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Volumn 10, Issue 3, 2011, Pages

Novel oxidative modifications in redox-active cysteine residues

Author keywords

[No Author keywords available]

Indexed keywords

ACRYLAMIDE; CYSTEINE DERIVATIVE; DEHYDROALANINE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MITOCHONDRIAL PROTEIN; NUCLEOSIDE DIPHOSPHATE KINASE A; PEROXIREDOXIN 6; SERINE; SULFENIC ACID DERIVATIVE; SULFINIC ACID DERIVATIVE; SULFONIC ACID DERIVATIVE; ALANINE; CYSTEINE; DRUG DERIVATIVE; MUTANT PROTEIN; NUCLEOSIDE DIPHOSPHATE KINASE; PEPTIDE; PRDX6 PROTEIN, MOUSE; RECOMBINANT PROTEIN;

EID: 79953185783     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.000513     Document Type: Article
Times cited : (78)

References (39)
  • 1
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett, B. S., and Stadtman, E. R. (1997) Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272, 20313-20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 2
    • 31344457662 scopus 로고    scopus 로고
    • Protein oxidation in plant mitochondria detected as oxidized tryptophan
    • Møller, I. M., and Kristensen, B. K. (2006) Protein oxidation in plant mitochondria detected as oxidized tryptophan. Free Radic. Biol. Med. 40, 430-435
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 430-435
    • Møller, I.M.1    Kristensen, B.K.2
  • 3
    • 69249158623 scopus 로고    scopus 로고
    • Mass spectrometry study of PRL-3 phosphatase inactivation by disulfide bond formation and cysteine into glycine conversion
    • Orsatti, L., Innocenti, F., Lo, Surdo, P., Talamo, F., and Barbato, G. (2009) Mass spectrometry study of PRL-3 phosphatase inactivation by disulfide bond formation and cysteine into glycine conversion. Rapid Commun. Mass Spectrom. 23, 2733-2740
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 2733-2740
    • Orsatti, L.1    Innocenti, F.2    Lo Surdo, P.3    Talamo, F.4    Barbato, G.5
  • 4
    • 40649107852 scopus 로고    scopus 로고
    • Dehydroalanine derived from cysteine is a common post-translational modification in human serum albumin
    • Bar-Or, R., Rael, L. T., and Bar-Or, D. (2008) Dehydroalanine derived from cysteine is a common post-translational modification in human serum albumin. Rapid Commun. Mass Spectrom. 22, 711-716
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 711-716
    • Bar-Or, R.1    Rael, L.T.2    Bar-Or, D.3
  • 5
    • 70349482669 scopus 로고    scopus 로고
    • Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies
    • Seo, Y. H., and Carroll, K. S. (2009) Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies. Proc. Natl. Acad. Sci. U.S.A. 106, 16163-16168
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16163-16168
    • Seo, Y.H.1    Carroll, K.S.2
  • 6
    • 38649084667 scopus 로고    scopus 로고
    • Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid
    • DOI 10.1110/ps.073096508
    • Salsbury, F. R., Jr., Knutson, S. T., Poole, L. B., and Fetrow, J. S. (2008) Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid. Protein Sci. 17, 299-312 (Pubitemid 351171842)
    • (2008) Protein Science , vol.17 , Issue.2 , pp. 299-312
    • Salsbury Jr., F.R.1    Knutson, S.T.2    Poole, L.B.3    Fetrow, J.S.4
  • 7
    • 67650732916 scopus 로고    scopus 로고
    • Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B
    • Shetty, V., and Neubert, T. A. (2009) Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B. J. Am. Soc. Mass Spectrom. 20, 1540-1548
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1540-1548
    • Shetty, V.1    Neubert, T.A.2
  • 8
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau, B., Labarre, J., and Toledano, M. B. (2003) ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425, 980-984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 9
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins
    • Woo, H. A., Jeong, W., Chang, T. S., Park, K. J., Park, S. J., Yang, J. S., and Rhee, S. G. (2005) Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. J. Biol. Chem. 280, 3125-3128
    • (2005) J. Biol. Chem. , vol.280 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2    Chang, T.S.3    Park, K.J.4    Park, S.J.5    Yang, J.S.6    Rhee, S.G.7
