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Volumn 33, Issue 2, 2014, Pages 147-156

Proteomics methods to study methionine oxidation

Author keywords

methionine oxidation; methionine sulfoxide; oxidative stress; PTM analysis; redox proteomics

Indexed keywords

CELLULAR CONTEXTS; CELLULAR SIGNALING; METHIONINE OXIDATION; METHIONINE RESIDUES; METHIONINE SULFOXIDE; PROTEIN FUNCTIONS; PROTEOMICS; PROTEOMICS METHODS;

EID: 84893817379     PISSN: 02777037     EISSN: 10982787     Source Type: Journal    
DOI: 10.1002/mas.21386     Document Type: Review
Times cited : (38)

References (69)
  • 1
    • 33746577830 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase in Helicobacter pylori: Interaction with methionine-rich proteins and stress-induced expression
    • DOI 10.1128/JB.00430-06
    • Alamuri P, Maier RJ,. 2006. Methionine sulfoxide reductase in Helicobacter pylori: Interaction with methionine-rich proteins and stress-induced expression. J Bacteriol 188: 5839-5850. (Pubitemid 44384092)
    • (2006) Journal of Bacteriology , vol.188 , Issue.16 , pp. 5839-5850
    • Alamuri, P.1    Maier, R.J.2
  • 2
    • 12844275002 scopus 로고    scopus 로고
    • The enzymology and biochemistry of methionine sulfoxide reductases
    • DOI 10.1016/j.bbapap.2004.09.016, PII S1570963904002535, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Boschi-Muller S, Olry A, Antoine M, Branlant G,. 2005. The enzymology and biochemistry of methionine sulfoxide reductases. Biochim Biophys Acta 1703: 231-238. (Pubitemid 40170446)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 231-238
    • Boschi-Muller, S.1    Olry, A.2    Antoine, M.3    Branlant, G.4
  • 3
    • 44549088533 scopus 로고    scopus 로고
    • The methionine sulfoxide reductases: Catalysis and substrate specificities
    • Boschi-Muller S, Gand A, Branlant G,. 2008. The methionine sulfoxide reductases: Catalysis and substrate specificities. Arch Biochem Biophys 474: 266-273.
    • (2008) Arch Biochem Biophys , vol.474 , pp. 266-273
    • Boschi-Muller, S.1    Gand, A.2    Branlant, G.3
  • 4
    • 0013958696 scopus 로고
    • Location of disulphide bridges by diagonal paper electrophoresis the disulphide bridges of bovine chymotrypsinogen A
    • Brown JR, Hartley BS,. 1966. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A. Biochem J 101: 214-228.
    • (1966) Biochem J , vol.101 , pp. 214-228
    • Brown, J.R.1    Hartley, B.S.2
  • 5
    • 33744474574 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Relevance to aging and protection against oxidative stress
    • DOI 10.1196/annals.1354.006
    • Cabreiro F, Picot CR, Friguet B, Petropoulos I,. 2006. Methionine sulfoxide reductases: Relevance to aging and protection against oxidative stress. Ann N Y Acad Sci 1067: 37-44. (Pubitemid 43806307)
    • (2006) Annals of the New York Academy of Sciences , vol.1067 , Issue.1 , pp. 37-44
    • Cabreiro, F.1    Picot, C.R.2    Friguet, B.3    Petropoulos, I.4
  • 7
    • 84866418481 scopus 로고    scopus 로고
    • Reactive nitrogen oxide species-induced post-translational modifications in human hemoglobin and the association with cigarette smoking
    • Chen HJ, Chen YC,. 2012. Reactive nitrogen oxide species-induced post-translational modifications in human hemoglobin and the association with cigarette smoking. Anal Chem 84: 7881-7890.
    • (2012) Anal Chem , vol.84 , pp. 7881-7890
    • Chen, H.J.1    Chen, Y.C.2
  • 9
    • 0016321645 scopus 로고
    • Diagonal chromatography for the selective purification of tyrosyl peptides
    • Cruickshank WH, Malchy BL, Kaplan H,. 1974. Diagonal chromatography for the selective purification of tyrosyl peptides. Can J Biochem 52: 1013-1017.
