메뉴 건너뛰기




Volumn 477, Issue , 2018, Pages 121-126

Oxidative stress in urea cycle disorders: Findings from clinical and basic research

Author keywords

Inborn errors of metabolism; Nitric oxide; Oxidative stress; Redox balance; Urea cycle disorders

Indexed keywords

AMMONIA; CARGLUMIC ACID; GLUTAMINE; NITRIC OXIDE;

EID: 85038026784     PISSN: 00098981     EISSN: 18733492     Source Type: Journal    
DOI: 10.1016/j.cca.2017.11.041     Document Type: Review
Times cited : (17)

References (74)
  • 1
    • 84931574902 scopus 로고    scopus 로고
    • Inborn errors of metabolism
    • (x)
    • El-Hattab, A.W., Inborn errors of metabolism. Clin. Perinatol. 42:2 (2015), 413–439 (x).
    • (2015) Clin. Perinatol. , vol.42 , Issue.2 , pp. 413-439
    • El-Hattab, A.W.1
  • 2
    • 84937250645 scopus 로고    scopus 로고
    • Redox signalling and mitochondrial stress responses; lessons from inborn errors of metabolism
    • Olsen, R.K., Cornelius, N., Gregersen, N., Redox signalling and mitochondrial stress responses; lessons from inborn errors of metabolism. J. Inherit. Metab. Dis. 38:4 (2015), 703–719.
    • (2015) J. Inherit. Metab. Dis. , vol.38 , Issue.4 , pp. 703-719
    • Olsen, R.K.1    Cornelius, N.2    Gregersen, N.3
  • 3
    • 84937250662 scopus 로고    scopus 로고
    • Signal transduction in inherited metabolic disorders: a model for a possible pathogenetic mechanism
    • Boneh, A., Signal transduction in inherited metabolic disorders: a model for a possible pathogenetic mechanism. J. Inherit. Metab. Dis. 38:4 (2015), 729–740.
    • (2015) J. Inherit. Metab. Dis. , vol.38 , Issue.4 , pp. 729-740
    • Boneh, A.1
  • 6
    • 84983372398 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaric and 3-methylglutaric acids impair redox status and energy production and transfer in rat heart: relevance for the pathophysiology of cardiac dysfunction in 3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency
    • da Rosa, M.S., Seminotti, B., Ribeiro, C.A., Parmeggiani, B., Grings, M., Wajner, M., Leipnitz, G., 3-Hydroxy-3-methylglutaric and 3-methylglutaric acids impair redox status and energy production and transfer in rat heart: relevance for the pathophysiology of cardiac dysfunction in 3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency. Free Radic. Res. 50:9 (2016), 997–1010.
    • (2016) Free Radic. Res. , vol.50 , Issue.9 , pp. 997-1010
    • da Rosa, M.S.1    Seminotti, B.2    Ribeiro, C.A.3    Parmeggiani, B.4    Grings, M.5    Wajner, M.6    Leipnitz, G.7
  • 7
    • 84878512756 scopus 로고    scopus 로고
    • In vivo experimental evidence that the major metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency induce oxidative stress in striatum of developing rats: a potential pathophysiological mechanism of striatal damage in this disorder
    • Fernandes, C.G., da Rosa, M.S., Seminotti, B., Pierozan, P., Martell, R.W., Lagranha, V.L., Busanello, E.N., Leipnitz, G., Wajner, M., In vivo experimental evidence that the major metabolites accumulating in 3-hydroxy-3-methylglutaryl-CoA lyase deficiency induce oxidative stress in striatum of developing rats: a potential pathophysiological mechanism of striatal damage in this disorder. Mol. Genet. Metab. 109:2 (2013), 144–153.
    • (2013) Mol. Genet. Metab. , vol.109 , Issue.2 , pp. 144-153
    • Fernandes, C.G.1    da Rosa, M.S.2    Seminotti, B.3    Pierozan, P.4    Martell, R.W.5    Lagranha, V.L.6    Busanello, E.N.7    Leipnitz, G.8    Wajner, M.9
  • 9
    • 67749117788 scopus 로고    scopus 로고
    • Profiling of oxidative stress in patients with inborn errors of metabolism
    • Mc Guire, P.J., Parikh, A., Diaz, G.A., Profiling of oxidative stress in patients with inborn errors of metabolism. Mol. Genet. Metab. 98:1–2 (2009), 173–180.
