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Volumn , Issue , 2013, Pages 1-42

The chemistry of Thiol oxidation and detection

Author keywords

Cysteine; Reactive nitrogen species; Reactive oxygen species; Reactive sulfur species; Thiol oxidation

Indexed keywords


EID: 84880047785     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-94-007-5787-5_1     Document Type: Chapter
Times cited : (61)

References (215)
  • 1
    • 79960049457 scopus 로고    scopus 로고
    • Development of a highly sensitive fluorescent probe for hydrogen peroxide
    • Abo M, Urano Y, Hanaoka K, Terai T, Komatsu T, Nagano T (2011) Development of a highly sensitive fluorescent probe for hydrogen peroxide. J Am Chem Soc 133:10629-10637
    • (2011) J Am Chem Soc , vol.133 , pp. 10629-10637
    • Abo, M.1    Urano, Y.2    Hanaoka, K.3    Terai, T.4    Komatsu, T.5    Nagano, T.6
  • 2
    • 0020627222 scopus 로고
    • Synthesis and pH-dependent stability of purine-6-sulfenic acid, a putative reactive metabolite of 6-thiopurine
    • Abraham RT, Benson LM, Jardine I (1983) Synthesis and pH-dependent stability of purine-6-sulfenic acid, a putative reactive metabolite of 6-thiopurine. J Med Chem 26:1523-1526
    • (1983) J Med Chem , vol.26 , pp. 1523-1526
    • Abraham, R.T.1    Benson, L.M.2    Jardine, I.3
  • 3
    • 0003698541 scopus 로고
    • Biological reactivity of hypochlorous acid: Implications for microbicidal mechanisms of leukocyte myeloperoxidase
    • Albrich JM, McCarthy CA, Hurst JK (1981) Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase. Proc Natl Acad Sci USA 78:210-214
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 210-214
    • Albrich, J.M.1    McCarthy, C.A.2    Hurst, J.K.3
  • 4
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • Alderton WK, Cooper CE, Knowles RG (2001) Nitric oxide synthases: structure, function and inhibition. Biochem J 357:593-615
    • (2001) Biochem J , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 5
    • 0001637467 scopus 로고
    • Formation and reactions of sulfenic acids in proteins
    • Allison WS(1976) Formation and reactions of sulfenic acids in proteins. Acc Chem Res 9:293-299
    • (1976) Acc Chem Res , vol.9 , pp. 293-299
    • Allison, W.S.1
  • 6
    • 0015930040 scopus 로고
    • The formation of a protein sulfenamide during the inactivation of the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by benzylamine
    • Allison WS, Benitez LV, Johnson CL (1973) The formation of a protein sulfenamide during the inactivation of the acyl phosphatase activity of oxidized glyceraldehyde-3-phosphate dehydrogenase by benzylamine. Biochem Biophys Res Commun 52:1403-1409
    • (1973) Biochem Biophys Res Commun , vol.52 , pp. 1403-1409
    • Allison, W.S.1    Benitez, L.V.2    Johnson, C.L.3
  • 7
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: Cause or consequence
    • Andersen JK (2004) Oxidative stress in neurodegeneration: cause or consequence? Nat Rev Neurosci 5:s18-s25
    • (2004) Nat Rev Neurosci , vol.5 , pp. s18-s25
    • Andersen, J.K.1
  • 8
    • 44649156956 scopus 로고    scopus 로고
    • Transition-metal-catalyzed synthesis of organosulfur compounds
    • Arisawa M, Yamaguchi M (2008) Transition-metal-catalyzed synthesis of organosulfur compounds. Pure Appl Chem 80:993-1003
    • (2008) Pure Appl Chem , vol.80 , pp. 993-1003
    • Arisawa, M.1    Yamaguchi, M.2
  • 9
    • 58149214250 scopus 로고    scopus 로고
    • Inorganic chemistry of defensive peroxidases in the human oral cavity
    • Ashby MT (2008) Inorganic chemistry of defensive peroxidases in the human oral cavity. J Dent Res 87:900-914
    • (2008) J Dent Res , vol.87 , pp. 900-914
    • Ashby, M.T.1
  • 10
    • 4143109074 scopus 로고    scopus 로고
    • Reactive sulfur species: Aqueous chemistry of sulfenyl thiocyanates
    • Ashby MT, Aneetha H (2004) Reactive sulfur species: aqueous chemistry of sulfenyl thiocyanates. J Am Chem Soc 126:10216-10217
    • (2004) J Am Chem Soc , vol.126 , pp. 10216-10217
    • Ashby, M.T.1    Aneetha, H.2
  • 11
    • 0023239358 scopus 로고
    • Colorimetric assay for methanesulfinic acid in biological samples
    • Babbs CF, GaleMJ (1987) Colorimetric assay for methanesulfinic acid in biological samples. Anal Biochem 163:67-73
    • (1987) Anal Biochem , vol.163 , pp. 67-73
    • Babbs, C.F.1    Gale, M.J.2
  • 12
    • 0030464437 scopus 로고    scopus 로고
    • A reassessment of the bond dissociation energies of peroxides. An ab initio study
    • Bach RB, Ayala PY, Schlegel HB (1996) A reassessment of the bond dissociation energies of peroxides. An ab initio study. J Am Chem Soc 118:12758-12765
    • (1996) J Am Chem Soc , vol.118 , pp. 12758-12765
    • Bach, R.B.1    Ayala, P.Y.2    Schlegel, H.B.3
  • 13
    • 77950795121 scopus 로고    scopus 로고
    • Nucleophilicity and nucleofugality of phenylsulfinate (PhSO2): A key to understanding its ambident reactivity
    • Baidya M, Kobayashi S, Mayr H (2010) Nucleophilicity and nucleofugality of phenylsulfinate (PhSO2): a key to understanding its ambident reactivity. J Am Chem Soc 132:4796-4805
    • (2010) J Am Chem Soc , vol.132 , pp. 4796-4805
    • Baidya, M.1    Kobayashi, S.2    Mayr, H.3
  • 14
    • 78249269178 scopus 로고    scopus 로고
    • Extracellular transsulfuration generates hydrogen sulfide from homocysteine and protects endothelium from redox stress
    • Bearden SE, Beard Jr RS, Pfau JC (2010) Extracellular transsulfuration generates hydrogen sulfide from homocysteine and protects endothelium from redox stress. Am J Physiol Heart Circ Physiol 299:H1568-H1576
    • (2010) Am J Physiol Heart Circ Physiol , vol.299 , pp. H1568-H1576
    • Bearden, S.E.1    Beard, Jr.R.S.2    Pfau, J.C.3
  • 16
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard K, Krause K-H (2007) The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev 87:245-313
    • (2007) Physiol Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.-H.2
  • 17
    • 0016256290 scopus 로고
    • The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins
    • Benitez LV, Allison WS (1974) The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins. J Biol Chem 249:6234-6243
    • (1974) J Biol Chem , vol.249 , pp. 6234-6243
    • Benitez, L.V.1    Allison, W.S.2
  • 18
    • 80053010069 scopus 로고    scopus 로고
    • A decade of bioorthogonal chemistry
    • Bertozzi CR (2011) A decade of bioorthogonal chemistry. Acc Chem Res 44:651
    • (2011) Acc Chem Res , vol.44 , pp. 651
    • Bertozzi, C.R.1
  • 21
    • 13044298399 scopus 로고
    • The chemistry of alkyl thiosulfinate esters. VI. Preparation and spectral studies
    • Block E, O'Conner J (1974) The chemistry of alkyl thiosulfinate esters. VI. Preparation and spectral studies. J Am Chem Soc 96:3921-3929
    • (1974) J Am Chem Soc , vol.96 , pp. 3921-3929
    • Block, E.1    O'conner, J.2
  • 22
    • 0032560621 scopus 로고    scopus 로고
    • Ionization-reactivity relationships for cysteine thiols in polypeptides
    • Bulaj G, Kortemme T, Goldenberg DP (1998) Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry 37:8965-8972
    • (1998) Biochemistry , vol.37 , pp. 8965-8972
    • Bulaj, G.1    Kortemme, T.2    Goldenberg, D.P.3
  • 26
    • 0032557570 scopus 로고    scopus 로고