    • (1974) Can J Biochem , vol.52 , pp. 1013-1017
    • Cruickshank, W.H.1    Malchy, B.L.2    Kaplan, H.3
  • 10
    • 84864748949 scopus 로고    scopus 로고
    • Modulating protein activity and cellular function by methionine residue oxidation
    • Cui ZJ, Han ZQ, Li ZY,. 2012. Modulating protein activity and cellular function by methionine residue oxidation. Amino Acids 43: 505-517.
    • (2012) Amino Acids , vol.43 , pp. 505-517
    • Cui, Z.J.1    Han, Z.Q.2    Li, Z.Y.3
  • 12
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • DOI 10.1016/j.bbapap.2004.08.007, PII S1570963904002183, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Davies MJ,. 2005. The oxidative environment and protein damage. Biochim Biophys Acta 1703: 93-109. (Pubitemid 40170433)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 93-109
    • Davies, M.J.1
  • 13
    • 0030610119 scopus 로고    scopus 로고
    • Oxidative of a critical methionine modulates DNA binding of the Drosophila melanogaster high mobility group protein, HMG-D
    • DOI 10.1016/S0014-5793(97)01059-4, PII S0014579397010594
    • Dow LK, Changela A, Hefner HE, Churchill ME,. 1997. Oxidation of a critical methionine modulates DNA binding of the Drosophila melanogaster high mobility group protein, HMG-D. FEBS Lett 414: 514-520. (Pubitemid 27390658)
    • (1997) FEBS Letters , vol.414 , Issue.3 , pp. 514-520
    • Dow, L.K.1    Changela, A.2    Hefner, H.E.3    Churchill, M.E.A.4
  • 15
    • 2442506617 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli
    • DOI 10.1038/sj.emboj.7600172
    • Ezraty B, Grimaud R, El Hassouni M, Moinier D, Barras F,. 2004. Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli. EMBO J 23: 1868-1877. (Pubitemid 38649649)
    • (2004) EMBO Journal , vol.23 , Issue.8 , pp. 1868-1877
    • Ezraty, B.1    Grimaud, R.2    El Hassouni, M.3    Moinier, D.4    Barras, F.5
  • 16
    • 12844259524 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases in prokaryotes
    • DOI 10.1016/j.bbapap.2004.08.017, PII S1570963904002262, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Ezraty B, Aussel L, Barras F,. 2005. Methionine sulfoxide reductases in prokaryotes. Biochim Biophys Acta 1703: 221-229. (Pubitemid 40170445)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 221-229
    • Ezraty, B.1    Aussel, L.2    Barras, F.3
  • 17
    • 79958027934 scopus 로고    scopus 로고
    • N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum
    • Forte GM, Pool MR, Stirling CJ,. 2011. N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum. PLoS Biol 9: e1001073.
    • (2011) PLoS Biol , vol.9
    • Forte, G.M.1    Pool, M.R.2    Stirling, C.J.3
  • 19
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • DOI 10.1038/nbt810
    • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J,. 2003. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol 21: 566-569. (Pubitemid 36532024)
    • (2003) Nature Biotechnology , vol.21 , Issue.5 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 20
    • 1842423659 scopus 로고    scopus 로고
    • Reversible labeling of cysteine-containing peptides allows their specific chromatographic isolation for non-gel proteome studies
    • DOI 10.1002/pmic.200300641
    • Gevaert K, Ghesquière B, Staes A, Martens L, Van Damme J, Thomas GR, Vandekerckhove J,. 2004. Reversible labeling of cysteine-containing peptides allows their specific chromatographic isolation for non-gel proteome studies. Proteomics 4: 897-908. (Pubitemid 38445950)
    • (2004) Proteomics , vol.4 , Issue.4 , pp. 897-908
    • Gevaert, K.1    Ghesquiere, B.2    Staes, A.3    Martens, L.4    Van Damme, J.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 21
    • 33744986528 scopus 로고    scopus 로고
    • Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: The proteome of human multipotent adult progenitor cells
    • DOI 10.1021/pr060026a
    • Gevaert K, Pinxteren J, Demol H, Hugelier K, Staes A, Van Damme J, Martens L, Vandekerckhove J,. 2006. Four stage liquid chromatographic selection of methionyl peptides for peptide-centric proteome analysis: The proteome of human multipotent adult progenitor cells. J Proteome Res 5: 1415-1428. (Pubitemid 43865811)
    • (2006) Journal of Proteome Research , vol.5 , Issue.6 , pp. 1415-1428
    • Gevaert, K.1    Pinxteren, J.2    Demol, H.3    Hugelier, K.4    Staes, A.5    Van Damme, J.6    Martens, L.7    Vandekerckhove, J.8
  • 23
    • 0010388069 scopus 로고
    • The reaction of iodoacetate with methionine
    • Gundlach HG, Moore S, Stein WH,. 1959. The reaction of iodoacetate with methionine. J Biol Chem 234: 1761-1764.
