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Volumn 74, Issue 11, 2011, Pages 2264-2273

Radiation-induced reductive modifications of sulfur-containing amino acids within peptides and proteins

Author keywords

Free radicals; Redox proteomics; Reductive stress; S containing amino acids

Indexed keywords

2 AMINOBUTYRIC ACID; ALANINE; CYSTEINE; FREE RADICAL; GLUTAREDOXIN; GLUTATHIONE; METHIONINE; METHIONINE SULFOXIDE REDUCTASE; POLYPEPTIDE; PROTEIN DISULFIDE ISOMERASE; SULFUR AMINO ACID; THIOREDOXIN;

EID: 80054873621     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.03.012     Document Type: Review
Times cited : (34)

References (54)
  • 1
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn C.C., Hampton M.B. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med 2008, 45:549-561.
    • (2008) Free Radic Biol Med , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 3
    • 57649198018 scopus 로고    scopus 로고
    • Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability
    • Paige J.S., Xu G., Stancevic B., Jaffrey S.R. Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability. Chem Biol 2008, 15:1307-1316.
    • (2008) Chem Biol , vol.15 , pp. 1307-1316
    • Paige, J.S.1    Xu, G.2    Stancevic, B.3    Jaffrey, S.R.4
  • 5
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • Reddie K.G., Carroll K.S. Expanding the functional diversity of proteins through cysteine oxidation. Curr Opin Chem Biol 2008, 12:746-754.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 6
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: tools, targets and reversal
    • Vogt W. Oxidation of methionyl residues in proteins: tools, targets and reversal. Free Radic Biol Med 1995, 18:93-105.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 7
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methionine residues of proteins: biological consequences
    • Stadtman E.R., Moskovitz J., Levine R.L. Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal 2003, 5:577-582.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 8
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
    • Weissbach H., Resnick L., Brot N. Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim Biophys Acta 2005, 1703:203-212.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 203-212
    • Weissbach, H.1    Resnick, L.2    Brot, N.3
  • 9
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo S., Levine R.L. Methionine in proteins defends against oxidative stress. FASEB J 2009, 23:464-472.
    • (2009) FASEB J , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 11
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins
    • Garrison W.M. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem Rev 1987, 87:381-398.
    • (1987) Chem Rev , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 12
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • Hawkins C.L., Davies M.J. Generation and propagation of radical reactions on proteins. Biochim Biophys Acta 2001, 1504:196-219.
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 13
    • 0036160119 scopus 로고    scopus 로고
    • Evidence in support of a concept or reductive stress
    • Lipinski B. Evidence in support of a concept or reductive stress. Br J Nutr 2002, 87:93-94.
    • (2002) Br J Nutr , vol.87 , pp. 93-94
    • Lipinski, B.1
  • 14
    • 12444296480 scopus 로고    scopus 로고
    • Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics
    • Dalle-Donne I., Scaloni A., Giustarini D., Cavarra E., Tell G., Lungarella G., et al. Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics. Mass Spectrom Rev 2005, 24:55-99.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 55-99