    • Nitric oxide-induced deamination of cytosine and guanine in deoxynucleosides and oligonucleotides
    • Caulfield JL, Wishnok JS, Tannenbaum SR (1998) Nitric oxide-induced deamination of cytosine and guanine in deoxynucleosides and oligonucleotides. J Biol Chem 273:12689-12695
    • (1998) J Biol Chem , vol.273 , pp. 12689-12695
    • Caulfield, J.L.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 27
    • 67649130281 scopus 로고    scopus 로고
    • Chemical modification of proteins at cysteine: Opportunities in chemistry and biology
    • Chalker JM, Bernardes GJL, Lin YA, Davis BG (2009) Chemical modification of proteins at cysteine: opportunities in chemistry and biology. Chem Asian J 4:630-640
    • (2009) Chem Asian J , vol.4 , pp. 630-640
    • Chalker, J.M.1    Bernardes, G.J.L.2    Lin, Y.A.3    Davis, B.G.4
  • 29
    • 9644273757 scopus 로고    scopus 로고
    • A selective cell-permeable optical probe for hydrogen peroxide in living cells
    • Chang MCY, Pralle A, Isacoff EY, Chang CJ (2004) A selective cell-permeable optical probe for hydrogen peroxide in living cells. J Am Chem Soc 126:15392-15393
    • (2004) J Am Chem Soc , vol.126 , pp. 15392-15393
    • Chang, M.C.Y.1    Pralle, A.2    Isacoff, E.Y.3    Chang, C.J.4
  • 30
    • 77955640917 scopus 로고    scopus 로고
    • Mapping protein cysteine sulfonic acid modifications with specific enrichment and mass spectrometry: An integrated approach to explore the cysteine oxidation
    • Chang YC, Huang CN, Lin CH, Chang HC, Wu CC (2010) Mapping protein cysteine sulfonic acid modifications with specific enrichment and mass spectrometry: an integrated approach to explore the cysteine oxidation. Proteomics 10:2961-2971
    • (2010) Proteomics , vol.10 , pp. 2961-2971
    • Chang, Y.C.1    Huang, C.N.2    Lin, C.H.3    Chang, H.C.4    Wu, C.C.5
  • 31
    • 59849120642 scopus 로고    scopus 로고
    • Hypobromous acid and bromamine production by neutrophils and modulation by superoxide
    • Chapman ALP, Skaff O, Senthilmohan R, Kettle AJ, Davies MJ (2009) Hypobromous acid and bromamine production by neutrophils and modulation by superoxide. Biochem J 417:773-781
    • (2009) Biochem J , vol.417 , pp. 773-781
    • Chapman, A.L.P.1    Skaff, O.2    Senthilmohan, R.3    Kettle, A.J.4    Davies, M.J.5
  • 32
    • 23244464769 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by a persulfide (BnSSH)
    • Chatterji T, Keerthi K, Gates KS (2005) Generation of reactive oxygen species by a persulfide (BnSSH). Bioorg Med Chem Lett 15:3921-3924
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 3921-3924
    • Chatterji, T.1    Keerthi, K.2    Gates, K.S.3
  • 33
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction by NADPH oxidase 4 localization
    • Chen K, Kirber MT, Xiao H, Yang Y, Keaney JF Jr (2008) Regulation of ROS signal transduction by NADPH oxidase 4 localization. J Cell Biol 181:1129-1139
    • (2008) J Cell Biol , vol.181 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney, J.F.5
  • 34
    • 66449109703 scopus 로고    scopus 로고
    • H2S biogenesis by human Cystathionine gamma-Lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
    • Chiku T, Padovani D, Zhu W, Singh S, Vitvitsky V, Banerjee R (2009) H2S biogenesis by human Cystathionine gamma-Lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia. J Biol Chem 248:11601-11612
    • (2009) J Biol Chem , vol.248 , pp. 11601-11612
    • Chiku, T.1    Padovani, D.2    Zhu, W.3    Singh, S.4    Vitvitsky, V.5    Banerjee, R.6
  • 35
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • Claiborne A, Miller H, Parsonage D, Ross RP (1993) Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J 7:1483-1490
    • (1993) FASEB J , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 36
    • 0000485601 scopus 로고
    • The dipole moment of hydrogen peroxide
    • Cohen EA, Pickett HM (1981) The dipole moment of hydrogen peroxide. J Mol Spectrosc 87: 582-585
    • (1981) J Mol Spectrosc , vol.87 , pp. 582-585
    • Cohen, E.A.1    Pickett, H.M.2
  • 37
    • 8344281472 scopus 로고    scopus 로고
    • Divergence of function in the thioredoxin fold suprafamily: Evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor
    • Copley SD, Novak WRP, Babbitt PC (2004) Divergence of function in the thioredoxin fold suprafamily: evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor. Biochemistry 43:13981-13995
    • (2004) Biochemistry , vol.43 , pp. 13981-13995
    • Copley, S.D.1    Novak, W.R.P.2    Babbitt, P.C.3
  • 38
    • 33845183598 scopus 로고
    • The chemistry of sulfenamides
    • Craine L, Raban M (1989) The chemistry of sulfenamides. Chem Rev 89:689-712
    • (1989) Chem Rev , vol.89 , pp. 689-712
    • Craine, L.1    Raban, M.2
  • 40
    • 18544362983 scopus 로고    scopus 로고
    • Identification of degradation products formed during performic oxidation of peptides and proteins by high-performance liquid chromatography with matrix-assisted laser desorption/ionization and tandem mass spectrometry
    • Dai J, Zhang Y, Wang J, Li X, Lu Z, Cai Y, Qian X (2005) Identification of degradation products formed during performic oxidation of peptides and proteins by high-performance liquid chromatography with matrix-assisted laser desorption/ionization and tandem mass spectrometry. Rapid Commun Mass Spectrom 19:1130-1138
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 1130-1138
    • Dai, J.1    Zhang, Y.2    Wang, J.3    Li, X.4    Lu, Z.5    Cai, Y.6    Qian, X.7
  • 42
    • 37049104059 scopus 로고
    • Arenesulphinic acids. Nitroso protecting reagents applicable to some nitrosoarenes
    • Darchen A, Moinet CJ (1976) Arenesulphinic acids. Nitroso protecting reagents applicable to some nitrosoarenes. J Chem Soc Chem Commun 20:820a-820a. doi:10.1039/C3976000820A
    • (1976) J Chem Soc Chem Commun , vol.20 , pp. 820a-820a
    • Darchen, A.1    Moinet, C.J.2
  • 43
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • Davies MJ, Hawkins CL, Pattison DI, Rees MD (2008) Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxid Redox Signal 10:1199-1234
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 44
    • 0000910788 scopus 로고
    • Chemistry of sulfenic acids. 7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogen bonding and electronegativity effects
    • Davis FA, Jenkins LA, Billmers RL (1986) Chemistry of sulfenic acids. 7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogen bonding and electronegativity effects. J Org Chem 51:1033-1040
    • (1986) J Org Chem , vol.51 , pp. 1033-1040
    • Davis, F.A.1    Jenkins, L.A.2    Billmers, R.L.3
  • 45
    • 0037414784 scopus 로고    scopus 로고
    • 20S Proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • Demasi M, Silva GM, Netto LES (2003) 20S Proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem 278:679-685
    • (2003) J Biol Chem , vol.278 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.S.3
  • 47
    • 0032902722 scopus 로고    scopus 로고
    • Guanylate cyclase and the NO/cGMP signaling pathway
    • Denninger JW, Marletta MA (1999) Guanylate cyclase and the NO/cGMP signaling pathway. Biochim Biophys Acta 1411:334-350
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 334-350
    • Denninger, J.W.1    Marletta, M.A.2
