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Volumn 352, Issue 2, 2007, Pages 556-559

Ablation of the mammalian methionine sulfoxide reductase A affects the expression level of cysteine deoxygenase

Author keywords

Cysteine deoxygenase; Oxidative stress; Post translation modification; Sulfur amino acids; Thiol groups

Indexed keywords

CYSTEINE DEOXYGENASE; ENZYME; METHIONINE SULFOXIDE REDUCTASE; METHIONINE SULFOXIDE REDUCTASE A; SELENIUM;

EID: 33751545962     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.11.063     Document Type: Article
Times cited : (9)

References (19)
  • 1
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • Moskovitz J. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim. Biophys. Acta 1703 (2005) 213-219
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 213-219
    • Moskovitz, J.1
  • 2
    • 0036297758 scopus 로고    scopus 로고
    • Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
    • Moskovitz J., Singh V.K., Requena J., Wilkinson B.J., Jayaswal R.K., and Stadtman E.R. Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity. Biochem. Biophys. Res. Commun. 290 (2002) 62-65
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 62-65
    • Moskovitz, J.1    Singh, V.K.2    Requena, J.3    Wilkinson, B.J.4    Jayaswal, R.K.5    Stadtman, E.R.6
  • 3
    • 0034640506 scopus 로고    scopus 로고
    • Identification and characterization of a putative active site for peptide-methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
    • Moskovitz J., Poston J.M., Berlett B.S., Nosworthy J.N., Szczepanowski R., and Stadtman E.R. Identification and characterization of a putative active site for peptide-methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J. Biol. Chem. 275 (2000) 14167-14172
    • (2000) J. Biol. Chem. , vol.275 , pp. 14167-14172
    • Moskovitz, J.1    Poston, J.M.2    Berlett, B.S.3    Nosworthy, J.N.4    Szczepanowski, R.5    Stadtman, E.R.6
  • 4
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage
    • Moskovitz J., Rahman M.A., Strassman J., Yancey S.O., Kushner S.R., Brot N., and Weissbach H. Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J. Bacteriol. 177 (1995) 502-507
    • (1995) J. Bacteriol. , vol.177 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5    Brot, N.6    Weissbach, H.7
  • 5
    • 0030955353 scopus 로고    scopus 로고
    • The yeast peptide- methionine sulfoxide reductase functions as an antioxidant in-vivo
    • Moskovitz J., Berlett B.S., Poston M.J., and Stadtman E.R. The yeast peptide- methionine sulfoxide reductase functions as an antioxidant in-vivo. Proc. Natl. Acad. Sci. USA 94 (1997) 9585-9589
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9585-9589
    • Moskovitz, J.1    Berlett, B.S.2    Poston, M.J.3    Stadtman, E.R.4
  • 7
    • 33646807833 scopus 로고    scopus 로고
    • Mammalian cysteine metabolism: new insights into regulation of cysteinemetabolism
    • Stipanuk M.H., Dominy Jr. J.E., Lee J.I., and Coloso R.M. Mammalian cysteine metabolism: new insights into regulation of cysteinemetabolism. J. Nutr. 136 (2006) 1652S-1659S
    • (2006) J. Nutr. , vol.136
    • Stipanuk, M.H.1    Dominy Jr., J.E.2    Lee, J.I.3    Coloso, R.M.4
  • 8
    • 33745854127 scopus 로고    scopus 로고
    • Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation
    • Simmons C.R., Liu Q., Huang Q., Hao Q., Begley T.P., Karplus P.A., and Stipanuk M.H. Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation. J. Biol. Chem. 281 (2006) 18723-18733
    • (2006) J. Biol. Chem. , vol.281 , pp. 18723-18733
    • Simmons, C.R.1    Liu, Q.2    Huang, Q.3    Hao, Q.4    Begley, T.P.5    Karplus, P.A.6    Stipanuk, M.H.7
  • 9
    • 15444380484 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of recombinant rat cysteine dioxygenase
    • Chai S.C., Jerkins A.A., Banik J.J., Shalev I., Pinkham J.L., Uden P.C., and Maroney M.J. Heterologous expression, purification, and characterization of recombinant rat cysteine dioxygenase. J. Biol. Chem. 280 (2005) 9865-9869
    • (2005) J. Biol. Chem. , vol.280 , pp. 9865-9869
    • Chai, S.C.1    Jerkins, A.A.2    Banik, J.J.3    Shalev, I.4    Pinkham, J.L.5    Uden, P.C.6    Maroney, M.J.7
