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Volumn 60, Issue , 2013, Pages 38-44

Glutathione defense mechanism in liver injury: Insights from animal models

Author keywords

Glutamate cysteine ligase; Glutathione; Liver injury; Oxidative stress; Steatohepatitis; Steatosis

Indexed keywords

2,3,7,8 TETRACHLORODIBENZO PARA DIOXIN; CHOLINE; GLUTATHIONE; METHIONINE; PARACETAMOL;

EID: 84881527586     PISSN: 02786915     EISSN: 18736351     Source Type: Journal    
DOI: 10.1016/j.fct.2013.07.008     Document Type: Review
Times cited : (208)

References (70)
  • 1
    • 84875550946 scopus 로고    scopus 로고
    • Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury
    • Abdelmegeed M.A., Jang S., Banerjee A., Hardwick J.P., Song B.J. Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury. Free Radic. Biol.Med. 2013, 60:211-222.
    • (2013) Free Radic. Biol.Med. , vol.60 , pp. 211-222
    • Abdelmegeed, M.A.1    Jang, S.2    Banerjee, A.3    Hardwick, J.P.4    Song, B.J.5
  • 2
    • 39749090649 scopus 로고    scopus 로고
    • Oxidative mechanisms in the pathogenesis of alcoholic liver disease
    • Albano E. Oxidative mechanisms in the pathogenesis of alcoholic liver disease. Mol. Aspects Med. 2008, 29:9-16.
    • (2008) Mol. Aspects Med. , vol.29 , pp. 9-16
    • Albano, E.1
  • 3
    • 0034489653 scopus 로고    scopus 로고
    • The glutathione peroxidases
    • Arthur J.R. The glutathione peroxidases. Cell Mol. Life Sci. 2000, 57:1825-1835.
    • (2000) Cell Mol. Life Sci. , vol.57 , pp. 1825-1835
    • Arthur, J.R.1
  • 4
    • 0022969399 scopus 로고
    • Exchange of cystine and glutamate across plasma membrane of human fibroblasts
    • Bannai S. Exchange of cystine and glutamate across plasma membrane of human fibroblasts. J. Biol. Chem. 1986, 261:2256-2263.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2256-2263
    • Bannai, S.1
  • 5
    • 56049125741 scopus 로고    scopus 로고
    • Genetic variation and gene expression in antioxidant related enzymes and risk of COPD: a systematic review
    • Bentley A.R., Emrani P., Cassano P.A. Genetic variation and gene expression in antioxidant related enzymes and risk of COPD: a systematic review. Thorax 2008, 63:956-961.
    • (2008) Thorax , vol.63 , pp. 956-961
    • Bentley, A.R.1    Emrani, P.2    Cassano, P.A.3
  • 7
    • 0032879826 scopus 로고    scopus 로고
    • The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency
    • Beutler E., Gelbart T., Kondo T., Matsunaga A.T. The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood 1999, 94:2890-2894.
    • (1999) Blood , vol.94 , pp. 2890-2894
    • Beutler, E.1    Gelbart, T.2    Kondo, T.3    Matsunaga, A.T.4
  • 8
    • 79551504926 scopus 로고    scopus 로고
    • Interaction of GAG trinucleotide repeat and C-129T polymorphisms impairs expression of the glutamate-cysteine ligase catalytic subunit gene
    • Butticaz C., Gysin R., Cuenod M., Do K.Q. Interaction of GAG trinucleotide repeat and C-129T polymorphisms impairs expression of the glutamate-cysteine ligase catalytic subunit gene. Free Radic. Biol.Med. 2011, 50:617-623.
    • (2011) Free Radic. Biol.Med. , vol.50 , pp. 617-623
    • Butticaz, C.1    Gysin, R.2    Cuenod, M.3    Do, K.Q.4
  • 9
    • 26644449682 scopus 로고    scopus 로고
    • Glutamate cysteine ligase catalysis: dependence on ATP and modifier subunit for regulation of tissue glutathione levels
    • Chen Y., Shertzer H.G., Schneider S.N., Nebert D.W., Dalton T.P. Glutamate cysteine ligase catalysis: dependence on ATP and modifier subunit for regulation of tissue glutathione levels. J. Biol.Chem. 2005, 280:33766-33774.