  • 10
    • 38049044980 scopus 로고    scopus 로고
    • Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace
    • Jönsson, T. J., Johnson, L. C., and Lowther, W. T. (2008) Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace. Nature 451, 98-101
    • (2008) Nature , vol.451 , pp. 98-101
    • Jönsson, T.J.1    Johnson, L.C.2    Lowther, W.T.3
  • 11
    • 34548255410 scopus 로고    scopus 로고
    • Recent advances and perspectives in the chemistry of sulfenic acids
    • Aversa, M. C., Barattucci, A., Bonaccorsi, P., and Giannetto, P. (2007) Recent advances and perspectives in the chemistry of sulfenic acids. Curr. Org. Chem. 11, 1034-1052
    • (2007) Curr. Org. Chem. , vol.11 , pp. 1034-1052
    • Aversa, M.C.1    Barattucci, A.2    Bonaccorsi, P.3    Giannetto, P.4
  • 12
    • 40849097418 scopus 로고    scopus 로고
    • Discovering mechanisms of signaling mediated cysteine oxidation
    • Poole, L. B., and Nelson, K. J. (2008) Discovering mechanisms of signaling mediated cysteine oxidation. Curr. Opin. Chem. Biol. 12, 18-24
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 18-24
    • Poole, L.B.1    Nelson, K.J.2
  • 13
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • Reddie, K. G., and Carroll, K. S. (2008) Expanding the functional diversity of proteins through cysteine oxidation. Curr. Opin. Chem. Biol. 12, 746-754
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 15
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207 (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 16
    • 34548175273 scopus 로고    scopus 로고
    • Systemic analysis of tyrosine phosphorylated proteins in angiopoietin-1 induced signaling pathway of endothelial cells
    • DOI 10.1021/pr070168k
    • Kim, Y. M., Seo, J., Kim, Y. H., Jeong, J., Joo, H. J., Lee, D. H., Koh, G. Y., and Lee, K. J. (2007) Systemic analysis of tyrosine phosphorylated proteins in angiopoietin-1 induced signaling pathway of endothelial cells. J. Proteome Res. 6, 3278-3290 (Pubitemid 47310212)
    • (2007) Journal of Proteome Research , vol.6 , Issue.8 , pp. 3278-3290
    • Young, M.K.1    Seo, J.2    Yung, H.K.3    Jeong, J.4    Hye, J.J.5    Lee, D.-H.6    Gou, Y.K.7    Lee, K.-J.8
  • 17
    • 39749099462 scopus 로고    scopus 로고
    • Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: Application to glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1021/pr700657y
    • Seo, J., Jeong, J., Kim, Y. M., Hwang, N., Paek, E., and Lee, K. J. (2008) Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase. J. Proteome Res. 7, 587-602 (Pubitemid 351294021)
    • (2008) Journal of Proteome Research , vol.7 , Issue.2 , pp. 587-602
    • Seo, J.1    Jeong, J.2    Young, M.K.3    Hwang, N.4    Paek, E.5    Lee, K.-J.6
  • 18
    • 73649112404 scopus 로고    scopus 로고
    • New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra
    • Choi, S., Jeong, J., Na, S., Lee, H. S., Kim, H. Y., Lee, K. J., and Paek, E. (2010) New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra. J. Proteome Res. 9, 626-635
    • (2010) J. Proteome Res. , vol.9 , pp. 626-635
    • Choi, S.1    Jeong, J.2    Na, S.3    Lee, H.S.4    Kim, H.Y.5    Lee, K.J.6    Paek, E.7
  • 19
    • 58149307960 scopus 로고    scopus 로고
    • Unrestrictive identification of multiple post-translational modifications from tandem mass spectrometry using an error-tolerant algorithm based on an extended sequence tag approach
    • Na, S., Jeong, J., Park, H., Lee, K. J., and Paek, E. (2008) Unrestrictive identification of multiple post-translational modifications from tandem mass spectrometry using an error-tolerant algorithm based on an extended sequence tag approach. Mol. Cell. Proteomics 7, 2452-2463
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2452-2463
    • Na, S.1    Jeong, J.2    Park, H.3    Lee, K.J.4    Paek, E.5
  • 20
    • 70349974843 scopus 로고    scopus 로고
    • Prediction of novel modifications by unrestrictive search of tandem mass spectra
    • Na, S., and Paek, E. (2009) Prediction of novel modifications by unrestrictive search of tandem mass spectra. J. Proteome Res. 8, 4418-4427
