메뉴 건너뛰기




Volumn 6, Issue 7, 2017, Pages

Evidence of Oxidative Stress and Secondary Mitochondrial Dysfunction in Metabolic and Non-Metabolic Disorders

Author keywords

Catalase; Coenzyme Q10; Electron transport chain; Glutathione; Methylmalonic acid; Methylmalonic acidemia; Mitochondria; Nitric oxide synthase; Nitrosative stress; Oxidative stress; Peroxisome; Phenylketonuria; Reactive nitrogen species; Reactive oxygen species; Sepsis; Superoxide dismutase

Indexed keywords

ANTIOXIDANT; CHEMOKINE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; LACTIC ACID; NITRIC OXIDE; PHENYLALANINE 4 MONOOXYGENASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; THIOBARBITURIC ACID REACTIVE SUBSTANCE; UBIDECARENONE; VERY LONG CHAIN FATTY ACID;

EID: 85030683478     PISSN: None     EISSN: 20770383     Source Type: Journal    
DOI: 10.3390/jcm6070071     Document Type: Review
Times cited : (103)

References (190)
  • 3
    • 0029918169 scopus 로고    scopus 로고
    • Mitochondrial damage: An important feature in a number of inborn errors of metabolism
    • Heales, S.J.; Bolanos, J.P.; Brand, M.P.; Clark, J.B.; Land, J.M. Mitochondrial damage: An important feature in a number of inborn errors of metabolism? J. Inherit. Metab. Dis. 1996, 19, 140-142.
    • (1996) J. Inherit. Metab. Dis , vol.19 , pp. 140-142
    • Heales, S.J.1    Bolanos, J.P.2    Brand, M.P.3    Clark, J.B.4    Land, J.M.5
  • 7
    • 0033152897 scopus 로고    scopus 로고
    • Plasma zinc, copper, and erythrocyte superoxide dismutase in children with phenylketonuria
    • Fisberg, R.M.; Silva-Femandes, M.E.; Fisberg, M.; Schmidt, B.J. Plasma zinc, copper, and erythrocyte superoxide dismutase in children with phenylketonuria. Nutrition 1999, 15, 449-452.
    • (1999) Nutrition , vol.15 , pp. 449-452
    • Fisberg, R.M.1    Silva-Femandes, M.E.2    Fisberg, M.3    Schmidt, B.J.4
  • 8
    • 0033806715 scopus 로고    scopus 로고
    • Antioxidant and thyroid hormone status in selenium-deficient phenylketonuric and hyperphenylalaninemic patients
    • Van Bakel, M.M.E.; Printzen, G.; Wermuth, B.; Wiesmann, U.N. Antioxidant and thyroid hormone status in selenium-deficient phenylketonuric and hyperphenylalaninemic patients. Am. J. Clin. Nutr. 2000, 72, 976-981.
    • (2000) Am. J. Clin. Nutr , vol.72 , pp. 976-981
    • van Bakel, M.M.E.1    Printzen, G.2    Wermuth, B.3    Wiesmann, U.N.4
  • 9
    • 84959018825 scopus 로고    scopus 로고
    • Oxidative stress and metabolic disorders: Pathogenesis and therapeutic strategies
    • Rani, V.; Deep, G.; Singh, R.K. Oxidative stress and metabolic disorders: Pathogenesis and therapeutic strategies. Life Sci. 2016, 148, 183-193.
    • (2016) Life Sci , vol.148 , pp. 183-193
    • Rani, V.1    Deep, G.2    Singh, R.K.3
  • 11
    • 33646354917 scopus 로고    scopus 로고
    • Rotenone-like action of the branch chain phytanic acid induces oxidative stress in mitochondria
    • Schonfeld, P.; Reiser, G. Rotenone-like action of the branch chain phytanic acid induces oxidative stress in mitochondria. J. Biol. Chem. 2006, 281, 7136-7142.
    • (2006) J. Biol. Chem , vol.281 , pp. 7136-7142
    • Schonfeld, P.1    Reiser, G.2
  • 13
    • 0032513135 scopus 로고    scopus 로고
    • Peroxidative damage to cardiac mitochondria: Cytochrome c oxidase and cardiolipin alterations
    • Paradies, G.; Ruggiero, F.M.; Petrosillo, G.; Quagliariello, E. Peroxidative damage to cardiac mitochondria: Cytochrome c oxidase and cardiolipin alterations. FEBS Lett. 1998, 424, 155-158.
    • (1998) FEBS Lett , vol.424 , pp. 155-158
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 14
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417, 1-13.
    • (2009) Biochem. J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 15
    • 84863315229 scopus 로고    scopus 로고
    • Oxidative stress in phenylketonuria: Future directions
    • Rocha, C.R.; Martins, M.J. Oxidative stress in phenylketonuria: Future directions. J. Inherit. Metab. Dis. 2012, 35, 381-398.
    • (2012) J. Inherit. Metab. Dis , vol.35 , pp. 381-398
    • Rocha, C.R.1    Martins, M.J.2
  • 16
    • 85009251306 scopus 로고    scopus 로고
    • Oxidative stress in sepsis: Pathophysiological implications justifying antioxidant co
    • Prauchner, C.A. Oxidative stress in sepsis: Pathophysiological implications justifying antioxidant co-therapy. Burns 2016, 43, 471-485.
    • (2016) Burns , vol.43 , pp. 471-485
    • Prauchner, C.A.1
  • 18
    • 61849155430 scopus 로고    scopus 로고
    • Phenylketonuria: An inborn error of phenylalanine metabolism
    • Williams, R.A.; Mamotte, C.D.; Burnett, J.R. Phenylketonuria: An inborn error of phenylalanine metabolism. Clin. Biochem. Rev. 2008, 29, 31-41.
    • (2008) Clin. Biochem. Rev , vol.29 , pp. 31-41
    • Williams, R.A.1    Mamotte, C.D.2    Burnett, J.R.3
  • 19
    • 84975774276 scopus 로고    scopus 로고
    • Parkinsonism in phenylketonuria: A consequence of dopamine depletion?
    • Velema, M.; Boot, E.; Engelen, M.; Hollak, C. Parkinsonism in phenylketonuria: A consequence of dopamine depletion? JIMD Rep. 2015, 20, 35-38.
    • (2015) JIMD Rep , vol.20 , pp. 35-38
    • Velema, M.1    Boot, E.2    Engelen, M.3    Hollak, C.4
  • 20
    • 0021990680 scopus 로고
    • Biochemical and neuropsychological effects of elevated plasma phenylalanine in patients with treated phenylketonuria
    • Krause, W.; Halminski, M.; McDonald, L.; Demure, P.; Salvo, R.; Friedes, S.R.; Elsas, L. Biochemical and neuropsychological effects of elevated plasma phenylalanine in patients with treated phenylketonuria. J. Clin. Investig. 1985, 75, 40-48.
    • (1985) J. Clin. Investig , vol.75 , pp. 40-48
    • Krause, W.1    Halminski, M.2    McDonald, L.3    Demure, P.4    Salvo, R.5    Friedes, S.R.6    Elsas, L.7
  • 23
    • 0031796244 scopus 로고    scopus 로고
    • Neurological aspects of adult phenylketonuria
    • Pietz, J. Neurological aspects of adult phenylketonuria. Curr. Opin. Neurol. 1998, 11, 679-688.