    • Dalle-Donne, I.1    Scaloni, A.2    Giustarini, D.3    Cavarra, E.4    Tell, G.5    Lungarella, G.6
  • 15
    • 0026448524 scopus 로고
    • Redox, radiation, and reductive bioactivation
    • Adams G.E. Redox, radiation, and reductive bioactivation. Radiat Res 1992, 132:129-139.
    • (1992) Radiat Res , vol.132 , pp. 129-139
    • Adams, G.E.1
  • 16
    • 34547681313 scopus 로고    scopus 로고
    • Human αB-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice
    • Rajasekaran N.S., Connell P., Christians E.S., Yan L.J., Taylor R.P., Orosz A., et al. Human αB-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice. Cell 2007, 130:427-439.
    • (2007) Cell , vol.130 , pp. 427-439
    • Rajasekaran, N.S.1    Connell, P.2    Christians, E.S.3    Yan, L.J.4    Taylor, R.P.5    Orosz, A.6
  • 19
    • 33750986793 scopus 로고    scopus 로고
    • The reaction of hydrogen atoms with methionine residues: a model of reductive radical stress causing tandem protein-lipid damage
    • Ferreri C., Manco I., Faraone-Mennella M.R., Torreggiani A., Tamba M., Manara S., et al. The reaction of hydrogen atoms with methionine residues: a model of reductive radical stress causing tandem protein-lipid damage. Chembiochem 2006, 7:1738-1744.
    • (2006) Chembiochem , vol.7 , pp. 1738-1744
    • Ferreri, C.1    Manco, I.2    Faraone-Mennella, M.R.3    Torreggiani, A.4    Tamba, M.5    Manara, S.6
  • 22
    • 34250659994 scopus 로고    scopus 로고
    • Reaction of hydrogen atom with Met-enkephalin and related peptides
    • Mozziconacci O., Bobrowski K., Ferreri C., Chatgilialoglu C. Reaction of hydrogen atom with Met-enkephalin and related peptides. Chem Eur J 2007, 13:2029-2033.
    • (2007) Chem Eur J , vol.13 , pp. 2029-2033
    • Mozziconacci, O.1    Bobrowski, K.2    Ferreri, C.3    Chatgilialoglu, C.4
  • 23
    • 0001065226 scopus 로고    scopus 로고
    • Rate constant determination for the reaction of hydroxyl and glutathione thiyl radicals with glutathione in aqueous solution
    • Mezyk S.P. Rate constant determination for the reaction of hydroxyl and glutathione thiyl radicals with glutathione in aqueous solution. J Phys Chem 1996, 100:8861-8866.
    • (1996) J Phys Chem , vol.100 , pp. 8861-8866
    • Mezyk, S.P.1
  • 24
    • 0030134581 scopus 로고    scopus 로고
    • LINAC/LASER Determination of the absolute rate constant for thiyl and hydroxyl radical reaction with sulfhydryls in aqueous solution: mercaptoethanol, cysteamine, and N-acetyl-l-cysteine
    • Mezyk S.P. LINAC/LASER Determination of the absolute rate constant for thiyl and hydroxyl radical reaction with sulfhydryls in aqueous solution: mercaptoethanol, cysteamine, and N-acetyl-l-cysteine. J Phys Chem 1996, 100:8295-8301.
    • (1996) J Phys Chem , vol.100 , pp. 8295-8301
    • Mezyk, S.P.1
  • 26
    • 77950787460 scopus 로고    scopus 로고
    • ESR study of disulfide neutral radical of α-keratin present in dried white human hair exposed to near-UV radiation
    • Yanagi N., Niwa M., Sakurai Y., Nakajima A., Kanaori K., Tajima K. ESR study of disulfide neutral radical of α-keratin present in dried white human hair exposed to near-UV radiation. Chem Lett 2010, 39:340-341.
    • (2010) Chem Lett , vol.39 , pp. 340-341
    • Yanagi, N.1    Niwa, M.2    Sakurai, Y.3    Nakajima, A.4    Kanaori, K.5    Tajima, K.6
  • 27
    • 20744457073 scopus 로고    scopus 로고
    • The influence of solid-state molecular organization on the reaction paths of thiyl radicals