  • 10
    • 0034584219 scopus 로고    scopus 로고
    • Expanding the circle 1975-1999: sulfur biochemistry and insights on the biological functions of taurine
    • Huxtable R.J. Expanding the circle 1975-1999: sulfur biochemistry and insights on the biological functions of taurine. Adv. Exp. Med. Biol. 483 (2000) 1-25
    • (2000) Adv. Exp. Med. Biol. , vol.483 , pp. 1-25
    • Huxtable, R.J.1
  • 11
    • 0030329438 scopus 로고    scopus 로고
    • Electrophysiological and electropharmological actions of taurine on cardiac cells
    • Satoh H. Electrophysiological and electropharmological actions of taurine on cardiac cells. Adv. Exp. Med. Biol. 403 (1996) 285-296
    • (1996) Adv. Exp. Med. Biol. , vol.403 , pp. 285-296
    • Satoh, H.1
  • 12
    • 0029906486 scopus 로고    scopus 로고
    • Taurine and neural cell damage. Transport of taurine in adult and developing mice
    • Saransarri P., and Oja S.S. Taurine and neural cell damage. Transport of taurine in adult and developing mice. Adv. Exp. Med. Biol. 403 (1996) 481-490
    • (1996) Adv. Exp. Med. Biol. , vol.403 , pp. 481-490
    • Saransarri, P.1    Oja, S.S.2
  • 13
    • 0025299455 scopus 로고
    • l-Cysteine, a bicarbonate- sensitive endogenous excitotoxin
    • Olney J.W., Zorumski C., Price M.T., and Labruyere J. l-Cysteine, a bicarbonate- sensitive endogenous excitotoxin. Science 248 (1990) 596-599
    • (1990) Science , vol.248 , pp. 596-599
    • Olney, J.W.1    Zorumski, C.2    Price, M.T.3    Labruyere, J.4
  • 14
    • 0031056511 scopus 로고    scopus 로고
    • Oxidation of dopamine in the presence of cysteine: characterization of new toxic products
    • Shen X.M., Zhang F., and Dryhurst G. Oxidation of dopamine in the presence of cysteine: characterization of new toxic products. Chem. Res. Toxicol. 10 (1997) 147-155
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 147-155
    • Shen, X.M.1    Zhang, F.2    Dryhurst, G.3
  • 15
    • 0027166220 scopus 로고
    • An amplified assay for thiols based on reactivation of papain
    • Singh R., Blattler W.A., and Collinson A.R. An amplified assay for thiols based on reactivation of papain. Anal. Biochem. 213 (1993) 49-56
    • (1993) Anal. Biochem. , vol.213 , pp. 49-56
    • Singh, R.1    Blattler, W.A.2    Collinson, A.R.3
  • 16
    • 0029935647 scopus 로고    scopus 로고
    • Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins
    • Moskovitz J., Wiessbach H., and Brot N. Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins. Proc. Natl. Acad. Sci. USA 93 (1996) 2095-2099
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2095-2099
    • Moskovitz, J.1    Wiessbach, H.2    Brot, N.3
  • 17
    • 33751513448 scopus 로고    scopus 로고
    • J. Moskovitz, Prolonged selenium deficient diet in MsrA knockout mice causes enhanced oxidative stress modification to proteins and affects the levels of antioxidant enzymes in a tissue-specific manner, Free Radic. Res., in-press.
  • 18
    • 32944454336 scopus 로고    scopus 로고
    • Regulation of cysteine dioxygenase degradation is mediated by intracellular cysteine levels and the ubiquitin-26S proteasome system in the living rat
    • Dominy Jr. J.E., Hirschberger L.L., Coloso R.M., and Stipanuk M.H. Regulation of cysteine dioxygenase degradation is mediated by intracellular cysteine levels and the ubiquitin-26S proteasome system in the living rat. Biochem. J. 394 (2006) 267-273
    • (2006) Biochem. J. , vol.394 , pp. 267-273
    • Dominy Jr., J.E.1    Hirschberger, L.L.2    Coloso, R.M.3    Stipanuk, M.H.4
  • 19
    • 0029912239 scopus 로고    scopus 로고
    • Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues
    • Moskovitz J., Jenkins N.A., Gilbert D.J., Coplend N.G., Jursky F., Weissbach H., and Brot N. Chromosomal localization of the mammalian peptide-methionine sulfoxide reductase gene and its differential expression in various tissues. Proc. Natl. Acad. Sci. USA 93 (1996) 3205-3208
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3205-3208
    • Moskovitz, J.1    Jenkins, N.A.2    Gilbert, D.J.3    Coplend, N.G.4    Jursky, F.5    Weissbach, H.6    Brot, N.7


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