    • (2009) Mol. Genet. Metab. , vol.98 , Issue.1-2 , pp. 173-180
    • Mc Guire, P.J.1    Parikh, A.2    Diaz, G.A.3
  • 10
  • 12
    • 85016260057 scopus 로고    scopus 로고
    • Free Radicals in Biology and Medicine
    • Fourth ed.
    • Gutteridge, B.H.a.J.M.C., Free Radicals in Biology and Medicine. Fourth ed., 2007.
    • (2007)
    • Gutteridge, B.H.A.J.M.C.1
  • 13
    • 0033213331 scopus 로고    scopus 로고
    • Chemistry, physiology and pathology of free radicals
    • Bergendi, L., Benes, L., Durackova, Z., Ferencik, M., Chemistry, physiology and pathology of free radicals. Life Sci. 65:18–19 (1999), 1865–1874.
    • (1999) Life Sci. , vol.65 , Issue.18-19 , pp. 1865-1874
    • Bergendi, L.1    Benes, L.2    Durackova, Z.3    Ferencik, M.4
  • 14
    • 0036285223 scopus 로고    scopus 로고
    • Nitric oxide modulates superoxide release and peroxynitrite formation in human blood vessels
    • Guzik, T.J., West, N.E., Pillai, R., Taggart, D.P., Channon, K.M., Nitric oxide modulates superoxide release and peroxynitrite formation in human blood vessels. Hypertension 39:6 (2002), 1088–1094.
    • (2002) Hypertension , vol.39 , Issue.6 , pp. 1088-1094
    • Guzik, T.J.1    West, N.E.2    Pillai, R.3    Taggart, D.P.4    Channon, K.M.5
  • 15
    • 77953523391 scopus 로고    scopus 로고
    • Reactive species and mitochondrial dysfunction: mechanistic significance of 4-hydroxynonenal
    • Roede, J.R., Jones, D.P., Reactive species and mitochondrial dysfunction: mechanistic significance of 4-hydroxynonenal. Environ. Mol. Mutagen. 51:5 (2010), 380–390.
    • (2010) Environ. Mol. Mutagen. , vol.51 , Issue.5 , pp. 380-390
    • Roede, J.R.1    Jones, D.P.2
  • 16
    • 84897421970 scopus 로고    scopus 로고
    • The Nrf2 regulatory network provides an interface between redox and intermediary metabolism
    • Hayes, J.D., Dinkova-Kostova, A.T., The Nrf2 regulatory network provides an interface between redox and intermediary metabolism. Trends Biochem. Sci. 39:4 (2014), 199–218.
    • (2014) Trends Biochem. Sci. , vol.39 , Issue.4 , pp. 199-218
    • Hayes, J.D.1    Dinkova-Kostova, A.T.2
  • 19
    • 85010604478 scopus 로고    scopus 로고
    • Impaired energy metabolism of senescent muscle satellite cells is associated with oxidative modifications of glycolytic enzymes
    • Baraibar, M.A., Hyzewicz, J., Rogowska-Wrzesinska, A., Bulteau, A.L., Prip-Buus, C., Butler-Browne, G., Friguet, B., Impaired energy metabolism of senescent muscle satellite cells is associated with oxidative modifications of glycolytic enzymes. Aging 8:12 (2016), 3375–3389.
    • (2016) Aging , vol.8 , Issue.12 , pp. 3375-3389
    • Baraibar, M.A.1    Hyzewicz, J.2    Rogowska-Wrzesinska, A.3    Bulteau, A.L.4    Prip-Buus, C.5    Butler-Browne, G.6    Friguet, B.7
  • 20
    • 84904551504 scopus 로고    scopus 로고
    • Insulin-like modulation of Akt/FoxO signaling by copper ions is independent of insulin receptor
    • Hamann, I., Petroll, K., Grimm, L., Hartwig, A., Klotz, L.O., Insulin-like modulation of Akt/FoxO signaling by copper ions is independent of insulin receptor. Arch. Biochem. Biophys. 558 (2014), 42–50.
    • (2014) Arch. Biochem. Biophys. , vol.558 , pp. 42-50
    • Hamann, I.1    Petroll, K.2    Grimm, L.3    Hartwig, A.4    Klotz, L.O.5
  • 21
    • 85027357889 scopus 로고    scopus 로고
    • The ability of exercise-associated oxidative stress to trigger redox-sensitive signalling responses
    • Webb, R., Hughes, M.G., Thomas, A.W., Morris, K., The ability of exercise-associated oxidative stress to trigger redox-sensitive signalling responses. Antioxidants (Basel), 6(3), 2017.