    • (1959) J Biol Chem , vol.234 , pp. 1761-1764
    • Gundlach, H.G.1    Moore, S.2    Stein, W.H.3
  • 24
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • DOI 10.1038/13690
    • Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R,. 1999. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17: 994-999. (Pubitemid 29474856)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 25
    • 70149092747 scopus 로고    scopus 로고
    • Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis
    • Hardin SC, Larue CT, Oh MH, Jain V, Huber SC,. 2009. Coupling oxidative signals to protein phosphorylation via methionine oxidation in Arabidopsis. Biochem J 422: 305-312.
    • (2009) Biochem J , vol.422 , pp. 305-312
    • Hardin, S.C.1    Larue, C.T.2    Oh, M.H.3    Jain, V.4    Huber, S.C.5
  • 26
    • 84455205549 scopus 로고    scopus 로고
    • Direct redox regulation of F-actin assembly and disassembly by Mical
    • Hung RJ, Pak CW, Terman JR,. 2011. Direct redox regulation of F-actin assembly and disassembly by Mical. Science 334: 1710-1713.
    • (2011) Science , vol.334 , pp. 1710-1713
    • Hung, R.J.1    Pak, C.W.2    Terman, J.R.3
  • 27
    • 77149120798 scopus 로고    scopus 로고
    • N-terminal acetylation of cellular proteins creates specific degradation signals
    • Hwang CS, Shemorry A, Varshavsky A,. 2010. N-terminal acetylation of cellular proteins creates specific degradation signals. Science 327: 973-977.
    • (2010) Science , vol.327 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 29
    • 84859222468 scopus 로고    scopus 로고
    • Electron transfer dissociation mass spectrometry in proteomics
    • Kim MS, Pandey A,. 2012. Electron transfer dissociation mass spectrometry in proteomics. Proteomics 12: 530-542.
    • (2012) Proteomics , vol.12 , pp. 530-542
    • Kim, M.S.1    Pandey, A.2
  • 31
    • 45749103200 scopus 로고    scopus 로고
    • Analysis of methionine/selenomethionine oxidation and methionine sulfoxide reductase function using methionine-rich proteins and antibodies against their oxidized forms
    • DOI 10.1021/bi800422s
    • Le DT, Liang X, Fomenko DE, Raza AS, Chong CK, Carlson BA, Hatfield DL, Gladyshev VN,. 2008. Analysis of methionine/selenomethionine oxidation and methionine sulfoxide reductase function using methionine-rich proteins and antibodies against their oxidized forms. Biochemistry 47: 6685-6694. (Pubitemid 351874295)
    • (2008) Biochemistry , vol.47 , Issue.25 , pp. 6685-6694
    • Dung, T.L.1    Liang, X.2    Fomenko, D.E.3    Raza, A.S.4    Chong, C.-K.5    Carlson, B.A.6    Hatfield, D.L.7    Gladyshev, V.N.8
  • 32
    • 82355173265 scopus 로고    scopus 로고
    • Non-invasive proteomic analysis of human skin keratins: Screening of methionine oxidation in keratins by mass spectrometry
    • Lee SH, Miyamoto K, Goto T, Oe T,. 2011. Non-invasive proteomic analysis of human skin keratins: Screening of methionine oxidation in keratins by mass spectrometry. J Proteomics 75: 435-449.
    • (2011) J Proteomics , vol.75 , pp. 435-449
    • Lee, S.H.1    Miyamoto, K.2    Goto, T.3    Oe, T.4
  • 33
    • 79960604985 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A is a stereospecific methionine oxidase
    • Lim JC, You Z, Kim G, Levine RL,. 2011. Methionine sulfoxide reductase A is a stereospecific methionine oxidase. Proc Natl Acad Sci USA 108: 10472-10477.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 10472-10477
    • Lim, J.C.1    You, Z.2    Kim, G.3    Levine, R.L.4
  • 34
    • 84864095297 scopus 로고    scopus 로고
    • Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A
    • Lim JC, Gruschus JM, Ghesquiere B, Kim G, Piszczek G, Tjandra N, Levine RL,. 2012. Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A. J Biol Chem 287: 25589-25595.
