Bal-Price, A.1    Brown, G.C.2
  • 9
    • 0029962693 scopus 로고    scopus 로고
    • Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage: Implications for neuronal/astrocytic trafficking and neurodegeneration
    • J.E. Barker, J.P. Bolaños, J.M. Land, J.B. Clark, and S.J.R. Heales Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage: implications for neuronal/astrocytic trafficking and neurodegeneration Dev. Neurosci. 18 1996 391 396
    • (1996) Dev. Neurosci. , vol.18 , pp. 391-396
    • Barker, J.E.1    Bolaños, J.P.2    Land, J.M.3    Clark, J.B.4    Heales, S.J.R.5
  • 11
    • 0034742653 scopus 로고    scopus 로고
    • Coenzymes Q9 and Q10, vitamin e and peroxidation in rat synaptic and non-synaptic occipital cerebral cortex mitochondria during ageing
    • M. Battino, S. Bompadre, L. Leone, R.F. Villa, and A. Gorini Coenzymes Q9 and Q10, vitamin E and peroxidation in rat synaptic and non-synaptic occipital cerebral cortex mitochondria during ageing Biol. Chem. 382 2001 925 931
    • (2001) Biol. Chem. , vol.382 , pp. 925-931
    • Battino, M.1    Bompadre, S.2    Leone, L.3    Villa, R.F.4    Gorini, A.5
  • 12
    • 0027477946 scopus 로고
    • Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases?
    • M.F. Beal, B.T. Hyman, and W. Koroshetz Do defects in mitochondrial energy metabolism underlie the pathology of neurodegenerative diseases? Trends Neurosci. 16 1993 125 131
    • (1993) Trends Neurosci. , vol.16 , pp. 125-131
    • Beal, M.F.1    Hyman, B.T.2    Koroshetz, W.3
  • 13
    • 0034057120 scopus 로고    scopus 로고
    • Oxidative stress and S-nitrosylation of proteins in cells
    • B. Beltran, A. Orsi, E. Clementi, and S. Moncada Oxidative stress and S-nitrosylation of proteins in cells Br. J. Pharmacol. 129 2000 953 960
    • (2000) Br. J. Pharmacol. , vol.129 , pp. 953-960
    • Beltran, B.1    Orsi, A.2    Clementi, E.3    Moncada, S.4
  • 14
    • 0028893441 scopus 로고
    • Increased number of NADPH-D-positive neurons within the substantia innominata in Alzheimer's disease
    • W.C. Benzing, and E.J. Mufson Increased number of NADPH-D-positive neurons within the substantia innominata in Alzheimer's disease Brain 670 1995 351 355
    • (1995) Brain , vol.670 , pp. 351-355
    • Benzing, W.C.1    Mufson, E.J.2
  • 15
    • 0021997074 scopus 로고
    • Poly(ADP-ribose) in the cellular response to DNA damage
    • N.A. Berger Poly(ADP-ribose) in the cellular response to DNA damage Radiat. Res. 101 1985 4 15
    • (1985) Radiat. Res. , vol.101 , pp. 4-15
    • Berger, N.A.1
  • 16
    • 0033961818 scopus 로고    scopus 로고
    • In vitro expression of N-acetyl aspartate by oligodendrocytes: Implications for proton magnetic resonance spectroscopy signal in vivo
    • K.K. Bhakoo, and D. Pearce In vitro expression of N-acetyl aspartate by oligodendrocytes: implications for proton magnetic resonance spectroscopy signal in vivo J. Neurochem. 74 2000 254 262
    • (2000) J. Neurochem. , vol.74 , pp. 254-262
    • Bhakoo, K.K.1    Pearce, D.2
  • 18
    • 0028145462 scopus 로고
    • Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes
    • J.P. Bolaños, S. Peuchen, S.J.R. Heales, J.M. Land, and J.B. Clark Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes J. Neurochem. 63 1994 910 916
    • (1994) J. Neurochem. , vol.63 , pp. 910-916
    • Bolaños, J.P.1    Peuchen, S.2    Heales, S.J.R.3    Land, J.M.4    Clark, J.B.5
  • 19
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary cultures
    • J.P. Bolaños, S.J.R. Heales, J.M. Land, and J.B. Clark Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary cultures J. Neurochem. 64 1995 1965 1972
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolaños, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 21
    • 0038233014 scopus 로고    scopus 로고
    • Nitric oxide-mediated mitochondrial damage in the brain: Mechanisms and implications for neurodegenerative diseases
    • J.P. Bolaños, A. Almeida, V. Stewart, S. Peuchen, J.M. Land, J.B. Clark, and S.J.R. Heales Nitric oxide-mediated mitochondrial damage in the brain: mechanisms and implications for neurodegenerative diseases J. Neurochem. 68 1997 2227 2240
    • (1997) J. Neurochem. , vol.68 , pp. 2227-2240
    • Bolaños, J.P.1    Almeida, A.2    Stewart, V.3    Peuchen, S.4    Land, J.M.5    Clark, J.B.6    Heales, S.J.R.7
  • 24
    • 0032740245 scopus 로고    scopus 로고
    • Endogenous nitric oxide synthesis: Biological functions and pathophysiology
    • D.S. Bredt Endogenous nitric oxide synthesis: biological functions and pathophysiology Free Radical Res. 31 1999 577 596
    • (1999) Free Radical Res. , vol.31 , pp. 577-596
    • Bredt, D.S.1
  • 25
    • 0030832712 scopus 로고    scopus 로고
    • Stimulation of glyceraldehyde-3-phosphate dehydrogenase by oxyhemoglobin
    • P.S. Brookes, J.M. Land, J.B. Clark, and S.J.R. Heales Stimulation of glyceraldehyde-3-phosphate dehydrogenase by oxyhemoglobin FEBS Lett. 416 1997 90 92
    • (1997) FEBS Lett. , vol.416 , pp. 90-92
    • Brookes, P.S.1    Land, J.M.2    Clark, J.B.3    Heales, S.J.R.4
  • 26
    • 0031970112 scopus 로고    scopus 로고
    • Peroxynitrite and brain mitochondria: Evidence for increased proton leak
    • P.S. Brookes, J.M. Land, J.B. Clark, and S.J.R. Heales Peroxynitrite and brain mitochondria: evidence for increased proton leak J. Neurochem. 70 1998 2195 2202
    • (1998) J. Neurochem. , vol.70 , pp. 2195-2202
    • Brookes, P.S.1    Land, J.M.2    Clark, J.B.3    Heales, S.J.R.4
  • 27
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase
    • G.C. Brown Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase FEBS Lett. 369 1995 136 139