    • (2017) Antioxidants (Basel) , vol.6 , Issue.3
    • Webb, R.1    Hughes, M.G.2    Thomas, A.W.3    Morris, K.4
  • 22
    • 85017190026 scopus 로고
    • Free radicals in biology and medicine
    • (Barry Halliwell, John M. C. Gutteridge)
    • Bannister, J.V., Free radicals in biology and medicine. Q. Rev. Biol. 61:3 (1986), 440–441 (Barry Halliwell, John M. C. Gutteridge).
    • (1986) Q. Rev. Biol. , vol.61 , Issue.3 , pp. 440-441
    • Bannister, J.V.1
  • 23
    • 0004026407 scopus 로고    scopus 로고
    • Lehninger Principles of Biochemistry
    • W.H. Freeman New York
    • Nelson, D.L., Lehninger, A.L., Cox, M.M., Lehninger Principles of Biochemistry. 2008, W.H. Freeman, New York.
    • (2008)
    • Nelson, D.L.1    Lehninger, A.L.2    Cox, M.M.3
  • 24
    • 0003720078 scopus 로고    scopus 로고
    • Urea cycle enzymes
    • A.L. Beaudet B. Vogelstein K.W. Kinzler S.E. Antonarakis A. Ballabio K.M. Gibson G. Mitchell The McGraw-Hill Companies, Inc. New York, NY
    • Brusilow, S.W., Horwich, A.L., Urea cycle enzymes. Beaudet, A.L., Vogelstein, B., Kinzler, K.W., Antonarakis, S.E., Ballabio, A., Gibson, K.M., Mitchell, G., (eds.) The Online Metabolic and Molecular Bases of Inherited Disease, 2014, The McGraw-Hill Companies, Inc., New York, NY.
    • (2014) The Online Metabolic and Molecular Bases of Inherited Disease
    • Brusilow, S.W.1    Horwich, A.L.2
  • 26
    • 51349141861 scopus 로고    scopus 로고
    • Hereditary urea cycle diseases in Finland
    • Keskinen, P., Siitonen, A., Salo, M., Hereditary urea cycle diseases in Finland. Acta Paediatr. 97:10 (2008), 1412–1419.
    • (2008) Acta Paediatr. , vol.97 , Issue.10 , pp. 1412-1419
    • Keskinen, P.1    Siitonen, A.2    Salo, M.3
  • 27
    • 85038029224 scopus 로고    scopus 로고
    • Integration of proteomics and metabolomics in exploring genetic and rare metabolic diseases
    • Costanzo, M., Zacchia, M., Bruno, G., Crisci, D., Caterino, M., Ruoppolo, M., Integration of proteomics and metabolomics in exploring genetic and rare metabolic diseases. Kidney Dis. (Basel) 3:2 (2017), 66–77.
    • (2017) Kidney Dis. (Basel) , vol.3 , Issue.2 , pp. 66-77
    • Costanzo, M.1    Zacchia, M.2    Bruno, G.3    Crisci, D.4    Caterino, M.5    Ruoppolo, M.6
  • 28
    • 0033506343 scopus 로고    scopus 로고
    • Neonatal onset ornithine transcarbamylase deficiency: a retrospective analysis
    • Maestri, N.E., Clissold, D., Brusilow, S.W., Neonatal onset ornithine transcarbamylase deficiency: a retrospective analysis. J. Pediatr. 134:3 (1999), 268–272.
    • (1999) J. Pediatr. , vol.134 , Issue.3 , pp. 268-272
    • Maestri, N.E.1    Clissold, D.2    Brusilow, S.W.3
  • 29
    • 0022178203 scopus 로고
    • Differentiation of transient hyperammonemia of the newborn and urea cycle enzyme defects by clinical presentation
    • Hudak, M.L., Jones, M.D. Jr., Brusilow, S.W., Differentiation of transient hyperammonemia of the newborn and urea cycle enzyme defects by clinical presentation. J. Pediatr. 107:5 (1985), 712–719.