    • (1998) Curr. Opin. Neurol , vol.11 , pp. 679-688
    • Pietz, J.1
  • 24
    • 0033835383 scopus 로고    scopus 로고
    • Behaviour in early treated phenylketonuria: A systematic review
    • Smith, I.; Knowles, J. Behaviour in early treated phenylketonuria: A systematic review. Eur. J. Pediatr. 2000, 159, S89-S93.
    • (2000) Eur. J. Pediatr , vol.159 , pp. S89-S93
    • Smith, I.1    Knowles, J.2
  • 27
    • 0033834983 scopus 로고    scopus 로고
    • Comments on the neuropathology of phenylketonuria
    • Dyer, C.A. Comments on the neuropathology of phenylketonuria. Eur. J. Pediatr. 2000, 159, S107-S108.
    • (2000) Eur. J. Pediatr , vol.159 , pp. S107-S108
    • Dyer, C.A.1
  • 28
    • 0033835893 scopus 로고    scopus 로고
    • The neuropathology of phenylketonuria: Human and animal studies
    • Huttenlocher, P.R. The neuropathology of phenylketonuria: Human and animal studies. Eur. J. Pediatr. 2000, 159, S102-S106.
    • (2000) Eur. J. Pediatr , vol.159 , pp. S102-S106
    • Huttenlocher, P.R.1
  • 29
    • 69449104991 scopus 로고    scopus 로고
    • Large neutral amino acids supplementation in phenylketonuric patients
    • Rocha, J.C.; Martel, F. Large neutral amino acids supplementation in phenylketonuric patients. J. Inherit. Metab. Dis. 2009, 32, 472-480.
    • (2009) J. Inherit. Metab. Dis , vol.32 , pp. 472-480
    • Rocha, J.C.1    Martel, F.2
  • 30
    • 84916931763 scopus 로고    scopus 로고
    • Metabolic disturbances in diseases with neurological involvement
    • Duarte, J.M.; Schuck, P.F.; Wenk, G.L.; Ferreira, G.C. Metabolic disturbances in diseases with neurological involvement. Aging Dis. 2013, 5, 238-255.
    • (2013) Aging Dis , vol.5 , pp. 238-255
    • Duarte, J.M.1    Schuck, P.F.2    Wenk, G.L.3    Ferreira, G.C.4
  • 34
    • 13544274222 scopus 로고    scopus 로고
    • Low total antioxidant status is implicated with high 8-hydroxy-2-deoxyguanosine serum concentrations in phenylketonuria
    • Schulpis, K.H.; Tsakiris, S.; Traeger-Synodinos, J.; Papassotiriou, I. Low total antioxidant status is implicated with high 8-hydroxy-2-deoxyguanosine serum concentrations in phenylketonuria. Clin. Biochem. 2005, 38, 239-242.
    • (2005) Clin. Biochem , vol.38 , pp. 239-242
    • Schulpis, K.H.1    Tsakiris, S.2    Traeger-Synodinos, J.3    Papassotiriou, I.4
  • 36
    • 0033968211 scopus 로고    scopus 로고
    • Selenium Kinetics and Changes in Glutathione Peroxidase Activities in Patients Receiving Long-Term Parenteral Nutrition and Effects of Supplementation With Selenite
    • Hatanaka, N.; Nakaden, H.; Yamamoto, Y.; Matsuo, S.; Fujikawa, T.; Matsusue, S. Selenium Kinetics and Changes in Glutathione Peroxidase Activities in Patients Receiving Long-Term Parenteral Nutrition and Effects of Supplementation With Selenite. Nutrition 2000, 16, 22-26.
    • (2000) Nutrition , vol.16 , pp. 22-26
    • Hatanaka, N.1    Nakaden, H.2    Yamamoto, Y.3    Matsuo, S.4    Fujikawa, T.5    Matsusue, S.6
  • 41
    • 0025910547 scopus 로고
    • Effect of phenylalanine derivatives on the main regulatory enzymes of hepatic cholesterogenesis
    • Castillo, M.; Martinez-Cayuela, M.; Zafra, M.F.; Garcia-Peregrin, E. Effect of phenylalanine derivatives on the main regulatory enzymes of hepatic cholesterogenesis. Mol. Cell Biochem. 1991, 105, 21-25.
    • (1991) Mol. Cell Biochem , vol.105 , pp. 21-25
    • Castillo, M.1    Martinez-Cayuela, M.2    Zafra, M.F.3    Garcia-Peregrin, E.4
  • 42
    • 0034283890 scopus 로고    scopus 로고
    • Is there a relationship between 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and forebrain pathology in the PKU mouse
    • Shefer, S.; Tint, G.S.; Jean-Guillaume, D.; Daikhin, E.; Kendler, A.; Nguyen, L.B.; Yudkoff, M.; Dyer, C.A. Is there a relationship between 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and forebrain pathology in the PKU mouse? J. Neurosci. Res. 2000, 61, 549-563.
    • (2000) J. Neurosci. Res , vol.61 , pp. 549-563
    • Shefer, S.1    Tint, G.S.2    Jean-Guillaume, D.3    Daikhin, E.4    Kendler, A.5    Nguyen, L.B.6    Yudkoff, M.7    Dyer, C.A.8
  • 44
    • 85114273389 scopus 로고    scopus 로고
    • Mononuclear cell coenzyme Q (Coq) Concentration and mitochondrial respiratory chain succinate cytochrome C reductase (complex li
    • Hargreaves, I.P.; Heales, S.J.; Briddon, A.; Land, J.M.; Lee, P.J. Mononuclear cell coenzyme Q (coq) Concentration and mitochondrial respiratory chain succinate cytochrome C reductase (complex li-iii) activity in phenyloketonuric patiens. J. Inher. Metab. Dis. 2002, 25, 18.
    • (2002) J. Inher. Metab. Dis , vol.25 , pp. 18
    • Hargreaves, I.P.1    Heales, S.J.2    Briddon, A.3    Land, J.M.4    Lee, P.J.5
  • 46
    • 64449085699 scopus 로고    scopus 로고
    • Assessment of mitochondrial respiratory chain function in hyperphenylalaninemia
    • Kyprianou, N.; Murphy, E.; Lee, P.; Hargreaves, I. Assessment of mitochondrial respiratory chain function in hyperphenylalaninemia. J. Inherit. Metab. 2009, 32, 289-296.
    • (2009) J. Inherit. Metab , vol.32 , pp. 289-296
    • Kyprianou, N.1    Murphy, E.2    Lee, P.3    Hargreaves, I.4
  • 47
    • 0033835283 scopus 로고    scopus 로고
    • Nutrition, physical growth, and bone density in treated phenylketonuria
    • Przyrembel, H.; Bremer, H.J. Nutrition, physical growth, and bone density in treated phenylketonuria. Eur. J. Pediatr. 2000, 159, S129-S135.
    • (2000) Eur. J. Pediatr , vol.159 , pp. S129-S135
    • Przyrembel, H.1    Bremer, H.J.2
  • 49
    • 77950868501 scopus 로고    scopus 로고
    • Dietary interventions for phenylketonuria
    • Poustie, V.J.; Wildgoose, J. Dietary interventions for phenylketonuria. Cochrane Libr. 2010, doi:10.1002/14651858.CD001304.pub2.
