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Volumn 65, Issue , 2013, Pages 1126-1133

Mechanism of protein decarbonylation

Author keywords

Carbonylation; Decarbonylation; Free radicals; Oxidant signaling; Oxidative stress; Peroxiredoxin; Protein oxidation; Reactive oxygen species; Redox signaling

Indexed keywords

2,4 DINITROPHENYLHYDRAZINE; 4 HYDROXYNONENAL; CARBONYL DERIVATIVE; CYSTEINE; GLUTAREDOXIN; GLUTATHIONE; MALONALDEHYDE; PEROXIREDOXIN 2; PEROXIREDOXIN 6; SMALL INTERFERING RNA; THIOL;

EID: 84884767245     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.09.005     Document Type: Article
Times cited : (51)

References (29)
  • 2
    • 0020427486 scopus 로고
    • Biology of disease. Free radicals and tissue injury
    • B.A. Freeman, and J.D. Crapo Biology of disease: free radicals and tissue injury Lab. Invest. 47 1982 412 426 (Pubitemid 13229679)
    • (1982) Laboratory Investigation , vol.47 , Issue.5 , pp. 412-426
    • Freeman, B.A.1    Crapo, J.D.2
  • 3
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • DOI 10.1074/jbc.272.33.20313
    • B.S. Berlett, and E.R. Stadtman Protein oxidation in aging, disease, and oxidative stress J. Biol. Chem. 272 1997 20313 20316 (Pubitemid 27355575)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 4
    • 84866042834 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress in the maintenance of myocardial function
    • Y. Zhang, C.G. Tocchetti, T. Krieg, and A.L. Moens Oxidative and nitrosative stress in the maintenance of myocardial function Free Radic. Biol. Med. 53 2012 1531 1540
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1531-1540
    • Zhang, Y.1    Tocchetti, C.G.2    Krieg, T.3    Moens, A.L.4
  • 5
    • 84875228208 scopus 로고    scopus 로고
    • Role of reactive oxygen species-mediated signaling in aging
    • (in press)
    • V.M. Labunskyy, and V.N. Gladyshev Role of reactive oxygen species-mediated signaling in aging Antioxid. Redox Signaling 2012 (in press)
    • (2012) Antioxid. Redox Signaling
    • Labunskyy, V.M.1    Gladyshev, V.N.2
  • 6
    • 33846331650 scopus 로고    scopus 로고
    • Oxidative stress and cancer: Have we moved forward?
    • DOI 10.1042/BJ20061131
    • B. Halliwell Oxidative stress and cancer: have we moved forward? Biochem. J. 401 2007 1 11 (Pubitemid 46115897)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 1-11
    • Halliwell, B.1
  • 7
    • 0029979744 scopus 로고    scopus 로고
    • Oxidants as stimulators of signal transduction
    • DOI 10.1016/S0891-5849(96)00275-4
    • Y.J. Suzuki, H.J. Forman, and A. Sevanian Oxidants as stimulators of signal transduction Free Radic. Biol. Med. 22 1997 269 285 (Pubitemid 26399334)
    • (1996) Free Radical Biology and Medicine , vol.22 , Issue.1-2 , pp. 269-285
    • Suzuki, Y.J.1    Forman, H.J.2    Sevanian, A.3
  • 8
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation
    • S.G. Rhee, Y.S. Bae, S.R. Lee, and J. Kwon Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation Sci. STKE 2000 2000 pe1
    • (2000) Sci. STKE , vol.2000 , pp. 1
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 10
    • 84871309537 scopus 로고    scopus 로고
    • Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation
    • T.H. Truong, and K.S. Carroll Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation Biochemistry 51 2012 9954 9965
    • (2012) Biochemistry , vol.51 , pp. 9954-9965
    • Truong, T.H.1    Carroll, K.S.2
  • 11
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • H.J. Forman, M. Maiorino, and F. Ursini Signaling functions of reactive oxygen species Biochemistry 49 2010 835 842
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 13