    • (1995) FEBS Lett. , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 28
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • G.C. Brown, and C.E. Cooper 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
  • 29
    • 0019322671 scopus 로고
    • Reactions of nitric oxide with cytochrome c oxidase
    • G.W. Brudvig, T.H. Stevens, and S.I. Chan Reactions of nitric oxide with cytochrome c oxidase Biochemistry 19 1980 5275 5285
    • (1980) Biochemistry , vol.19 , pp. 5275-5285
    • Brudvig, G.W.1    Stevens, T.H.2    Chan, S.I.3
  • 31
    • 0001627970 scopus 로고
    • Inhibition of smooth muscle in the taenia coli
    • G. Burnstock, G. Campbell, M. Bennett, and M. Holman Inhibition of smooth muscle in the taenia coli Nature 200 1963 581 582
    • (1963) Nature , vol.200 , pp. 581-582
    • Burnstock, G.1    Campbell, G.2    Bennett, M.3    Holman, M.4
  • 32
    • 0032810909 scopus 로고    scopus 로고
    • Beta-amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • L. Canevari, J.B. Clark, and T.E. Bates Beta-amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria FEBS Lett. 457 1999 131 134
    • (1999) FEBS Lett. , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 33
    • 0012701946 scopus 로고    scopus 로고
    • Amyloid β peptide inhibits mitochondrial enzymes and function
    • L. Canevari, C.S. Casley, M.A. Sharpe, and J.M. Land Amyloid β peptide inhibits mitochondrial enzymes and function J. Neurochem. 76 Suppl. 1 2001 30
    • (2001) J. Neurochem. , vol.76 , Issue.1 SUPPL. , pp. 30
    • Canevari, L.1    Casley, C.S.2    Sharpe, M.A.3    Land, J.M.4
  • 34
    • 0033989493 scopus 로고    scopus 로고
    • Reduced apoptosis after nerve growth factor and serum withdrawal: Conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer
    • G.W. Carlile, R.M. Chalmers-Redman, N.A. Tatton, A. Pong, K.E. Borden, and W.G. Tatton Reduced apoptosis after nerve growth factor and serum withdrawal: conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer Mol. Pharmacol. 57 2000 2 12
    • (2000) Mol. Pharmacol. , vol.57 , pp. 2-12
    • Carlile, G.W.1    Chalmers-Redman, R.M.2    Tatton, N.A.3    Pong, A.4    Borden, K.E.5    Tatton, W.G.6
  • 36
    • 0036272650 scopus 로고    scopus 로고
    • β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • C.S. Casley, L. Canevari, J.M. Land, J.B. Clark, and M.A. Sharpe β-Amyloid inhibits integrated mitochondrial respiration and key enzyme activities J. Neurochem. 80 2002 91 100
    • (2002) J. Neurochem. , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 38
    • 0026598930 scopus 로고
    • Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium: Evidence for free radical involvement
    • M.J.W. Cleeter, J.M. Cooper, and A.H.V. Schapira Irreversible inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium: evidence for free radical involvement J. Neurochem. 58 1992 786 789
    • (1992) J. Neurochem. , vol.58 , pp. 786-789
    • Cleeter, M.J.W.1    Cooper, J.M.2    Schapira, A.H.V.3
  • 39
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective role of glutathione
    • E. Clementi, G.C. Brown, M. Feelisch, and S. Moncada Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective role of glutathione Proc. Natl. Acad. Sci. USA 95 1998 7631 7636
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 40
    • 0031788691 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase abnormality in metabolically stressed Huntington disease fibroblasts
    • A.J. Cooper, K.F. Sheu, J.R. Burke, W.J. Strittmatter, and JP. Blass Glyceraldehyde 3-phosphate dehydrogenase abnormality in metabolically stressed Huntington disease fibroblasts Dev. Neurosci. 20 1998 462 468
    • (1998) Dev. Neurosci. , vol.20 , pp. 462-468
    • Cooper, A.J.1    Sheu, K.F.2    Burke, J.R.3    Strittmatter, W.J.4    Blass, J.P.5
  • 42
    • 0033389550 scopus 로고    scopus 로고
    • Implication of poly(ADP-ribose) polymerase (PARP) in neurodegeneration and brain energy metabolism. Decreases in mouse brain NAD+ and ATP caused by MPTP are prevented by the PARP inhibitor benzamide
    • C. Cosi, and M. Marien Implication of poly(ADP-ribose) polymerase (PARP) in neurodegeneration and brain energy metabolism. Decreases in mouse brain NAD+ and ATP caused by MPTP are prevented by the PARP inhibitor benzamide Ann. NY Acad Sci. 890 1999 227 239
    • (1999) Ann. NY Acad Sci. , vol.890 , pp. 227-239
    • Cosi, C.1    Marien, M.2
  • 43
    • 0030581308 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase inhibitors protect against MPTP-induced depletions of striatal dopamine and cortical noradrenaline in C57B1/6 mice
    • C. Cosi, F. Colpaert, W. Koek, A. Degryse, and M. Marien Poly(ADP-ribose) polymerase inhibitors protect against MPTP-induced depletions of striatal dopamine and cortical noradrenaline in C57B1/6 mice Brain Res. 729 1996 264 269
    • (1996) Brain Res. , vol.729 , pp. 264-269
    • Cosi, C.1    Colpaert, F.2    Koek, W.3    Degryse, A.4    Marien, M.5
  • 44
    • 0030574060 scopus 로고    scopus 로고
    • Benzamide, an inhibitor of poly(ADP-ribose) polymerase, attenuates methamphetamine-induced dopamine neurotoxicity in the C57B1/6N mouse
    • C. Cosi, P. Chopin, and M. Marien Benzamide, an inhibitor of poly(ADP-ribose) polymerase, attenuates methamphetamine-induced dopamine neurotoxicity in the C57B1/6N mouse Brain Res. 735 1996 343 348
    • (1996) Brain Res. , vol.735 , pp. 343-348
    • Cosi, C.1    Chopin, P.2    Marien, M.3
  • 47
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • M. Crompton The mitochondrial permeability transition pore and its role in cell death Biochem. J. 341 1999 233 249