    • (2012) J Biol Chem , vol.287 , pp. 25589-25595
    • Lim, J.C.1    Gruschus, J.M.2    Ghesquiere, B.3    Kim, G.4    Piszczek, G.5    Tjandra, N.6    Levine, R.L.7
  • 35
    • 0025100395 scopus 로고
    • High-performance liquid chromatography of rat and mouse islet polypeptides: Potential risk of oxidation of methionine residues during sample preparation
    • DOI 10.1016/S0378-4347(00)82299-9
    • Linde S, Nielsen JH, Hansen B, Welinder BS,. 1990. High-performance liquid chromatography of rat and mouse islet polypeptides: Potential risk of oxidation of methionine residues during sample preparation. J Chromatogr 530: 29-37. (Pubitemid 20256486)
    • (1990) Journal of Chromatography - Biomedical Applications , vol.530 , Issue.1 , pp. 29-37
    • Linde, S.1    Nielsen, J.H.2    Hansen, B.3    Welinder, B.S.4
  • 40
    • 78649444069 scopus 로고    scopus 로고
    • Deficiency of methionine sulfoxide reductase A causes cellular dysfunction and mitochondrial damage in cardiac myocytes under physical and oxidative stresses
    • Nan C, Li Y, Jean-Charles PY, Chen G, Kreymerman A, Prentice H, Weissbach H, Huang X,. 2010. Deficiency of methionine sulfoxide reductase A causes cellular dysfunction and mitochondrial damage in cardiac myocytes under physical and oxidative stresses. Biochem Biophys Res Commun 402: 608-613.
    • (2010) Biochem Biophys Res Commun , vol.402 , pp. 608-613
    • Nan, C.1    Li, Y.2    Jean-Charles, P.Y.3    Chen, G.4    Kreymerman, A.5    Prentice, H.6    Weissbach, H.7    Huang, X.8
  • 41
  • 42
    • 64549133370 scopus 로고    scopus 로고
    • Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies
    • Oien DB, Canello T, Gabizon R, Gasset M, Lundquist BL, Burns JM, Moskovitz J,. 2009. Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies. Arch Biochem Biophys 485: 35-40.
    • (2009) Arch Biochem Biophys , vol.485 , pp. 35-40
    • Oien, D.B.1    Canello, T.2    Gabizon, R.3    Gasset, M.4    Lundquist, B.L.5    Burns, J.M.6    Moskovitz, J.7
  • 44
    • 70449517524 scopus 로고    scopus 로고
    • Caloric restriction alleviates abnormal locomotor activity and dopamine levels in the brain of the methionine sulfoxide reductase A knockout mouse
    • Oien DB, Osterhaus GL, Lundquist BL, Fowler SC, Moskovitz J,. 2010b. Caloric restriction alleviates abnormal locomotor activity and dopamine levels in the brain of the methionine sulfoxide reductase A knockout mouse. Neurosci Lett 468: 38-41.
    • (2010) Neurosci Lett , vol.468 , pp. 38-41
    • Oien, D.B.1    Osterhaus, G.L.2    Lundquist, B.L.3    Fowler, S.C.4    Moskovitz, J.5
  • 45
    • 84874023762 scopus 로고    scopus 로고
    • Decreased phosphorylation and increased methionine oxidation of alpha-synuclein in the methionine sulfoxide reductase a knockout mouse
    • Oien DB, Carrasco GA, Moskovitz J,. 2011. Decreased phosphorylation and increased methionine oxidation of alpha-synuclein in the methionine sulfoxide reductase a knockout mouse. J Amino Acids 2011: 721094.
