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Volumn 1844, Issue 12, 2014, Pages 2315-2330

Chemical-proteomic strategies to investigate cysteine posttranslational modifications

Author keywords

Glutathionylation; Lipid derived electrophile; Nitrosation; Oxidation; Palmitoylation; Prenylation

Indexed keywords

ANTIBODY; BIOTIN; CYSTEINE; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE ANTIBODY; ISOPRENE; NUCLEOPHILE; SULFENIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84908193840     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.09.024     Document Type: Review
Times cited : (59)

References (189)
  • 1
    • 84874081337 scopus 로고    scopus 로고
    • Diverse functional roles of reactive cysteines
    • N.J. Pace, and E. Weerapana Diverse functional roles of reactive cysteines ACS Chem. Biol. 8 2013 283 296
    • (2013) ACS Chem. Biol. , vol.8 , pp. 283-296
    • Pace, N.J.1    Weerapana, E.2
  • 2
    • 84906365698 scopus 로고
    • Dissociation constants of cystine, cysteine, thioglycollic acid and alpha-thiolactic acid
    • R.K. Cannan, and B.C. Knight Dissociation constants of cystine, cysteine, thioglycollic acid and alpha-thiolactic acid Biochem. J. 21 1927 1384 1390
    • (1927) Biochem. J. , vol.21 , pp. 1384-1390
    • Cannan, R.K.1    Knight, B.C.2
  • 3
    • 0023654889 scopus 로고
    • Identification and reactivity of the catalytic site of pig liver thioltransferase
    • Z.R. Gan, and W.W. Wells Identification and reactivity of the catalytic site of pig liver thioltransferase J. Biol. Chem. 262 1987 6704 6707
    • (1987) J. Biol. Chem. , vol.262 , pp. 6704-6707
    • Gan, Z.R.1    Wells, W.W.2
  • 4
    • 0025788552 scopus 로고
    • Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis
    • Y.F. Yang, and W.W. Wells Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis J. Biol. Chem. 266 1991 12759 12765
    • (1991) J. Biol. Chem. , vol.266 , pp. 12759-12765
    • Yang, Y.F.1    Wells, W.W.2
  • 5
    • 84883674898 scopus 로고    scopus 로고
    • The redox biochemistry of protein sulfenylation and sulfinylation
    • M. Lo Conte, and K.S. Carroll The redox biochemistry of protein sulfenylation and sulfinylation J. Biol. Chem. 288 2013 26480 26488
    • (2013) J. Biol. Chem. , vol.288 , pp. 26480-26488
    • Lo Conte, M.1    Carroll, K.S.2
  • 6
    • 84884194110 scopus 로고    scopus 로고
    • Regulation of protein function and signaling by reversible cysteine S-nitrosylation
    • N. Gould, P.T. Doulias, M. Tenopoulou, K. Raju, and H. Ischiropoulos Regulation of protein function and signaling by reversible cysteine S-nitrosylation J. Biol. Chem. 288 2013 26473 26479
    • (2013) J. Biol. Chem. , vol.288 , pp. 26473-26479
    • Gould, N.1    Doulias, P.T.2    Tenopoulou, M.3    Raju, K.4    Ischiropoulos, H.5
  • 7
    • 78649484651 scopus 로고    scopus 로고
    • Control of mature protein function by allosteric disulfide bonds
    • I. Azimi, J.W. Wong, and P.J. Hogg Control of mature protein function by allosteric disulfide bonds Antioxid. Redox Signal. 14 2011 113 126
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 113-126
    • Azimi, I.1    Wong, J.W.2    Hogg, P.J.3
  • 11
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • F.L. Zhang, and P.J. Casey Protein prenylation: molecular mechanisms and functional consequences Annu. Rev. Biochem. 65 1996 241 269
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 12
    • 84872539180 scopus 로고    scopus 로고
    • Fat chance! Getting a grip on a slippery modification
    • C.T. Tom, and B.R. Martin Fat chance! Getting a grip on a slippery modification ACS Chem. Biol. 8 2013 46 57
    • (2013) ACS Chem. Biol. , vol.8 , pp. 46-57
    • Tom, C.T.1    Martin, B.R.2
  • 13
    • 84888602175 scopus 로고    scopus 로고
    • Orphan PTMs: Rare, yet functionally important modifications of cysteine
    • D.A. Shannon, and E. Weerapana Orphan PTMs: Rare, yet functionally important modifications of cysteine Biopolymers 101 2013 156 164
    • (2013) Biopolymers , vol.101 , pp. 156-164
    • Shannon, D.A.1    Weerapana, E.2
  • 15
    • 79251614656 scopus 로고    scopus 로고
    • Cysteine/cystine redox signaling in cardiovascular disease
    • Y.M. Go, and D.P. Jones Cysteine/cystine redox signaling in cardiovascular disease Free Radic. Biol. Med. 50 2011 495 509
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 495-509
    • Go, Y.M.1    Jones, D.P.2
  • 16
    • 84859341928 scopus 로고    scopus 로고
    • Targeting protein lipidation in disease
    • M.D. Resh Targeting protein lipidation in disease Trends Mol. Med. 18 2012 206 214
    • (2012) Trends Mol. Med. , vol.18 , pp. 206-214
    • Resh, M.D.1
  • 17
    • 84868622900 scopus 로고    scopus 로고
    • Chasing cysteine oxidative modifications: Proteomic tools for characterizing cysteine redox status
    • C.I. Murray, and J.E. Van Eyk Chasing cysteine oxidative modifications: proteomic tools for characterizing cysteine redox status Circ. Cardiovasc. Genet. 5 2012 591
    • (2012) Circ. Cardiovasc. Genet. , vol.5 , pp. 591
    • Murray, C.I.1    Van Eyk, J.E.2
  • 19
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • K.G. Reddie, and K.S. Carroll Expanding the functional diversity of proteins through cysteine oxidation Curr. Opin. Chem. Biol. 12 2008 746 754
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 20
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. Cerevisiae sulphiredoxin
    • B. Biteau, J. Labarre, and M.B. Toledano ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin Nature 425 2003 980 984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 21
    • 40849097418 scopus 로고    scopus 로고
    • Discovering mechanisms of signaling-mediated cysteine oxidation
    • L.B. Poole, and K.J. Nelson Discovering mechanisms of signaling-mediated cysteine oxidation Curr. Opin. Chem. Biol. 12 2008 18 24
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 18-24
    • Poole, L.B.1    Nelson, K.J.2
  • 23
    • 0037036358 scopus 로고    scopus 로고
    • Reversible inactivation of the tumor suppressor PTEN by H2O2
    • S.R. Lee, K.S. Yang, J. Kwon, C. Lee, W. Jeong, and S.G. Rhee Reversible inactivation of the tumor suppressor PTEN by H2O2 J. Biol. Chem. 277 2002 20336 20342
    • (2002) J. Biol. Chem. , vol.277 , pp. 20336-20342
    • Lee, S.R.1    Yang, K.S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 24