  • 48
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu JM, Tanner KG (1998) Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37:5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 49
    • 48249118740 scopus 로고    scopus 로고
    • A targetable fluorescent probe for imaging hydrogen peroxide in the mitochondria of living cells
    • Dickinson BC, Chang CJ (2008) A targetable fluorescent probe for imaging hydrogen peroxide in the mitochondria of living cells. J Am Chem Soc 130:9638-9639
    • (2008) J Am Chem Soc , vol.130 , pp. 9638-9639
    • Dickinson, B.C.1    Chang, C.J.2
  • 51
    • 0030220474 scopus 로고    scopus 로고
    • Generation of nitric oxide from S-nitrosothiols using protein-bound Cu2C sources
    • Dicks AP, Williams DL (1996) Generation of nitric oxide from S-nitrosothiols using protein-bound Cu2C sources. Chem Biol 8:655-659
    • (1996) Chem Biol , vol.8 , pp. 655-659
    • Dicks, A.P.1    Williams, D.L.2
  • 52
    • 0030778083 scopus 로고    scopus 로고
    • Novel application of 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole to identify cysteine sulfenic acid in the aphc component of alkyl hydroperoxide reductase
    • Ellis HR, Poole LB (1997) Novel application of 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole to identify cysteine sulfenic acid in the aphc component of alkyl hydroperoxide reductase. Biochemistry 36:15013-15018
    • (1997) Biochemistry , vol.36 , pp. 15013-15018
    • Ellis, H.R.1    Poole, L.B.2
  • 53
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-77
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 54
    • 77249096370 scopus 로고    scopus 로고
    • Regulation of cardiovascular cell function by hydrogen sulfide (H2S) cell biochemistry and function
    • Elsey DJ, Fowkes RC, Baxter GF (2010) Regulation of cardiovascular cell function by hydrogen sulfide (H2S) cell biochemistry and function. Cell Biochem Funct 28:95-106
    • (2010) Cell Biochem Funct , vol.28 , pp. 95-106
    • Elsey, D.J.1    Fowkes, R.C.2    Baxter, G.F.3
  • 56
    • 0347719283 scopus 로고    scopus 로고
    • Theoretical insights into the mechanism for thiolDdisulfide exchange
    • Fernandes PA, Ramos MJ (2004) Theoretical insights into the mechanism for thiolDdisulfide exchange. Chemistry 10:257-266
    • (2004) Chemistry , vol.10 , pp. 257-266
    • Fernandes, P.A.1    Ramos, M.J.2
  • 57
    • 64749101531 scopus 로고    scopus 로고
    • Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
    • Ferrer-Sueta G, Radi R (2009) Chemical biology of peroxynitrite: kinetics, diffusion, and radicals. ACS Chem Biol 4:161-177
    • (2009) ACS Chem Biol , vol.4 , pp. 161-177
    • Ferrer-Sueta, G.1    Radi, R.2
  • 58
    • 0015842752 scopus 로고
    • Superoxide dismutase: A comparison of rate constants
    • Forman HJ, Fridovich I (1973) Superoxide dismutase: a comparison of rate constants. Arch Biochem Biophys 158:396-400
    • (1973) Arch Biochem Biophys , vol.158 , pp. 396-400
    • Forman, H.J.1    Fridovich, I.2
  • 60
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu X, Kassim SY, Parks WC, Heinecke JW (2001) Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem 276:41279-41287
    • (2001) J Biol Chem , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 61
    • 79961193678 scopus 로고    scopus 로고
    • Superoxide dismutases: Role in redox signaling, vascular function, and diseases
    • Fukai T, Masuko U-F (2011) Superoxide dismutases: role in redox signaling, vascular function, and diseases. Antioxid Redox Signal 15:1583-1603
    • (2011) Antioxid Redox Signal , vol.15 , pp. 1583-1603
    • Fukai, T.1    Masuko, U.-F.2
  • 62
    • 4544387352 scopus 로고    scopus 로고
    • Glyco-SeS: Selenenylsulfide-mediated protein glycoconjugation-a new strategy in post-translational modification
    • Gamblin DP, Garnier P, van Kasteren S, Oldham NJ, Fairbanks AJ, Davis BG (2004) Glyco-SeS: selenenylsulfide-mediated protein glycoconjugation-a new strategy in post-translational modification. Angew Chem Int Ed 43:828-833
    • (2004) Angew Chem Int Ed , vol.43 , pp. 828-833
    • Gamblin, D.P.1    Garnier, P.2    Van Kasteren, S.3    Oldham, N.J.4    Fairbanks, A.J.5    Davis, B.G.6
  • 63
    • 0036606781 scopus 로고    scopus 로고
    • Reactive sulphur species: An in vitro investigation of the oxidation properties of disulphide S-oxides
    • Giles GI, Tasker KM, Collins C, Giles NM, O'rourke E, Jacob C (2002) Reactive sulphur species: an in vitro investigation of the oxidation properties of disulphide S-oxides. Biochem J 364(Pt 2):579-585
    • (2002) Biochem J , vol.364 , pp. 579-585
    • Giles, G.I.1    Tasker, K.M.2    Collins, C.3    Giles, N.M.4    O'rourke, E.5    Jacob, C.6
  • 64
    • 34548148201 scopus 로고    scopus 로고
    • Hydrogen peroxide: A metabolic by-product or a common mediator of ageing signals
    • Giorgio M, Trinei M, Migliaccio E, Pelicci PG (2007) Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? Nat Rev Mol Cell Biol 8:722-728
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 722-728
    • Giorgio, M.1    Trinei, M.2    Migliaccio, E.3    Pelicci, P.G.4
  • 65
    • 0029991199 scopus 로고    scopus 로고
    • Mechanism of the nitrosation of thiols and amines by oxygenated NO solutions: The nature of the nitrosating intermediates
    • Goldstein S, Czapski G (1996) Mechanism of the nitrosation of thiols and amines by oxygenated NO solutions: the nature of the nitrosating intermediates. J Am Chem Soc 118:3419-3425
    • (1996) J Am Chem Soc , vol.118 , pp. 3419-3425
    • Goldstein, S.1    Czapski, G.2
  • 66
    • 0030894735 scopus 로고    scopus 로고
    • Synthesis, structure, and reactions of a sulfenic acid bearing a novel bowl-type substituent: The first synthesis of a stable sulfenic acid by direct oxidation of a thiol
    • Goto K, Holler M, Okazak R (1997) Synthesis, structure, and reactions of a sulfenic acid bearing a novel bowl-type substituent: the first synthesis of a stable sulfenic acid by direct oxidation of a thiol. J Am Chem Soc 119:1460-1461
    • (1997) J Am Chem Soc , vol.119 , pp. 1460-1461
    • Goto, K.1    Holler, M.2    Okazak, R.3
  • 67
    • 0842328499 scopus 로고    scopus 로고
    • Reaction of stable sulfenic and selenenic acids containing a bowl-type steric protection group with a phosphine. Elucidation of the mechanism of reduction of sulfenic and selenenic acids
    • Goto K, Shimada K, Nagahama M, Okazaki R, Kawashima T (2003) Reaction of stable sulfenic and selenenic acids containing a bowl-type steric protection group with a phosphine. Elucidation of the mechanism of reduction of sulfenic and selenenic acids. Chem Lett 32:1080-1081
    • (2003) Chem Lett , vol.32 , pp. 1080-1081
    • Goto, K.1    Shimada, K.2    Nagahama, M.3    Okazaki, R.4    Kawashima, T.5
  • 68
    • 13344283840 scopus 로고
    • Zur desoxygenierung von tritylthionitrit
    • Haake M (1972) Zur desoxygenierung von tritylthionitrit. Tetrahedron Lett 13:33-39
    • (1972) Tetrahedron Lett , vol.13 , pp. 33-39
    • Haake, M.1
  • 69
    • 58849148335 scopus 로고    scopus 로고
    • Quantifying the global cellular thiol-disulfide status
    • Hansen RE, Roth D, Winther JR (2009) Quantifying the global cellular thiol-disulfide status. Proc Natl Acad Sci USA 106:422-427