    • (1985) J. Pediatr. , vol.107 , Issue.5 , pp. 712-719
    • Hudak, M.L.1    Jones, M.D.2    Brusilow, S.W.3
  • 30
    • 84864283628 scopus 로고    scopus 로고
    • Early clinical manifestations and eating patterns in patients with urea cycle disorders
    • Gardeitchik, T., Humphrey, M., Nation, J., Boneh, A., Early clinical manifestations and eating patterns in patients with urea cycle disorders. J. Pediatr. 161:2 (2012), 328–332.
    • (2012) J. Pediatr. , vol.161 , Issue.2 , pp. 328-332
    • Gardeitchik, T.1    Humphrey, M.2    Nation, J.3    Boneh, A.4
  • 33
    • 85037999001 scopus 로고    scopus 로고
    • R.A. Pagon M.P. Adam H.H. Ardinger et al. University of Washington, Seattle Seattle (WA) (2003 Apr 29 [Updated 2017 Jun 22]. GeneReviews® [Internet])
    • Nicholas Ah Mew, K.L.S., CGC, Gropman, Andrea L., Lanpher, Brendan C., Chapman, Kimberly A., Summar, Marshall L., Pagon, R.A., Adam, M.P., Ardinger, H.H., et al., (eds.) Urea Cycle Disorders Overview, 1993–2017, University of Washington, Seattle, Seattle (WA) (2003 Apr 29 [Updated 2017 Jun 22]. GeneReviews® [Internet]).
    • (2017) Urea Cycle Disorders Overview
    • Nicholas Ah Mew, K.L.S.1    CGC2    Gropman, A.L.3    Lanpher, B.C.4    Chapman, K.A.5    Summar, M.L.6
  • 34
    • 79958852822 scopus 로고    scopus 로고
    • Neonatal astrocyte damage is sufficient to trigger progressive striatal degeneration in a rat model of glutaric acidemia-I
    • Olivera-Bravo, S., Fernandez, A., Sarlabos, M.N., Rosillo, J.C., Casanova, G., Jimenez, M., Barbeito, L., Neonatal astrocyte damage is sufficient to trigger progressive striatal degeneration in a rat model of glutaric acidemia-I. PLoS One, 6(6), 2011, e20831.
    • (2011) PLoS One , vol.6 , Issue.6
    • Olivera-Bravo, S.1    Fernandez, A.2    Sarlabos, M.N.3    Rosillo, J.C.4    Casanova, G.5    Jimenez, M.6    Barbeito, L.7
  • 36
    • 0037310995 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress in ammonia neurotoxicity
    • Norenberg, M.D., Oxidative and nitrosative stress in ammonia neurotoxicity. Hepatology 37:2 (2003), 245–248.
    • (2003) Hepatology , vol.37 , Issue.2 , pp. 245-248
    • Norenberg, M.D.1
  • 37
    • 0038509984 scopus 로고    scopus 로고
    • Ammonia neurotoxicity: role of the mitochondrial permeability transition
    • Rama Rao, K.V., Jayakumar, A.R., Norenberg, D.M., Ammonia neurotoxicity: role of the mitochondrial permeability transition. Metab. Brain Dis. 18:2 (2003), 113–127.
    • (2003) Metab. Brain Dis. , vol.18 , Issue.2 , pp. 113-127
    • Rama Rao, K.V.1    Jayakumar, A.R.2    Norenberg, D.M.3
  • 38
    • 84875706447 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress in ammonia neurotoxicity
    • Skowronska, M., Albrecht, J., Oxidative and nitrosative stress in ammonia neurotoxicity. Neurochem. Int. 62:5 (2013), 731–737.
    • (2013) Neurochem. Int. , vol.62 , Issue.5 , pp. 731-737
    • Skowronska, M.1    Albrecht, J.2
  • 39
    • 84884800246 scopus 로고    scopus 로고
    • Osmotic and oxidative/nitrosative stress in ammonia toxicity and hepatic encephalopathy
    • Gorg, B., Schliess, F., Haussinger, D., Osmotic and oxidative/nitrosative stress in ammonia toxicity and hepatic encephalopathy. Arch. Biochem. Biophys. 536:2 (2013), 158–163.
    • (2013) Arch. Biochem. Biophys. , vol.536 , Issue.2 , pp. 158-163
    • Gorg, B.1    Schliess, F.2    Haussinger, D.3
  • 41
    • 0037135221 scopus 로고    scopus 로고
    • Arginine administration reduces catalase activity in midbrain of rats
    • Delwing, D., Dutra-Filho, C.S., Wannmacher, C.M., Wajner, M., Wyse, A.T., Arginine administration reduces catalase activity in midbrain of rats. Neuroreport 13:10 (2002), 1301–1304.