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • A. Salmeen, J.N. Andersen, M.P. Myers, T.C. Meng, J.A. Hinks, N.K. Tonks, and D. Barford Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate Nature 423 2003 769 773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 27
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • L.I. Leichert, and U. Jakob Protein thiol modifications visualized in vivo Plos Biol. 2 2004 1723 1737
    • (2004) Plos Biol. , vol.2 , pp. 1723-1737
    • Leichert, L.I.1    Jakob, U.2
  • 28
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • J.W. Baty, M.B. Hampton, and C.C. Winterbourn Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis Proteomics 2 2002 1261 1266
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 29
    • 26944462004 scopus 로고    scopus 로고
    • Fluorescence thiol modification assay: Oxidatively modified proteins in Bacillus subtilis
    • F. Hochgrafe, J. Mostertz, D. Albrecht, and M. Hecker Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis Mol. Microbiol. 58 2005 409 425
    • (2005) Mol. Microbiol. , vol.58 , pp. 409-425
    • Hochgrafe, F.1    Mostertz, J.2    Albrecht, D.3    Hecker, M.4
  • 31
    • 0033567060 scopus 로고    scopus 로고
    • A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry
    • E.B. Getz, M. Xiao, T. Chakrabarty, R. Cooke, and P.R. Selvin A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry Anal. Biochem. 273 1999 73 80
    • (1999) Anal. Biochem. , vol.273 , pp. 73-80
    • Getz, E.B.1    Xiao, M.2    Chakrabarty, T.3    Cooke, R.4    Selvin, P.R.5
  • 33
    • 34547592709 scopus 로고    scopus 로고
    • Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: Implications for mitochondrial redox signaling
    • T.R. Hurd, T.A. Prime, M.E. Harbour, K.S. Lilley, and M.P. Murphy Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling J. Biol. Chem. 282 2007 22040 22051
    • (2007) J. Biol. Chem. , vol.282 , pp. 22040-22051
    • Hurd, T.R.1    Prime, T.A.2    Harbour, M.E.3    Lilley, K.S.4    Murphy, M.P.5
  • 34
    • 59249084350 scopus 로고    scopus 로고
    • Protein-thiol oxidation, from single proteins to proteome-wide analyses
    • N. Le Moan, F. Tacnet, and M.B. Toledano Protein-thiol oxidation, from single proteins to proteome-wide analyses Methods Mol. Biol. 476 2008 181 198
    • (2008) Methods Mol. Biol. , vol.476 , pp. 181-198
    • Le Moan, N.1    Tacnet, F.2    Toledano, M.B.3
  • 35
    • 82355181024 scopus 로고    scopus 로고
    • Thiol redox proteomics seen with fluorescent eyes: The detection of cysteine oxidative modifications by fluorescence derivatization and 2-DE
    • A. Izquierdo-Alvarez, and A. Martinez-Ruiz Thiol redox proteomics seen with fluorescent eyes: the detection of cysteine oxidative modifications by fluorescence derivatization and 2-DE J. Proteomics 75 2011 329 338
    • (2011) J. Proteomics , vol.75 , pp. 329-338
    • Izquierdo-Alvarez, A.1    Martinez-Ruiz, A.2
  • 37
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • S.P. Gygi, B. Rist, S.A. Gerber, F. Turecek, M.H. Gelb, and R. Aebersold Quantitative analysis of complex protein mixtures using isotope-coded affinity tags Nat. Biotechnol. 17 1999 994 999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 38
    • 2642576571 scopus 로고    scopus 로고
    • Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols
    • M. Sethuraman, M.E. McComb, T. Heibeck, C.E. Costello, and R.A. Cohen Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols Mol. Cell. Proteomics 3 2004 273 278
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 273-278
    • Sethuraman, M.1    McComb, M.E.2    Heibeck, T.3    Costello, C.E.4    Cohen, R.A.5
  • 39
    • 11144252625 scopus 로고    scopus 로고
    • Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures
    • M. Sethuraman, M.E. McComb, H. Huang, S. Huang, T. Heibeck, C.E. Costello, and R.A. Cohen Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures J. Proteome Res. 3 2004 1228 1233
    • (2004) J. Proteome Res. , vol.3 , pp. 1228-1233
    • Sethuraman, M.1    McComb, M.E.2    Huang, H.3    Huang, S.4    Heibeck, T.5    Costello, C.E.6    Cohen, R.A.7
  • 41
    • 80054858298 scopus 로고    scopus 로고
    • The oxidized thiol proteome in fission yeast - Optimization of an ICAT-based method to identify H2O2-oxidized proteins
    • S. Garcia-Santamarina, S. Boronat, G. Espadas, J. Ayte, H. Molina, and E. Hidalgo The oxidized thiol proteome in fission yeast - optimization of an ICAT-based method to identify H2O2-oxidized proteins J. Proteomics 74 2011 2476 2486
    • (2011) J. Proteomics , vol.74 , pp. 2476-2486
    • Garcia-Santamarina, S.1    Boronat, S.2    Espadas, G.3    Ayte, J.4    Molina, H.5    Hidalgo, E.6
  • 42
    • 84899542656 scopus 로고    scopus 로고
    • Monitoring in vivo reversible cysteine oxidation in proteins using ICAT and mass spectrometry
    • S. Garcia-Santamarina, S. Boronat, A. Domenech, J. Ayte, H. Molina, and E. Hidalgo Monitoring in vivo reversible cysteine oxidation in proteins using ICAT and mass spectrometry Nat. Protoc. 9 2014 1131 1145
    • (2014) Nat. Protoc. , vol.9 , pp. 1131-1145
    • Garcia-Santamarina, S.1    Boronat, S.2    Domenech, A.3    Ayte, J.4    Molina, H.5    Hidalgo, E.6
  • 45
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • A.T. Saurin, H. Neubert, J.P. Brennan, and P. Eaton Widespread sulfenic acid formation in tissues in response to hydrogen peroxide Proc. Natl. Acad. Sci. U. S. A. 101 2004 17982 17987
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17982-17987
    • Saurin, A.T.1    Neubert, H.2    Brennan, J.P.3    Eaton, P.4
  • 48
    • 84890120403 scopus 로고
    • Sulfenic acid chemistry, detection and cellular lifetime
    • V. Gupta, and K.S. Carroll Sulfenic acid chemistry, detection and cellular lifetime Biochim. Biophys. Acta Gen. Subj. 2014 1840 847 875
    • (1840) Biochim. Biophys. Acta Gen. Subj. , vol.2014 , pp. 847-875
    • Gupta, V.1    Carroll, K.S.2
  • 49
    • 27944488351 scopus 로고    scopus 로고
    • Synthesis of chemical probes to map sulfenic acid modifications on proteins
    • L.B. Poole, B.B. Zeng, S.A. Knaggs, M. Yakubu, and S.B. King Synthesis of chemical probes to map sulfenic acid modifications on proteins Bioconjug. Chem. 16 2005 1624 1628
    • (2005) Bioconjug. Chem. , vol.16 , pp. 1624-1628
    • Poole, L.B.1    Zeng, B.B.2    Knaggs, S.A.3    Yakubu, M.4    King, S.B.5
  • 50
    • 84888301385 scopus 로고    scopus 로고
    • Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids
    • J.A. Reisz, E. Bechtold, S.B. King, L.B. Poole, and C.M. Furdui Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids FEBS J. 280 2013 6150 6161