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 48
    • 0345491834 scopus 로고    scopus 로고
    • Long-term plasticity of intrinsic excitability: Learning rules and mechanisms
    • G. Daoudal, and D. Debanne Long-term plasticity of intrinsic excitability: learning rules and mechanisms Learn. Memory 10 2003 456 465
    • (2003) Learn. Memory , vol.10 , pp. 456-465
    • Daoudal, G.1    Debanne, D.2
  • 49
    • 0029873904 scopus 로고    scopus 로고
    • Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria
    • G.P. Davey, and J.B. Clark Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria J. Neurochem. 66 1996 1617 1624
    • (1996) J. Neurochem. , vol.66 , pp. 1617-1624
    • Davey, G.P.1    Clark, J.B.2
  • 53
    • 0033979993 scopus 로고    scopus 로고
    • Inflammation and stroke: Putative role for cytokines, adhesion molecules and iNOS in brain response to ischemia
    • G. del Zoppo, I. Ginis, J.M. Hallenbeck, C. Iadecola, X. Wang, and G.Z. Feuerstein Inflammation and stroke: putative role for cytokines, adhesion molecules and iNOS in brain response to ischemia Brain Pathol. 10 2000 95 112
    • (2000) Brain Pathol. , vol.10 , pp. 95-112
    • Del Zoppo, G.1    Ginis, I.2    Hallenbeck, J.M.3    Iadecola, C.4    Wang, X.5    Feuerstein, G.Z.6
  • 54
    • 0028792005 scopus 로고
    • Reversible decreases in N-acetylaspartate after acute brain injury
    • N. DeStefano, P.M. Matthews, and D.L. Arnold Reversible decreases in N-acetylaspartate after acute brain injury Magn. Res. Med. 34 1995 721 727
    • (1995) Magn. Res. Med. , vol.34 , pp. 721-727
    • Destefano, N.1    Matthews, P.M.2    Arnold, D.L.3
  • 55
    • 0028124916 scopus 로고
    • Nitric oxide synthase activation is elevated in brain microvessels in Alzheimer's disease
    • M.A. Dorheim, W.R. Tracey, J.S. Pollock, and P. Grammas Nitric oxide synthase activation is elevated in brain microvessels in Alzheimer's disease Biochem. Biophys. Res. Commun. 205 1994 659 665
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 659-665
    • Dorheim, M.A.1    Tracey, W.R.2    Pollock, J.S.3    Grammas, P.4
  • 56
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • R. Dringen Metabolism and functions of glutathione in brain Prog. Neurobiol. 62 2000 649 671
    • (2000) Prog. Neurobiol. , vol.62 , pp. 649-671
    • Dringen, R.1
  • 57
    • 0033555806 scopus 로고    scopus 로고
    • Synthesis of the antioxidant glutathione in neurons: Supply by astrocytes of cys-gly as precursor for neuronal glutathione
    • R. Dringen, B. Pfeiffer, and B. Hamprecht Synthesis of the antioxidant glutathione in neurons: supply by astrocytes of cys-gly as precursor for neuronal glutathione J. Neurosci. 19 1999 562 569
    • (1999) J. Neurosci. , vol.19 , pp. 562-569
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 58
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • X. Du, T. Matsumura, D. Edelstein, L. Rossetti, Z. Zsengeller, C. Szabo, and M. Brownlee Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells Clin. Invest. 112 2003 1049 1057
    • (2003) Clin. Invest. , vol.112 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3    Rossetti, L.4    Zsengeller, Z.5    Szabo, C.6    Brownlee, M.7
  • 59
    • 0026034352 scopus 로고
    • NMDA receptor in rat hippocampus induces cyclic GMP formation through the l-arginine-nitric oxide pathway
    • S.J. East, and J. Garthwaite NMDA receptor in rat hippocampus induces cyclic GMP formation through the l-arginine-nitric oxide pathway Neurosci. Lett. 123 1991 17 19
    • (1991) Neurosci. Lett. , vol.123 , pp. 17-19
    • East, S.J.1    Garthwaite, J.2
  • 60
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • L. Ernster, and G. Dallner Biochemical, physiological and medical aspects of ubiquinone function Biochim. Biophys. Acta 1271 1995 195 204
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 61
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • T.G. Frey, and C.A. Mannella The internal structure of mitochondria Trends Biochem. Sci. 25 2000 319 324
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 62
    • 0031571757 scopus 로고    scopus 로고
    • 2+ independent permeabilisation of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross linking and lipid peroxidation
    • 2+ independent permeabilisation of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross linking and lipid peroxidation Arch. Biochem. Biophys. 345 1997 243 250
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 243-250
    • Gadelha, F.R.1    Thomson, L.2    Fagian, M.M.3    Costa, A.D.T.4    Radi, R.5    Vercesi, A.E.6
  • 63
    • 0028917372 scopus 로고
    • Nitric oxide signalling in the central nervous system
    • J. Garthwaite, and C.L. Boulton Nitric oxide signalling in the central nervous system Ann. Rev. Physiol. 57 1995 683 706
    • (1995) Ann. Rev. Physiol. , vol.57 , pp. 683-706
    • Garthwaite, J.1    Boulton, C.L.2
  • 64
    • 0024462440 scopus 로고
    • NMDA receptor activation induces nitric oxide synthesis from arginine in rat brain slices
    • J. Garthwaite, G. Garthwaite, R.M. Palmer, and S. Moncada NMDA receptor activation induces nitric oxide synthesis from arginine in rat brain slices Eur. J. Pharmacol. 172 1989 413 416
    • (1989) Eur. J. Pharmacol. , vol.172 , pp. 413-416
    • Garthwaite, J.1    Garthwaite, G.2    Palmer, R.M.3    Moncada, S.4
  • 65
    • 0038308447 scopus 로고    scopus 로고
    • Differential effect of nitric oxide on glutathione metabolism and mitochondrial function in astrocytes and neurones: Implications for neuroprotection/neurodegeneration?