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 422-427
    • Hansen, R.E.1    Roth, D.2    Winther, J.R.3
  • 70
    • 0011790730 scopus 로고
    • Organic sulfur chemistry. 33. Chemistry of sulfenic sulfonic thioanhydrides. Solvent-dependent sulfur extrusion
    • Harpp DN, Ash DK, Smith RA (1979) Organic sulfur chemistry. 33. Chemistry of sulfenic sulfonic thioanhydrides. Solvent-dependent sulfur extrusion. J Org Chem 44:4135-4140
    • (1979) J Org Chem , vol.44 , pp. 4135-4140
    • Harpp, D.N.1    Ash, D.K.2    Smith, R.A.3
  • 71
    • 70449679220 scopus 로고    scopus 로고
    • The role of hypothiocyanous acid (HOSCN) in biological systems
    • Hawkins CL (2009) The role of hypothiocyanous acid (HOSCN) in biological systems. Free Radic Res 43:1147-1158
    • (2009) Free Radic Res , vol.43 , pp. 1147-1158
    • Hawkins, C.L.1
  • 72
    • 0003294513 scopus 로고
    • Lumazinesulfenates-a new class of stable sulfenic acids
    • Heckel A, Pfleiderer W (1983) Lumazinesulfenates-a new class of stable sulfenic acids. Tetrahedron Lett 24:5047-5050
    • (1983) Tetrahedron Lett , vol.24 , pp. 5047-5050
    • Heckel, A.1    Pfleiderer, W.2
  • 74
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N (2002) The biochemistry and physiology of S-nitrosothiols. Annu Rev Pharmacol Toxicol 42:585-600
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 585-600
    • Hogg, N.1
  • 75
    • 37049109654 scopus 로고
    • The ambident nucleophilicity of sulphenate anions
    • Hogg DR, Robinson A (1979) The ambident nucleophilicity of sulphenate anions. J Chem Soc Perkin Trans 1:1125-1128
    • (1979) J Chem Soc Perkin Trans , vol.1 , pp. 1125-1128
    • Hogg, D.R.1    Robinson, A.2
  • 76
    • 0034256633 scopus 로고    scopus 로고
    • Reaction of ascorbic acid with snitrosothiols: Clear evidence for two distinct reaction pathways
    • Holmes AJ, Williams DLH (2000) Reaction of ascorbic acid with snitrosothiols: clear evidence for two distinct reaction pathways. J Chem Soc Perkin Trans 2:1639-1644
    • (2000) J Chem Soc Perkin Trans , vol.2 , pp. 1639-1644
    • Holmes, A.J.1    Williams, D.L.H.2
  • 77
    • 1642314171 scopus 로고    scopus 로고
    • Interior surface modification of bacteriophage MS2
    • Hooker JM, Kovacs EW, Francis MB (2004) Interior surface modification of bacteriophage MS2. J Am Chem Soc 126:3718-3719
    • (2004) J Am Chem Soc , vol.126 , pp. 3718-3719
    • Hooker, J.M.1    Kovacs, E.W.2    Francis, M.B.3
  • 78
    • 33746070773 scopus 로고    scopus 로고
    • An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay
    • Huang B, Chen C (2006) An ascorbate-dependent artifact that interferes with the interpretation of the biotin switch assay. Free Radic Biol Med 41:562-567
    • (2006) Free Radic Biol Med , vol.41 , pp. 562-567
    • Huang, B.1    Chen, C.2
  • 79
    • 33847046018 scopus 로고    scopus 로고
    • Modification of protein by disulfide S-monoxide and disulfide S-dioxide: Distinctive effects on PKC
    • Huang KP, Huang FL, Shetty PK, Yergey AL (2007) Modification of protein by disulfide S-monoxide and disulfide S-dioxide: distinctive effects on PKC. Biochemistry 46:1961-1971
    • (2007) Biochemistry , vol.46 , pp. 1961-1971
    • Huang, K.P.1    Huang, F.L.2    Shetty, P.K.3    Yergey, A.L.4
  • 80
    • 70350050576 scopus 로고    scopus 로고
    • Thiol and Sulfenic Acid Oxidation of AhpE, the One-Cysteine Peroxiredoxin from Mycobacterium tuberculosis: Kinetics, Acidity Constants, and Conformational Dynamics
    • Hugo M, Turell L, Manta B, Botti H, Monteiro G, Netto LES, Alvarez B (2009) Thiol and Sulfenic Acid Oxidation of AhpE, the One-Cysteine Peroxiredoxin from Mycobacterium tuberculosis: Kinetics, Acidity Constants, and Conformational Dynamics. Biochemistry 48:9416-9426
    • (2009) Biochemistry , vol.48 , pp. 9416-9426
    • Hugo, M.1    Turell, L.2    Manta, B.3    Botti, H.4    Monteiro, G.5    Netto, L.E.S.6    Alvarez, B.7
  • 82
    • 79953724030 scopus 로고    scopus 로고
    • Open season for hunting and trapping post-translational cysteine modifications in proteins and enzymes
    • Jacob C, Ba LA (2011) Open season for hunting and trapping post-translational cysteine modifications in proteins and enzymes. Chembiochem 12:841-844
    • (2011) Chembiochem , vol.12 , pp. 841-844
    • Jacob, C.1    Ba, L.A.2
  • 84
    • 33845186258 scopus 로고
    • Reactivity of nucleophilic reagents towards esters
    • Jencks WP, Carriulo JC (1960) Reactivity of nucleophilic reagents towards esters. J Am Chem Soc 82:1778-1786
    • (1960) J Am Chem Soc , vol.82 , pp. 1778-1786
    • Jencks, W.P.1    Carriulo, J.C.2
  • 85
    • 64549161166 scopus 로고    scopus 로고
    • Kinetic and thermodynamic aspects of cellular thioldisulfide redox regulation
    • Jensen KS, Hansen RE, Winther JR (2009) Kinetic and thermodynamic aspects of cellular thioldisulfide redox regulation. Antioxid Redox Signal 11:1047-1058
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1047-1058
    • Jensen, K.S.1    Hansen, R.E.2    Winther, J.R.3
  • 86
    • 38049044980 scopus 로고    scopus 로고
    • Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace
    • Jönsson TJ, Johnson LC, Lowther WT (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
  • 87
    • 0038182543 scopus 로고    scopus 로고
    • Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism
    • Jourd'heuil D, Jourd'heuil FL, Feelisch M (2003) Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism. J Biol Chem 278:15720-15726
    • (2003) J Biol Chem , vol.278 , pp. 15720-15726
    • Jourd'heuil, D.1    Jourd'heuil, F.L.2    Feelisch, M.3
  • 88
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil O, Banerjee R (2010) Redox biochemistry of hydrogen sulfide. J Biol Chem 285: 21903-21907
    • (2010) J Biol Chem , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 89
    • 0015894552 scopus 로고
    • Studies on "lactam antibiotics. I. A novel conversion of penicillins into cephalosporins
    • Kamiya T, Teraji T, Saito Y, Hasimoto M, Nakaguchi O, Oka T (1973) Studies on "lactam antibiotics. I. A novel conversion of penicillins into cephalosporins. Tetrahedron Lett 14: 3001-3004
    • (1973) Tetrahedron Lett , vol.14 , pp. 3001-3004
    • Kamiya, T.1    Teraji, T.2    Saito, Y.3    Hasimoto, M.4    Nakaguchi, O.5    Oka, T.6
  • 92
    • 74049084627 scopus 로고    scopus 로고
    • Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: How are S-nitrosothiols formed
    • Keszler A, Zhang Y, Hogg N (2010) Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: how are S-nitrosothiols formed? Free Radic Biol Med 48:55-64
    • (2010) Free Radic Biol Med , vol.48 , pp. 55-64
    • Keszler, A.1    Zhang, Y.2    Hogg, N.3
  • 93
    • 77953152341 scopus 로고    scopus 로고
    • Reactivity of sodium arenesulfinates in the substitution reaction to "-functionalized allyl bromides
    • Khamis G, Stoevaa S, Aleksieva D (2010) Reactivity of sodium arenesulfinates in the substitution reaction to "-functionalized allyl bromides. J Phys Org Chem 23:461-467
    • (2010) J Phys Org Chem , vol.23 , pp. 461-467
    • Khamis, G.1    Stoevaa, S.2    Aleksieva, D.3
  • 95
    • 33947474444 scopus 로고
    • Studies in stereochemistry. XXXII. Mechanism of elimination of sulfoxides