    • (2013) FEBS J. , vol.280 , pp. 6150-6161
    • Reisz, J.A.1    Bechtold, E.2    King, S.B.3    Poole, L.B.4    Furdui, C.M.5
  • 51
    • 43949085368 scopus 로고    scopus 로고
    • A chemical approach for detecting sulfenic acid-modified proteins in living cells
    • K.G. Reddie, Y.H. Seo, W.B. Muse Iii, S.E. Leonard, and K.S. Carroll A chemical approach for detecting sulfenic acid-modified proteins in living cells Mol. Biosyst. 4 2008 521 531
    • (2008) Mol. Biosyst. , vol.4 , pp. 521-531
    • Reddie, K.G.1    Seo, Y.H.2    Muse, W.B.3    Leonard, S.E.4    Carroll, K.S.5
  • 52
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells
    • S.E. Leonard, K.G. Reddie, and K.S. Carroll Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells ACS Chem. Biol. 4 2009 783 799
    • (2009) ACS Chem. Biol. , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 54
    • 79551676040 scopus 로고    scopus 로고
    • Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone
    • Y.H. Seo, and K.S. Carroll Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone Angew. Chem. Int. Ed. Engl. 50 2011 1342 1345
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 1342-1345
    • Seo, Y.H.1    Carroll, K.S.2
  • 55
    • 84894259397 scopus 로고    scopus 로고
    • Inductively coupled plasma mass spectrometry-based method for the specific quantification of sulfenic acid in peptides and proteins
    • A.H. El-Khatib, D. Esteban-Fernandez, and M.W. Linscheid Inductively coupled plasma mass spectrometry-based method for the specific quantification of sulfenic acid in peptides and proteins Anal. Chem. 86 2014 1943 1948
    • (2014) Anal. Chem. , vol.86 , pp. 1943-1948
    • El-Khatib, A.H.1    Esteban-Fernandez, D.2    Linscheid, M.W.3
  • 59
  • 60
    • 84861182619 scopus 로고    scopus 로고
    • S-Glutathionylation signaling in cell biology: Progress and prospects
    • A. Pastore, and F. Piemonte S-Glutathionylation signaling in cell biology: progress and prospects Eur. J. Pharm. Sci. 46 2012 279 292
    • (2012) Eur. J. Pharm. Sci. , vol.46 , pp. 279-292
    • Pastore, A.1    Piemonte, F.2
  • 64
    • 65249182226 scopus 로고    scopus 로고
    • Methods for analysis of protein glutathionylation and their application to photosynthetic organisms
    • X.H. Gao, M. Bedhomme, D. Veyel, M. Zaffagnini, and S.D. Lemaire Methods for analysis of protein glutathionylation and their application to photosynthetic organisms Mol. Plant 2 2009 218 235
    • (2009) Mol. Plant , vol.2 , pp. 218-235
    • Gao, X.H.1    Bedhomme, M.2    Veyel, D.3    Zaffagnini, M.4    Lemaire, S.D.5
  • 66
    • 84864285556 scopus 로고    scopus 로고
    • H(2)S signalling through protein sulfhydration and beyond
    • B.D. Paul, and S.H. Snyder H(2)S signalling through protein sulfhydration and beyond Nat. Rev. Mol. Cell Biol. 13 2012 499 507
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 499-507
    • Paul, B.D.1    Snyder, S.H.2
  • 68
    • 84879776406 scopus 로고    scopus 로고
    • Persulfide reactivity in the detection of protein s-sulfhydration
    • J. Pan, and K.S. Carroll Persulfide reactivity in the detection of protein s-sulfhydration ACS Chem. Biol. 8 2013 1110 1116
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1110-1116
    • Pan, J.1    Carroll, K.S.2
  • 69
    • 0026004924 scopus 로고
    • Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages
    • K. Rokutan, J.A. Thomas, and R.B. Johnston Jr. Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages J. Immunol. 147 1991 260 264
    • (1991) J. Immunol. , vol.147 , pp. 260-264
    • Rokutan, K.1    Thomas, J.A.2    Johnston, R.B.3
  • 70
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • V. Ravichandran, T. Seres, T. Moriguchi, J.A. Thomas, and R.B. Johnston Jr. S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes J. Biol. Chem. 269 1994 25010 25015
    • (1994) J. Biol. Chem. , vol.269 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston, R.B.5
  • 72
    • 0034641689 scopus 로고    scopus 로고
    • Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation
    • D.M. Sullivan, N.B. Wehr, M.M. Fergusson, R.L. Levine, and T. Finkel Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation Biochemistry 39 2000 11121 11128
    • (2000) Biochemistry , vol.39 , pp. 11121-11128
    • Sullivan, D.M.1    Wehr, N.B.2    Fergusson, M.M.3    Levine, R.L.4    Finkel, T.5
  • 73
    • 84895813462 scopus 로고    scopus 로고
    • CO-releasing molecules and increased heme oxygenase-1 induce protein S-glutathionylation to modulate NF-kappaB activity in endothelial cells
    • P.Y. Yeh, C.Y. Li, C.W. Hsieh, Y.C. Yang, P.M. Yang, and B.S. Wung CO-releasing molecules and increased heme oxygenase-1 induce protein S-glutathionylation to modulate NF-kappaB activity in endothelial cells Free Radic. Biol. Med. 70 2014 1 13
    • (2014) Free Radic. Biol. Med. , vol.70 , pp. 1-13
    • Yeh, P.Y.1    Li, C.Y.2    Hsieh, C.W.3    Yang, Y.C.4    Yang, P.M.5    Wung, B.S.6
  • 74
    • 84906347101 scopus 로고    scopus 로고
    • Metabolic synthesis of clickable glutathione for chemoselective detection of glutathionylation
    • K.T. Samarasinghe, D.N. Munkanatta Godage, G.C. VanHecke, and Y.H. Ahn Metabolic synthesis of clickable glutathione for chemoselective detection of glutathionylation J. Am. Chem. Soc. 136 2014 11566 11569
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 11566-11569
    • Samarasinghe, K.T.1    Munkanatta Godage, D.N.2    Vanhecke, G.C.3    Ahn, Y.H.4
  • 75
    • 2642673620 scopus 로고    scopus 로고
    • Isolation of anti-glutathione antibodies from a phage display library
    • M. Hirose, T. Hayano, H. Shirai, H. Nakamura, and M. Kikuchi Isolation of anti-glutathione antibodies from a phage display library Protein Eng. 11 1998 243 248
    • (1998) Protein Eng. , vol.11 , pp. 243-248
    • Hirose, M.1    Hayano, T.2    Shirai, H.3    Nakamura, H.4    Kikuchi, M.5
  • 76
    • 12844254556 scopus 로고    scopus 로고
    • Detection of S-glutathionylated proteins by glutathione S-transferase overlay
    • G. Cheng, Y. Ikeda, Y. Iuchi, and J. Fujii Detection of S-glutathionylated proteins by glutathione S-transferase overlay Arch. Biochem. Biophys. 435 2005 42 49
    • (2005) Arch. Biochem. Biophys. , vol.435 , pp. 42-49
    • Cheng, G.1    Ikeda, Y.2    Iuchi, Y.3    Fujii, J.4
  • 77
    • 84875720244 scopus 로고    scopus 로고
    • Glutaredoxins in thiol/disulfide exchange
