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Volumn 19, Issue 4, 2014, Pages 140-147

Determination of oxidative protein modifications using mass spectrometry

Author keywords

Oxidation; Proteomics; Tandem mass spectrometry

Indexed keywords

AMINO ACID; DODECYL SULFATE SODIUM; PHOSPHOPEPTIDE; PROTEIN; TRYPSIN;

EID: 84901340994     PISSN: 13510002     EISSN: 17432928     Source Type: Journal    
DOI: 10.1179/1351000214y.0000000089     Document Type: Review
Times cited : (12)

References (32)
  • 1
    • 79951906200 scopus 로고    scopus 로고
    • Thiol-based redox switches and gene regulation
    • Antelmann H, Helmann JD. Thiol-based redox switches and gene regulation. Antioxid Redox Signal 2011;14:1049-63.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1049-1063
    • Antelmann, H.1    Helmann, J.D.2
  • 2
    • 0342333739 scopus 로고
    • OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins
    • Christman MF, Storz G, Ames BN. OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc Natl Acad Sci USA 1989;86:3484-8.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3484-3488
    • Christman, M.F.1    Storz, G.2    Ames, B.N.3
  • 3
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methion-ine residues of proteins: Biological consequences
    • Stadtman ER, Moskovitz J, Levine RL. Oxidation of methion-ine residues of proteins: biological consequences. Antioxid Redox Signal 2003;5:577-82.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 4
    • 80052560779 scopus 로고    scopus 로고
    • Oxidative modifications of DAMPs suppress inflammation: The case for S100A8 and S100A9
    • Lim SY, Raftery MJ, Geczy CL. Oxidative modifications of DAMPs suppress inflammation: the case for S100A8 and S100A9. Antioxid Redox Signal 2011;15:2235-48.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 2235-2248
    • Lim, S.Y.1    Raftery, M.J.2    Geczy, C.L.3
  • 5
    • 0034282230 scopus 로고    scopus 로고
    • Biomarkers of myeloperoxidase-derived hypochlorous acid
    • Winterbourn CC, Kettle AJ. Biomarkers of myeloperoxidase-derived hypochlorous acid. Free Radic Biol Med 2000;29:403-9.
    • (2000) Free Radic Biol Med , vol.29 , pp. 403-409
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 6
    • 0032513141 scopus 로고    scopus 로고
    • Oxidation of high density lipoproteins. I. Formation of methionine sulfoxide in apolipoproteins AI and AII is an early event that accompanies lipid peroxidation and can be enhanced by alpha-tocopherol
    • Garner B, Witting PK, Waldeck AR, Christison JK, Raftery M, Stocker R. Oxidation of high density lipoproteins. I. Formation of methionine sulfoxide in apolipoproteins AI and AII is an early event that accompanies lipid peroxidation and can be enhanced by alpha-tocopherol. J Biol Chem 1998;273:6080-7.
    • (1998) J Biol Chem , vol.273 , pp. 6080-6087
    • Garner, B.1    Witting, P.K.2    Waldeck, A.R.3    Christison, J.K.4    Raftery, M.5    Stocker, R.6
  • 7
    • 77956210622 scopus 로고    scopus 로고
    • Use of dimedone-based chemical probes for sulfenic acid detection methods to visualize and identify labeled proteins
    • Nelson KJ, Klomsiri C, Codreanu SG, Soito L, Liebler DC, Rogers LC, et al. Use of dimedone-based chemical probes for sulfenic acid detection methods to visualize and identify labeled proteins. Methods Enzymol 2010;473:95-115.
    • (2010) Methods Enzymol , vol.473 , pp. 95-115
    • Nelson, K.J.1    Klomsiri, C.2    Codreanu, S.G.3    Soito, L.4    Liebler, D.C.5    Rogers, L.C.6
  • 8
    • 77953911347 scopus 로고    scopus 로고
    • Mass spec-trometric identification of oxidative modifications of tryptophan residues in proteins: Chemical artifact or post-translational modification?
    • Perdivara I, Deterding LJ, Przybylski M, Tomer KB. Mass spec-trometric identification of oxidative modifications of tryptophan residues in proteins: chemical artifact or post-translational modification? J Am Soc Mass Spectrom 2010;21:1114-7.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1114-1117