    • (2002) Neuroreport , vol.13 , Issue.10 , pp. 1301-1304
    • Delwing, D.1    Dutra-Filho, C.S.2    Wannmacher, C.M.3    Wajner, M.4    Wyse, A.T.5
  • 42
    • 84867045011 scopus 로고    scopus 로고
    • Continuous exposure to L-arginine induces oxidative stress and physiological tolerance in cultured human endothelial cells
    • Mohan, S., Wu, C.C., Shin, S., Fung, H.L., Continuous exposure to L-arginine induces oxidative stress and physiological tolerance in cultured human endothelial cells. Amino Acids 43:3 (2012), 1179–1188.
    • (2012) Amino Acids , vol.43 , Issue.3 , pp. 1179-1188
    • Mohan, S.1    Wu, C.C.2    Shin, S.3    Fung, H.L.4
  • 43
    • 0035960895 scopus 로고    scopus 로고
    • In vitro stimulation of oxidative stress in cerebral cortex of rats by the guanidino compounds accumulating in hyperargininemia
    • Wyse, A.T., Bavaresco, C.S., Hagen, M.E., Delwing, D., Wannmacher, C.M., Severo Dutra-Filho, C., Wajner, M., In vitro stimulation of oxidative stress in cerebral cortex of rats by the guanidino compounds accumulating in hyperargininemia. Brain Res. 923:1–2 (2001), 50–57.
    • (2001) Brain Res. , vol.923 , Issue.1-2 , pp. 50-57
    • Wyse, A.T.1    Bavaresco, C.S.2    Hagen, M.E.3    Delwing, D.4    Wannmacher, C.M.5    Severo Dutra-Filho, C.6    Wajner, M.7
  • 44
    • 0022360929 scopus 로고
    • Characterization of normal, glutathione-deficient and arginase-deficient sheep erythrocytes by 1H-NMR spectroscopy
    • Rabenstein, D.L., Young, J.D., Wolowyk, M.W., Razi, M.T., Arnold, A.P., Tucker, E.M., Characterization of normal, glutathione-deficient and arginase-deficient sheep erythrocytes by 1H-NMR spectroscopy. Biochim. Biophys. Acta 846:2 (1985), 200–207.
    • (1985) Biochim. Biophys. Acta , vol.846 , Issue.2 , pp. 200-207
    • Rabenstein, D.L.1    Young, J.D.2    Wolowyk, M.W.3    Razi, M.T.4    Arnold, A.P.5    Tucker, E.M.6
  • 46
    • 84937523592 scopus 로고    scopus 로고
    • Ornithine in vivo administration disrupts redox homeostasis and decreases synaptic Na(+), K (+)-ATPase activity in cerebellum of adolescent rats: implications for the pathogenesis of Hyperornithinemia-Hyperammonemia-Homocitrullinuria (HHH) syndrome
    • Zanatta, A., Viegas, C.M., Hickmann, F.H., de Oliveira Monteiro, W., Sitta, A., de Moura Coelho, D., Vargas, C.R., Leipnitz, G., Wajner, M., Ornithine in vivo administration disrupts redox homeostasis and decreases synaptic Na(+), K (+)-ATPase activity in cerebellum of adolescent rats: implications for the pathogenesis of Hyperornithinemia-Hyperammonemia-Homocitrullinuria (HHH) syndrome. Cell. Mol. Neurobiol. 35:6 (2015), 797–806.
    • (2015) Cell. Mol. Neurobiol. , vol.35 , Issue.6 , pp. 797-806
    • Zanatta, A.1    Viegas, C.M.2    Hickmann, F.H.3    de Oliveira Monteiro, W.4    Sitta, A.5    de Moura Coelho, D.6    Vargas, C.R.7    Leipnitz, G.8    Wajner, M.9
  • 47
    • 84880266905 scopus 로고    scopus 로고
    • Disturbance of redox homeostasis by ornithine and homocitrulline in rat cerebellum: a possible mechanism of cerebellar dysfunction in HHH syndrome
    • Zanatta, A., Viegas, C.M., Tonin, A.M., Busanello, E.N., Grings, M., Moura, A.P., Leipnitz, G., Wajner, M., Disturbance of redox homeostasis by ornithine and homocitrulline in rat cerebellum: a possible mechanism of cerebellar dysfunction in HHH syndrome. Life Sci. 93:4 (2013), 161–168.