    • (2005) J. Biol.Chem. , vol.280 , pp. 33766-33774
    • Chen, Y.1    Shertzer, H.G.2    Schneider, S.N.3    Nebert, D.W.4    Dalton, T.P.5
  • 13
    • 84862910264 scopus 로고    scopus 로고
    • Glutathione-deficient mice are susceptible to TCDD-induced hepatocellular toxicity but resistant to steatosis
    • Chen Y., Krishan M., Nebert D.W., Shertzer H.G. Glutathione-deficient mice are susceptible to TCDD-induced hepatocellular toxicity but resistant to steatosis. Chem. Res. Toxicol. 2012, 25:94-100.
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 94-100
    • Chen, Y.1    Krishan, M.2    Nebert, D.W.3    Shertzer, H.G.4
  • 16
    • 0034694871 scopus 로고    scopus 로고
    • Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous
    • Dalton T.P., Dieter M.Z., Yang Y., Shertzer H.G., Nebert D.W. Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous. Biochem. Biophys. Res.Commun. 2000, 279:324-329.
    • (2000) Biochem. Biophys. Res.Commun. , vol.279 , pp. 324-329
    • Dalton, T.P.1    Dieter, M.Z.2    Yang, Y.3    Shertzer, H.G.4    Nebert, D.W.5
  • 18
    • 0035035655 scopus 로고    scopus 로고
    • Detoxification of reactive oxygen species by anonpeptidyl mimic of superoxide dismutase cures acetaminophen-induced acute liver failure in the mouse
    • Ferret P.J., Hammoud R., Tulliez M., Tran A., Trebeden H., Jaffray P., Malassagne B., Calmus Y., Weill B., Batteux F. Detoxification of reactive oxygen species by anonpeptidyl mimic of superoxide dismutase cures acetaminophen-induced acute liver failure in the mouse. Hepatology 2001, 33:1173-1180.
    • (2001) Hepatology , vol.33 , pp. 1173-1180
    • Ferret, P.J.1    Hammoud, R.2    Tulliez, M.3    Tran, A.4    Trebeden, H.5    Jaffray, P.6    Malassagne, B.7    Calmus, Y.8    Weill, B.9    Batteux, F.10
  • 19
    • 0028229899 scopus 로고
    • Effect of chronic ethanol feeding on glutathione and functional integrity of mitochondria in periportal and perivenous rat hepatocytes
    • Garcia-Ruiz C., Morales A., Ballesta A., Rodes J., Kaplowitz N., Fernandez-Checa J.C. Effect of chronic ethanol feeding on glutathione and functional integrity of mitochondria in periportal and perivenous rat hepatocytes. J. Clin.Invest. 1994, 94:193-201.
    • (1994) J. Clin.Invest. , vol.94 , pp. 193-201
    • Garcia-Ruiz, C.1    Morales, A.2    Ballesta, A.3    Rodes, J.4    Kaplowitz, N.5    Fernandez-Checa, J.C.6
  • 20
    • 33750622197 scopus 로고    scopus 로고
    • Subcellular compartmentalization of glutathione: correlations with parameters of oxidative stress related togenotoxicity
    • Green R.M., Graham M., O'Donovan M.R., Chipman J.K., Hodges N.J. Subcellular compartmentalization of glutathione: correlations with parameters of oxidative stress related togenotoxicity. Mutagenesis 2006, 21:383-390.
    • (2006) Mutagenesis , vol.21 , pp. 383-390
    • Green, R.M.1    Graham, M.2    O'Donovan, M.R.3    Chipman, J.K.4    Hodges, N.J.5
  • 21
    • 0001547757 scopus 로고
    • Origin and turnover of mitochondrial glutathione
    • Griffith O.W., Meister A. Origin and turnover of mitochondrial glutathione. Proc. Natl. Acad. Sci. USA 1985, 82:4668-4672.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4668-4672
    • Griffith, O.W.1    Meister, A.2
  • 23
    • 0037818355 scopus 로고    scopus 로고
    • A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathioneproduction
    • Hamilton D., Wu J.H., Alaoui-Jamali M., Batist G. A novel missense mutation in the gamma-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathioneproduction. Blood 2003, 102:725-730.
    • (2003) Blood , vol.102 , pp. 725-730
    • Hamilton, D.1    Wu, J.H.2    Alaoui-Jamali, M.3    Batist, G.4
  • 25
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N. The biochemistry and physiology of S-nitrosothiols. Annu. Rev. Pharmacol. Toxicol. 2002, 42:585-600.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 585-600
    • Hogg, N.1
  • 26
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A.J., Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992, 257:1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 27
    • 79954615800 scopus 로고    scopus 로고
    • Current issues with acetaminophen hepatotoxicity-a clinically relevant model to test the efficacy of natural products
    • Jaeschke H., McGill M.R., Williams C.D., Ramachandran A. Current issues with acetaminophen hepatotoxicity-a clinically relevant model to test the efficacy of natural products. Life Sci. 2011, 88:737-745.