    • (2011) J Amino Acids , vol.2011 , pp. 721094
    • Oien, D.B.1    Carrasco, G.A.2    Moskovitz, J.3
  • 46
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M,. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 47
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • DOI 10.1021/ac0498617
    • Pinkse MW, Uitto PM, Hilhorst MJ, Ooms B, Heck AJ,. 2004. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal Chem 76: 3935-3943. (Pubitemid 38943662)
    • (2004) Analytical Chemistry , vol.76 , Issue.14 , pp. 3935-3943
    • Pinkse, M.W.H.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.R.5
  • 48
    • 73249129955 scopus 로고    scopus 로고
    • Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils
    • Rosen H, Klebanoff SJ, Wang Y, Brot N, Heinecke JW, Fu X,. 2009. Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils. Proc Natl Acad Sci USA 106: 18686-18691.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18686-18691
    • Rosen, H.1    Klebanoff, S.J.2    Wang, Y.3    Brot, N.4    Heinecke, J.W.5    Fu, X.6
  • 49
    • 84859722209 scopus 로고    scopus 로고
    • An electrophoretic mobility shift assay for methionine sulfoxide in proteins
    • Saunders CC, Stites WE,. 2012. An electrophoretic mobility shift assay for methionine sulfoxide in proteins. Anal Biochem 421: 767-769.
    • (2012) Anal Biochem , vol.421 , pp. 767-769
    • Saunders, C.C.1    Stites, W.E.2
  • 50
    • 80655128135 scopus 로고    scopus 로고
    • Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant
    • Sideri TC, Koloteva-Levine N, Tuite MF, Grant CM,. 2011. Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant. J Biol Chem 286: 38924-38931.
    • (2011) J Biol Chem , vol.286 , pp. 38924-38931
    • Sideri, T.C.1    Koloteva-Levine, N.2    Tuite, M.F.3    Grant, C.M.4
  • 51
    • 84869217993 scopus 로고    scopus 로고
    • Total ApoE and ApoE4 isoform assays in an Alzheimer's disease case-control study by targeted mass spectrometry (n = 669): A pilot assay for methionine-containing proteotypic peptides
    • Simon R, Girod M, Fonbonne C, Salvador A, Clement Y, Lanteri P, Amouyel P, Lambert JC, Lemoine J,. 2012. Total ApoE and ApoE4 isoform assays in an Alzheimer's disease case-control study by targeted mass spectrometry (n = 669): A pilot assay for methionine-containing proteotypic peptides. Mol Cell Proteomics 11: 1389-1403.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1389-1403
    • Simon, R.1    Girod, M.2    Fonbonne, C.3    Salvador, A.4    Clement, Y.5    Lanteri, P.6    Amouyel, P.7    Lambert, J.C.8    Lemoine, J.9
  • 52
    • 0030811288 scopus 로고    scopus 로고
    • Identification of hydrogen peroxide oxidation sites of αA- and αB-crystallins
    • Smith JB, Jiang X, Abraham EC,. 1997. Identification of hydrogen peroxide oxidation sites of alpha A- and alpha B-crystallins. Free Radic Res 26: 103-111. (Pubitemid 27365864)
    • (1997) Free Radical Research , vol.26 , Issue.2 , pp. 103-111
    • Smith, J.B.1    Jiang, X.2    Abraham, E.C.3
  • 54
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of Methionine Residues of Proteins: Biological Consequences
    • Stadtman ER, Moskovitz J, Levine RL,. 2003. Oxidation of methionine residues of proteins: Biological consequences. Antioxid Redox Signal 5: 577-582. (Pubitemid 37315145)
    • (2003) Antioxidants and Redox Signaling , vol.5 , Issue.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 56
    • 4444271864 scopus 로고    scopus 로고
    • Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18
    • DOI 10.1021/pr049956p
    • Staes A, Demol H, Van Damme J, Martens L, Vandekerckhove J, Gevaert K,. 2004. Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18. J Proteome Res 3: 786-791. (Pubitemid 39166239)
    • (2004) Journal of Proteome Research , vol.3 , Issue.4 , pp. 786-791
    • Staes, A.1    Demol, H.2    Van Damme, J.3    Martens, L.4    Vandekerckhove, J.5    Gevaert, K.6
  • 57
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • DOI 10.1016/S0092-8674(01)00495-0
    • Stamler JS, Lamas S, Fang FC,. 2001. Nitrosylation. The prototypic redox-based signaling mechanism. Cell 106: 675-683. (Pubitemid 32900659)
    • (2001) Cell , vol.106 , Issue.6 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 58
    • 0031812471 scopus 로고    scopus 로고
    • The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses
    • DOI 10.1002/elps.1150190614
    • Swiderek KM, Davis MT, Lee TD,. 1998. The identification of peptide modifications derived from gel-separated proteins using electrospray triple quadrupole and ion trap analyses. Electrophoresis 19: 989-997. (Pubitemid 28239968)
    • (1998) Electrophoresis , vol.19 , Issue.6 , pp. 989-997
    • Swiderek, K.M.1    Davis, M.T.2    Lee, T.D.3
  • 59
    • 65249142849 scopus 로고    scopus 로고
    • Protein-repairing methionine sulfoxide reductases in photosynthetic organisms: Gene organization, reduction mechanisms, and physiological roles
    • Tarrago L, Laugier E, Rey P,. 2009. Protein-repairing methionine sulfoxide reductases in photosynthetic organisms: Gene organization, reduction mechanisms, and physiological roles. Mol Plant 2: 202-217.