    • Kingsbury CA, Cram DJ (1960) Studies in stereochemistry. XXXII. Mechanism of elimination of sulfoxides. J Am Chem Soc 82:1810-1819
    • (1960) J Am Chem Soc , vol.82 , pp. 1810-1819
    • Kingsbury, C.A.1    Cram, D.J.2
  • 96
    • 64549140250 scopus 로고    scopus 로고
    • New insights into the S-nitrosothiolascorbate reaction. the formation of nitroxyl
    • Kirsch M, Buscher AM, Aker S, Schulz R, de Groot H (2009) New insights into the S-nitrosothiolascorbate reaction. The formation of nitroxyl. Org Biomol Chem 7:1954-1962
    • (2009) Org Biomol Chem , vol.7 , pp. 1954-1962
    • Kirsch, M.1    Buscher, A.M.2    Aker, S.3    Schulz, R.4    De Groot, H.5
  • 97
    • 0030781227 scopus 로고    scopus 로고
    • Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis
    • Kissner R, Nauser T, Bugnon P, Lye PG, Koppenol WH (1997) Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis. Chem Res Toxicol 10:1285-1292
    • (1997) Chem Res Toxicol , vol.10 , pp. 1285-1292
    • Kissner, R.1    Nauser, T.2    Bugnon, P.3    Lye, P.G.4    Koppenol, W.H.5
  • 99
    • 79954486027 scopus 로고    scopus 로고
    • Development of an Si-rhodamine-based far-red to near-infrared fluorescence probe selective for hypochlorous acid and its applications for biological imaging
    • Koide Y, Urano Y, Hanaoka K, Terai T, Nagano T (2011) Development of an Si-rhodamine-based far-red to near-infrared fluorescence probe selective for hypochlorous acid and its applications for biological imaging. J Am Chem Soc 133:5680-5682
    • (2011) J Am Chem Soc , vol.133 , pp. 5680-5682
    • Koide, Y.1    Urano, Y.2    Hanaoka, K.3    Terai, T.4    Nagano, T.5
  • 101
    • 83655165310 scopus 로고    scopus 로고
    • H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response
    • ra86
    • Krishnan N, Fu C, Pappin DJ, Tonks NK (2011) H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci Signal 4:ra86
    • (2011) Sci Signal , vol.4
    • Krishnan, N.1    Fu, C.2    Pappin, D.J.3    Tonks, N.K.4
  • 102
    • 0037724313 scopus 로고
    • Electrophilic displacement reactions. IX. Effects of substituents on rates of reactions between hydrogen peroxide and benzeneboronic acid
    • Kuivila HG, Armour AG (1957) Electrophilic displacement reactions. IX. Effects of substituents on rates of reactions between hydrogen peroxide and benzeneboronic acid. J Am Chem Soc 79:5659-5662
    • (1957) J Am Chem Soc , vol.79 , pp. 5659-5662
    • Kuivila, H.G.1    Armour, A.G.2
  • 104
    • 34247846153 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B (PTP1B) by Peroxymonophosphate (DO3POOH)
    • LaButti J, Chowdhury G, Reilly TJ, Gates KS (2007) Redox regulation of protein tyrosine phosphatase 1B (PTP1B) by Peroxymonophosphate (DO3POOH). J Am Chem Soc 129:5320-5321
    • (2007) J Am Chem Soc , vol.129 , pp. 5320-5321
    • Labutti, J.1    Chowdhury, G.2    Reilly, T.J.3    Gates, K.S.4
  • 105
    • 34547399134 scopus 로고    scopus 로고
    • A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR
    • Lee JW, Soonsanga S, Helmann JD (2007) A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR. Proc Natl Acad Sci USA 104:8743-8748
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8743-8748
    • Lee, J.W.1    Soonsanga, S.2    Helmann, J.D.3
  • 106
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cell
    • Leonard SE, Reddie KG, Carroll KS (2009) Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cell. ACS Chem Biol 4:783-799
    • (2009) ACS Chem Biol , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 109
    • 82355164580 scopus 로고    scopus 로고
    • Identification of protein nitrosothiols using phosphinemediated selective reduction
    • Li S, Wang H, Xian M, Whorton R (2012) Identification of protein nitrosothiols using phosphinemediated selective reduction. Nitric Oxide 26:20-26
    • (2012) Nitric Oxide , vol.26 , pp. 20-26
    • Li, S.1    Wang, H.2    Xian, M.3    Whorton, R.4
  • 110
    • 33846432398 scopus 로고    scopus 로고
    • Metal-based turn-on fluorescent probes for sensing nitric oxide
    • Lim ML, Lippard SJ (2007) Metal-based turn-on fluorescent probes for sensing nitric oxide. Acc Chem Res 40:41-51
    • (2007) Acc Chem Res , vol.40 , pp. 41-51
    • Lim, M.L.1    Lippard, S.J.2
  • 111
    • 57649213405 scopus 로고    scopus 로고
    • Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity
    • Lim JC, Choi HI, Park YS, Nam HW, Woo HA, Kwon KS, Kim YS, Rhee SG, Kim K, Chae HZ (2008) Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity. J Biol Chem 283:28873-28880
    • (2008) J Biol Chem , vol.283 , pp. 28873-28880
    • Lim, J.C.1    Choi, H.I.2    Park, Y.S.3    Nam, H.W.4    Woo, H.A.5    Kwon, K.S.6    Kim, Y.S.7    Rhee, S.G.8    Kim, K.9    Chae, H.Z.10
  • 112
    • 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 108:10472-10477
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 10472-10477
    • Lim, J.C.1    You, Z.2    Kim, G.3    Levine, R.L.4
  • 113
    • 0008476548 scopus 로고
    • Selective reduction of nitro-heterocycles with sodium sulfide in aqueous p-dioxane
    • Lin Y-I, Lang SA Jr (1980) Selective reduction of nitro-heterocycles with sodium sulfide in aqueous p-dioxane. J Heterocycl Chem 17:1273-1275
    • (1980) J Heterocycl Chem , vol.17 , pp. 1273-1275
    • Lin, Y.-I.1    Lang, S.A.2
  • 114
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind C, Gerdes R, Hamnell Y, Schuppe-Koistinen I, von Lowenhielm HB, Holmgren A, Cotgreave IA (2002) Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch Biochem Biophys 406:229-240
    • (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
  • 115
    • 79959901325 scopus 로고    scopus 로고
    • Reaction-based fluorescent probes for selective imaging of hydrogen sulfide in living cells
    • Lippert AR, New EJ, Chang CJ (2011) Reaction-based fluorescent probes for selective imaging of hydrogen sulfide in living cells. J Am Chem Soc 133:10078-10080
    • (2011) J Am Chem Soc , vol.133 , pp. 10078-10080
    • Lippert, A.R.1    New, E.J.2    Chang, C.J.3
  • 116
    • 0015349242 scopus 로고
    • Kinetics of the reversible reaction of papain with 5, 50-dithiobis-(2-nitrobenzoate) dianion: Evidence for nucleophilic reactivity in the un-ionized thiol group of cysteine-25 and for general acid catalysis by histidine-159 of the reaction of the 5-mercapto-2-nitrobenzoate dianion with the papain-5-mercapto-2-nitrobenzoate mixed disulphide
    • Little G, Brocklehurst K (1972) Kinetics of the reversible reaction of papain with 5, 50-dithiobis-(2-nitrobenzoate) dianion: evidence for nucleophilic reactivity in the un-ionized thiol group of cysteine-25 and for general acid catalysis by histidine-159 of the reaction of the 5-mercapto-2-nitrobenzoate dianion with the papain-5-mercapto-2-nitrobenzoate mixed disulphide. Biochem J 128:475-477
    • (1972) Biochem J , vol.128 , pp. 475-477
    • Little, G.1    Brocklehurst, K.2
  • 118
    • 50949098899 scopus 로고    scopus 로고
    • Hypothiocyanous acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous acid or hypobromous acid
    • LloydMM, Van Reyk DM, DaviesMJ, Hawkins CL (2008) Hypothiocyanous acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous acid or hypobromous acid. Biochem J 414:271-280
    • (2008) Biochem J , vol.414 , pp. 271-280