    • M.E. Gegg, B. Beltran, S. Salas-Pino, J.P. Bolaños, J.B. Clark, S. Moncada, and S.J.R. Heales Differential effect of nitric oxide on glutathione metabolism and mitochondrial function in astrocytes and neurones: implications for neuroprotection/neurodegeneration? J. Neurochem. 86 2003 228 237
    • (2003) J. Neurochem. , vol.86 , pp. 228-237
    • Gegg, M.E.1    Beltran, B.2    Salas-Pino, S.3    Bolaños, J.P.4    Clark, J.B.5    Moncada, S.6    Heales, S.J.R.7
  • 66
    • 0026655617 scopus 로고
    • Interferon-γ and tumor necrosis factor synergize to induce nitric oxide production and inhibit mitochondrial respiration in vascular smooth muscle cells
    • Y. Geng, G.K. Hansson, and E. Holme Interferon-γ and tumor necrosis factor synergize to induce nitric oxide production and inhibit mitochondrial respiration in vascular smooth muscle cells Circ. Res. 71 1992 1268 1276
    • (1992) Circ. Res. , vol.71 , pp. 1268-1276
    • Geng, Y.1    Hansson, G.K.2    Holme, E.3
  • 67
    • 0024836368 scopus 로고
    • The effects of l-arginine and NG-monomethyl l-arginine on the response of the rat anococcygeus muscle to NANC nerve stimulation
    • J.S. Gillespie, X.R. Liu, and W. Martin The effects of l-arginine and NG-monomethyl l-arginine on the response of the rat anococcygeus muscle to NANC nerve stimulation Br. J. Pharmacol. 98 1989 1080 1082
    • (1989) Br. J. Pharmacol. , vol.98 , pp. 1080-1082
    • Gillespie, J.S.1    Liu, X.R.2    Martin, W.3
  • 68
    • 0029969350 scopus 로고    scopus 로고
    • Nature of inhibition of mitochondrial respiratory complex I by 6-hydroxydopamine
    • Y. Glinka, K.F. Tipton, and M.B.H. Youdim Nature of inhibition of mitochondrial respiratory complex I by 6-hydroxydopamine J. Neurochem. 66 1996 2004 2010
    • (1996) J. Neurochem. , vol.66 , pp. 2004-2010
    • Glinka, Y.1    Tipton, K.F.2    Youdim, M.B.H.3
  • 70
    • 0029976959 scopus 로고    scopus 로고
    • Reduced brain edema and infarction volume in mice lacking the neuronal isoform of nitric oxide synthase after transient MCA occlusion
    • H. Hara, P.L. Huang, N. Panahian, M.C. Fishman, and M.A.. Moskowitz Reduced brain edema and infarction volume in mice lacking the neuronal isoform of nitric oxide synthase after transient MCA occlusion J. Cerebr. Blood Flow Metab. 16 1996 605 611
    • (1996) J. Cerebr. Blood Flow Metab. , vol.16 , pp. 605-611
    • Hara, H.1    Huang, P.L.2    Panahian, N.3    Fishman, M.C.4    Moskowitz, M.A.5
  • 71
    • 0036391974 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a regulator of chemokine production: Relevance for the pathogenesis of shock and inflammation
    • G. Hasko, J.G. Mabley, Z.H. Nemeth, P. Pacher, E.A. Deitch, and C. Szabo Poly(ADP-ribose) polymerase is a regulator of chemokine production: relevance for the pathogenesis of shock and inflammation Mol. Med. 8 2002 189 283
    • (2002) Mol. Med. , vol.8 , pp. 189-283
    • Hasko, G.1    Mabley, J.G.2    Nemeth, Z.H.3    Pacher, P.4    Deitch, E.A.5    Szabo, C.6
  • 72
    • 0036175622 scopus 로고    scopus 로고
    • Impairment of brain mitochondrial function by reactive nitrogen species: The role of glutathione in dictating susceptibility
    • S.J.R. Heales, and J.P. Bolaños Impairment of brain mitochondrial function by reactive nitrogen species: the role of glutathione in dictating susceptibility Neurochem. Int. 1157 2002 1 6
    • (2002) Neurochem. Int. , vol.1157 , pp. 1-6
    • Heales, S.J.R.1    Bolaños, J.P.2
  • 73
    • 0028799706 scopus 로고
    • Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration
    • S.J.R. Heales, S.E.C. Davies, T.E. Bates, and J.B. Clark Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration Neurochem. Res. 20 1995 31 38
    • (1995) Neurochem. Res. , vol.20 , pp. 31-38
    • Heales, S.J.R.1    Davies, S.E.C.2    Bates, T.E.3    Clark, J.B.4
  • 76
    • 1542348215 scopus 로고    scopus 로고
    • Neurodegeneration or Neuroprotection: The pivotal role of astrocytes
    • S.J.R. Heales, A.A.J. Lam, A.J. Duncan, and J.M. Land Neurodegeneration or Neuroprotection: the pivotal role of astrocytes Neurochem. Res. 29 2004 513 519
    • (2004) Neurochem. Res. , vol.29 , pp. 513-519
    • Heales, S.J.R.1    Lam, A.A.J.2    Duncan, A.J.3    Land, J.M.4
  • 78
    • 0036682171 scopus 로고    scopus 로고
    • Glutathione release from cultured brain cells: Multidrug resistance protein 1 mediates the release of GSH from rat astroglial cells
    • J. Hirrlinger, J.B. Schulz, and R. Dringen Glutathione release from cultured brain cells: multidrug resistance protein 1 mediates the release of GSH from rat astroglial cells J. Neurosci. Res. 69 2002 318 326
    • (2002) J. Neurosci. Res. , vol.69 , pp. 318-326
    • Hirrlinger, J.1    Schulz, J.B.2    Dringen, R.3
  • 79
    • 0040830408 scopus 로고    scopus 로고
    • Nitric oxide, the enigmatic neuronal messenger: Its role in synaptic plasticity
    • C. Holscher Nitric oxide, the enigmatic neuronal messenger: its role in synaptic plasticity Trends Neurosci. 20 1997 298 303
    • (1997) Trends Neurosci. , vol.20 , pp. 298-303
    • Holscher, C.1
  • 80
    • 0031104935 scopus 로고    scopus 로고