    • C.H. Lillig, and C. Berndt Glutaredoxins in thiol/disulfide exchange Antioxid. Redox Signal. 18 2013 1654 1665
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 1654-1665
    • Lillig, C.H.1    Berndt, C.2
  • 78
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • C. Lind, R. Gerdes, Y. Hamnell, I. Schuppe-Koistinen, H.B. von Lowenhielm, A. Holmgren, and I.A. Cotgreave Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis Arch. Biochem. Biophys. 406 2002 229 240
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    Von Lowenhielm, H.B.5    Holmgren, A.6    Cotgreave, I.A.7
  • 79
    • 84872277775 scopus 로고    scopus 로고
    • Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling
    • B.C. Smith, and M.A. Marletta Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling Curr. Opin. Chem. Biol. 16 2012 498 506
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 498-506
    • Smith, B.C.1    Marletta, M.A.2
  • 84
    • 73649121243 scopus 로고    scopus 로고
    • Structural analysis of cysteine S-nitrosylation: A modified acid-based motif and the emerging role of trans-nitrosylation
    • S.M. Marino, and V.N. Gladyshev Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation J. Mol. Biol. 395 2010 844 859
    • (2010) J. Mol. Biol. , vol.395 , pp. 844-859
    • Marino, S.M.1    Gladyshev, V.N.2
  • 85
    • 78049288138 scopus 로고    scopus 로고
    • Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation
    • P.T. Doulias, J.L. Greene, T.M. Greco, M. Tenopoulou, S.H. Seeholzer, R.L. Dunbrack, and H. Ischiropoulos Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation Proc. Natl. Acad. Sci. U. S. A. 107 2010 16958 16963
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 16958-16963
    • Doulias, P.T.1    Greene, J.L.2    Greco, T.M.3    Tenopoulou, M.4    Seeholzer, S.H.5    Dunbrack, R.L.6    Ischiropoulos, H.7
  • 86
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • M. Benhar, M.T. Forrester, D.T. Hess, and J.S. Stamler Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins Science 320 2008 1050 1054
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 87
    • 34547427294 scopus 로고    scopus 로고
    • Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells
    • D.A. Mitchell, S.U. Morton, N.B. Fernhoff, and M.A. Marletta Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells Proc. Natl. Acad. Sci. U. S. A. 104 2007 11609 11614
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 11609-11614
    • Mitchell, D.A.1    Morton, S.U.2    Fernhoff, N.B.3    Marletta, M.A.4
  • 90
    • 84888594209 scopus 로고    scopus 로고
    • Strategies for profiling native S-nitrosylation
    • J.D. Majmudar, and B.R. Martin Strategies for profiling native S-nitrosylation Biopolymers 101 2013 173 179
    • (2013) Biopolymers , vol.101 , pp. 173-179
    • Majmudar, J.D.1    Martin, B.R.2
  • 92
    • 0032080124 scopus 로고    scopus 로고
    • Development of chemiluminescence-based methods for specific quantitation of nitrosylated thiols
    • A. Samouilov, and J.L. Zweier Development of chemiluminescence-based methods for specific quantitation of nitrosylated thiols Anal. Biochem. 258 1998 322 330
    • (1998) Anal. Biochem. , vol.258 , pp. 322-330
    • Samouilov, A.1    Zweier, J.L.2
  • 93
    • 84864627599 scopus 로고    scopus 로고
    • Chemical methods for the direct detection and labeling of S-nitrosothiols
    • E. Bechtold, and S.B. King Chemical methods for the direct detection and labeling of S-nitrosothiols Antioxid. Redox Signal. 17 2012 981 991
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 981-991
    • Bechtold, E.1    King, S.B.2
  • 95
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • S.R. Jaffrey, and S.H. Snyder The biotin switch method for the detection of S-nitrosylated proteins Sci. STKE 2001 2001 pl1
    • (2001) Sci. STKE , vol.2001 , pp. 1
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 96
    • 78649889548 scopus 로고    scopus 로고
    • S-alkylating labeling strategy for site-specific identification of the s-nitrosoproteome
    • Y.J. Chen, W.C. Ku, P.Y. Lin, H.C. Chou, and K.H. Khoo S-alkylating labeling strategy for site-specific identification of the s-nitrosoproteome J. Proteome Res. 9 2010 6417 6439
    • (2010) J. Proteome Res. , vol.9 , pp. 6417-6439
    • Chen, Y.J.1    Ku, W.C.2    Lin, P.Y.3    Chou, H.C.4    Khoo, K.H.5
  • 97
    • 77954142212 scopus 로고    scopus 로고
    • Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP)
    • B. Huang, and C. Chen Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP) Free Radic. Biol. Med. 49 2010 447 456
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 447-456
    • Huang, B.1    Chen, C.2
  • 98
    • 32244445145 scopus 로고    scopus 로고
    • SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures
    • G. Hao, B. Derakhshan, L. Shi, F. Campagne, and S.S. Gross SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures Proc. Natl. Acad. Sci. U. S. A. 103 2006 1012 1017
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 1012-1017
    • Hao, G.1    Derakhshan, B.2    Shi, L.3    Campagne, F.4    Gross, S.S.5
  • 100
    • 84934442218 scopus 로고    scopus 로고
    • Simultaneous identification and quantification of nitrosylation sites by combination of biotin switch and ICAT labeling
    • A. Fares, C. Nespoulous, M. Rossignol, and J.B. Peltier Simultaneous identification and quantification of nitrosylation sites by combination of biotin switch and ICAT labeling Methods Mol. Biol. 1072 2014 609 620
    • (2014) Methods Mol. Biol. , vol.1072 , pp. 609-620
    • Fares, A.1    Nespoulous, C.2    Rossignol, M.3    Peltier, J.B.4
  • 101
    • 84881488174 scopus 로고    scopus 로고
    • Quantification of mitochondrial S-nitrosylation by CysTMT(6) switch assay
    • C.I. Murray, H.S. Chung, H. Uhrigshardt, and J.E. Van Eyk Quantification of mitochondrial S-nitrosylation by CysTMT(6) switch assay Methods Mol. Biol. 1005 2013 169 179
    • (2013) Methods Mol. Biol. , vol.1005 , pp. 169-179
    • Murray, C.I.1    Chung, H.S.2    Uhrigshardt, H.3    Van Eyk, J.E.4
  • 102
    • 77955576782 scopus 로고    scopus 로고
    • Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach
    • M. Benhar, J.W. Thompson, M.A. Moseley, and J.S. Stamler Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach Biochemistry 49 2010 6963 6969
    • (2010) Biochemistry , vol.49 , pp. 6963-6969
    • Benhar, M.1    Thompson, J.W.2    Moseley, M.A.3    Stamler, J.S.4
  • 104
    • 84856717563 scopus 로고    scopus 로고
    • Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay
    • (M111 013441)
    • C.I. Murray, H. Uhrigshardt, R.N. O'Meally, R.N. Cole, and J.E. Van Eyk Identification and quantification of S-nitrosylation by cysteine reactive tandem mass tag switch assay Mol. Cell. Proteomics 11 2012 (M111 013441)
    • (2012) Mol. Cell. Proteomics , vol.11
    • Murray, C.I.1    Uhrigshardt, H.2    O'Meally, R.N.3    Cole, R.N.4    Van Eyk, J.E.5
  • 105
    • 77955492720 scopus 로고    scopus 로고
    • Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): Implications for the regulation of mitochondrial function by reversible S-nitrosation
    • E.T. Chouchani, T.R. Hurd, S.M. Nadtochiy, P.S. Brookes, I.M. Fearnley, K.S. Lilley, R.A. Smith, and M.P. Murphy Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation Biochem. J. 430 2010 49 59
    • (2010) Biochem. J. , vol.430 , pp. 49-59
    • Chouchani, E.T.1    Hurd, T.R.2    Nadtochiy, S.M.3    Brookes, P.S.4    Fearnley, I.M.5    Lilley, K.S.6    Smith, R.A.7    Murphy, M.P.8
  • 106
    • 73249139291 scopus 로고    scopus 로고
    • A "fluorescence switch" technique increases the sensitivity of proteomic detection and identification of S-nitrosylated proteins
    • D. Tello, C. Tarin, P. Ahicart, R. Breton-Romero, S. Lamas, and A. Martinez-Ruiz A "fluorescence switch" technique increases the sensitivity of proteomic detection and identification of S-nitrosylated proteins Proteomics 9 2009 5359 5370
    • (2009) Proteomics , vol.9 , pp. 5359-5370
    • Tello, D.1    Tarin, C.2    Ahicart, P.3    Breton-Romero, R.4    Lamas, S.5    Martinez-Ruiz, A.6
  • 107
    • 0034256633 scopus 로고    scopus 로고
    • Reaction of ascorbic acid with S-nitrosothiols: Clear evidence for two distinct reaction pathways
    • A.J. Holmes, and D.L.H. Williams Reaction of ascorbic acid with S-nitrosothiols: clear evidence for two distinct reaction pathways J. Chem. Soc. Perkin Trans. 2 2000 1639 1644
    • (2000) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1639-1644
    • Holmes, A.J.1    Williams, D.L.H.2
  • 109
    • 33746070773 scopus 로고    scopus 로고
    • An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
    • B. Huang, and C. Chen An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay Free Radic. Biol. Med. 41 2006 562 567
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 562-567
    • Huang, B.1    Chen, C.2
  • 110
    • 34347268109 scopus 로고    scopus 로고
    • Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress
    • M.T. Forrester, M.W. Foster, and J.S. Stamler Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress J. Biol. Chem. 282 2007 13977 13983
    • (2007) J. Biol. Chem. , vol.282 , pp. 13977-13983
    • Forrester, M.T.1    Foster, M.W.2    Stamler, J.S.3
  • 111
    • 84873735581 scopus 로고    scopus 로고
    • RBC-NOS-dependent S-nitrosylation of cytoskeletal proteins improves RBC deformability
    • M. Grau, S. Pauly, J. Ali, K. Walpurgis, M. Thevis, W. Bloch, and F. Suhr RBC-NOS-dependent S-nitrosylation of cytoskeletal proteins improves RBC deformability PLoS One 8 2013 e56759
    • (2013) PLoS One , vol.8 , pp. 56759
    • Grau, M.1    Pauly, S.2    Ali, J.3    Walpurgis, K.4    Thevis, M.5    Bloch, W.6    Suhr, F.7
  • 113
    • 84872577684 scopus 로고    scopus 로고
    • Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation
    • P.T. Doulias, M. Tenopoulou, J.L. Greene, K. Raju, and H. Ischiropoulos Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation Sci. Signal. 6 2013 rs1
    • (2013) Sci. Signal. , vol.6 , pp. 1
    • Doulias, P.T.1    Tenopoulou, M.2    Greene, J.L.3    Raju, K.4    Ischiropoulos, H.5
  • 115
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • E. Saxon, and C.R. Bertozzi Cell surface engineering by a modified Staudinger reaction Science 287 2000 2007 2010
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 116
    • 52449112301 scopus 로고    scopus 로고
    • Fast reductive ligation of S-nitrosothiols
    • H. Wang, and M. Xian Fast reductive ligation of S-nitrosothiols Angew. Chem. Int. Ed. Engl. 47 2008 6598 6601
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 6598-6601
    • Wang, H.1    Xian, M.2
  • 117
    • 61449128324 scopus 로고    scopus 로고
    • Exploration of the "traceless" reductive ligation of S-nitrosothiols
    • J. Zhang, H. Wang, and M. Xian Exploration of the "traceless" reductive ligation of S-nitrosothiols Org. Lett. 11 2009 477 480
    • (2009) Org. Lett. , vol.11 , pp. 477-480
    • Zhang, J.1    Wang, H.2    Xian, M.3
  • 118
    • 67749133720 scopus 로고    scopus 로고
    • An unexpected Bis-ligation of S-nitrosothiols
    • J. Zhang, H. Wang, and M. Xian An unexpected Bis-ligation of S-nitrosothiols J. Am. Chem. Soc. 131 2009 3854 3855
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3854-3855
    • Zhang, J.1    Wang, H.2    Xian, M.3
  • 119
    • 77956596119 scopus 로고    scopus 로고
    • Reductive ligation mediated one-step disulfide formation of S-nitrosothiols
    • J. Zhang, S. Li, D. Zhang, H. Wang, A.R. Whorton, and M. Xian Reductive ligation mediated one-step disulfide formation of S-nitrosothiols Org. Lett. 12 2010 4208 4211
    • (2010) Org. Lett. , vol.12 , pp. 4208-4211
    • Zhang, J.1    Li, S.2    Zhang, D.3    Wang, H.4    Whorton, A.R.5    Xian, M.6
  • 122
    • 34347369084 scopus 로고    scopus 로고
    • Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets
    • P.A. Konstantinopoulos, M.V. Karamouzis, and A.G. Papavassiliou Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets Nat. Rev. Drug Discov. 6 2007 541 555
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 541-555
    • Konstantinopoulos, P.A.1    Karamouzis, M.V.2    Papavassiliou, A.G.3
  • 123
    • 33644748150 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Geranylgeranylation of Rab GTPases
    • K.F. Leung, R. Baron, and M.C. Seabra Thematic review series: lipid posttranslational modifications. Geranylgeranylation of Rab GTPases J. Lipid Res. 47 2006 467 475
    • (2006) J. Lipid Res. , vol.47 , pp. 467-475
    • Leung, K.F.1    Baron, R.2    Seabra, M.C.3
  • 124
    • 77953773167 scopus 로고    scopus 로고
    • The chemical toolbox for monitoring protein fatty acylation and prenylation
    • R.N. Hannoush, and J. Sun The chemical toolbox for monitoring protein fatty acylation and prenylation Nat. Chem. Biol. 6 2010 498 506
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 498-506
    • Hannoush, R.N.1    Sun, J.2
  • 125