    • Lloyd, M.M.1    Van Reyk, D.M.2    Davies, M.J.3    Hawkins, C.L.4
  • 119
    • 84862692522 scopus 로고    scopus 로고
    • Chemoselective ligation of sulfinic acids with aryl-nitroso compounds (2012)
    • Lo Conte M, Carroll KS (2012) Chemoselective ligation of sulfinic acids with aryl-nitroso compounds (2012) Angew Chem Inter Ed 51:6502-6505
    • (2012) Angew Chem Inter Ed , vol.51 , pp. 6502-6505
    • Lo Conte, M.1    Carroll, K.S.2
  • 120
    • 14344251523 scopus 로고    scopus 로고
    • Kinetics and mechanism of the reaction of cysteine and hydrogen peroxide in aqueous solution
    • Luo D, Smith SW, Anderson BD (2004) Kinetics and mechanism of the reaction of cysteine and hydrogen peroxide in aqueous solution. J Pharm Sci 94:304-316
    • (2004) J Pharm Sci , vol.94 , pp. 304-316
    • Luo, D.1    Smith, S.W.2    Anderson, B.D.3
  • 121
    • 0019350010 scopus 로고
    • Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates
    • Maker HS, Weiss C, Silides DJ, Cohen G (1981) Coupling of dopamine oxidation (monoamine oxidase activity) to glutathione oxidation via the generation of hydrogen peroxide in rat brain homogenates. J Neurochem 36:589-593
    • (1981) J Neurochem , vol.36 , pp. 589-593
    • Maker, H.S.1    Weiss, C.2    Silides, D.J.3    Cohen, G.4
  • 122
    • 78649486199 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: Studies with a novel anti-dimedone sulfenic acid antibody
    • Maller C, Schröder E, Eaton P (2011) Glyceraldehyde 3-phosphate dehydrogenase is unlikely to mediate hydrogen peroxide signaling: studies with a novel anti-dimedone sulfenic acid antibody. Antioxid Redox Signal 14:49-60
    • (2011) Antioxid Redox Signal , vol.14 , pp. 49-60
    • Maller, C.1    Schröder, E.2    Eaton, P.3
  • 123
    • 0029560675 scopus 로고
    • Taurine chioramine, a product of activated neutrophils, inhibits in vitro the generation of nitric oxide and other macrophage inflammatory mediators
    • Marcinkiewicz J, Grabowska A, Bereta J, Stelmaszynska T (1995) Taurine chioramine, a product of activated neutrophils, inhibits in vitro the generation of nitric oxide and other macrophage inflammatory mediators. J Leukco Biol 58:667-674
    • (1995) J Leukco Biol , vol.58 , pp. 667-674
    • Marcinkiewicz, J.1    Grabowska, A.2    Bereta, J.3    Stelmaszynska, T.4
  • 124
    • 0031460696 scopus 로고    scopus 로고
    • Peroxynitrite rapidly permeates phospholipid membranes
    • Marla SS, Lee J, Groves JT (1997) Peroxynitrite rapidly permeates phospholipid membranes. Proc Natl Acad Sci USA 94:14243-14248
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14243-14248
    • Marla, S.S.1    Lee, J.2    Groves, J.T.3
  • 125
    • 0023953313 scopus 로고
    • Protein reactions with methyl and ethyl vinyl sulfones
    • Masri MS, Friedman M (1988) Protein reactions with methyl and ethyl vinyl sulfones. J Protein Chem 7:49-54
    • (1988) J Protein Chem , vol.7 , pp. 49-54
    • Masri, M.S.1    Friedman, M.2
  • 128
    • 0348014634 scopus 로고    scopus 로고
    • Improved beta-elimination-based affinity purification strategy for enrichment of phosphopeptides
    • McLachlin DT, Chait BT (2003) Improved beta-elimination-based affinity purification strategy for enrichment of phosphopeptides. Anal Chem 75:6826-6836
    • (2003) Anal Chem , vol.75 , pp. 6826-6836
    • McLachlin, D.T.1    Chait, B.T.2
  • 129
    • 33646761969 scopus 로고    scopus 로고
    • IB is a sensitive target for oxidation by cell-permeable chloramines: Inhibition of NF-B activity by glycine chloramine through methionine oxidation
    • Midwinter RG, Cheah F-C, Moskovitz J, Vissers MC, Winterbourn CC (2006) IB is a sensitive target for oxidation by cell-permeable chloramines: inhibition of NF-B activity by glycine chloramine through methionine oxidation. Biochem J 396:71-78
    • (2006) Biochem J , vol.396 , pp. 71-78
    • Midwinter, R.G.1    Cheah, F.-C.2    Moskovitz, J.3    Vissers, M.C.4    Winterbourn, C.C.5
  • 130
    • 77957652745 scopus 로고    scopus 로고
    • Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
    • Miller EW, Dickinson BC, Chang CJ (2010) Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc Natl Acad Sci USA 107:15681-15686
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15681-15686
    • Miller, E.W.1    Dickinson, B.C.2    Chang, C.J.3
  • 131
    • 0036667914 scopus 로고    scopus 로고
    • A spectrophotometric assay for allicin, alliin, and alliinase (alliin lyase) with a chromogenic thiol: Reaction of 4-mercaptopyridine with thiosulfinates
    • Miron T, Shin I, Feigenblat G, Weiner L, Mirelman D, Wilchek M, Rabinkov A (2002) A spectrophotometric assay for allicin, alliin, and alliinase (alliin lyase) with a chromogenic thiol: reaction of 4-mercaptopyridine with thiosulfinates. Anal Biochem 307:76-83
    • (2002) Anal Biochem , vol.307 , pp. 76-83
    • Miron, T.1    Shin, I.2    Feigenblat, G.3    Weiner, L.4    Mirelman, D.5    Wilchek, M.6    Rabinkov, A.7
  • 132
    • 34247604468 scopus 로고    scopus 로고
    • Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C
    • Monteiro G, Horta BB, Pimenta DC, Augusto O, Netto LES (2007) Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C. Proc Natl Acad Sci 104:4886-4891
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 4886-4891
    • Monteiro, G.1    Horta, B.B.2    Pimenta, D.C.3    Augusto, O.4    Netto, L.E.S.5
  • 133
    • 79953032428 scopus 로고    scopus 로고
    • Kinetics and mechanism of S-nitrosothiol acid-catalyzed hydrolysis: Sulfur activation promotes facile NOCrelease
    • Moran EE, Timerghazin QK, Kwong E, English AM (2011) Kinetics and mechanism of S-nitrosothiol acid-catalyzed hydrolysis: sulfur activation promotes facile NOCrelease. J Phys Chem B 115:3112-3126
    • (2011) J Phys Chem B , vol.115 , pp. 3112-3126
    • Moran, E.E.1    Timerghazin, Q.K.2    Kwong, E.3    English, A.M.4
  • 135
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: Delivering sulfur in biosynthetic pathways
    • Mueller EG (2006) Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol 2:185-194
    • (2006) Nat Chem Biol , vol.2 , pp. 185-194
    • Mueller, E.G.1
  • 136
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP (2009) How mitochondria produce reactive oxygen species. Biochem J 417:1-13
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 139
    • 36148995826 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid
    • Nagy P, Ashby MT (2007a) Reactive sulfur species: kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid. J Am Chem Soc 129:14082-14091
    • (2007) J Am Chem Soc , vol.129 , pp. 14082-14091
    • Nagy, P.1    Ashby, M.T.2
  • 140
    • 35148881746 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanism of the hydrolysis of cysteine thiosulfinate ester
    • Nagy P, Ashby MT (2007b) Reactive sulfur species: kinetics and mechanism of the hydrolysis of cysteine thiosulfinate ester. Chem Res Toxicol 20:1364-1372
    • (2007) Chem Res Toxicol , vol.20 , pp. 1364-1372
    • Nagy, P.1    Ashby, M.T.2
  • 141
    • 77958095282 scopus 로고    scopus 로고
    • Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides
    • Nagy P, Winterbourn CC (2010) Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides. Chem Res Toxicol 23:1541-1543