    • (2009) J. Proteome Res. , vol.8 , pp. 4418-4427
    • Na, S.1    Paek, E.2
  • 21
    • 0031592829 scopus 로고    scopus 로고
    • Rapid Purification and Characterization of Nucleoside Diphosphate Kinase Isoforms Using ATP-Sepharose Affinity Column Chromatography
    • Kim, S. Y., Chang, K. H., Doh, H. J., Jung, J. A., Kim, E, Sim, C. J., and Lee, K. J. (1997) Rapid purification and characterization of nucleoside diphosphate kinase isoforms using ATP-sepharose affinity column chromatography. Mol. Cells 7, 630-634 (Pubitemid 127477546)
    • (1997) Molecules and Cells , vol.7 , Issue.5 , pp. 630-634
    • Kim, S.Y.1    Chang, K.H.2    Doh, H.-J.3    Jung, J.A.4    Kim, E.5    Sim, C.J.6    Lee, K.-J.7
  • 22
    • 0034702812 scopus 로고    scopus 로고
    • Oxidative modification of nucleoside diphosphate kinase and its identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • DOI 10.1021/bi000267a
    • Song, E. J., Kim, Y. S., Chung, J. Y., Kim, E., Chae, S. K., and Lee, K. J. (2000) Oxidative modification of nucleoside diphosphate kinase and its identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Biochemistry 39, 10090-10097 (Pubitemid 30663030)
    • (2000) Biochemistry , vol.39 , Issue.33 , pp. 10090-10097
    • Eun, J.S.1    Yang, S.K.2    Ji, Y.C.3    Kim, E.4    Chae, S.-K.5    Lee, K.-J.6
  • 23
    • 20244365497 scopus 로고    scopus 로고
    • P38γ regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP
    • DOI 10.1038/sj.emboj.7600578
    • Sabio, G., Arthur, J. S., Kuma, Y., Peggie, M., Carr, J., Murray-Tait, V., Centeno, F., Goedert, M., Morrice, N. A., and Cuenda, A. (2005) p38γ regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP free Guadalupe. EMBO J. 24, 1134-1145 (Pubitemid 40516597)
    • (2005) EMBO Journal , vol.24 , Issue.6 , pp. 1134-1145
    • Sabio, G.1    Arthur, J.S.C.2    Kuma, Y.3    Peggie, M.4    Carr, J.5    Murray-Tait, V.6    Centeno, F.7    Goedert, M.8    Morrice, N.A.9    Cuenda, A.10
  • 24
    • 71049133596 scopus 로고    scopus 로고
    • Multiple functions of Nm23-H1 are regulated by oxido-reduction system
    • Lee, E., Jeong, J., Kim, S. E., Song, E. J., Kang, S. W., and Lee, K. J. (2009) Multiple functions of Nm23-H1 are regulated by oxido-reduction system. PLoS ONE 4, e7949
    • (2009) PLoS ONE , vol.4
    • Lee, E.1    Jeong, J.2    Kim, S.E.3    Song, E.J.4    Kang, S.W.5    Lee, K.J.6
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 70350091586 scopus 로고    scopus 로고
    • Oxidative modifications of glyceraldehyde-3-phosphate dehydrogenase play a key role in its multiple cellular functions
    • Hwang, N. R., Yim, S. H., Kim, Y. M., Jeong, J., Song, E. J., Lee, Y., Lee, J. H., Choi, S., and Lee, K. J. (2009) Oxidative modifications of glyceraldehyde-3-phosphate dehydrogenase play a key role in its multiple cellular functions. Biochem. J. 423, 253-264
    • (2009) Biochem. J. , vol.423 , pp. 253-264
    • Hwang, N.R.1    Yim, S.H.2    Kim, Y.M.3    Jeong, J.4    Song, E.J.5    Lee, Y.6    Lee, J.H.7    Choi, S.8    Lee, K.J.9
  • 27
    • 0035565633 scopus 로고    scopus 로고
    • Similarity between condensed phase and gas phase chemistry: Fragmentation of peptides containing oxidized cysteine residues and its implications for proteomics
    • Steen, H., and Mann, M. (2001) Similarity between condensed phase and gas phase chemistry: fragmentation of peptides containing oxidized cysteine residues and its implications for proteomics. J. Am. Soc. Mass Spectrom. 12, 228-232
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 228-232
    • Steen, H.1    Mann, M.2
  • 28
    • 84954586181 scopus 로고
    • Substitution of arylsulfonyl imidazolides by hydrogen peroxide: Aryl sulfonic peracis as oxidants for olefins
    • Schulz, M., Kluge, R., and Lipke, M. (1993) Substitution of arylsulfonyl imidazolides by hydrogen peroxide: aryl sulfonic peracis as oxidants for olefins. Synlett. 915-918
    • (1993) Synlett. , pp. 915-918
    • Schulz, M.1    Kluge, R.2    Lipke, M.3
  • 29
    • 70349406739 scopus 로고    scopus 로고
    • Facile formation of dehydroalanine from S-nitrosocysteins