    • A role for nitric oxide in LTP
    • E.P. Huang A role for nitric oxide in LTP Curr. Biol. 7 1997 R141 R143
    • (1997) Curr. Biol. , vol.7
    • Huang, E.P.1
  • 82
    • 0032902721 scopus 로고    scopus 로고
    • Relationships between nitric oxide, nitroxyl ion, nitrosonium cation and peroxynitrite
    • M.N. Hughes Relationships between nitric oxide, nitroxyl ion, nitrosonium cation and peroxynitrite Biochim. Biophys. Acta 1411 1999 263 272
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 263-272
    • Hughes, M.N.1
  • 83
    • 0037378023 scopus 로고    scopus 로고
    • Neuroinflammatory processes in Parkinson's disease
    • S. Hunot, and E.C. Hirsch Neuroinflammatory processes in Parkinson's disease Ann. Neurol. 53 2003 S49 S60
    • (2003) Ann. Neurol. , vol.53
    • Hunot, S.1    Hirsch, E.C.2
  • 85
    • 0035896372 scopus 로고    scopus 로고
    • Nitric-oxide-induced inhibition of glyceraldehyde-3-phosphate dehydrogenase may mediate reduced endothelial cell monolayer integrity in an in vitro model blood-brain barrier
    • R.D. Hurst, S. Ama, A. Hurst, and J.B. Clark Nitric-oxide-induced inhibition of glyceraldehyde-3-phosphate dehydrogenase may mediate reduced endothelial cell monolayer integrity in an in vitro model blood-brain barrier Brain Res. 894 2001 181 188
    • (2001) Brain Res. , vol.894 , pp. 181-188
    • Hurst, R.D.1    Ama, S.2    Hurst, A.3    Clark, J.B.4
  • 86
    • 0030426279 scopus 로고    scopus 로고
    • An antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase blocks age-induced apoptosis of mature cerebrocortical neurons in culture
    • R. Ishitani, M. Kimura, K. Sunaga, N. Katsube, M. Tanaka, and D.M. Chuang An antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase blocks age-induced apoptosis of mature cerebrocortical neurons in culture J. Pharmacol. Exp. Ther. 278 1996 447 454
    • (1996) J. Pharmacol. Exp. Ther. , vol.278 , pp. 447-454
    • Ishitani, R.1    Kimura, M.2    Sunaga, K.3    Katsube, N.4    Tanaka, M.5    Chuang, D.M.6
  • 87
    • 0026635461 scopus 로고
    • Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease
    • P. Jenner, D.T. Dexter, J. Sian, A.H.V. Schapira, and C.D. Marsden Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease Ann. Neurol. 32 1992 S82 S87
    • (1992) Ann. Neurol. , vol.32
    • Jenner, P.1    Dexter, D.T.2    Sian, J.3    Schapira, A.H.V.4    Marsden, C.D.5
  • 90
    • 0024401216 scopus 로고
    • Age-related changes in the lipid compositions of rat and human tissues
    • A. Kalen, E.L. Appelkvist, and G. Dallner Age-related changes in the lipid compositions of rat and human tissues Lipids 24 1989 579 584
    • (1989) Lipids , vol.24 , pp. 579-584
    • Kalen, A.1    Appelkvist, E.L.2    Dallner, G.3
  • 92
    • 0141639911 scopus 로고    scopus 로고
    • Coenzyme Q intake elevates the mitochondrial and tissue levels of Coenzyme Q and alpha-tocopherol in young mice
    • S. Kamzalov, N. Sumien, M.J. Forster, and R.S. Sohal Coenzyme Q intake elevates the mitochondrial and tissue levels of Coenzyme Q and alpha-tocopherol in young mice J. Nutr. 133 2003 3175 3180
    • (2003) J. Nutr. , vol.133 , pp. 3175-3180
    • Kamzalov, S.1    Sumien, N.2    Forster, M.J.3    Sohal, R.S.4
  • 94
    • 0033230821 scopus 로고    scopus 로고
    • Excitotoxic mitochondrial depolarisation requires both calcium and nitric oxide in rat hippocampal neurons
    • J. Keelan, O. Vergun, and M.R. Duchen Excitotoxic mitochondrial depolarisation requires both calcium and nitric oxide in rat hippocampal neurons J. Physiol. 520 1999 797 813
    • (1999) J. Physiol. , vol.520 , pp. 797-813
    • Keelan, J.1    Vergun, O.2    Duchen, M.R.3
  • 96
    • 77957014831 scopus 로고
    • 1 particle, and reconstitution of succinate cytchrome c reductase
    • 1 particle, and reconstitution of succinate cytchrome c reductase Methods Enzymol. 10 1967 216 225
    • (1967) Methods Enzymol. , vol.10 , pp. 216-225
    • King, T.E.1
  • 98
    • 0030800033 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in the central nervous system: Induction by calcium cycling-dependent and -independent pathways
    • B.S. Kristal, and J.M. Dubinsky Mitochondrial permeability transition in the central nervous system: induction by calcium cycling-dependent and -independent pathways J. Neurochem. 69 1997 524 538
    • (1997) J. Neurochem. , vol.69 , pp. 524-538
    • Kristal, B.S.1    Dubinsky, J.M.2
  • 101
    • 0034662806 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA and activity of mitochondrial enzymes in chronic active lesions of multiple sclerosis
    • F. Lu, M. Selak, J. O'Connor, S. Croul, C. Lorenzana, C. Butunoi, and B. Kalman Oxidative damage to mitochondrial DNA and activity of mitochondrial enzymes in chronic active lesions of multiple sclerosis J. Neurol. Sci. 177 2000 95 103
    • (2000) J. Neurol. Sci. , vol.177 , pp. 95-103
    • Lu, F.1    Selak, M.2    O'Connor, J.3    Croul, S.4    Lorenzana, C.5    Butunoi, C.6    Kalman, B.7
  • 103
    • 0029143062 scopus 로고
    • Oxygen free radicals enhance the nitric oxide-induced covalent NAD(+)-linkage to neuronal glyceraldehyde-3-phosphate dehydrogenase