    • Perdivara, I.1    Deterding, L.J.2    Przybylski, M.3    Tomer, K.B.4
  • 9
    • 0035823537 scopus 로고    scopus 로고
    • Novel intra-and inter-molecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation
    • Raftery MJ, Yang Z, Valenzuela SM, Geczy CL. Novel intra-and inter-molecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation. J Biol Chem 2001;276:33393-401.
    • (2001) J Biol Chem , vol.276 , pp. 33393-33401
    • Raftery, M.J.1    Yang, Z.2    Valenzuela, S.M.3    Geczy, C.L.4
  • 10
    • 0035565231 scopus 로고    scopus 로고
    • Detection of 25,000 molecules of substance P by MALDI-TOF mass spectrometry and investigations into the fundamental limits of detection in MALDI
    • Keller BO, Li L. Detection of 25,000 molecules of substance P by MALDI-TOF mass spectrometry and investigations into the fundamental limits of detection in MALDI. J Am Soc Mass Spectrom 2001;12:1055-63.
    • (2001) J Am Soc Mass Spectrom , vol.12 , pp. 1055-1063
    • Keller, B.O.1    Li, L.2
  • 11
    • 79960350266 scopus 로고    scopus 로고
    • Membrane-based emitter for coupling microfluidics with ultrasensitive nanoelectrospray ionization-mass spectrometry
    • Sun X, Kelly RT, Tang K, Smith RD. Membrane-based emitter for coupling microfluidics with ultrasensitive nanoelectrospray ionization-mass spectrometry. Anal Chem 2011;83:5797-803.
    • (2011) Anal Chem , vol.83 , pp. 5797-5803
    • Sun, X.1    Kelly, R.T.2    Tang, K.3    Smith, R.D.4
  • 12
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 1988;60:2299-301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 13
    • 0033105179 scopus 로고    scopus 로고
    • Two-layer sample preparation: A method for MALDI-MS analysis of complex peptide and protein mixtures
    • Dai Y, Whittal RM, Li L. Two-layer sample preparation: a method for MALDI-MS analysis of complex peptide and protein mixtures. Anal Chem 1999;71:1087-91.
    • (1999) Anal Chem , vol.71 , pp. 1087-1091
    • Dai, Y.1    Whittal, R.M.2    Li, L.3
  • 14
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomole-cules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Electrospray ionization for mass spectrometry of large biomole-cules. Science 1989;246:64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 15
    • 0242354113 scopus 로고    scopus 로고
    • Shifts in peptide and protein charge state distributions with varying spray tip orifice diameter in nanoelectros-pray Fourier transform ion cyclotron resonance mass spectrometry
    • Li Y, Cole RB. Shifts in peptide and protein charge state distributions with varying spray tip orifice diameter in nanoelectros-pray Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 2003;75:5739-46.
    • (2003) Anal Chem , vol.75 , pp. 5739-5746
    • Li, Y.1    Cole, R.B.2
  • 19
    • 0035048372 scopus 로고    scopus 로고
    • Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues
    • Stoeckli M, Chaurand P, Hallahan DE, Caprioli RM. Imaging mass spectrometry: a new technology for the analysis of protein expression in mammalian tissues. Nat Med 2001;7:493-6.
    • (2001) Nat Med , vol.7 , pp. 493-496
    • Stoeckli, M.1    Chaurand, P.2    Hallahan, D.E.3    Caprioli, R.M.4
  • 20
    • 84876099509 scopus 로고    scopus 로고
    • Analysis of tissue specimens by matrix-assisted laser desorption/ionization imaging mass spec-trometry in biological and clinical research
    • Norris JL, Caprioli RM. Analysis of tissue specimens by matrix-assisted laser desorption/ionization imaging mass spec-trometry in biological and clinical research. Chem Rev 2013; 113:2309-42.
    • (2013) Chem Rev , vol.113 , pp. 2309-2342
    • Norris, J.L.1    Caprioli, R.M.2
  • 21
    • 44449162195 scopus 로고    scopus 로고
    • Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level
    • Hanke S, Besir H, Oesterhelt D, Mann M. Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level. J Proteome Res 2008;7:1118-30.
    • (2008) J Proteome Res , vol.7 , pp. 1118-1130
    • Hanke, S.1    Besir, H.2    Oesterhelt, D.3    Mann, M.4
  • 22
    • 79959958529 scopus 로고    scopus 로고
    • Performance characteristics of a new hybrid quadrupole time-of-flight tandem mass spectrometer (TripleTOF 5600)
    • Andrews GL, Simons BL, Young JB, Hawkridge AM, Muddiman DC. Performance characteristics of a new hybrid quadrupole time-of-flight tandem mass spectrometer (TripleTOF 5600). Anal Chem 2011;83:5442-6.
    • (2011) Anal Chem , vol.83 , pp. 5442-5446
    • Andrews, G.L.1    Simons, B.L.2    Young, J.B.3    Hawkridge, A.M.4    Muddiman, D.C.5
  • 24
    • 0031568420 scopus 로고    scopus 로고
    • Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level
    • McCormack AL, Schieltz DM, Goode B, Yang S, Barnes G, Drubin D, et al. Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level. Anal Chem 1997;69:767-76.
    • (1997) Anal Chem , vol.69 , pp. 767-776
    • McCormack, A.L.1    Schieltz, D.M.2    Goode, B.3    Yang, S.4    Barnes, G.5    Drubin, D.6
  • 25
    • 84874589189 scopus 로고    scopus 로고
    • Mapping and analysis of phosphorylation sites: A quick guide for cell biologists
    • Dephoure N, Gould KL, Gygi SP, Kellogg DR. Mapping and analysis of phosphorylation sites: a quick guide for cell biologists. Mol Biol Cell 2013;24:535-42.
    • (2013) Mol Biol Cell , vol.24 , pp. 535-542
    • Dephoure, N.1    Gould, K.L.2    Gygi, S.P.3    Kellogg, D.R.4
  • 26
    • 84875055792 scopus 로고    scopus 로고
    • Interconversion of the peptide isoforms of aspartate: Stability of isoaspartates
    • Hooi MY, Raftery MJ, Truscott RJ. Interconversion of the peptide isoforms of aspartate: stability of isoaspartates. Mech Ageing Dev 2013;134:103-9.
    • (2013) Mech Ageing Dev , vol.134 , pp. 103-109
    • Hooi, M.Y.1    Raftery, M.J.2    Truscott, R.J.3
  • 27
    • 84863072274 scopus 로고    scopus 로고
    • Electron transfer dissociation (ETD) of peptides containing intrachain disulfide bonds
    • Cole SR, Ma X, Zhang X, Xia Y. Electron transfer dissociation (ETD) of peptides containing intrachain disulfide bonds. J Am Soc Mass Spectrom 2012;23:310-20.
    • (2012) J Am Soc Mass Spectrom , vol.23 , pp. 310-320
    • Cole, S.R.1    Ma, X.2    Zhang, X.3    Xia, Y.4
  • 29
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, Kirschner MW, Gygi SP. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 2003;100: 6940-5.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 30
    • 77954754565 scopus 로고    scopus 로고
    • Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach
    • Held JM, Danielson SR, Behring JB, Atsriku C, Britton DJ, Puckett RL, et al. Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach. Mol Cell Proteomics 2010;9:1400-10.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1400-1410
    • Held, J.M.1    Danielson, S.R.2    Behring, J.B.3    Atsriku, C.4    Britton, D.J.5    Puckett, R.L.6
  • 31
    • 0042164949 scopus 로고    scopus 로고
    • Redox proteomics: Identification of oxida-tively modified proteins
    • Ghezzi P, Bonetto V. Redox proteomics: identification of oxida-tively modified proteins. Proteomics 2003;3:1145-53.
    • (2003) Proteomics , vol.3 , pp. 1145-1153
    • Ghezzi, P.1    Bonetto, V.2
  • 32
    • 0036391454 scopus 로고    scopus 로고
    • Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags
    • Gygi SP, Rist B, Griffin TJ, Eng J, Aebersold R. Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags. J Proteome Res 2002;1:47-54.
    • (2002) J Proteome Res , vol.1 , pp. 47-54
    • Gygi, S.P.1    Rist, B.2    Griffin, T.J.3    Eng, J.4    Aebersold, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.