    • Faucitano A., Buttafava A., Marini M., Chatgilialoglu C. The influence of solid-state molecular organization on the reaction paths of thiyl radicals. Chemphyschem 2005, 6:1100-1107.
    • (2005) Chemphyschem , vol.6 , pp. 1100-1107
    • Faucitano, A.1    Buttafava, A.2    Marini, M.3    Chatgilialoglu, C.4
  • 28
    • 0016382603 scopus 로고
    • Reactions of phenylalanine derivatives, methionine derivatives, and their mixtures in aqueous solution with pulse-radiolytically generated H atoms
    • Lichtin N.N., Shafferman A. Reactions of phenylalanine derivatives, methionine derivatives, and their mixtures in aqueous solution with pulse-radiolytically generated H atoms. Radiat Res 1974, 60:432-440.
    • (1974) Radiat Res , vol.60 , pp. 432-440
    • Lichtin, N.N.1    Shafferman, A.2
  • 29
    • 0017709884 scopus 로고
    • Reactions of aqueous l-methionine, l-phenylalanine, l-methionyl-l-phenylalanine, l-phenylalanyl-l-methionine and their mixtures with H atoms during steady radiolysis at pH 6.5
    • Mee L.K., Adelstein S.J., Steinhart C.M., Lichtin N.N. Reactions of aqueous l-methionine, l-phenylalanine, l-methionyl-l-phenylalanine, l-phenylalanyl-l-methionine and their mixtures with H atoms during steady radiolysis at pH 6.5. Radiat Res 1977, 71:493-504.
    • (1977) Radiat Res , vol.71 , pp. 493-504
    • Mee, L.K.1    Adelstein, S.J.2    Steinhart, C.M.3    Lichtin, N.N.4
  • 30
    • 75149159746 scopus 로고    scopus 로고
    • Radiation chemical studies of methionine in aqueous solution: understanding the role of molecular oxygen
    • Barata-Vallejo S., Ferreri C., Postigo A., Chatgilialoglu C. Radiation chemical studies of methionine in aqueous solution: understanding the role of molecular oxygen. Chem Res Toxicol 2010, 23:258-263.
    • (2010) Chem Res Toxicol , vol.23 , pp. 258-263
    • Barata-Vallejo, S.1    Ferreri, C.2    Postigo, A.3    Chatgilialoglu, C.4
  • 31
    • 44849110325 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins modified by nitric oxide-derived species
    • Salzano A.M., D'Ambrosio C., Scaloni A. Mass spectrometric characterization of proteins modified by nitric oxide-derived species. Methods Enzymol 2008, 440:3-15.
    • (2008) Methods Enzymol , vol.440 , pp. 3-15
    • Salzano, A.M.1    D'Ambrosio, C.2    Scaloni, A.3
  • 32
    • 33749522859 scopus 로고    scopus 로고
    • Mass spectrometry of protein modifications by reactive oxygen and nitrogen species
    • Schöneich C., Sharov V.S. Mass spectrometry of protein modifications by reactive oxygen and nitrogen species. Free Radic Biol Med 2006, 41:1507-1520.
    • (2006) Free Radic Biol Med , vol.41 , pp. 1507-1520
    • Schöneich, C.1    Sharov, V.S.2
  • 36
    • 52049096677 scopus 로고    scopus 로고
    • The reductive desulfurization of Met and Cys residues in bovine RNAse A associated with the trans lipid formation in a mimetic model of biological membranes
    • Ferreri C., Chatgilialoglu C., Torreggiani A., Salzano A.M., Renzone G., Scaloni A. The reductive desulfurization of Met and Cys residues in bovine RNAse A associated with the trans lipid formation in a mimetic model of biological membranes. J Proteome Res 2008, 7:2007-2015.
    • (2008) J Proteome Res , vol.7 , pp. 2007-2015
    • Ferreri, C.1    Chatgilialoglu, C.2    Torreggiani, A.3    Salzano, A.M.4    Renzone, G.5    Scaloni, A.6
  • 38
    • 66349121915 scopus 로고    scopus 로고
    • Zinc and cadmium complexes of a plant metallothionein under radical stress: desulfurisation reactions associated with the formation of trans lipids in model membranes