    • (2011) Life Sci. , vol.88 , pp. 737-745
    • Jaeschke, H.1    McGill, M.R.2    Williams, C.D.3    Ramachandran, A.4
  • 30
    • 0037454012 scopus 로고    scopus 로고
    • Association of polymorphism in glutamate-cysteine ligase catalytic subunit gene with coronary vasomotor dysfunction and myocardialinfarction
    • Koide S., Kugiyama K., Sugiyama S., Nakamura S., Fukushima H., Honda O., Yoshimura M., Ogawa H. Association of polymorphism in glutamate-cysteine ligase catalytic subunit gene with coronary vasomotor dysfunction and myocardialinfarction. J. Am. Coll. Cardiol. 2003, 41:539-545.
    • (2003) J. Am. Coll. Cardiol. , vol.41 , pp. 539-545
    • Koide, S.1    Kugiyama, K.2    Sugiyama, S.3    Nakamura, S.4    Fukushima, H.5    Honda, O.6    Yoshimura, M.7    Ogawa, H.8
  • 31
    • 0029841209 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione metabolism and its role in hepatotoxicity
    • Kretzschmar M. Regulation of hepatic glutathione metabolism and its role in hepatotoxicity. Exp. Toxicol. Pathol. 1996, 48:439-446.
    • (1996) Exp. Toxicol. Pathol. , vol.48 , pp. 439-446
    • Kretzschmar, M.1
  • 34
    • 0033067354 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis: current concepts and controversies
    • Lu S.C. Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J. 1999, 13:1169-1183.
    • (1999) FASEB J. , vol.13 , pp. 1169-1183
    • Lu, S.C.1
  • 35
    • 0018470912 scopus 로고
    • Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase
    • Luthman M., Eriksson S., Holmgren A., Thelander L. Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase. Proc. Natl. Acad. Sci. USA 1979, 76:2158-2162.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2158-2162
    • Luthman, M.1    Eriksson, S.2    Holmgren, A.3    Thelander, L.4
  • 40
    • 0020122527 scopus 로고
    • Metabolism and function of glutathione: an overview
    • Meister A. Metabolism and function of glutathione: an overview. Biochem. Soc. Trans. 1982, 10:78-79.
    • (1982) Biochem. Soc. Trans. , vol.10 , pp. 78-79
    • Meister, A.1
  • 41
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 1988, 263:17205-17208.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 42
    • 0026343403 scopus 로고
    • Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy
    • Meister A. Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy. Pharmacol. Ther. 1991, 51:155-194.
    • (1991) Pharmacol. Ther. , vol.51 , pp. 155-194
    • Meister, A.1
  • 44
    • 0037172653 scopus 로고    scopus 로고
    • Polymorphism in the 5'-flanking region ofhuman glutamate-cysteine ligase modifier subunit gene is associated with myocardial infarction
    • Nakamura S., Kugiyama K., Sugiyama S., Miyamoto S., Koide S., Fukushima H., Honda O., Yoshimura M., Ogawa H. Polymorphism in the 5'-flanking region ofhuman glutamate-cysteine ligase modifier subunit gene is associated with myocardial infarction. Circulation 2002, 105:2968-2973.
    • (2002) Circulation , vol.105 , pp. 2968-2973
    • Nakamura, S.1    Kugiyama, K.2    Sugiyama, S.3    Miyamoto, S.4    Koide, S.5    Fukushima, H.6    Honda, O.7    Yoshimura, M.8    Ogawa, H.9
  • 45
    • 0141615873 scopus 로고    scopus 로고
    • Polymorphism in glutamate-cysteine ligase modifier subunit gene is associated with impairment of nitric oxide-mediated coronary vasomotorfunction
    • Nakamura S., Sugiyama S., Fujioka D., Kawabata K., Ogawa H., Kugiyama K. Polymorphism in glutamate-cysteine ligase modifier subunit gene is associated with impairment of nitric oxide-mediated coronary vasomotorfunction. Circulation 2003, 108:1425-1427.
    • (2003) Circulation , vol.108 , pp. 1425-1427
    • Nakamura, S.1    Sugiyama, S.2    Fujioka, D.3    Kawabata, K.4    Ogawa, H.5    Kugiyama, K.6
  • 46
    • 0027922810 scopus 로고
    • Role of the Ah receptor and the dioxin-inducible [Ah] gene battery in toxicity, cancer, and signal transduction
    • Nebert D.W., Puga A., Vasiliou V. Role of the Ah receptor and the dioxin-inducible [Ah] gene battery in toxicity, cancer, and signal transduction. Ann. N.Y. Acad. Sci. 1993, 685:624-640.