    • P. Marin, M. Maus, J. Bockaert, J. Glowinski, and J. Premont Oxygen free radicals enhance the nitric oxide-induced covalent NAD(+)-linkage to neuronal glyceraldehyde-3-phosphate dehydrogenase Biochem. J. 309 1995 891 898
    • (1995) Biochem. J. , vol.309 , pp. 891-898
    • Marin, P.1    Maus, M.2    Bockaert, J.3    Glowinski, J.4    Premont, J.5
  • 105
    • 0031882897 scopus 로고    scopus 로고
    • Nitric oxide causes glutamate release from brain synaptosomes
    • K.S. McNaught, and G.C. Brown Nitric oxide causes glutamate release from brain synaptosomes J. Neurochem. 70 1998 1541 1546
    • (1998) J. Neurochem. , vol.70 , pp. 1541-1546
    • McNaught, K.S.1    Brown, G.C.2
  • 107
    • 0029924622 scopus 로고    scopus 로고
    • In vivo expression of inducible nitric oxide synthase in cerebellar neurons
    • D. Minc-Golomb, G. Yadid, I. Tsarfaty, J.H. Resau, and J.P. Schwartz In vivo expression of inducible nitric oxide synthase in cerebellar neurons J. Neurochem. 66 1996 1504 1509
    • (1996) J. Neurochem. , vol.66 , pp. 1504-1509
    • Minc-Golomb, D.1    Yadid, G.2    Tsarfaty, I.3    Resau, J.H.4    Schwartz, J.P.5
  • 108
    • 0028061167 scopus 로고
    • Nitric oxide as a potential pathological mechanism in demyelination: Its differential effects on primary glial cells in vitro
    • B. Mitrovic, L.J. Ignarro, S. Montestruque, A. Smoll, and J.E. Merrill Nitric oxide as a potential pathological mechanism in demyelination: its differential effects on primary glial cells in vitro Neuroscience 61 1994 575 585
    • (1994) Neuroscience , vol.61 , pp. 575-585
    • Mitrovic, B.1    Ignarro, L.J.2    Montestruque, S.3    Smoll, A.4    Merrill, J.E.5
  • 109
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology and pharmacology
    • D. Moncada, R.M.J. Plamer, and E.A. Higgs Nitric oxide: physiology, pathophysiology and pharmacology Pharmacol. Rev. 43 1991 109 142
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, D.1    Plamer, R.M.J.2    Higgs, E.A.3
  • 110
    • 0030611217 scopus 로고    scopus 로고
    • International Union: Of pharmacology, nomenclature in nitric oxide research
    • S. Moncada, A. Higgs, and R. Furchgott International Union: of pharmacology, nomenclature in nitric oxide research Pharmacol. Rev. 49 1997 137 142
    • (1997) Pharmacol. Rev. , vol.49 , pp. 137-142
    • Moncada, S.1    Higgs, A.2    Furchgott, R.3
  • 113
    • 0015289197 scopus 로고
    • N-acetyl-l-aspartic acid content in human neural tumours and bovine peripheral nervous tissues
    • J.V. Nadier, and J.R. Cooper N-acetyl-l-aspartic acid content in human neural tumours and bovine peripheral nervous tissues J. Neurochem. 19 1972 313 319
    • (1972) J. Neurochem. , vol.19 , pp. 313-319
    • Nadier, J.V.1    Cooper, J.R.2
  • 116
    • 0030298459 scopus 로고    scopus 로고
    • Cyclosporin a delays mitochondrial depolarization induced by N-methyl-d-aspartate in cortical neurons: Evidence of the mitochondrial permeability transition
    • A.L. Nieminen, T.G. Petrie, J.J. LeMasters, and W.R. Selman Cyclosporin A delays mitochondrial depolarization induced by N-methyl-d-aspartate in cortical neurons: evidence of the mitochondrial permeability transition Neuroscience 75 1996 993 997
    • (1996) Neuroscience , vol.75 , pp. 993-997
    • Nieminen, A.L.1    Petrie, T.G.2    Lemasters, J.J.3    Selman, W.R.4
  • 119
    • 0028306269 scopus 로고
    • Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin a
    • M.A. Packer, and M.P. Murphy Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A FEBS Lett. 345 1994 237 240
    • (1994) FEBS Lett. , vol.345 , pp. 237-240
    • Packer, M.A.1    Murphy, M.P.2
  • 120
    • 0018622817 scopus 로고
    • Synthesis of N-acetyl-l-aspartate by rat mitochondria and its involvement in mitochondrial/cytosolic carbon transport
    • T.B. Patel, and J.B. Clark Synthesis of N-acetyl-l-aspartate by rat mitochondria and its involvement in mitochondrial/cytosolic carbon transport Biochem. J. 184 1979 539 546
    • (1979) Biochem. J. , vol.184 , pp. 539-546
    • Patel, T.B.1    Clark, J.B.2
  • 121
    • 0036330255 scopus 로고    scopus 로고
    • Nitric oxide and differential effects of ATP on mitochondrial permeability transition
    • C.A. Piantadosi, L.G. Tatro, and A.R. Whorton Nitric oxide and differential effects of ATP on mitochondrial permeability transition Nitric Oxide 6 2002 45 60
    • (2002) Nitric Oxide , vol.6 , pp. 45-60
    • Piantadosi, C.A.1    Tatro, L.G.2    Whorton, A.R.3
  • 122
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • J.J. Poderoso, M.C. Carreras, C.L. Lisdero, N.A. Riobo, F. Schopfer, and A.D. Boveris 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
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.L.3    Riobo, N.A.4    Schopfer, F.5    Boveris, A.D.6
  • 126
    • 0031439343 scopus 로고    scopus 로고
    • Nitric oxide donors reversibly block axonal conduction: Demyelinated axons are especially susceptible
    • E.J. Redford, R. Kapoor, and K.J. Smith Nitric oxide donors reversibly block axonal conduction: demyelinated axons are especially susceptible Brain 120 1997 2149 2157