    • (2010) Cochrane Libr
    • Poustie, V.J.1    Wildgoose, J.2
  • 50
    • 0026764376 scopus 로고
    • Bone mineral status in children with phenylketonuria—Relationship to nutritional intake and phenylalanine control
    • McMurry, M.P.; Chan, G.M.; Leonard, C.O.; Ernst, S.L. Bone mineral status in children with phenylketonuria—Relationship to nutritional intake and phenylalanine control. Am. J. Clin. Nutr. 1992, 55, 997-1004.
    • (1992) Am. J. Clin. Nutr , vol.55 , pp. 997-1004
    • McMurry, M.P.1    Chan, G.M.2    Leonard, C.O.3    Ernst, S.L.4
  • 51
    • 0027621797 scopus 로고
    • Trace elements balance in treated phenylketonuria children. Consequences of selenium deficiency on lipid peroxidation
    • Wilke, B.C.; Vidailhet, M.; Richard, M.J.; Ducros, V.; Arnaud, J.; Favier, A. Trace elements balance in treated phenylketonuria children. Consequences of selenium deficiency on lipid peroxidation. Arch. Latinoam. Nutr. 1993, 43,119-122.
    • (1993) Arch. Latinoam. Nutr , vol.43 , pp. 119-122
    • Wilke, B.C.1    Vidailhet, M.2    Richard, M.J.3    Ducros, V.4    Arnaud, J.5    Favier, A.6
  • 52
    • 84975703520 scopus 로고    scopus 로고
    • Metal
    • Ragsdale, S. Metal-carbon bonds in enzymes and cofactors. Coord. Chem. Rev. 2010, 254, 1948-1949.
    • (2010) Coord. Chem. Rev , vol.254 , pp. 1948-1949
    • Ragsdale, S.1
  • 54
    • 0025903652 scopus 로고
    • Inadequate iron availability as a possible cause of low serum carnitine concentrations in patients with phenylketonuria
    • Bohler, H.; Ulrich, K.; Endres, W.; Behbehani, A.W.; Wendel, U. Inadequate iron availability as a possible cause of low serum carnitine concentrations in patients with phenylketonuria. Eur. J. Pediatr. 1991, 15, 425-428.
    • (1991) Eur. J. Pediatr , vol.15 , pp. 425-428
    • Bohler, H.1    Ulrich, K.2    Endres, W.3    Behbehani, A.W.4    Wendel, U.5
  • 55
    • 30544455318 scopus 로고    scopus 로고
    • Antioxidant and antiradical activities of L-carnitine
    • Gullcin, I. Antioxidant and antiradical activities of L-carnitine. Life Sci. 2006, 78, 803-811.
    • (2006) Life Sci , vol.78 , pp. 803-811
    • Gullcin, I.1
  • 56
    • 79959601660 scopus 로고    scopus 로고
    • Oxidative stress in phenylketonuria: What is the evidence? Cell Mol
    • Ribas, G.S.; Sitta, A.; Wajner, M.; Vargas, C.R. Oxidative stress in phenylketonuria: What is the evidence? Cell Mol. Neurobiol. 2011, 31, 653-662.
    • (2011) Neurobiol , vol.31 , pp. 653-662
    • Ribas, G.S.1    Sitta, A.2    Wajner, M.3    Vargas, C.R.4
  • 57
    • 0037180440 scopus 로고    scopus 로고
    • Identification of the gene responsible for the cblA complementation group of vitamin B12responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements
    • Dobson, C.M.; Wai, T.; Leclerc, D.; Wilson, A.; Wu, X.; Dore, C.; Hudson, T.; Rosenblatt, D.S.; Gravel, R.A. Identification of the gene responsible for the cblA complementation group of vitamin B12responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements. Proc. Natl. Acad. Sci. USA 2002, 99, 15554-15559.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15554-15559
    • Dobson, C.M.1    Wai, T.2    Leclerc, D.3    Wilson, A.4    Wu, X.5    Dore, C.6    Hudson, T.7    Rosenblatt, D.S.8    Gravel, R.A.9
  • 58
    • 0002911516 scopus 로고    scopus 로고
    • Disorders of propionate and methylmalonate metabolism
    • Scriver, C.R., Beaudet, A.L., Sky, W.S., Valle, D., Eds.; McGraw-Hill: New York, NY, USA
    • Fenton, W.A.; Gravel, R.A.A.; Rosenblatt, D.S. Disorders of propionate and methylmalonate metabolism. In The Metabolic and Molecular Bases of Inherited Disease; Scriver, C.R., Beaudet, A.L., Sky, W.S., Valle, D., Eds.; McGraw-Hill: New York, NY, USA, 2011; pp. 2165-2193.
    • (2011) The Metabolic and Molecular Bases of Inherited Disease , pp. 2165-2193
    • Fenton, W.A.1    Gravel, R.A.A.2    Rosenblatt, D.S.3
  • 61
    • 84875320931 scopus 로고    scopus 로고
    • Isolated methylmalonic acidemia
    • Pagon, R.A., Adam, M.P., Ardinger, H.H., Wallace, S.E., Amemiya, A., Bean, L.J.H., Bird, T.D., Ledbetter, N., Mefford, H.C., Smith, R.J.H., et al., Eds.; University of Washington: Seattle, WA, USA
    • Manoli, I.; Sloan, J.L.; Venditti, C.P. Isolated methylmalonic acidemia. In Genereviews [Internet]; Pagon, R.A., Adam, M.P., Ardinger, H.H., Wallace, S.E., Amemiya, A., Bean, L.J.H., Bird, T.D., Ledbetter, N., Mefford, H.C., Smith, R.J.H., et al., Eds.; University of Washington: Seattle, WA, USA; pp. 1993-2017.
    • Genereviews [Internet] , pp. 1993-2017
    • Manoli, I.1    Sloan, J.L.2    Venditti, C.P.3
  • 62
    • 0020324363 scopus 로고
    • Comparison of cytosolic and mitochondrial enzyme alterations in the livers of propionic or methylmalonic acidemia: A reduction of cytochrome oxidase activity
    • Hayasaka, K.; Metoki, K.; Satoh, T.; Narisawa, K.; Tada, K.; Kawakami, T.; Matsuo, N.; Aoki, T. Comparison of cytosolic and mitochondrial enzyme alterations in the livers of propionic or methylmalonic acidemia: A reduction of cytochrome oxidase activity. Tohoku J. Exp. Med. 1982, 137, 329-333.
    • (1982) Tohoku J. Exp. Med , vol.137 , pp. 329-333
    • Hayasaka, K.1    Metoki, K.2    Satoh, T.3    Narisawa, K.4    Tada, K.5    Kawakami, T.6    Matsuo, N.7    Aoki, T.8
  • 63
    • 36749012527 scopus 로고    scopus 로고
    • Methylmalonic acidaemia leads to increased production reactive oxygen species and induction of apoptosis through the mitocondrial/caspase pathway
    • Richard, E.; Alvarez-Barrientos, A.; Perez, B.; Desviat, L.R.; Ugarte, M. Methylmalonic acidaemia leads to increased production reactive oxygen species and induction of apoptosis through the mitocondrial/caspase pathway. J. Pathol. 2007, 213, 453-461.