    • (2010) Chem Res Toxicol , vol.23 , pp. 1541-1543
    • Nagy, P.1    Winterbourn, C.C.2
  • 142
    • 33646078598 scopus 로고    scopus 로고
    • Thiocyanate is an efficient endogenous scavenger of the phagocytic killing agent hypobromous acid
    • Nagy P, Beal JL, Ashby MT (2006) Thiocyanate is an efficient endogenous scavenger of the phagocytic killing agent hypobromous acid. Chem Res Toxicol 19:587-593
    • (2006) Chem Res Toxicol , vol.19 , pp. 587-593
    • Nagy, P.1    Beal, J.L.2    Ashby, M.T.3
  • 143
    • 35948954266 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanisms of the reaction of cysteine thiosulfinate ester with cysteine to give cysteine sulfenic acid
    • Nagy P, Lemma K, Ashby MT (2007) Reactive sulfur species: kinetics and mechanisms of the reaction of cysteine thiosulfinate ester with cysteine to give cysteine sulfenic acid. J Org Chem 72:8838-8846
    • (2007) J Org Chem , vol.72 , pp. 8838-8846
    • Nagy, P.1    Lemma, K.2    Ashby, M.T.3
  • 144
    • 72749119238 scopus 로고    scopus 로고
    • Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione
    • Nagy P, Jameson GN, Winterbourn CC (2009) Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione. Chem Res Toxicol 22:1833-1840
    • (2009) Chem Res Toxicol , vol.22 , pp. 1833-1840
    • Nagy, P.1    Jameson, G.N.2    Winterbourn, C.C.3
  • 145
    • 79955967159 scopus 로고    scopus 로고
    • Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide. A kinetic and computational study
    • Nagy P, Karton A, Betz A, Peskin AV, Pace P, O'Reilly RJ, Hampton MB, Radom L, Winterbourn CC (2011) Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide. A kinetic and computational study. J Biol Chem 286(20):18048-18055
    • (2011) J Biol Chem , vol.286 , Issue.20 , pp. 18048-18055
    • Nagy, P.1    Karton, A.2    Betz, A.3    Peskin, A.V.4    Pace, P.5    O'reilly, R.J.6    Hampton, M.B.7    Radom, L.8    Winterbourn, C.C.9
  • 146
    • 0000721402 scopus 로고
    • A stable sulfenic acid, 9-triptycenesulfenic acid: Its isolation and characterization
    • Nakamura N (1983) A stable sulfenic acid, 9-triptycenesulfenic acid: its isolation and characterization. J Am Chem Soc 105:7172-7173
    • (1983) J Am Chem Soc , vol.105 , pp. 7172-7173
    • Nakamura, N.1
  • 149
    • 79955577659 scopus 로고    scopus 로고
    • Reversion of sulfenamide prodrugs in the presence of free thiol-containing proteins
    • Nti-Addae KW, Laurence JS, Skinner AL, Stella VJ (2011) Reversion of sulfenamide prodrugs in the presence of free thiol-containing proteins. J Pharm Sci 100:3023-3027
    • (2011) J Pharm Sci , vol.100 , pp. 3023-3027
    • Nti-Addae, K.W.1    Laurence, J.S.2    Skinner, A.L.3    Stella, V.J.4
  • 150
    • 9344226175 scopus 로고
    • Kinetics of the addition of substituted benzenesulfinic acids to p-benzoquinone
    • Ogata Y, Sawaki Y, Isono M (1970) Kinetics of the addition of substituted benzenesulfinic acids to p-benzoquinone. Tetrahedron 26:731-736
    • (1970) Tetrahedron , vol.26 , pp. 731-736
    • Ogata, Y.1    Sawaki, Y.2    Isono, M.3
  • 151
    • 2142721825 scopus 로고    scopus 로고
    • HysTag-a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain
    • Olsen JV, Andersen JR, Nielsen PA, Nielsen ML, Figeys D, Mann M, Wisniewski JR (2004) HysTag-a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain. Mol Cell Prot 3:82-92
    • (2004) Mol Cell Prot , vol.3 , pp. 82-92
    • Olsen, J.V.1    Andersen, J.R.2    Nielsen, P.A.3    Nielsen, M.L.4    Figeys, D.5    Mann, M.6    Wisniewski, J.R.7
  • 152
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher P, Beckman JS, Liaudet L (2007) Nitric oxide and peroxynitrite in health and disease. Physiol Rev 87:315-424
    • (2007) Physiol Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 153
    • 70349808080 scopus 로고    scopus 로고
    • Synthesis of neamine-derived pseudodisaccharides by stereo-and regio-selective functional group transformations
    • Pang L-J, Wang D, Zhou J, Zhang L-H, Ye X-S (2009) Synthesis of neamine-derived pseudodisaccharides by stereo-and regio-selective functional group transformations. Org Biomol Chem 7:4252-4266
    • (2009) Org Biomol Chem , vol.7 , pp. 4252-4266
    • Pang, L.-J.1    Wang, D.2    Zhou, J.3    Zhang, L.-H.4    Ye, X.-S.5
  • 154
    • 0036936764 scopus 로고    scopus 로고
    • Reaction of [18F] 4-fluorobenzenediazonium cations with cysteine or the cysteinyl group: Preparation of 18F-labeled S-aryl-cysteine and a radiolabeled peptide
    • Patt J, Patt M (2002) Reaction of [18F] 4-fluorobenzenediazonium cations with cysteine or the cysteinyl group: preparation of 18F-labeled S-aryl-cysteine and a radiolabeled peptide. J Label Compd Radiopharm 45:1229-1238
    • (2002) J Label Compd Radiopharm , vol.45 , pp. 1229-1238
    • Patt, J.1    Patt, M.2
  • 155
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds
    • Pattison DI, Davies MJ (2001) Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds. Chem Res Toxicol 14:1453-1464
    • (2001) Chem Res Toxicol , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 156
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • Paulsen CE, Carroll KS (2010) Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol 5:47-62
    • (2010) ACS Chem Biol , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 158
    • 78049506720 scopus 로고    scopus 로고
    • HKGreen-3: A rhodol-based fluorescent probe for peroxynitrite
    • Peng T, Yang D (2010) HKGreen-3: a rhodol-based fluorescent probe for peroxynitrite. Org Lett 12:4932-4935
    • (2010) Org Lett , vol.12 , pp. 4932-4935
    • Peng, T.1    Yang, D.2
  • 159
    • 0033550050 scopus 로고    scopus 로고
    • Inhibition of cathepsin K by nitric oxide donors: Evidence for the formation of mixed disulfides and a sulfenic acid
    • Percival MD, OuelletM, Campagnolo C, Claveau D, Li C (1999) Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Biochemistry 38:13574-13583
    • (1999) Biochemistry , vol.38 , pp. 13574-13583
    • Percival, M.D.1    Ouellet, M.2    Campagnolo, C.3    Claveau, D.4    Li, C.5
  • 161
    • 27944488351 scopus 로고    scopus 로고
    • Synthesis of chemical probes to Map sulfenic acid modifications on proteins
    • Poole B, Zeng B-B, Knaggs SA, Yakubu M, King SB (2005) Synthesis of chemical probes to Map sulfenic acid modifications on proteins. Bioconjug Chem 16:1624-1628
    • (2005) Bioconjug Chem , vol.16 , pp. 1624-1628
    • Poole, B.1    Zeng, B.-B.2    Knaggs, S.A.3    Yakubu, M.4    King, S.B.5
  • 163
    • 37149012352 scopus 로고    scopus 로고
    • Fenton chemistry in biology and medicine
    • Prousek J (2007) Fenton chemistry in biology and medicine. Pure Appl Chem 79:2325-2338
    • (2007) Pure Appl Chem , vol.79 , pp. 2325-2338
    • Prousek, J.1
  • 167
    • 0035823537 scopus 로고    scopus 로고
    • Novel intra-and inter-molecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation
    • Raftery MJ, Yang Z, Valenzuela SM, Geczy CL (2001) Novel intra-and inter-molecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation. J Biol Chem 276:33393-33401
    • (2001) J Biol Chem , vol.276 , pp. 33393-33401
    • Raftery, M.J.1    Yang, Z.2    Valenzuela, S.M.3    Geczy, C.L.4
  • 168