    • (1997) Brain , vol.120 , pp. 2149-2157
    • Redford, E.J.1    Kapoor, R.2    Smith, K.J.3
  • 127
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH: Ubiquinone reductase activity through peroxynitrite formation
    • N.A. Riobo, E. Clementi, M. Melani, A. Boveris, E. Cadenas, S. Moncada, and J.J. Poderoso Nitric oxide inhibits mitochondrial NADH: ubiquinone reductase activity through peroxynitrite formation Biochem. J. 359 2000 139 145
    • (2000) Biochem. J. , vol.359 , pp. 139-145
    • Riobo, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 129
    • 0030988138 scopus 로고    scopus 로고
    • Nitric oxide synthase in models of focal ischemia
    • A.F. Samdani, T.M. Dawson, and V.L. Dawson Nitric oxide synthase in models of focal ischemia Stroke 28 1997 1283 1288
    • (1997) Stroke , vol.28 , pp. 1283-1288
    • Samdani, A.F.1    Dawson, T.M.2    Dawson, V.L.3
  • 131
  • 132
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein
    • H. Schulze, A. Schuler, D. Stuber, H. Dobeli, H. Langen, and G. Huber Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein J. Neurochem. 60 1993 1915 1922
    • (1993) J. Neurochem. , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuler, A.2    Stuber, D.3    Dobeli, H.4    Langen, H.5    Huber, G.6
  • 134
    • 0142021035 scopus 로고    scopus 로고
    • Aging, amyloid, and Alzheimer's disease: A perspective in honor of Carl Cotman
    • D.J. Selkoe Aging, amyloid, and Alzheimer's disease: a perspective in honor of Carl Cotman Neurochem. Res. 28 2003 1705 1713
    • (2003) Neurochem. Res. , vol.28 , pp. 1705-1713
    • Selkoe, D.J.1
  • 135
    • 0032553302 scopus 로고    scopus 로고
    • Interaction of peroxynitrite with mitochondrial cytochrome oxidase
    • M.A. Sharpe, and C.E. Cooper Interaction of peroxynitrite with mitochondrial cytochrome oxidase J. Biol. Chem. 273 1998 30961 30972
    • (1998) J. Biol. Chem. , vol.273 , pp. 30961-30972
    • Sharpe, M.A.1    Cooper, C.E.2
  • 137
    • 0026710436 scopus 로고
    • Characterization and localization of nitric oxide synthase in non-adrenergic non-cholinergic nerves from bovine retractor penis muscles
    • H. Sheng, H.H. Schmidt, M. Nakane, J.A. Mitchell, J.S. Pollock, U. Fostermann, and F. Murad Characterization and localization of nitric oxide synthase in non-adrenergic non-cholinergic nerves from bovine retractor penis muscles Br. J. Pharmacol. 106 1992 768 773
    • (1992) Br. J. Pharmacol. , vol.106 , pp. 768-773
    • Sheng, H.1    Schmidt, H.H.2    Nakane, M.3    Mitchell, J.A.4    Pollock, J.S.5    Fostermann, U.6    Murad, F.7
  • 140
    • 0036175596 scopus 로고    scopus 로고
    • Mitochondrial contributions to tissue damage in stroke
    • N.R. Sims, and M.F. Anderson Mitochondrial contributions to tissue damage in stroke Neurochem. Int. 40 2002 511 526
    • (2002) Neurochem. Int. , vol.40 , pp. 511-526
    • Sims, N.R.1    Anderson, M.F.2
  • 141
    • 0030746213 scopus 로고    scopus 로고
    • Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase in normal cell function and in cell pathology
    • M.A. Sirover Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase in normal cell function and in cell pathology J. Cell. Biochem. 66 1997 133 140
    • (1997) J. Cell. Biochem. , vol.66 , pp. 133-140
    • Sirover, M.A.1
  • 142
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • M.A. Sirover New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase Biochim. Biophys. Acta 1432 1999 159 184
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 143
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanism to eliminate superoxide-producing mitochondria and cell
    • V.P. Skulachev Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanism to eliminate superoxide-producing mitochondria and cell FEBS Lett. 397 1996 7 10
    • (1996) FEBS Lett. , vol.397 , pp. 7-10
    • Skulachev, V.P.1
  • 144
    • 0035281786 scopus 로고    scopus 로고
    • The world according to PARP
    • S. Smith The world according to PARP Trends Biochem. Sci. 26 2001 174 179
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 174-179
    • Smith, S.1
  • 145
    • 0013292906 scopus 로고    scopus 로고
    • The role of nitric oxide in multiple sclerosis
    • K.J. Smith, and H. Lassmann The role of nitric oxide in multiple sclerosis Lancet Neurol. 1 2002 232 241
    • (2002) Lancet Neurol. , vol.1 , pp. 232-241
    • Smith, K.J.1    Lassmann, H.2
  • 148
    • 0030582764 scopus 로고    scopus 로고
    • Long-term potentiation is reduced in mice that are doubly mutant in endothelial and neuronal nitric oxide synthase
    • H. Son, R.D. Hawkins, K. Martin, M. Keibler, P. Huang, M.C. Fishman, and E.R. Kander Long-term potentiation is reduced in mice that are doubly mutant in endothelial and neuronal nitric oxide synthase Cell 87 1996 1015 1023
    • (1996) Cell , vol.87 , pp. 1015-1023
    • Son, H.1    Hawkins, R.D.2    Martin, K.3    Keibler, M.4    Huang, P.5    Fishman, M.C.6    Kander, E.R.7
  • 150
    • 0037303479 scopus 로고    scopus 로고
    • Nitric oxide-induced mitochondrial dysfunction: Implications for neurodegeneration