    • (2007) J. Pathol , vol.213 , pp. 453-461
    • Richard, E.1    Alvarez-Barrientos, A.2    Perez, B.3    Desviat, L.R.4    Ugarte, M.5
  • 64
    • 0014326756 scopus 로고
    • Methylmalonic academia. A disorder associated with acidosis, hyperlycaemia, and hyperlactatemia
    • Lindblad, B.; Lindblad, B.S.; Olin, P.; Svanberg, B.; Zetterstrom, R. Methylmalonic academia. A disorder associated with acidosis, hyperlycaemia, and hyperlactatemia. Acta Paediatr. Scand. 1968, 57, 417-424.
    • (1968) Acta Paediatr. Scand , vol.57 , pp. 417-424
    • Lindblad, B.1    Lindblad, B.S.2    Olin, P.3    Svanberg, B.4    Zetterstrom, R.5
  • 65
    • 0037177804 scopus 로고    scopus 로고
    • Neurodegeneration in Methylmalonic Aciduria Involves Inhibition of Complex II and the Tricarboxylic Acid Cycle, and Synergistically Acting Excitotoxicity
    • Okun, J.C.; Horster, F.; Farkas, L.; Feyh, P.; Hinz, A.; Sauer, S.; Hoffman, G.F.; Unisicker, K.; Mayatepek, E.; Kolker, S. Neurodegeneration in Methylmalonic Aciduria Involves Inhibition of Complex II and the Tricarboxylic Acid Cycle, and Synergistically Acting Excitotoxicity. J. Biol. Chem. 2002, 277, 14674-14680.
    • (2002) J. Biol. Chem , vol.277 , pp. 14674-14680
    • Okun, J.C.1    Horster, F.2    Farkas, L.3    Feyh, P.4    Hinz, A.5    Sauer, S.6    Hoffman, G.F.7    Unisicker, K.8    Mayatepek, E.9    Kolker, S.10
  • 67
    • 0025836574 scopus 로고
    • Decreased activities of ubiqunol; ferricytochrome c oxidoreductase (Complex III) and ferrocytochrome c: Oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin [C-lactam]-induced methylmalonic aciduria
    • Krahenbuhl, S.; Chang, M.; Brass, E.P.; Hoppel, C.L. Decreased activities of ubiqunol; ferricytochrome c oxidoreductase (complex III) and ferrocytochrome c: Oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin [C-lactam]-induced methylmalonic aciduria. J. Biol. Chem. 1991, 266, 20998-21003.
    • (1991) J. Biol. Chem , vol.266 , pp. 20998-21003
    • Krahenbuhl, S.1    Chang, M.2    Brass, E.P.3    Hoppel, C.L.4
  • 71
    • 17044382491 scopus 로고    scopus 로고
    • Chronic administration of methylmaloic acid (MMA) to rats causes proteinuria and renal tubular injury (abstract)
    • Kashtan, C.E.; Abousedira, M.; Rozen, S.; Manivel, J.C.; McCann, M.; Tuchman, M. Chronic administration of methylmaloic acid (MMA) to rats causes proteinuria and renal tubular injury (abstract). Pediatr. Res. 1998, 43, 309.
    • (1998) Pediatr. Res , vol.43 , pp. 309
    • Kashtan, C.E.1    Abousedira, M.2    Rozen, S.3    Manivel, J.C.4    McCann, M.5    Tuchman, M.6
  • 73
    • 0024365988 scopus 로고
    • Focal changes in the globi pallidi associated with neurological dysfunction in methylmalonic academia
    • De Souza, C.; Piesowicz, A.T.; Brett, E.M.; Leonard, J.V. Focal changes in the globi pallidi associated with neurological dysfunction in methylmalonic academia. Neuropediatrics 1989, 20, 199-201.
    • (1989) Neuropediatrics , vol.20 , pp. 199-201
    • de Souza, C.1    Piesowicz, A.T.2    Brett, E.M.3    Leonard, J.V.4
  • 74
    • 0028040720 scopus 로고
    • CT and MR of the brain in disorders of propionate and methylmalonate metabolism
    • Brismar, J.; Ozand, P.T. CT and MR of the brain in disorders of propionate and methylmalonate metabolism. Am. J. Neuroradiol. 1994, 15, 1459-1473.
    • (1994) Am. J. Neuroradiol , vol.15 , pp. 1459-1473
    • Brismar, J.1    Ozand, P.T.2
  • 77
    • 0035033273 scopus 로고    scopus 로고
    • Multi
    • Trinh, B.C.; Melhem, E.R.; Barker, P.B. Multi-slice proton MR spectroscopy and diffusion-weighted imaging in methylmalonic acidemia: Report of two cases and review of the literature. Am. J. Neuroradiol. 2001, 22, 831-833.
    • (2001) Am. J. Neuroradiol , vol.22 , pp. 831-833
    • Trinh, B.C.1    Melhem, E.R.2    Barker, P.B.3
  • 78
    • 0024246645 scopus 로고
    • Acute extrapyramidal syndrome in methylmalonic acidemia: “Metabolic stroke” involving the globus pallidus
    • Heidenreich, R.; Natowicz, M.; Hainline, B.E.; Berman, P.; Kelley, R.I.; Hillman, R.E.; Berry, G.T. Acute extrapyramidal syndrome in methylmalonic acidemia: “Metabolic stroke” involving the globus pallidus. J. Pediatr. 1988, 113, 1022-1027.
    • (1988) J. Pediatr , vol.113 , pp. 1022-1027
    • Heidenreich, R.1    Natowicz, M.2    Hainline, B.E.3    Berman, P.4    Kelley, R.I.5    Hillman, R.E.6    Berry, G.T.7
  • 80
    • 17044386245 scopus 로고    scopus 로고
    • Methylmalonic acid—An endogenous toxin? Cell Mol
    • Kolker, S.; Okun, J.G. Methylmalonic acid—An endogenous toxin? Cell Mol. Life Sci. 2005, 62, 621-624.
    • (2005) Life Sci , vol.62 , pp. 621-624
    • Kolker, S.1    Okun, J.G.2
  • 82
    • 0035879332 scopus 로고    scopus 로고
    • Inhibition of mitochondrial complex II induces a long-term potentiation of NMDA-mediated synaptic excitation in the striatum requiring endogenous dopamine
    • Calabresi, P.; Gubellini, P.; Picconi, B.; Centonze, D.; Pisani, A.; Bonsi, P.; Greengard, P.; Hipskind, R.A.; Borrelli, E.; Bernardi, G. Inhibition of mitochondrial complex II induces a long-term potentiation of NMDA-mediated synaptic excitation in the striatum requiring endogenous dopamine. J. Neurosci. 2001, 21, 5110-5120.