    • 80052999602 scopus 로고    scopus 로고
    • Bioorthogonal chemical reporters for analyzing protein lipidation and lipid trafficking
    • H.C. Hang, J.P. Wilson, and G. Charron Bioorthogonal chemical reporters for analyzing protein lipidation and lipid trafficking Acc. Chem. Res. 44 2011 699 708
    • (2011) Acc. Chem. Res. , vol.44 , pp. 699-708
    • Hang, H.C.1    Wilson, J.P.2    Charron, G.3
  • 126
    • 84880891125 scopus 로고    scopus 로고
    • Chemical reporters for biological discovery
    • M. Grammel, and H.C. Hang Chemical reporters for biological discovery Nat. Chem. Biol. 9 2013 475 484
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 475-484
    • Grammel, M.1    Hang, H.C.2
  • 127
    • 80054075348 scopus 로고    scopus 로고
    • Exploring protein lipidation with chemical biology
    • H.C. Hang, and M.E. Linder Exploring protein lipidation with chemical biology Chem. Rev. 111 2011 6341 6358
    • (2011) Chem. Rev. , vol.111 , pp. 6341-6358
    • Hang, H.C.1    Linder, M.E.2
  • 128
    • 0026585607 scopus 로고
    • Protein prenylation in Schizosaccharomyces pombe
    • T. Giannakouros, J. Armstrong, and A.I. Magee Protein prenylation in Schizosaccharomyces pombe FEBS Lett. 297 1992 103 106
    • (1992) FEBS Lett. , vol.297 , pp. 103-106
    • Giannakouros, T.1    Armstrong, J.2    Magee, A.I.3
  • 129
    • 0024316475 scopus 로고
    • Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans
    • W.R. Schafer, R. Kim, R. Sterne, J. Thorner, S.H. Kim, and J. Rine Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans Science 245 1989 379 385
    • (1989) Science , vol.245 , pp. 379-385
    • Schafer, W.R.1    Kim, R.2    Sterne, R.3    Thorner, J.4    Kim, S.H.5    Rine, J.6
  • 134
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • A.E. Speers, and B.F. Cravatt Profiling enzyme activities in vivo using click chemistry methods Chem. Biol. 11 2004 535 546
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 136
    • 78650092789 scopus 로고    scopus 로고
    • Alkynyl-farnesol reporters for detection of protein S-prenylation in cells
    • G. Charron, L.K. Tsou, W. Maguire, J.S. Yount, and H.C. Hang Alkynyl-farnesol reporters for detection of protein S-prenylation in cells Mol. Biosyst. 7 2011 67 73
    • (2011) Mol. Biosyst. , vol.7 , pp. 67-73
    • Charron, G.1    Tsou, L.K.2    Maguire, W.3    Yount, J.S.4    Hang, H.C.5
  • 137
    • 84879730573 scopus 로고    scopus 로고
    • Prenylome profiling reveals S-farnesylation is crucial for membrane targeting and antiviral activity of ZAP long-isoform
    • G. Charron, M.M. Li, M.R. MacDonald, and H.C. Hang Prenylome profiling reveals S-farnesylation is crucial for membrane targeting and antiviral activity of ZAP long-isoform Proc. Natl. Acad. Sci. U. S. A. 110 2013 11085 11090
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 11085-11090
    • Charron, G.1    Li, M.M.2    Macdonald, M.R.3    Hang, H.C.4
  • 138
    • 78049354410 scopus 로고    scopus 로고
    • Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins
    • S.S. Ivanov, G. Charron, H.C. Hang, and C.R. Roy Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins J. Biol. Chem. 285 2010 34686 34698
    • (2010) J. Biol. Chem. , vol.285 , pp. 34686-34698
    • Ivanov, S.S.1    Charron, G.2    Hang, H.C.3    Roy, C.R.4
  • 140
    • 0028999666 scopus 로고
    • Detecting radiolabeled lipid-modified proteins in polyacrylamide gels
    • A.I. Magee, J. Wootton, and J. de Bony Detecting radiolabeled lipid-modified proteins in polyacrylamide gels Methods Enzymol. 250 1995 330 336
    • (1995) Methods Enzymol. , vol.250 , pp. 330-336
    • Magee, A.I.1    Wootton, J.2    De Bony, J.3
  • 141
    • 77957067307 scopus 로고    scopus 로고
    • Regulation of Ras localization by acylation enables a mode of intracellular signal propagation
    • A. Lorentzen, A. Kinkhabwala, O. Rocks, N. Vartak, and P.I. Bastiaens Regulation of Ras localization by acylation enables a mode of intracellular signal propagation Sci. Signal. 3 2010 ra68
    • (2010) Sci. Signal. , vol.3 , pp. 68
    • Lorentzen, A.1    Kinkhabwala, A.2    Rocks, O.3    Vartak, N.4    Bastiaens, P.I.5
  • 143
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • R.C. Drisdel, and W.N. Green Labeling and quantifying sites of protein palmitoylation Biotechniques 36 2004 276 285
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 144
    • 34447115260 scopus 로고    scopus 로고
    • Palmitoylated proteins: Purification and identification
    • J. Wan, A.F. Roth, A.O. Bailey, and N.G. Davis Palmitoylated proteins: purification and identification Nat. Protoc. 2 2007 1573 1584
    • (2007) Nat. Protoc. , vol.2 , pp. 1573-1584
    • Wan, J.1    Roth, A.F.2    Bailey, A.O.3    Davis, N.G.4
  • 146
    • 84861212051 scopus 로고    scopus 로고
    • Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23
    • C. Ivaldi, B.R. Martin, S. Kieffer-Jaquinod, A. Chapel, T. Levade, J. Garin, and A. Journet Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23 PLoS One 7 2012 e37187
    • (2012) PLoS One , vol.7 , pp. 37187
    • Ivaldi, C.1    Martin, B.R.2    Kieffer-Jaquinod, S.3    Chapel, A.4    Levade, T.5    Garin, J.6    Journet, A.7
  • 147
    • 47849089020 scopus 로고    scopus 로고
    • Identification of CKAP4/p63 as a major substrate of the palmitoyl acyltransferase DHHC2, a putative tumor suppressor, using a novel proteomics method
    • J. Zhang, S.L. Planey, C. Ceballos, S.M. Stevens Jr., S.K. Keay, and D.A. Zacharias Identification of CKAP4/p63 as a major substrate of the palmitoyl acyltransferase DHHC2, a putative tumor suppressor, using a novel proteomics method Mol. Cell. Proteomics 7 2008 1378 1388
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1378-1388
    • Zhang, J.1    Planey, S.L.2    Ceballos, C.3    Stevens, S.M.4    Keay, S.K.5    Zacharias, D.A.6
  • 149
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • B.R. Martin, and B.F. Cravatt Large-scale profiling of protein palmitoylation in mammalian cells Nat. Methods 6 2009 135 138
    • (2009) Nat. Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 150
    • 67650803380 scopus 로고    scopus 로고
    • Imaging the lipidome: Omega-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins
    • R.N. Hannoush, and N. Arenas-Ramirez Imaging the lipidome: omega-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins ACS Chem. Biol. 4 2009 581 587
    • (2009) ACS Chem. Biol. , vol.4 , pp. 581-587
    • Hannoush, R.N.1    Arenas-Ramirez, N.2