    • Wang, H., Zang, Z., and Xian, M. (2009) Facile formation of dehydroalanine from S-nitrosocysteins. J. Am. Chem. Soc. 131, 13238-13239
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13238-13239
    • Wang, H.1    Zang, Z.2    Xian, M.3
  • 31
    • 0000542759 scopus 로고
    • Electrophilic sulfur transfer reactions in organic synthesis. Preparation of a diastereomer of the key macrocyclic component of griseoviridin
    • Liu, L., Tanke, R. S., and Miller, M. J. (1986) Electrophilic sulfur transfer reactions in organic synthesis. Preparation of a diastereomer of the key macrocyclic component of griseoviridin. J. Org. Chem. 51, 5332-5337
    • (1986) J. Org. Chem. , vol.51 , pp. 5332-5337
    • Liu, L.1    Tanke, R.S.2    Miller, M.J.3
  • 32
    • 64149109414 scopus 로고    scopus 로고
    • Efficient substitution reaction from cysteine to the serine residue of glycosylated polypeptide: Repetitive petide segment ligation strategy and the synthesis of glycosylated tetracontapeptide having acid libile sialyl-Tn antigens
    • Okamoto, R., Soumura, S., and Kajihara, Y. (2009) Efficient substitution reaction from cysteine to the serine residue of glycosylated polypeptide: repetitive petide segment ligation strategy and the synthesis of glycosylated tetracontapeptide having acid libile sialyl-Tn antigens. J. Org. Chem. 74, 2494-2501
    • (2009) J. Org. Chem. , vol.74 , pp. 2494-2501
    • Okamoto, R.1    Soumura, S.2    Kajihara, Y.3
  • 33
    • 0141510042 scopus 로고    scopus 로고
    • Regeneration of peroxiredoxins during recovery after oxidative stress: Only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress
    • Chevallet, M., Wagner, E., Luche, S., van Dorsselaer, A., Leize-Wagner, E., and Rabilloud, T. (2003) Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress. J. Biol. Chem. 278, 37146-37153
    • (2003) J. Biol. Chem. , vol.278 , pp. 37146-37153
    • Chevallet, M.1    Wagner, E.2    Luche, S.3    Van Dorsselaer, A.4    Leize-Wagner, E.5    Rabilloud, T.6
  • 34
    • 0037106326 scopus 로고    scopus 로고
    • A method for detection of overoxidation of cysteines: Peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress
    • Wagner, E., Luche, S., Penna, L., Chevallet, M., Van Dorsselaer, A., Leize- Wagner, E., and Rabilloud, T. (2002) A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. Biochem. J. 366, 777-785
    • (2002) Biochem. J. , vol.366 , pp. 777-785
    • Wagner, E.1    Luche, S.2    Penna, L.3    Chevallet, M.4    Van Dorsselaer, A.5    Leize-Wagner, E.6    Rabilloud, T.7
  • 35
  • 36
    • 70450240741 scopus 로고    scopus 로고
    • Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin
    • Roussel, X., Kriznik, A., Richard, C., Rahuel-Clermont, S., and Branlant, G. (2009) Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin. J. Biol. Chem. 284, 33048-33055
    • (2009) J. Biol. Chem. , vol.284 , pp. 33048-33055
    • Roussel, X.1    Kriznik, A.2    Richard, C.3    Rahuel-Clermont, S.4    Branlant, G.5
  • 37
    • 63049086405 scopus 로고    scopus 로고
    • Artifactual sulfation of silver-stained proteins: Implications for the assignment of phosphorylation and sulfation sites
    • Gharib, M., Marcantonio, M., Lehmann, S. G., Courcelles, M., Meloche, S., Verreault, A., and Thibault, P. (2009) Artifactual sulfation of silver-stained proteins: Implications for the assignment of phosphorylation and sulfation sites. Mol. Cell. Proteomics 8, 506-518
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 506-518
    • Gharib, M.1    Marcantonio, M.2    Lehmann, S.G.3    Courcelles, M.4    Meloche, S.5    Verreault, A.6    Thibault, P.7
  • 39
    • 33846635882 scopus 로고    scopus 로고
    • High-throughput identification of catalytic redox-active cysteine Residues
    • Fomenko, D. E., Xing, W., Adair, B. M., Thomas, D. J., and Gladyshev, V. N. (2007) High-throughput identification of catalytic redox-active cysteine Residues. Science. 315, 387-389
    • (2007) Science , vol.315 , pp. 387-389
    • Fomenko, D.E.1    Xing, W.2    Adair, B.M.3    Thomas, D.J.4    Gladyshev, V.N.5


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