    • (1993) Ann. N.Y. Acad. Sci. , vol.685 , pp. 624-640
    • Nebert, D.W.1    Puga, A.2    Vasiliou, V.3
  • 47
    • 79960184881 scopus 로고    scopus 로고
    • A GAG trinucleotide-repeat polymorphism in the gene for glutathione biosynthetic enzyme, GCLC, affects gene expression through translation
    • Nichenametla S.N., Lazarus P., Richie J.P. A GAG trinucleotide-repeat polymorphism in the gene for glutathione biosynthetic enzyme, GCLC, affects gene expression through translation. FASEB J. 2011, 25:2180-2187.
    • (2011) FASEB J. , vol.25 , pp. 2180-2187
    • Nichenametla, S.N.1    Lazarus, P.2    Richie, J.P.3
  • 48
    • 84884818409 scopus 로고    scopus 로고
    • A functional trinucleotide repeat polymorphism in the 5'-untranslated region of the glutathione biosynthetic gene GCLC is associated with increased risk for lung and aerodigestive tract cancers
    • May 18. [Epub ahead of print]
    • Nichenametla S.N., Muscat J.E., Liao J.G., Lazarus P., Richie J.P. A functional trinucleotide repeat polymorphism in the 5'-untranslated region of the glutathione biosynthetic gene GCLC is associated with increased risk for lung and aerodigestive tract cancers. Mol.Carcinogen. 2012, May 18. [Epub ahead of print].
    • (2012) Mol.Carcinogen.
    • Nichenametla, S.N.1    Muscat, J.E.2    Liao, J.G.3    Lazarus, P.4    Richie, J.P.5
  • 49
    • 14844313300 scopus 로고    scopus 로고
    • Physiological and pathological aspects of GSH metabolism
    • Njalsson R., Norgren S. Physiological and pathological aspects of GSH metabolism. Acta Paediatr. 2005, 94:132-137.
    • (2005) Acta Paediatr. , vol.94 , pp. 132-137
    • Njalsson, R.1    Norgren, S.2
  • 50
    • 19044381583 scopus 로고    scopus 로고
    • Post-translational disulfide modifications in cell signaling-role of inter-protein, intra-protein, S-glutathionyl, and S-cysteaminyl disulfide modifications in signal transmission
    • O'Brian C.A., Chu F. Post-translational disulfide modifications in cell signaling-role of inter-protein, intra-protein, S-glutathionyl, and S-cysteaminyl disulfide modifications in signal transmission. Free Radic. Res. 2005, 39:471-480.
    • (2005) Free Radic. Res. , vol.39 , pp. 471-480
    • O'Brian, C.A.1    Chu, F.2
  • 51
    • 0036080591 scopus 로고    scopus 로고
    • Nonalcoholic steatosis and steatohepatitis. V. Mitochondrial dysfunction in steatohepatitis
    • Pessayre D., Mansouri A., Fromenty B. Nonalcoholic steatosis and steatohepatitis. V. Mitochondrial dysfunction in steatohepatitis. Am. J. Phys. Gastrointest. Liver Phys. 2002, 282:G193-G199.
    • (2002) Am. J. Phys. Gastrointest. Liver Phys. , vol.282
    • Pessayre, D.1    Mansouri, A.2    Fromenty, B.3
  • 55
    • 0016635533 scopus 로고
    • Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione
    • Richman P.G., Meister A. Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione. J. Biol. Chem. 1975, 250:1422-1426.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1422-1426
    • Richman, P.G.1    Meister, A.2
  • 56
    • 0036785479 scopus 로고    scopus 로고
    • Reactive intermediates and the dynamics of glutathione transferases
    • Rinaldi R., Eliasson E., Swedmark S., Morgenstern R. Reactive intermediates and the dynamics of glutathione transferases. Drug Metab Dispos. 2002, 30:1053-1058.
    • (2002) Drug Metab Dispos. , vol.30 , pp. 1053-1058
    • Rinaldi, R.1    Eliasson, E.2    Swedmark, S.3    Morgenstern, R.4
  • 57
    • 50049097587 scopus 로고    scopus 로고
    • Mechanisms of hepatic steatosis in mice fed a lipogenic methionine choline-deficient diet
    • Rinella M.E., Elias M.S., Smolak R.R., Fu T., Borensztajn J., Green R.M. Mechanisms of hepatic steatosis in mice fed a lipogenic methionine choline-deficient diet. J. LipidRes. 2008, 49:1068-1076.