    • (2001) J. Neurosci , vol.21 , pp. 5110-5120
    • Calabresi, P.1    Gubellini, P.2    Picconi, B.3    Centonze, D.4    Pisani, A.5    Bonsi, P.6    Greengard, P.7    Hipskind, R.A.8    Borrelli, E.9    Bernardi, G.10
  • 85
    • 62649107795 scopus 로고    scopus 로고
    • Inherited disorders affecting mitochondrial function are associated with glutathione deficiency and hypocitrullinemia
    • Atkuri, K.R.; Cowan, T.M.; Kwan, T.; Ng, A.; Herzenberg, L.A.; Herzenberg, LA.; Enns, G.M. Inherited disorders affecting mitochondrial function are associated with glutathione deficiency and hypocitrullinemia. Proc. Natl. Acad. Sci. USA 2009, 106, 3941-3944.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3941-3944
    • Atkuri, K.R.1    Cowan, T.M.2    Kwan, T.3    Ng, A.4    Herzenberg, L.A.5    Herzenberg, L.A.6    Enns, G.M.7
  • 89
    • 13844276595 scopus 로고    scopus 로고
    • Glutathione deficiency in patients with mitochondrial disease: Implications for pathogenesis and treatment
    • Hargreaves, I.P.; Sheena, Y.; Land, J.M.; Heales, S.J. Glutathione deficiency in patients with mitochondrial disease: Implications for pathogenesis and treatment. J. Inherit. Metab. Dis. 2005, 28, 1-88.
    • (2005) J. Inherit. Metab. Dis , vol.28 , pp. 1-88
    • Hargreaves, I.P.1    Sheena, Y.2    Land, J.M.3    Heales, S.J.4
  • 90
    • 84867097606 scopus 로고    scopus 로고
    • Patients with organic acidaemias have an alteredthiol status
    • Salmi, H.; Leonard, J.; Lapatto, R. Patients with organic acidaemias have an alteredthiol status. Acta Paediatr. 2012, 101, e505-e508.
    • (2012) Acta Paediatr , vol.101 , pp. e505-e508
    • Salmi, H.1    Leonard, J.2    Lapatto, R.3
  • 92
    • 0038028427 scopus 로고    scopus 로고
    • Ubiquinone: Cholesterol’s reclusive cousin
    • Hargreaves, I.P. Ubiquinone: Cholesterol’s reclusive cousin. Ann. Clin. Biochem. 2003, 40, 207-218.
    • (2003) Ann. Clin. Biochem , vol.40 , pp. 207-218
    • Hargreaves, I.P.1
  • 100
    • 77953216242 scopus 로고    scopus 로고
    • General aspects and neuropathology of X-linked adrenoleukodystrophy
    • Ferrer, I.; Aubourg, P.; Pujol, A. General aspects and neuropathology of X-linked adrenoleukodystrophy. Brain Pathol. 2010, 20, 817-830.
    • (2010) Brain Pathol , vol.20 , pp. 817-830
    • Ferrer, I.1    Aubourg, P.2    Pujol, A.3
  • 102
    • 0033970326 scopus 로고    scopus 로고
    • Adrenomyeloneuropathy: A neuropathologic review featuring its noninflammatory myelopathy
    • Powers, J.M.; DeCiero, D.P.; Ito, M.; Moser, A.B.; Moser, H.W. Adrenomyeloneuropathy: A neuropathologic review featuring its noninflammatory myelopathy. J. Neuropathol. Exp. Neurol. 2000, 59, 89-102.
    • (2000) J. Neuropathol. Exp. Neurol , vol.59 , pp. 89-102
    • Powers, J.M.1    Deciero, D.P.2    Ito, M.3    Moser, A.B.4    Moser, H.W.5
  • 104
    • 0026085762 scopus 로고
    • Beta oxidation of fatty acids
    • Schulz, H. Beta oxidation of fatty acids. Biochim. Biophys. Acta 1991, 1081, 109-120.
    • (1991) Biochim. Biophys. Acta , vol.1081 , pp. 109-120
    • Schulz, H.1
  • 105
    • 33845326985 scopus 로고    scopus 로고
    • Peroxisomal beta-oxidation- a metabolic pathway with multiple functions
    • Poirier, Y.; Antonenkov, V.D.; Glumoff, T.; Hiltunen, J.K. Peroxisomal beta-oxidation- a metabolic pathway with multiple functions. Biochim. Biophys. Acta 2006, 1763, 1413-1426.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1413-1426
    • Poirier, Y.1    Antonenkov, V.D.2    Glumoff, T.3    Hiltunen, J.K.4
  • 106
    • 0023477159 scopus 로고
    • Localization of xanthine oxidase in crystalline cores of peroxisomes. A cytochemical and biochemical study
    • Angermuller, S.; Bruder, G.; Volkl, A.; Wesch, H.; Fahimi, H.D. Localization of xanthine oxidase in crystalline cores of peroxisomes. A cytochemical and biochemical study. Eur. J. Cell Biol. 1987, 45, 137-144.
    • (1987) Eur. J. Cell Biol , vol.45 , pp. 137-144
    • Angermuller, S.1    Bruder, G.2    Volkl, A.3    Wesch, H.4    Fahimi, H.D.5
  • 110
    • 8644221211 scopus 로고    scopus 로고
    • Mammalian peroxisomes and reactive oxygen species
    • Schrader, M.; Fahimi, H.D. Mammalian peroxisomes and reactive oxygen species. Histochem. Cell Biol. 2004, 122, 383-393.
    • (2004) Histochem. Cell Biol , vol.122 , pp. 383-393
    • Schrader, M.1    Fahimi, H.D.2
  • 111
    • 84864050485 scopus 로고    scopus 로고
    • Role of peroxisomes in ROS/RNS-metabolism: Implications for human disease
    • Fransen, M.; Nordgren, M.; Wang, B.; Apanasets, O. Role of peroxisomes in ROS/RNS-metabolism: Implications for human disease. Biochim. Biophys. Acta 2012, 1822, 1363-1373.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1363-1373
    • Fransen, M.1    Nordgren, M.2    Wang, B.3    Apanasets, O.4
  • 113
    • 0034799180 scopus 로고    scopus 로고
    • Mitochondrial alterations caused by defective peroxisomal biogenesis in a mouse model of Zellweger syndrome (PEX5 knock out mouse)
    • Baumgart, E.; Vanhorebeek, I.; Grabenbauer, M.; Borgers, M.; Declercq, P.E.; Fahimi, H.D.; Baes, M. Mitochondrial alterations caused by defective peroxisomal biogenesis in a mouse model of Zellweger syndrome (PEX5 knock out mouse). Am. J. Pathol. 2001, 159, 1477-1494.
    • (2001) Am. J. Pathol , vol.159 , pp. 1477-1494
    • Baumgart, E.1    Vanhorebeek, I.2    Grabenbauer, M.3    Borgers, M.4    Declercq, P.E.5    Fahimi, H.D.6    Baes, M.7
  • 118
    • 0029094333 scopus 로고
    • Interactions of a very long chain fatty acid with model membranes and serum albumin. Implications for the pathogenesis of adrenoleukodystrophy
    • Ho, J.K.; Moser, H.; Kishimoto, Y.; Hamilton, J.A. Interactions of a very long chain fatty acid with model membranes and serum albumin. Implications for the pathogenesis of adrenoleukodystrophy. J. Clin. Investig. 1995, 96, 1455-1463.
    • (1995) J. Clin. Investig , vol.96 , pp. 1455-1463
    • Ho, J.K.1    Moser, H.2    Kishimoto, Y.3    Hamilton, J.A.4
  • 119
    • 0020516562 scopus 로고
    • Mitochondrial myopathy of cerebrohepato-renal (Zellweger) syndrome
    • Sarnat, H.B.; Machin, G.; Darwish, H.Z.; Rubin, S.Z. Mitochondrial myopathy of cerebrohepato-renal (Zellweger) syndrome. Can. J. Neurol. Sci. 1983, 10, 170-177.