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • T. Finkel Signal transduction by reactive oxygen species J. Cell Biol. 194 2011 7 15
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 14
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • DOI 10.1016/S0891-5849(02)00765-7, PII S0891584902007657
    • R.L. Levine Carbonyl modified proteins in cellular regulation, aging, and disease Free Radic. Biol. Med. 32 2002 790 796 (Pubitemid 34439249)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 790-796
    • Levine, R.L.1
  • 17
    • 84866862372 scopus 로고    scopus 로고
    • Sultana, R. Redox proteomics in selected neurodegenerative disorders: From its infancy to future applications
    • D.A. Butterfield, M. Perluigi, T. Reed, T. Muharib, C.P. Hughes, and R.A. Robinson Sultana, R. Redox proteomics in selected neurodegenerative disorders: from its infancy to future applications Antioxid. Redox Signaling 17 2012 1610 1655
    • (2012) Antioxid. Redox Signaling , vol.17 , pp. 1610-1655
    • Butterfield, D.A.1    Perluigi, M.2    Reed, T.3    Muharib, T.4    Hughes, C.P.5    Robinson, R.A.6
  • 18
    • 75149149380 scopus 로고    scopus 로고
    • Protein carbonylation in skeletal muscles: Impact on function
    • E. Barreiro, and S.N. Hussain Protein carbonylation in skeletal muscles: impact on function Antioxid. Redox Signaling 12 2010 417 429
    • (2010) Antioxid. Redox Signaling , vol.12 , pp. 417-429
    • Barreiro, E.1    Hussain, S.N.2
  • 19
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • DOI 10.1038/sj.emboj.7600599
    • T. Nyström Role of oxidative carbonylation in protein quality control and senescence EMBO J. 24 2005 1311 1317 (Pubitemid 40593052)
    • (2005) EMBO Journal , vol.24 , Issue.7 , pp. 1311-1317
    • Nystrom, T.1
  • 20
    • 39449105514 scopus 로고    scopus 로고
    • Protein carbonylation as a novel mechanism in redox signaling
    • DOI 10.1161/CIRCRESAHA.107.159814
    • C.M. Wong, A.K. Cheema, L. Zhang, and Y.J. Suzuki Protein carbonylation as a novel mechanism in redox signaling Circ. Res. 102 2008 310 318 (Pubitemid 351271651)
    • (2008) Circulation Research , vol.102 , Issue.3 , pp. 310-318
    • Wong, C.M.1    Cheema, A.K.2    Zhang, L.3    Suzuki, Y.J.4
  • 22
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • R.L. Levine, J.A. Williams, E.R. Stadtman, and E. Shacter Carbonyl assays for determination of oxidatively modified proteins Methods Enzymol. 233 1994 346 357
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 23
    • 84861130344 scopus 로고    scopus 로고
    • Proposed role of primary protein carbonylation in cell signaling
    • C.M. Wong, G. Bansal, L. Marcocci, and Y.J. Suzuki Proposed role of primary protein carbonylation in cell signaling Redox Rep. 17 2012 90 94
    • (2012) Redox Rep. , vol.17 , pp. 90-94
    • Wong, C.M.1    Bansal, G.2    Marcocci, L.3    Suzuki, Y.J.4
  • 26
    • 52049088770 scopus 로고    scopus 로고
    • Oxidative stress and covalent modification of protein with bioactive aldehydes
    • P.A. Grimsrud, H. Xie, T.J. Griffin, and D.A. Bernlohr Oxidative stress and covalent modification of protein with bioactive aldehydes J. Biol. Chem. 283 2008 21837 21841
    • (2008) J. Biol. Chem. , vol.283 , pp. 21837-21841
    • Grimsrud, P.A.1    Xie, H.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 27
    • 77955455232 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins and their oxidation sites
    • A.G. Madian, and F.E. Regnier Proteomic identification of carbonylated proteins and their oxidation sites J. Proteome Res. 9 2010 3766 3780
    • (2010) J. Proteome Res. , vol.9 , pp. 3766-3780
    • Madian, A.G.1    Regnier, F.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.