    • V.C. Stewart, and S.J.R. Heales Nitric oxide-induced mitochondrial dysfunction: implications for neurodegeneration Free Radical Biol. Med. 34 2002 287 303
    • (2002) Free Radical Biol. Med. , vol.34 , pp. 287-303
    • Stewart, V.C.1    Heales, S.J.R.2
  • 151
    • 0031972780 scopus 로고    scopus 로고
    • Pretreatment of astrocytes with interferon-α/β prevents neuronal mitochondrial respiratory chain damage
    • V.C. Stewart, J.M. Land, J.B. Clark, and S.J.R. Heales Pretreatment of astrocytes with interferon-α/β prevents neuronal mitochondrial respiratory chain damage J. Neurochem. 70 1998 432 434
    • (1998) J. Neurochem. , vol.70 , pp. 432-434
    • Stewart, V.C.1    Land, J.M.2    Clark, J.B.3    Heales, S.J.R.4
  • 152
    • 0033914409 scopus 로고    scopus 로고
    • Astrocyte-derived nitric oxide causes both reversible and irreversible damage to the neuronal mitochondrial respiratory chain
    • V.C. Stewart, M.A. Sharpe, J.B. Clark, and S.J.R. Heales Astrocyte-derived nitric oxide causes both reversible and irreversible damage to the neuronal mitochondrial respiratory chain J. Neurochem. 75 2000 694 700
    • (2000) J. Neurochem. , vol.75 , pp. 694-700
    • Stewart, V.C.1    Sharpe, M.A.2    Clark, J.B.3    Heales, S.J.R.4
  • 155
    • 0030000690 scopus 로고    scopus 로고
    • DNA strand breakage, activation of poly-ADP ribosy synthestase, and cellular energy depletion are involved in the cytotoxity of macrophages and smooth muscle cells exposed to peroxynitrite
    • C. Szabo, B. Zingarelli, M. O'Conner, and A.L. Salzman DNA strand breakage, activation of poly-ADP ribosy synthestase, and cellular energy depletion are involved in the cytotoxity of macrophages and smooth muscle cells exposed to peroxynitrite Proc. Natl. Acad. Sci. USA 93 1996 1753 1758
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1753-1758
    • Szabo, C.1    Zingarelli, B.2    O'Conner, M.3    Salzman, A.L.4
  • 156
    • 0036229947 scopus 로고    scopus 로고
    • Propargylamines induce antiapoptotic new protein synthesis in serum- and nerve growth factor (NGF)-withdrawn, NGF-differentiated PC-12 cells
    • W.G. Tatton, R.M. Chalmers-Redman, W.J. Ju, M. Mammen, G.W. Carlile, A.W. Pong, and N.A. Tatton Propargylamines induce antiapoptotic new protein synthesis in serum- and nerve growth factor (NGF)-withdrawn, NGF-differentiated PC-12 cells J. Pharmacol. Exp. Ther. 301 2002 753 764
    • (2002) J. Pharmacol. Exp. Ther. , vol.301 , pp. 753-764
    • Tatton, W.G.1    Chalmers-Redman, R.M.2    Ju, W.J.3    Mammen, M.4    Carlile, G.W.5    Pong, A.W.6    Tatton, N.A.7
  • 158
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-ribose) polymerase inhibitors
    • L. Virag, and C. Szabo The therapeutic potential of poly(ADP-ribose) polymerase inhibitors Pharmacol. Rev. 54 2002 375 429
    • (2002) Pharmacol. Rev. , vol.54 , pp. 375-429
    • Virag, L.1    Szabo, C.2
  • 163
    • 0017187544 scopus 로고
    • The kinetic mechanism of rat kidney gamma-glutamylcysteine synthetase
    • B. Yip, and F.B. Rudolph The kinetic mechanism of rat kidney gamma-glutamylcysteine synthetase J. Biol. Chem. 251 1976 3563 3568
    • (1976) J. Biol. Chem. , vol.251 , pp. 3563-3568
    • Yip, B.1    Rudolph, F.B.2
  • 164
    • 0026686667 scopus 로고
    • Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3- phosphate dehydrogenase
    • J. Zhang, and S.H. Snyder Nitric oxide stimulates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase Proc. Natl. Acad. Sci. USA 5 1992 9382 9385
    • (1992) Proc. Natl. Acad. Sci. USA , vol.5 , pp. 9382-9385
    • Zhang, J.1    Snyder, S.H.2
  • 165
    • 0027954427 scopus 로고
    • Characterisation of the calmodulin-binding domain of rat cerebellar nitric oxide synthase
    • M. Zhang, and H.J. Vogel Characterisation of the calmodulin-binding domain of rat cerebellar nitric oxide synthase J. Biol. Chem. 269 1994 981 985
    • (1994) J. Biol. Chem. , vol.269 , pp. 981-985
    • Zhang, M.1    Vogel, H.J.2
  • 166
    • 0028874051 scopus 로고
    • Inhibition of brain microglial respiratory chain enzyme activity in experimental autoimmune encephalomyelitis of the Lewis rat
    • J. Zielasek, H. Reichmann, H. Kunzig, S. Jung, H.P. Hartung, and K.V. Toyka Inhibition of brain microglial respiratory chain enzyme activity in experimental autoimmune encephalomyelitis of the Lewis rat Neurosci. Lett. 184 1995 129 132
    • (1995) Neurosci. Lett. , vol.184 , pp. 129-132
    • Zielasek, J.1    Reichmann, H.2    Kunzig, H.3    Jung, S.4    Hartung, H.P.5    Toyka, K.V.6
  • 167
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • M. Zoratti, and I. Szabo The mitochondrial permeability transition Biochim. Biophys. Acta 1241 1995 139 176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 168
    • 0031740696 scopus 로고    scopus 로고
    • Modulation of LTP induction by NMDA receptor activation and nitric oxide release
    • C.F. Zorumski, and Y. Izumi Modulation of LTP induction by NMDA receptor activation and nitric oxide release Prog. Brain Res. 118 1998 173 182
    • (1998) Prog. Brain Res. , vol.118 , pp. 173-182
    • Zorumski, C.F.1    Izumi, Y.2


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