    • (1983) Can. J. Neurol. Sci , vol.10 , pp. 170-177
    • Sarnat, H.B.1    Machin, G.2    Darwish, H.Z.3    Rubin, S.Z.4
  • 120
    • 0021333334 scopus 로고
    • Mitochondrial myopathy with loosely coupled oxidative phosphorylation in a case of Zellweger syndrome
    • Muller-Hocker, J.; Walther, J.R.; Bise, K.; Pongratz, D.; Hubner, G. Mitochondrial myopathy with loosely coupled oxidative phosphorylation in a case of Zellweger syndrome. Virchows Arch. B Cell Pathol. Zell-Pathol. 1984, 45, 125-138.
    • (1984) Virchows Arch. B Cell Pathol. Zell , vol.45 , pp. 125-138
    • Muller-Hocker, J.1    Walther, J.R.2    Bise, K.3    Pongratz, D.4    Hubner, G.5
  • 126
    • 84871818839 scopus 로고    scopus 로고
    • Oxidative stress modulates mitochondrial failure and cyclophilin D function in X-linked adrenoleukodystrophy
    • Lopez-Erauskin, J.; Galino, J.; Bianchi, P.; Fourcade, S.; Andreu, A.L.; Ferrer, I.; Munoz-Pinedo, C.; Pujol, A. Oxidative stress modulates mitochondrial failure and cyclophilin D function in X-linked adrenoleukodystrophy. Brain 2012, 135, 3584-3598.
    • (2012) Brain , vol.135 , pp. 3584-3598
    • Lopez-Erauskin, J.1    Galino, J.2    Bianchi, P.3    Fourcade, S.4    Andreu, A.L.5    Ferrer, I.6    Munoz-Pinedo, C.7    Pujol, A.8
  • 127
    • 77953191945 scopus 로고    scopus 로고
    • Pathomechanisms underlying X-adrenoleukodystrophy: A three-hit hypothesis
    • Singh, I.; Pujol, A. Pathomechanisms underlying X-adrenoleukodystrophy: A three-hit hypothesis. Brain Pathol. 2010, 20, 838-844.
    • (2010) Brain Pathol , vol.20 , pp. 838-844
    • Singh, I.1    Pujol, A.2
  • 128
    • 84864032314 scopus 로고    scopus 로고
    • Oxidative stress underlying axonal degeneration in adrenoleukodystrophy: A paradigm for multifactorial neurodegenerative diseases?
    • Galea, E.; Launay, N.; Portero-Otin, M.; Ruiz, M.; Pamplona, R.; Aubourg, P.; Ferrer, I.; Pujol, A. Oxidative stress underlying axonal degeneration in adrenoleukodystrophy: A paradigm for multifactorial neurodegenerative diseases? Biochim. Biophys. Acta 2012, 9, 1475-1488.
    • (2012) Biochim. Biophys. Acta , vol.9 , pp. 1475-1488
    • Galea, E.1    Launay, N.2    Portero-Otin, M.3    Ruiz, M.4    Pamplona, R.5    Aubourg, P.6    Ferrer, I.7    Pujol, A.8
  • 131
    • 85114283653 scopus 로고    scopus 로고
    • In vitro effects of N-acetyl-L-cysteine on glutathione and sulfhryl levels in X-linked adrenoleukodystrophy patients
    • Marchetti, D.P.; Donida, B.; Deon, M.; Jacques, C.E.; Jardim, L.B.; Vargas, C.R. In vitro effects of N-acetyl-L-cysteine on glutathione and sulfhryl levels in X-linked adrenoleukodystrophy patients. Clin. Biomed. Res. 2017, 37, 33-37.
    • (2017) Clin. Biomed. Res , vol.37 , pp. 33-37
    • Marchetti, D.P.1    Donida, B.2    Deon, M.3    Jacques, C.E.4    Jardim, L.B.5    Vargas, C.R.6
  • 133
    • 85020196500 scopus 로고    scopus 로고
    • XPG gene polymorphisms and cancer susceptibility: Evidence from 47 studies
    • Huang, J.; Liu, X.; Tang, L.L.; Long, J.T.; Zhu, J.; Hua, R.X.; Li, J. XPG gene polymorphisms and cancer susceptibility: Evidence from 47 studies. Oncotarget 2017, doi:10.18632/oncotarget.16146.
    • (2017) Oncotarget
    • Huang, J.1    Liu, X.2    Tang, L.L.3    Long, J.T.4    Zhu, J.5    Hua, R.X.6    Li, J.7
  • 136
  • 137
  • 138
    • 77955443002 scopus 로고    scopus 로고
    • Melanocytes are deficient in repair of oxidative DNA damage and UV-induced photoproducts
    • Wang, H.T.; Choi, B.; Tang, M.S. Melanocytes are deficient in repair of oxidative DNA damage and UV-induced photoproducts. Proc. Natl. Acad. Sci. USA 2010, 107, 12180-12185.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12180-12185
    • Wang, H.T.1    Choi, B.2    Tang, M.S.3
  • 142
    • 44949263779 scopus 로고    scopus 로고
    • The 8,5′-cyclopurine-2′-deoxynucleosides: Candidate neurodegenerative DNA lesions in xeroderma pigmentosum, and unique probes of transcription and nucleotide excision repair
    • Brooks, P.J. The 8,5′-cyclopurine-2′-deoxynucleosides: Candidate neurodegenerative DNA lesions in xeroderma pigmentosum, and unique probes of transcription and nucleotide excision repair. DNA Repair 2008, 7, 1168-1179.
    • (2008) DNA Repair , vol.7 , pp. 1168-1179
    • Brooks, P.J.1
  • 143
    • 60549092906 scopus 로고    scopus 로고
    • Roles of oxidative stress in xeroderma pigmentosum
    • Hayashi, M.; Ahmad, S.I.; Hanaoka, F. Roles of oxidative stress in xeroderma pigmentosum. Adv. Exp. Med. Biol. 2008, 637, 120-127.
    • (2008) Adv. Exp. Med. Biol , vol.637 , pp. 120-127
    • Hayashi, M.1    Ahmad, S.I.2    Hanaoka, F.3
  • 144
    • 84878537085 scopus 로고    scopus 로고
    • Oxidative DNA damage and nucleotide excision repair
    • Melis, J.P.; van Steeg, H.; Luijten, M. Oxidative DNA damage and nucleotide excision repair. Antioxid. Redox Signal. 2013, 18, 2409-2419.
    • (2013) Antioxid. Redox Signal , vol.18 , pp. 2409-2419
    • Melis, J.P.1    van Steeg, H.2    Luijten, M.3
  • 145
    • 0027370825 scopus 로고
    • Characterization of molecular defects in xeroderma pigmentosum group C
    • Li, L.; Bales, E.S.; Peterson, C.A.; Legerski, R.J. Characterization of molecular defects in xeroderma pigmentosum group C. Nat. Genet. 1993, 5, 413-417.