    • Torreggiani A., Domènech J., Ferreri C., Orihuela R., Atrian S., Capdevila M., et al. Zinc and cadmium complexes of a plant metallothionein under radical stress: desulfurisation reactions associated with the formation of trans lipids in model membranes. Chem Eur J 2009, 15:6015-6024.
    • (2009) Chem Eur J , vol.15 , pp. 6015-6024
    • Torreggiani, A.1    Domènech, J.2    Ferreri, C.3    Orihuela, R.4    Atrian, S.5    Capdevila, M.6
  • 39
    • 0028290484 scopus 로고
    • Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules
    • Callender R., Deng H. Nonresonance Raman difference spectroscopy: a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules. Annu Rev Biophys Biomol Struct 1994, 23:215-245.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 215-245
    • Callender, R.1    Deng, H.2
  • 40
    • 18444419164 scopus 로고    scopus 로고
    • Raman spectroscopy of proteins: from peptides to large assemblies
    • Tuma R. Raman spectroscopy of proteins: from peptides to large assemblies. J Raman Spectrosc 2005, 36:307-319.
    • (2005) J Raman Spectrosc , vol.36 , pp. 307-319
    • Tuma, R.1
  • 43
    • 4444339833 scopus 로고    scopus 로고
    • Oxidative DNA damage and disease: induction, repair and significance
    • Evans M.D., Dizdaroglu M., Cooke M.S. Oxidative DNA damage and disease: induction, repair and significance. Mutat Res 2004, 567:1-61.
    • (2004) Mutat Res , vol.567 , pp. 1-61
    • Evans, M.D.1    Dizdaroglu, M.2    Cooke, M.S.3
  • 45
    • 0004273681 scopus 로고    scopus 로고
    • New RRC Oxford University Press Inc, New York
    • New RRC Liposomes. A practical approach 1997, Oxford University Press Inc, New York.
    • (1997) Liposomes. A practical approach
  • 46
    • 22244448041 scopus 로고    scopus 로고
    • Trans lipids: the free radical path
    • Chatgilialoglu C., Ferreri C. Trans lipids: the free radical path. Acc Chem Res 2005, 38:441-448.
    • (2005) Acc Chem Res , vol.38 , pp. 441-448
    • Chatgilialoglu, C.1    Ferreri, C.2
  • 47
    • 26944461594 scopus 로고    scopus 로고
    • Geometrical trans lipid isomers: a new target for lipidomics
    • Ferreri C., Chatgilialoglu C. Geometrical trans lipid isomers: a new target for lipidomics. Chembiochem 2005, 6:1722-1734.
    • (2005) Chembiochem , vol.6 , pp. 1722-1734
    • Ferreri, C.1    Chatgilialoglu, C.2
  • 48
  • 49
  • 51
    • 0019323538 scopus 로고
    • Effects of phospholipid fatty acid composition and membrane fluidity on the activity of bovine brain phospholipid exchange protein
    • Helmkamp G.M. Effects of phospholipid fatty acid composition and membrane fluidity on the activity of bovine brain phospholipid exchange protein. Biochemistry 1980, 19:2050-2056.
    • (1980) Biochemistry , vol.19 , pp. 2050-2056
    • Helmkamp, G.M.1
  • 52
    • 33644753078 scopus 로고    scopus 로고
    • Comparison of phosphatidylcholine vesicle properties related to geometrical isomerism
    • Ferreri C., Pierotti S., Barbieri A., Zambonin L., Landi L., Rasi S., et al. Comparison of phosphatidylcholine vesicle properties related to geometrical isomerism. Photochem Photobiol 2006, 82:274-280.
    • (2006) Photochem Photobiol , vol.82 , pp. 274-280
    • Ferreri, C.1    Pierotti, S.2    Barbieri, A.3    Zambonin, L.4    Landi, L.5    Rasi, S.6
  • 53
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of l-cysteine catalyzed by the nifS gene product
    • Zheng L., White R.H., Cash V.L., Dean D.R. Mechanism for the desulfurization of l-cysteine catalyzed by the nifS gene product. Biochemistry 1994, 33:4714-4720.
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4


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