  • 154
    • 84855253929 scopus 로고    scopus 로고
    • DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells
    • Y. Li, B.R. Martin, B.F. Cravatt, and S.L. Hofmann DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells J. Biol. Chem. 287 2012 523 530
    • (2012) J. Biol. Chem. , vol.287 , pp. 523-530
    • Li, Y.1    Martin, B.R.2    Cravatt, B.F.3    Hofmann, S.L.4
  • 156
    • 84880959257 scopus 로고    scopus 로고
    • Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast
    • M.M. Zhang, P.Y. Wu, F.D. Kelly, P. Nurse, and H.C. Hang Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast PLoS Biol. 11 2013 e1001597
    • (2013) PLoS Biol. , vol.11 , pp. 1001597
    • Zhang, M.M.1    Wu, P.Y.2    Kelly, F.D.3    Nurse, P.4    Hang, H.C.5
  • 157
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: New concepts and molecular mechanisms
    • A. Higdon, A.R. Diers, J.Y. Oh, A. Landar, and V.M. Darley-Usmar Cell signalling by reactive lipid species: new concepts and molecular mechanisms Biochem. J. 442 2012 453 464
    • (2012) Biochem. J. , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.R.2    Oh, J.Y.3    Landar, A.4    Darley-Usmar, V.M.5
  • 158
    • 84860439798 scopus 로고
    • Nitroalkylation-A redox sensitive signaling pathway
    • A.C. Geisler, and T.K. Rudolph Nitroalkylation-a redox sensitive signaling pathway Biochim. Biophys. Acta 2012 1820 777 784
    • (1820) Biochim. Biophys. Acta , vol.2012 , pp. 777-784
    • Geisler, A.C.1    Rudolph, T.K.2
  • 159
    • 80054072517 scopus 로고    scopus 로고
    • Formation and signaling actions of electrophilic lipids
    • F.J. Schopfer, C. Cipollina, and B.A. Freeman Formation and signaling actions of electrophilic lipids Chem. Rev. 111 2011 5997 6021
    • (2011) Chem. Rev. , vol.111 , pp. 5997-6021
    • Schopfer, F.J.1    Cipollina, C.2    Freeman, B.A.3
  • 160
    • 84878884100 scopus 로고    scopus 로고
    • The lipid peroxidation product 4-hydroxy-2-nonenal: Advances in chemistry and analysis
    • C.M. Spickett The lipid peroxidation product 4-hydroxy-2-nonenal: Advances in chemistry and analysis Redox Biol. 1 2013 145 152
    • (2013) Redox Biol. , vol.1 , pp. 145-152
    • Spickett, C.M.1
  • 161
    • 37249090364 scopus 로고    scopus 로고
    • Cyclooxygenase-2-mediated metabolism of arachidonic acid to 15-oxo-eicosatetraenoic acid by rat intestinal epithelial cells
    • S.H. Lee, K. Rangiah, M.V. Williams, A.Y. Wehr, R.N. DuBois, and I.A. Blair Cyclooxygenase-2-mediated metabolism of arachidonic acid to 15-oxo-eicosatetraenoic acid by rat intestinal epithelial cells Chem. Res. Toxicol. 20 2007 1665 1675
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1665-1675
    • Lee, S.H.1    Rangiah, K.2    Williams, M.V.3    Wehr, A.Y.4    Dubois, R.N.5    Blair, I.A.6
  • 162
    • 80054702892 scopus 로고    scopus 로고
    • 15-Deoxy-Delta(1)(2), (1)(4)-prostaglandin J(2), an electrophilic lipid mediator of anti-inflammatory and pro-resolving signaling
    • Y.J. Surh, H.K. Na, J.M. Park, H.N. Lee, W. Kim, I.S. Yoon, and D.D. Kim 15-Deoxy-Delta(1)(2), (1)(4)-prostaglandin J(2), an electrophilic lipid mediator of anti-inflammatory and pro-resolving signaling Biochem. Pharmacol. 82 2011 1335 1351
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1335-1351
    • Surh, Y.J.1    Na, H.K.2    Park, J.M.3    Lee, H.N.4    Kim, W.5    Yoon, I.S.6    Kim, D.D.7
  • 163
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, and H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radic. Biol. Med. 11 1991 81 128
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 164
    • 38949089246 scopus 로고    scopus 로고
    • Protein damage by reactive electrophiles: Targets and consequences
    • D.C. Liebler Protein damage by reactive electrophiles: targets and consequences Chem. Res. Toxicol. 21 2008 117 128
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 117-128
    • Liebler, D.C.1
  • 165
    • 77952650680 scopus 로고    scopus 로고
    • Systems analysis of protein modification and cellular responses induced by electrophile stress
    • A.T. Jacobs, and L.J. Marnett Systems analysis of protein modification and cellular responses induced by electrophile stress Acc. Chem. Res. 43 2010 673 683
    • (2010) Acc. Chem. Res. , vol.43 , pp. 673-683
    • Jacobs, A.T.1    Marnett, L.J.2
  • 166
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • A.L. Levonen, A. Landar, A. Ramachandran, E.K. Ceaser, D.A. Dickinson, G. Zanoni, J.D. Morrow, and V.M. Darley-Usmar Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products Biochem. J. 378 2004 373 382
    • (2004) Biochem. J. , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandran, A.3    Ceaser, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 168
    • 25644451257 scopus 로고    scopus 로고
    • Modification of heat shock protein 90 by 4-hydroxynonenal in a rat model of chronic alcoholic liver disease
    • D.L. Carbone, J.A. Doorn, Z. Kiebler, B.R. Ickes, and D.R. Petersen Modification of heat shock protein 90 by 4-hydroxynonenal in a rat model of chronic alcoholic liver disease J. Pharmacol. Exp. Ther. 315 2005 8 15
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 8-15
    • Carbone, D.L.1    Doorn, J.A.2    Kiebler, Z.3    Ickes, B.R.4    Petersen, D.R.5
  • 169
    • 0346634902 scopus 로고    scopus 로고
    • Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry
    • F. Fenaille, J.C. Tabet, and P.A. Guy Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry Anal. Chem. 74 2002 6298 6304
    • (2002) Anal. Chem. , vol.74 , pp. 6298-6304
    • Fenaille, F.1    Tabet, J.C.2    Guy, P.A.3
  • 170
    • 80054873045 scopus 로고    scopus 로고
    • To tag or not to tag: A comparative evaluation of immunoaffinity-labeling and tandem mass spectrometry for the identification and localization of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation
    • J. Guo, and L. Prokai To tag or not to tag: a comparative evaluation of immunoaffinity-labeling and tandem mass spectrometry for the identification and localization of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation J. Proteomics 74 2011 2360 2369
    • (2011) J. Proteomics , vol.74 , pp. 2360-2369
    • Guo, J.1    Prokai, L.2
  • 171
    • 80052998418 scopus 로고    scopus 로고
    • Exploring the biology of lipid peroxidation-derived protein carbonylation
    • K.S. Fritz, and D.R. Petersen Exploring the biology of lipid peroxidation-derived protein carbonylation Chem. Res. Toxicol. 24 2011 1411 1419