    • (2009) Mol Plant , vol.2 , pp. 202-217
    • Tarrago, L.1    Laugier, E.2    Rey, P.3
  • 60
    • 84863797987 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding
    • Tarrago L, Kaya A, Weerapana E, Marino SM, Gladyshev VN,. 2012a. Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding. J Biol Chem 287: 24448-24459.
    • (2012) J Biol Chem , vol.287 , pp. 24448-24459
    • Tarrago, L.1    Kaya, A.2    Weerapana, E.3    Marino, S.M.4    Gladyshev, V.N.5
  • 62
    • 84859366447 scopus 로고    scopus 로고
    • Protease signalling: The cutting edge
    • Turk B, Turk D, Turk V,. 2012. Protease signalling: The cutting edge. EMBO J 31: 1630-1643.
    • (2012) EMBO J , vol.31 , pp. 1630-1643
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 63
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt W,. 1995. Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic Biol Med 18: 93-105.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 64
    • 0023282993 scopus 로고
    • Analysis of peptides containing oxidized methionine and/or tryptophan by fast atom bombardment mass spectrometry
    • Wagner RM, Fraser BA,. 1987. Analysis of peptides containing oxidized methionine and/or tryptophan by fast atom bombardment mass spectrometry. Biomed Environ Mass Spectrom 14: 69-72.
    • (1987) Biomed Environ Mass Spectrom , vol.14 , pp. 69-72
    • Wagner, R.M.1    Fraser, B.A.2
  • 65
    • 84865297316 scopus 로고    scopus 로고
    • Wanted and wanting: Antibody against methionine sulfoxide
    • Wehr NB, Levine RL,. 2012. Wanted and wanting: Antibody against methionine sulfoxide. Free Radic Biol Med 53: 1222-1225.
    • (2012) Free Radic Biol Med , vol.53 , pp. 1222-1225
    • Wehr, N.B.1    Levine, R.L.2
  • 66
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: History and cellular role in protecting against oxidative damage
    • DOI 10.1016/j.bbapap.2004.10.004, PII S1570963904002870, Mewthionine Oxidation and Methionine Sulfoxide Reductases
    • Weissbach H, Resnick L, Brot N,. 2005. Methionine sulfoxide reductases: History and cellular role in protecting against oxidative damage. Biochim Biophys Acta 1703: 203-212. (Pubitemid 40170443)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1703 , Issue.2 , pp. 203-212
    • Weissbach, H.1    Resnick, L.2    Brot, N.3
  • 67
    • 76649124599 scopus 로고    scopus 로고
    • Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I
    • Wong YQ, Binger KJ, Howlett GJ, Griffin MD,. 2010. Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proc Natl Acad Sci USA 107: 1977-1982.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1977-1982
    • Wong, Y.Q.1    Binger, K.J.2    Howlett, G.J.3    Griffin, M.D.4
  • 68
    • 47649096893 scopus 로고    scopus 로고
    • Origin and evolution of the protein-repairing enzymes methionine sulphoxide reductases
    • DOI 10.1111/j.1469-185X.2008.00042.x
    • Zhang XH, Weissbach H,. 2008. Origin and evolution of the protein-repairing enzymes methionine sulphoxide reductases. Biol Rev Camb Philos Soc 83: 249-257. (Pubitemid 352020257)
    • (2008) Biological Reviews , vol.83 , Issue.3 , pp. 249-257
    • Zhang, X.-H.1    Weissbach, H.2
  • 69


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