    • (2013) Life Sci. , vol.93 , Issue.4 , pp. 161-168
    • Zanatta, A.1    Viegas, C.M.2    Tonin, A.M.3    Busanello, E.N.4    Grings, M.5    Moura, A.P.6    Leipnitz, G.7    Wajner, M.8
  • 48
    • 84966602568 scopus 로고    scopus 로고
    • Ornithine and homocitrulline impair mitochondrial function, decrease antioxidant defenses and induce cell death in menadione-stressed rat cortical astrocytes: potential mechanisms of neurological dysfunction in HHH syndrome
    • Zanatta, A., Rodrigues, M.D., Amaral, A.U., Souza, D.G., Quincozes-Santos, A., Wajner, M., Ornithine and homocitrulline impair mitochondrial function, decrease antioxidant defenses and induce cell death in menadione-stressed rat cortical astrocytes: potential mechanisms of neurological dysfunction in HHH syndrome. Neurochem. Res. 41:9 (2016), 2190–2198.
    • (2016) Neurochem. Res. , vol.41 , Issue.9 , pp. 2190-2198
    • Zanatta, A.1    Rodrigues, M.D.2    Amaral, A.U.3    Souza, D.G.4    Quincozes-Santos, A.5    Wajner, M.6
  • 49
    • 70349305101 scopus 로고    scopus 로고
    • Evidence that the major metabolites accumulating in hyperornithinemia-hyperammonemia-homocitrullinuria syndrome induce oxidative stress in brain of young rats
    • Amaral, A.U., Leipnitz, G., Fernandes, C.G., Seminotti, B., Zanatta, A., Viegas, C.M., Dutra-Filho, C.S., Wajner, M., Evidence that the major metabolites accumulating in hyperornithinemia-hyperammonemia-homocitrullinuria syndrome induce oxidative stress in brain of young rats. Int. J. Dev. Neurosci. 27:7 (2009), 635–641.
    • (2009) Int. J. Dev. Neurosci. , vol.27 , Issue.7 , pp. 635-641
    • Amaral, A.U.1    Leipnitz, G.2    Fernandes, C.G.3    Seminotti, B.4    Zanatta, A.5    Viegas, C.M.6    Dutra-Filho, C.S.7    Wajner, M.8
  • 50
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • Knowles, R.G., Moncada, S., Nitric oxide synthases in mammals. Biochem. J. 298:Pt 2 (1994), 249–258.
    • (1994) Biochem. J. , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 51
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • Ghafourifar, P., Richter, C., Nitric oxide synthase activity in mitochondria. FEBS Lett. 418:3 (1997), 291–296.
    • (1997) FEBS Lett. , vol.418 , Issue.3 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 54
    • 0034618752 scopus 로고    scopus 로고
    • Regulation of nitric oxide production by arginine metabolic enzymes
    • Mori, M., Gotoh, T., Regulation of nitric oxide production by arginine metabolic enzymes. Biochem. Biophys. Res. Commun. 275:3 (2000), 715–719.
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , Issue.3 , pp. 715-719
    • Mori, M.1    Gotoh, T.2
  • 55
    • 4744344225 scopus 로고    scopus 로고
    • Clinical consequences of urea cycle enzyme deficiencies and potential links to arginine and nitric oxide metabolism
    • (Discussion 2796S–2797S)
    • Scaglia, F., Brunetti-Pierri, N., Kleppe, S., Marini, J., Carter, S., Garlick, P., Jahoor, F., O'Brien, W., Lee, B., Clinical consequences of urea cycle enzyme deficiencies and potential links to arginine and nitric oxide metabolism. J. Nutr. 134:10 Suppl (2004), 2775S–2782S (Discussion 2796S–2797S).
    • (2004) J. Nutr. , vol.134 , Issue.10 , pp. 2775S-2782S
    • Scaglia, F.1    Brunetti-Pierri, N.2    Kleppe, S.3    Marini, J.4    Carter, S.5    Garlick, P.6    Jahoor, F.7    O'Brien, W.8    Lee, B.9
  • 56
    • 77950338275 scopus 로고    scopus 로고
    • Current concepts in the pathogenesis of urea cycle disorders
    • Braissant, O., Current concepts in the pathogenesis of urea cycle disorders. Mol. Genet. Metab. 100:Suppl. 1 (2010), S3–S12.