    • (1993) Nat. Genet , vol.5 , pp. 413-417
    • Li, L.1    Bales, E.S.2    Peterson, C.A.3    Legerski, R.J.4
  • 151
  • 153
    • 0027220259 scopus 로고
    • Enhanced expression of mitochondrial genes in xeroderma pigmentosum fibroblast strains from various complementation groups
    • Rothe, M.; Werner, D.; Thielmann, H.W. Enhanced expression of mitochondrial genes in xeroderma pigmentosum fibroblast strains from various complementation groups. J. Cancer Res. Clin. Oncol. 1993, 119, 675-684.
    • (1993) J. Cancer Res. Clin. Oncol , vol.119 , pp. 675-684
    • Rothe, M.1    Werner, D.2    Thielmann, H.W.3
  • 154
    • 0036657493 scopus 로고    scopus 로고
    • Skin cancer in organ transplant recipients: Epidemiology, pathogenesis and management
    • Berg, D.; Otley, C.C. Skin cancer in organ transplant recipients: Epidemiology, pathogenesis and management. J. Am. Acad. Dermatol. 2002, 47, 1-17.
    • (2002) J. Am. Acad. Dermatol , vol.47 , pp. 1-17
    • Berg, D.1    Otley, C.C.2
  • 156
    • 0031405766 scopus 로고    scopus 로고
    • Retroviral-mediated correction of DNA repair defect in xeroderma pigmentosa cells is associated with recovery of catalase activity
    • Quillet, X.; Chevallier-Lagente, O.; Zeng, L.; Calvayrac, R.; Mezzina, M.; Sarasin, A.; Vuillaume, M. Retroviral-mediated correction of DNA repair defect in xeroderma pigmentosa cells is associated with recovery of catalase activity. Mutat. Res. DNA Repair 1997, 385, 235-242.
    • (1997) Mutat. Res. DNA Repair , vol.385 , pp. 235-242
    • Quillet, X.1    Chevallier-Lagente, O.2    Zeng, L.3    Calvayrac, R.4    Mezzina, M.5    Sarasin, A.6    Vuillaume, M.7
  • 157
    • 0031957207 scopus 로고    scopus 로고
    • Serum concentration of coenzyme Q in xeroderma pigmentosum
    • Taneka, J.; Nagai, T.; Okada, S. Serum concentration of coenzyme Q in xeroderma pigmentosum. Rinsho Shinkeigaku Clin. Neurol. 1998, 38, 57-59.
    • (1998) Rinsho Shinkeigaku Clin. Neurol , vol.38 , pp. 57-59
    • Taneka, J.1    Nagai, T.2    Okada, S.3
  • 158
    • 85007085361 scopus 로고    scopus 로고
    • Genetic therapy of xeroderma pigmentosa, analysis of strategies and translation
    • Goncalves-Maia, M.; Magnaldo, T. Genetic therapy of xeroderma pigmentosa, analysis of strategies and translation. Exp. Opin. Orphan Drugs 2017, 5, 5-17.
    • (2017) Exp. Opin. Orphan Drugs , vol.5 , pp. 5-17
    • Goncalves-Maia, M.1    Magnaldo, T.2
  • 159
    • 0026710191 scopus 로고
    • Definitions for sepsis and organ failure and guidelines for the use of innovative therapies in sepsis
    • Bone, R.C.; Balk, R.A.; Cerra, F.B.; Dellinger, R.P.; Fein, A.M.; Knaus, W.A.; Schein, R.M.; Sibbald, W.J. Definitions for sepsis and organ failure and guidelines for the use of innovative therapies in sepsis. Chest 1992, 101, 1644-1655.
    • (1992) Chest , vol.101 , pp. 1644-1655
    • Bone, R.C.1    Balk, R.A.2    Cerra, F.B.3    Dellinger, R.P.4    Fein, A.M.5    Knaus, W.A.6    Schein, R.M.7    Sibbald, W.J.8
  • 160
    • 33644874086 scopus 로고    scopus 로고
    • Acute kidney injury, mortality, length of stay, and costs in hospitalized patients
    • Chertow, G.M.; Burdick, E.; Honour, M.; Bonventre, J.V.; Bates, D.W. Acute kidney injury, mortality, length of stay, and costs in hospitalized patients. J. Am. Soc. Nephr. 2005, 16, 3365-3370.
    • (2005) J. Am. Soc. Nephr , vol.16 , pp. 3365-3370
    • Chertow, G.M.1    Burdick, E.2    Honour, M.3    Bonventre, J.V.4    Bates, D.W.5
  • 163
    • 84961289578 scopus 로고    scopus 로고
    • Acute kidney injury in severe sepsis: Pathophysiology, diagnosis, and treatment recommendations
    • Keir, I.; Kellum, J.A. Acute kidney injury in severe sepsis: Pathophysiology, diagnosis, and treatment recommendations. J. Veter. Emerg. Crit. Care 2015, 25, 200-209.
    • (2015) J. Veter. Emerg. Crit. Care , vol.25 , pp. 200-209
    • Keir, I.1    Kellum, J.A.2
  • 164
    • 34748927007 scopus 로고    scopus 로고
    • Mechanisms of sepsis-induced organ dysfunction
    • Abraham, E.; Singer, M. Mechanisms of sepsis-induced organ dysfunction. Crit. Care Med. 2007, 35, 2408-2416.
    • (2007) Crit. Care Med , vol.35 , pp. 2408-2416
    • Abraham, E.1    Singer, M.2
  • 165
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through
    • Martin, G.S.; Mannino, D.M.; Eaton, S.; Moss, M. The epidemiology of sepsis in the United States from 1979 through 2000. N. Engl. J. Med. 2000, 348, 1546-1554.
    • (2000) N. Engl. J. Med , vol.2000 , Issue.348 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3    Moss, M.4
  • 168
    • 78049351929 scopus 로고    scopus 로고
    • Long-term cognitive impairment and functional disability among survivors of severe sepsis
    • Iwashyna, T.J.; Ely, E.W.; Smith, D.M.; Langa, K.M. Long-term cognitive impairment and functional disability among survivors of severe sepsis. JAMA 2010, 304, 1787-1794.
    • (2010) JAMA , vol.304 , pp. 1787-1794
    • Iwashyna, T.J.1    Ely, E.W.2    Smith, D.M.3    Langa, K.M.4
  • 169
    • 0035083570 scopus 로고    scopus 로고
    • Different sensitivity of a rabbit heart and skeletal muscle to endotoxin-induced impairment of mitochondrial function
    • Trumbeckaite, S.; Opalka, J.R.; Neuhof, C.; Zierz, S.; Gellerich, F.N. Different sensitivity of a rabbit heart and skeletal muscle to endotoxin-induced impairment of mitochondrial function. Eur. J. Biochem. 2001, 268, 1422-1429.
    • (2001) Eur. J. Biochem , vol.268 , pp. 1422-1429
    • Trumbeckaite, S.1    Opalka, J.R.2    Neuhof, C.3    Zierz, S.4    Gellerich, F.N.5
  • 170
    • 0036100141 scopus 로고    scopus 로고
    • Myocardial dysfunction in sepsis: No role for NO
    • Belcher, E.; Mitchell, J.; Evans, T. Myocardial dysfunction in sepsis: No role for NO. Heart 2000, 87, 507-509.
    • (2000) Heart , vol.87 , pp. 507-509
    • Belcher, E.1    Mitchell, J.2    Evans, T.3
  • 171
    • 84891655634 scopus 로고    scopus 로고
    • The role of mitochondrial dysfunction in sepsis-induced multi-organ failure
    • Singer, M. The role of mitochondrial dysfunction in sepsis-induced multi-organ failure. Landes Biosci. 2014, 5, 66-72.