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1411-1419
    • Fritz, K.S.1    Petersen, D.R.2
  • 172
    • 0029965252 scopus 로고    scopus 로고
    • Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis
    • A. Nakamura, and S. Goto Analysis of protein carbonyls with 2,4-dinitrophenyl hydrazine and its antibodies by immunoblot in two-dimensional gel electrophoresis J. Biochem. 119 1996 768 774
    • (1996) J. Biochem. , vol.119 , pp. 768-774
    • Nakamura, A.1    Goto, S.2
  • 173
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification: Examination by western blot immunoassay
    • E. Shacter, J.A. Williams, M. Lim, and R.L. Levine Differential susceptibility of plasma proteins to oxidative modification: examination by western blot immunoassay Free Radic. Biol. Med. 17 1994 429 437
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 174
    • 33750350410 scopus 로고    scopus 로고
    • Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard's P reagent
    • H. Mirzaei, and F. Regnier Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard's P reagent J. Chromatogr. A 1134 2006 122 133
    • (2006) J. Chromatogr. A , vol.1134 , pp. 122-133
    • Mirzaei, H.1    Regnier, F.2
  • 175
    • 84862190616 scopus 로고    scopus 로고
    • Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides
    • J. Tamarit, A. de Hoogh, E. Obis, D. Alsina, E. Cabiscol, and J. Ros Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides J. Proteomics 75 2012 3778 3788
    • (2012) J. Proteomics , vol.75 , pp. 3778-3788
    • Tamarit, J.1    De Hoogh, A.2    Obis, E.3    Alsina, D.4    Cabiscol, E.5    Ros, J.6
  • 176
    • 33749457861 scopus 로고    scopus 로고
    • New role for an old probe: Affinity labeling of oxylipid protein conjugates by N'-aminooxymethylcarbonylhydrazino d-biotin
    • J. Chavez, J. Wu, B. Han, W.G. Chung, and C.S. Maier New role for an old probe: affinity labeling of oxylipid protein conjugates by N'-aminooxymethylcarbonylhydrazino d-biotin Anal. Chem. 78 2006 6847 6854
    • (2006) Anal. Chem. , vol.78 , pp. 6847-6854
    • Chavez, J.1    Wu, J.2    Han, B.3    Chung, W.G.4    Maier, C.S.5
  • 178
    • 34248233116 scopus 로고    scopus 로고
    • Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates
    • B. Han, J.F. Stevens, and C.S. Maier Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates Anal. Chem. 79 2007 3342 3354
    • (2007) Anal. Chem. , vol.79 , pp. 3342-3354
    • Han, B.1    Stevens, J.F.2    Maier, C.S.3
  • 179
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry
    • M.R. Roe, H. Xie, S. Bandhakavi, and T.J. Griffin Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry Anal. Chem. 79 2007 3747 3756
    • (2007) Anal. Chem. , vol.79 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 180
    • 77953911842 scopus 로고    scopus 로고
    • Targeted 18O-labeling for improved proteomic analysis of carbonylated peptides by mass spectrometry
    • M.R. Roe, T.F. McGowan, L.V. Thompson, and T.J. Griffin Targeted 18O-labeling for improved proteomic analysis of carbonylated peptides by mass spectrometry J. Am. Soc. Mass Spectrom. 21 2010 1190 1203
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1190-1203
    • Roe, M.R.1    McGowan, T.F.2    Thompson, L.V.3    Griffin, T.J.4
  • 181
    • 80054814240 scopus 로고    scopus 로고
    • Isotope-coded dimethyl tagging for differential quantification of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation
    • N. Rauniyar, and L. Prokai Isotope-coded dimethyl tagging for differential quantification of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation J. Mass Spectrom. 46 2011 976 985
    • (2011) J. Mass Spectrom. , vol.46 , pp. 976-985
    • Rauniyar, N.1    Prokai, L.2
  • 182
    • 84866104375 scopus 로고    scopus 로고
    • A comparative 'bottom up' proteomics strategy for the site-specific identification and quantification of protein modifications by electrophilic lipids
    • B. Han, M. Hare, S. Wickramasekara, Y. Fang, and C.S. Maier A comparative 'bottom up' proteomics strategy for the site-specific identification and quantification of protein modifications by electrophilic lipids J. Proteomics 75 2012 5724 5733
    • (2012) J. Proteomics , vol.75 , pp. 5724-5733
    • Han, B.1    Hare, M.2    Wickramasekara, S.3    Fang, Y.4    Maier, C.S.5
  • 184
    • 33645459848 scopus 로고    scopus 로고
    • Identification of novel protein targets for modification by 15-deoxy-Delta12,14-prostaglandin J2 in mesangial cells reveals multiple interactions with the cytoskeleton
    • K. Stamatakis, F.J. Sanchez-Gomez, and D. Perez-Sala Identification of novel protein targets for modification by 15-deoxy-Delta12,14-prostaglandin J2 in mesangial cells reveals multiple interactions with the cytoskeleton J. Am. Soc. Nephrol. 17 2006 89 98
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 89-98
    • Stamatakis, K.1    Sanchez-Gomez, F.J.2    Perez-Sala, D.3
  • 186
    • 41649118986 scopus 로고    scopus 로고
    • Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives
    • A. Vila, K.A. Tallman, A.T. Jacobs, D.C. Liebler, N.A. Porter, and L.J. Marnett Identification of protein targets of 4-hydroxynonenal using click chemistry for ex vivo biotinylation of azido and alkynyl derivatives Chem. Res. Toxicol. 21 2008 432 444
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 432-444
    • Vila, A.1    Tallman, K.A.2    Jacobs, A.T.3    Liebler, D.C.4    Porter, N.A.5    Marnett, L.J.6
  • 187
    • 71049139267 scopus 로고    scopus 로고
    • An azido-biotin reagent for use in the isolation of protein adducts of lipid-derived electrophiles by streptavidin catch and photorelease
    • H.Y. Kim, K.A. Tallman, D.C. Liebler, and N.A. Porter An azido-biotin reagent for use in the isolation of protein adducts of lipid-derived electrophiles by streptavidin catch and photorelease Mol. Cell. Proteomics 8 2009 2080 2089
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2080-2089
    • Kim, H.Y.1    Tallman, K.A.2    Liebler, D.C.3    Porter, N.A.4
  • 188
    • 84894619225 scopus 로고    scopus 로고
    • A chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles
    • C. Wang, E. Weerapana, M.M. Blewett, and B.F. Cravatt A chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles Nat. Methods 11 2014 79 85
    • (2014) Nat. Methods , vol.11 , pp. 79-85
    • Wang, C.1    Weerapana, E.2    Blewett, M.M.3    Cravatt, B.F.4


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