    • (2010) Mol. Genet. Metab. , vol.100 , pp. S3-S12
    • Braissant, O.1
  • 57
    • 0036182380 scopus 로고    scopus 로고
    • Calcium and oxidative stress: from cell signaling to cell death
    • Ermak, G., Davies, K.J., Calcium and oxidative stress: from cell signaling to cell death. Mol. Immunol. 38:10 (2002), 713–721.
    • (2002) Mol. Immunol. , vol.38 , Issue.10 , pp. 713-721
    • Ermak, G.1    Davies, K.J.2
  • 59
    • 84860471028 scopus 로고    scopus 로고
    • Statins lower calcium-induced oxidative stress in isolated mitochondria
    • Parihar, A., Parihar, M.S., Zenebe, W.J., Ghafourifar, P., Statins lower calcium-induced oxidative stress in isolated mitochondria. Hum. Exp. Toxicol. 31:4 (2012), 355–363.
    • (2012) Hum. Exp. Toxicol. , vol.31 , Issue.4 , pp. 355-363
    • Parihar, A.1    Parihar, M.S.2    Zenebe, W.J.3    Ghafourifar, P.4
  • 60
    • 0033615544 scopus 로고    scopus 로고
    • Mitochondrial nitric-oxide synthase stimulation causes cytochrome c release from isolated mitochondria. Evidence for intramitochondrial peroxynitrite formation
    • Ghafourifar, P., Schenk, U., Klein, S.D., Richter, C., Mitochondrial nitric-oxide synthase stimulation causes cytochrome c release from isolated mitochondria. Evidence for intramitochondrial peroxynitrite formation. J. Biol. Chem. 274:44 (1999), 31185–31188.
    • (1999) J. Biol. Chem. , vol.274 , Issue.44 , pp. 31185-31188
    • Ghafourifar, P.1    Schenk, U.2    Klein, S.D.3    Richter, C.4
  • 61
  • 62
    • 33745907851 scopus 로고    scopus 로고
    • Inefficient spin trapping of superoxide in the presence of nitric-oxide: implications for studies on nitric-oxide synthase uncoupling
    • Pignitter, M., Gorren, A.C., Nedeianu, S., Schmidt, K., Mayer, B., Inefficient spin trapping of superoxide in the presence of nitric-oxide: implications for studies on nitric-oxide synthase uncoupling. Free Radic. Biol. Med. 41:3 (2006), 455–463.
    • (2006) Free Radic. Biol. Med. , vol.41 , Issue.3 , pp. 455-463
    • Pignitter, M.1    Gorren, A.C.2    Nedeianu, S.3    Schmidt, K.4    Mayer, B.5
  • 63
    • 3342967877 scopus 로고    scopus 로고
    • Nitric oxide synthesis in ornithine transcarbamylase deficiency: possible involvement of low no synthesis in clinical manifestations of urea cycle defect
    • Nagasaka, H., Komatsu, H., Ohura, T., Sogo, T., Inui, A., Yorifuji, T., Murayama, K., Takayanagi, M., Kikuta, H., Kobayashi, K., Nitric oxide synthesis in ornithine transcarbamylase deficiency: possible involvement of low no synthesis in clinical manifestations of urea cycle defect. J. Pediatr. 145:2 (2004), 259–262.
    • (2004) J. Pediatr. , vol.145 , Issue.2 , pp. 259-262
    • Nagasaka, H.1    Komatsu, H.2    Ohura, T.3    Sogo, T.4    Inui, A.5    Yorifuji, T.6    Murayama, K.7    Takayanagi, M.8    Kikuta, H.9    Kobayashi, K.10
  • 64
    • 84891372955 scopus 로고    scopus 로고
    • Characteristics of NO cycle coupling with urea cycle in non-hyperammonemic carriers of ornithine transcarbamylase deficiency
    • Nagasaka, H., Yorifuji, T., Egawa, H., Inui, A., Fujisawa, T., Komatsu, H., Tsukahara, H., Uemoto, S., Inomata, Y., Characteristics of NO cycle coupling with urea cycle in non-hyperammonemic carriers of ornithine transcarbamylase deficiency. Mol. Genet. Metab. 109:3 (2013), 251–254.