    • (2014) Landes Biosci , vol.5 , pp. 66-72
    • Singer, M.1
  • 172
    • 84905872645 scopus 로고    scopus 로고
    • Evidence of oxidative stress and mitochondrial respiratory chain dysfunction in an in vitro model of sepsis-induced kidney injury
    • Quoilin, C.; Mouithys-Mickalad, A.; Lecart, S.; Fontaine-Aupart, M.P.; Hoebeke, M. Evidence of oxidative stress and mitochondrial respiratory chain dysfunction in an in vitro model of sepsis-induced kidney injury. Biochim. Biophys. Acta Bioenerg. 2014, 1837, 1790-1800.
    • (2014) Biochim. Biophys. Acta Bioenerg , vol.1837 , pp. 1790-1800
    • Quoilin, C.1    Mouithys-Mickalad, A.2    Lecart, S.3    Fontaine-Aupart, M.P.4    Hoebeke, M.5
  • 173
    • 0036513249 scopus 로고    scopus 로고
    • Does nitric oxide modulate mitochondrial energy generation and apoptosis
    • Moncada, S.; Erusalimsky, J.D. Does nitric oxide modulate mitochondrial energy generation and apoptosis? Nat. Rev. Mol. Cell Biol. 2002, 3, 214-220.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 214-220
    • Moncada, S.1    Erusalimsky, J.D.2
  • 176
    • 20444473456 scopus 로고    scopus 로고
    • Protective effect of β-glucan against oxidative organ injury in a rat model of sepsis
    • Sener, G.; Toklu, H.; Ercan, F.; Erkanli, G. Protective effect of β-glucan against oxidative organ injury in a rat model of sepsis. Int. Immunopharmacol. 2005, 5, 1387-1396.
    • (2005) Int. Immunopharmacol , vol.5 , pp. 1387-1396
    • Sener, G.1    Toklu, H.2    Ercan, F.3    Erkanli, G.4
  • 177
    • 33644885245 scopus 로고    scopus 로고
    • Vitamins C and E protect hepatic cytochrome P450 dysfunction induced by polymicrobial sepsis
    • Kim, J-Y.; Lee, S-M. Vitamins C and E protect hepatic cytochrome P450 dysfunction induced by polymicrobial sepsis. Eur. J. Pharmacol. 2006, 534, 202-209.
    • (2006) Eur. J. Pharmacol , vol.534 , pp. 202-209
    • Kim, J.-Y.1    Lee, S.-M.2
  • 178
    • 33846587450 scopus 로고    scopus 로고
    • Shenkin, A. Effect of selenium supplementation on biochemical markers and outcome in critically ill patients
    • Mishra, V.; Baines, M.; Perry, S.E.; McLaughlin, P.J.; Carson, J.; Wenstone, R.; Shenkin, A. Effect of selenium supplementation on biochemical markers and outcome in critically ill patients. Clin. Nutr. 2007, 26, 41-50.
    • (2007) Clin. Nutr , vol.26 , pp. 41-50
    • Mishra, V.1    Baines, M.2    Perry, S.E.3    McLaughlin, P.J.4    Carson, J.5    Wenstone, R.6
  • 179
    • 33845954738 scopus 로고    scopus 로고
    • Selenium in intensive care (SIC): Results of a prospective randomized, placebo-controlled, multiple-centre study in patients with severe systemic inflammatory response syndrome, sepsis and septic shock
    • Angstwurm, M.W.; Engelman, L.; Zimmermann, T.; Lehmann, C.; Spes, C.H.; Abel, P.; Strau, R.; Meier-Hellmann, A.; Insel, R.; Radke, J. et al. Selenium in intensive care (SIC): Results of a prospective randomized, placebo-controlled, multiple-centre study in patients with severe systemic inflammatory response syndrome, sepsis and septic shock. Crit. Care Med. 2007, 35, 118-126.
    • (2007) Crit. Care Med , vol.35 , pp. 118-126
    • Angstwurm, M.W.1    Engelman, L.2    Zimmermann, T.3    Lehmann, C.4    Spes, C.H.5    Abel, P.6    Strau, R.7    Meier-Hellmann, A.8    Insel, R.9    Radke, J.10
  • 180
    • 79959412738 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in sepsis
    • Galley, H.F. Oxidative stress and mitochondrial dysfunction in sepsis. Brit. J. Anaesth. 2011, 107, 57-64.
    • (2011) Brit. J. Anaesth , vol.107 , pp. 57-64
    • Galley, H.F.1
  • 182
    • 0027534583 scopus 로고
    • Modulation of membrane phospholipid fatty acid composition and food restriction
    • Laganiere, S.; Yu, B.P. Modulation of membrane phospholipid fatty acid composition and food restriction. Gerontology 1993, 39, 7-18.
    • (1993) Gerontology , vol.39 , pp. 7-18
    • Laganiere, S.1    Yu, B.P.2
  • 183
    • 0142028110 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and mitochondrial DNA
    • Kang, D.; Hamasaki, N. Mitochondrial oxidative stress and mitochondrial DNA. Clin. Chem. Lab. Med. 2003, 41, 1281-1288.
    • (2003) Clin. Chem. Lab. Med , vol.41 , pp. 1281-1288
    • Kang, D.1    Hamasaki, N.2
  • 184
    • 34248653209 scopus 로고    scopus 로고
    • Inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: Implications for the pathogenesis and treatment of mitochondrial encephalomyopathies
    • Hargreaves, I.P.; Duncan, A.J.; Wu, L.; Agrawal, A.; Land, J.M.; Heales, S.J. Inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: Implications for the pathogenesis and treatment of mitochondrial encephalomyopathies. Mitochondrion 2007, 7, 284-287.
    • (2007) Mitochondrion , vol.7 , pp. 284-287
    • Hargreaves, I.P.1    Duncan, A.J.2    Wu, L.3    Agrawal, A.4    Land, J.M.5    Heales, S.J.6
  • 185
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher, P.; Beckman, J.S.; Liaudet, L. Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 2007, 87, 315-424.
    • (2007) Physiol. Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 188
    • 85028346703 scopus 로고    scopus 로고
    • Glutathione as a Redox Biomarker in Mitochondrial Disease-Implications for Therapy
    • Enns, G.M.; Cowan, T.M. Glutathione as a Redox Biomarker in Mitochondrial Disease-Implications for Therapy. J. Clin. Med. 2017, doi:10.3390/jcm6050050.
    • (2017) J. Clin. Me
    • Enns, G.M.1    Cowan, T.M.2
  • 190
    • 84964999321 scopus 로고    scopus 로고
    • NrF2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration
    • Homstrom, K.H.; Baird, L.; Zhang, Y.; Hargreaves, I.; Chalasani, A.; Land, J.M.; Abramov, A.Y. NrF2 impacts cellular bioenergetics by controlling substrate availability for mitochondrial respiration. Biol Open 2013, 2, 761-770.
    • (2013) Biol Open , vol.2 , pp. 761-770
    • Homstrom, K.H.1    Baird, L.2    Zhang, Y.3    Hargreaves, I.4    Chalasani, A.5    Land, J.M.6    Abramov, A.Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.