    • (2008) J. LipidRes. , vol.49 , pp. 1068-1076
    • Rinella, M.E.1    Elias, M.S.2    Smolak, R.R.3    Fu, T.4    Borensztajn, J.5    Green, R.M.6
  • 58
    • 4244167028 scopus 로고    scopus 로고
    • Patients with genetic defects in the gamma-glutamyl cycle
    • Ristoff E., Larsson A. Patients with genetic defects in the gamma-glutamyl cycle. Chem. Biol. Interact. 1998, 111-112:113-121.
    • (1998) Chem. Biol. Interact. , pp. 113-121
    • Ristoff, E.1    Larsson, A.2
  • 60
    • 21844446870 scopus 로고    scopus 로고
    • Glutathione redox state regulates mitochondrial reactive oxygen production
    • Shen D., Dalton T.P., Nebert D.W., Shertzer H.G. Glutathione redox state regulates mitochondrial reactive oxygen production. J. Biol. Chem. 2005, 280:25305-25312.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25305-25312
    • Shen, D.1    Dalton, T.P.2    Nebert, D.W.3    Shertzer, H.G.4
  • 63
    • 0024331933 scopus 로고
    • Metabolism of N-acetyl-L-cysteine. Some structural requirements for the deacetylation and consequences for the oral bioavailability
    • Sjodin K., Nilsson E., Hallberg A., Tunek A. Metabolism of N-acetyl-L-cysteine. Some structural requirements for the deacetylation and consequences for the oral bioavailability. Biochem. Pharmacol. 1989, 38:3981-3985.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 3981-3985
    • Sjodin, K.1    Nilsson, E.2    Hallberg, A.3    Tunek, A.4
  • 64
    • 0029684657 scopus 로고    scopus 로고
    • Nutritional and hormonal regulation of glutathione homeostasis
    • Taylor C.G., Nagy L.E., Bray T.M. Nutritional and hormonal regulation of glutathione homeostasis. Curr. Top. Cell. Regul. 1996, 34:189-208.
    • (1996) Curr. Top. Cell. Regul. , vol.34 , pp. 189-208
    • Taylor, C.G.1    Nagy, L.E.2    Bray, T.M.3
  • 65
    • 72649102227 scopus 로고    scopus 로고
    • Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme
    • Toppo S., Flohe L., Ursini F., Vanin S., Maiorino M. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim. Biophys.Acta 2009, 1790:1486-1500.
    • (2009) Biochim. Biophys.Acta , vol.1790 , pp. 1486-1500
    • Toppo, S.1    Flohe, L.2    Ursini, F.3    Vanin, S.4    Maiorino, M.5
  • 67
    • 34547975404 scopus 로고    scopus 로고
    • Essential pathogenic and metabolic differences in steatosis induced by choline or methione-choline deficient diets in a rat model
    • Vetelainen R., van V.A., van Gulik T.M. Essential pathogenic and metabolic differences in steatosis induced by choline or methione-choline deficient diets in a rat model. J. Gastroenterol. Hepatol. 2007, 22:1526-1533.
    • (2007) J. Gastroenterol. Hepatol. , vol.22 , pp. 1526-1533
    • Vetelainen, R.1    van, V.A.2    van Gulik, T.M.3
  • 69
    • 0037147240 scopus 로고    scopus 로고
    • Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm(-/-) knockout mouse. Novel model system for a severely compromised oxidative stress response
    • Yang Y., Dieter M.Z., Chen Y., Shertzer H.G., Nebert D.W., Dalton T.P. Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm(-/-) knockout mouse. Novel model system for a severely compromised oxidative stress response. J. Biol.Chem. 2002, 277:49446-49452.
    • (2002) J. Biol.Chem. , vol.277 , pp. 49446-49452
    • Yang, Y.1    Dieter, M.Z.2    Chen, Y.3    Shertzer, H.G.4    Nebert, D.W.5    Dalton, T.P.6
  • 70
    • 84859060800 scopus 로고    scopus 로고
    • Gpx4 ablation in adult mice results in a lethal phenotype accompanied by neuronal loss inbrain
    • Yoo S.E., Chen L., Na R., Liu Y., Rios C., Van R.H., Richardson A., Ran Q. Gpx4 ablation in adult mice results in a lethal phenotype accompanied by neuronal loss inbrain. Free Radic. Biol. Med. 2012, 52:1820-1827.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1820-1827
    • Yoo, S.E.1    Chen, L.2    Na, R.3    Liu, Y.4    Rios, C.5    Van, R.H.6    Richardson, A.7    Ran, Q.8


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