    • (2013) Mol. Genet. Metab. , vol.109 , Issue.3 , pp. 251-254
    • Nagasaka, H.1    Yorifuji, T.2    Egawa, H.3    Inui, A.4    Fujisawa, T.5    Komatsu, H.6    Tsukahara, H.7    Uemoto, S.8    Inomata, Y.9
  • 67
    • 84938117650 scopus 로고    scopus 로고
    • Evaluating the oxidative stress in inflammation: role of melatonin
    • Sanchez, A., Calpena, A.C., Clares, B., Evaluating the oxidative stress in inflammation: role of melatonin. Int. J. Mol. Sci. 16:8 (2015), 16981–17004.
    • (2015) Int. J. Mol. Sci. , vol.16 , Issue.8 , pp. 16981-17004
    • Sanchez, A.1    Calpena, A.C.2    Clares, B.3
  • 68
    • 84958671482 scopus 로고    scopus 로고
    • Cross talk between ER stress, oxidative stress, and inflammation in health and disease
    • Dandekar, A., Mendez, R., Zhang, K., Cross talk between ER stress, oxidative stress, and inflammation in health and disease. Methods Mol. Biol. 1292 (2015), 205–214.
    • (2015) Methods Mol. Biol. , vol.1292 , pp. 205-214
    • Dandekar, A.1    Mendez, R.2    Zhang, K.3
  • 69
    • 84893716925 scopus 로고    scopus 로고
    • The role of oxidative stress during inflammatory processes
    • Lugrin, J., Rosenblatt-Velin, N., Parapanov, R., Liaudet, L., The role of oxidative stress during inflammatory processes. Biol. Chem. 395:2 (2014), 203–230.
    • (2014) Biol. Chem. , vol.395 , Issue.2 , pp. 203-230
    • Lugrin, J.1    Rosenblatt-Velin, N.2    Parapanov, R.3    Liaudet, L.4
  • 70
    • 63449091161 scopus 로고    scopus 로고
    • Sustaining hypercitrullinemia, hypercholesterolemia and augmented oxidative stress in Japanese children with aspartate/glutamate carrier isoform 2-citrin-deficiency even during the silent period
    • Nagasaka, H., Okano, Y., Tsukahara, H., Shigematsu, Y., Momoi, T., Yorifuji, J., Miida, T., Ohura, T., Kobayashi, K., Saheki, T., Hirano, K., Takayanagi, M., Yorifuji, T., Sustaining hypercitrullinemia, hypercholesterolemia and augmented oxidative stress in Japanese children with aspartate/glutamate carrier isoform 2-citrin-deficiency even during the silent period. Mol. Genet. Metab. 97:1 (2009), 21–26.
    • (2009) Mol. Genet. Metab. , vol.97 , Issue.1 , pp. 21-26
    • Nagasaka, H.1    Okano, Y.2    Tsukahara, H.3    Shigematsu, Y.4    Momoi, T.5    Yorifuji, J.6    Miida, T.7    Ohura, T.8    Kobayashi, K.9    Saheki, T.10    Hirano, K.11    Takayanagi, M.12    Yorifuji, T.13
  • 71
    • 0035145334 scopus 로고    scopus 로고
    • Alternative pathway therapy for urea cycle disorders: twenty years later
    • (Discussion S54–5)
    • Batshaw, M.L., MacArthur, R.B., Tuchman, M., Alternative pathway therapy for urea cycle disorders: twenty years later. J. Pediatr. 138:1 Suppl (2001), S46–54 (Discussion S54–5).
    • (2001) J. Pediatr. , vol.138 , Issue.1 , pp. S46-54
    • Batshaw, M.L.1    MacArthur, R.B.2    Tuchman, M.3
  • 72
    • 0023515054 scopus 로고
    • Treatment of urea cycle disorders
    • Batshaw, M.L., Monahan, P.S., Treatment of urea cycle disorders. Enzyme 38:1–4 (1987), 242–250.
    • (1987) Enzyme , vol.38 , Issue.1-4 , pp. 242-250
    • Batshaw, M.L.1    Monahan, P.S.2
  • 74
    • 79951693205 scopus 로고    scopus 로고
    • Argininosuccinate lyase deficiency-argininosuccinic aciduria and beyond
    • Erez, A., Nagamani, S.C., Lee, B., Argininosuccinate lyase deficiency-argininosuccinic aciduria and beyond. Am. J. Med. Genet. C: Semin. Med. Genet. 157C:1 (2011), 45–53.
    • (2011) Am. J. Med. Genet. C: Semin. Med. Genet. , vol.157C , Issue.1 , pp. 45-53
    • Erez, A.1    Nagamani, S.C.2    Lee, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.