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • Reddie KG, Carroll KS (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
  • 169
    • 79951643450 scopus 로고    scopus 로고
    • Multiple functions of peroxiredoxins: Peroxidases, sensors and regulators of the intracellular messenger H2O2, and protein chaperones
    • Rhee SG, Woo HA (2011) Multiple functions of peroxiredoxins: peroxidases, sensors and regulators of the intracellular messenger H2O2, and protein chaperones. Antioxid Redox Signal 15:781-794
    • (2011) Antioxid Redox Signal , vol.15 , pp. 781-794
    • Rhee, S.G.1    Woo, H.A.2
  • 170
    • 0001023083 scopus 로고
    • The reaction of diazonium salts with nucleophiles. VIII. the formation of diazosulfones and the application of linear free energy equations to diazonium salt reactions
    • Ritchie CD, Saltiel JD, Lewis ES (1961) The reaction of diazonium salts with nucleophiles. VIII. The formation of diazosulfones and the application of linear free energy equations to diazonium salt reactions. J Am Chem Soc 83:4601-4605
    • (1961) J Am Chem Soc , vol.83 , pp. 4601-4605
    • Ritchie, C.D.1    Saltiel, J.D.2    Lewis, E.S.3
  • 171
    • 79959340042 scopus 로고    scopus 로고
    • Protein sulfenic acid formation: From cellular damage to redox regulation
    • Roos G, Messens J (2011) Protein sulfenic acid formation: from cellular damage to redox regulation. Free Radic Biol Med 51:314-326
    • (2011) Free Radic Biol Med , vol.51 , pp. 314-326
    • Roos, G.1    Messens, J.2
  • 172
  • 173
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • Saurin AT, Neubert H, Brennan JP, Eaton P (2004) Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc Natl Acad Sci 101:17982-17987
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 17982-17987
    • Saurin, A.T.1    Neubert, H.2    Brennan, J.P.3    Eaton, P.4
  • 174
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon E, Bertozzi CR (2000) Cell surface engineering by a modified Staudinger reaction. Science 287:2007-2010
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 176
    • 70349482669 scopus 로고    scopus 로고
    • Profiling protein thiol oxidation in tumor cells using sulfenic acidspecific antibodies
    • Seo YH, Carroll KS (2009) Profiling protein thiol oxidation in tumor cells using sulfenic acidspecific antibodies. Proc Natl Acad Sci USA 106:16163-16168
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16163-16168
    • Seo, Y.H.1    Carroll, K.S.2
  • 177
    • 79551676040 scopus 로고    scopus 로고
    • Quantification of protein sulfenic acid modifications using isotopecoded dimedone and iododimedone
    • Seo YH, Carroll KS (2011) Quantification of protein sulfenic acid modifications using isotopecoded dimedone and iododimedone. Angew Chem Int Ed 50:1342-1345
    • (2011) Angew Chem Int Ed , vol.50 , pp. 1342-1345
    • Seo, Y.H.1    Carroll, K.S.2
  • 178
    • 67650732916 scopus 로고    scopus 로고
    • Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B
    • Shetty V, Neubert TA (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
  • 179
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, WilmM, Vorm O, MannM(1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68:850-858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 180
    • 33846277598 scopus 로고    scopus 로고
    • Selective reduction of peptide isothiazolidin-3-ones
    • Shiau TP, Erlanson DA, Gordon EM (2006) Selective reduction of peptide isothiazolidin-3-ones. Org Lett 8:5697-5699
    • (2006) Org Lett , vol.8 , pp. 5697-5699
    • Shiau, T.P.1    Erlanson, D.A.2    Gordon, E.M.3
  • 181
    • 23744499223 scopus 로고    scopus 로고
    • A chemical model for redox regulation of protein tyrosine phosphatase 1B (PTP1B) activity
    • Sivaramakrishnan S, Keerthi K, Gates KS (2005) A chemical model for redox regulation of protein tyrosine phosphatase 1B (PTP1B) activity. J Am Chem Soc 127:10830-10831
    • (2005) J Am Chem Soc , vol.127 , pp. 10830-10831
    • Sivaramakrishnan, S.1    Keerthi, K.2    Gates, K.S.3
  • 182
    • 28644447669 scopus 로고    scopus 로고
    • Interaction of hypohalous acids and heme peroxidases with unsaturated phosphatidylcholines
    • Spalteholz H, Wenske K, Arnhold J (2005) Interaction of hypohalous acids and heme peroxidases with unsaturated phosphatidylcholines. Biofactors 24:67-76
    • (2005) Biofactors , vol.24 , pp. 67-76
    • Spalteholz, H.1    Wenske, K.2    Arnhold, J.3
  • 183
    • 0032171410 scopus 로고    scopus 로고
    • Oxidative chemistry of nitric oxide: The roles of superoxide, peroxynitrite, and carbon dioxide
    • Squadrito GL, Pryor WA (1998) Oxidative chemistry of nitric oxide: the roles of superoxide, peroxynitrite, and carbon dioxide. Free Radic Biol Med 25:392-403
    • (1998) Free Radic Biol Med , vol.25 , pp. 392-403
    • Squadrito, G.L.1    Pryor, W.A.2
  • 184
    • 0034641689 scopus 로고    scopus 로고
    • Identification of oxidantsensitive proteins: TNF-alpha induces protein glutathiolation
    • Sullivan DM, Wehr NB, Fergusson MM, Levine RL, Finkel T (2000) Identification of oxidantsensitive proteins: TNF-alpha induces protein glutathiolation. Biochemistry 39:11121-11128
    • (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
  • 185
    • 52649151914 scopus 로고    scopus 로고
    • A highly specific BODIPY-based fluorescent probe for the detection of hypochlorous acid
    • Sun ZN, Liu FQ, Chen Y, Tam PK, Yang D (2008) A highly specific BODIPY-based fluorescent probe for the detection of hypochlorous acid. Org Lett 10:2171-2174
    • (2008) Org Lett , vol.10 , pp. 2171-2174
    • Sun, Z.N.1    Liu, F.Q.2    Chen, Y.3    Tam, P.K.4    Yang, D.5
  • 186
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabo C, Ischiropoulos H, Radi R (2007) Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discov 6:662-680
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 187
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized gluthathione
    • Szajewski RP, Whitesides GM (1980) Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized gluthathione. J Am Chem Soc 102:2011-2026
    • (1980) J Am Chem Soc , vol.102 , pp. 2011-2026
    • Szajewski, R.P.1    Whitesides, G.M.2
  • 188
    • 4344672779 scopus 로고    scopus 로고
    • Direct determination of thiol pKa by isothermal titration microcalorimetry
    • Tajc SG, Tolbert BS, Basavappa R, Miller BL (2004) Direct determination of thiol pKa by isothermal titration microcalorimetry. J Am Chem Soc 126:10508-10509
    • (2004) J Am Chem Soc , vol.126 , pp. 10508-10509
    • Tajc, S.G.1    Tolbert, B.S.2    Basavappa, R.3    Miller, B.L.4
  • 189
    • 0029943657 scopus 로고    scopus 로고
    • Kinetic characterization of the endogenous glutathione transferase activity of octopus lens S-crystallin
    • Tang SS, Chang GGJ (1996) Kinetic characterization of the endogenous glutathione transferase activity of octopus lens S-crystallin. Biochemistry 119:1182-1188
    • (1996) Biochemistry , vol.119 , pp. 1182-1188
    • Tang, S.S.1    Chang, G.G.J.2
  • 190
    • 35548974677 scopus 로고    scopus 로고
    • The mammalian N-end rule pathway: New insights into its components and physiological roles
    • Tasaki T, Kwon YT (2007) The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem Sci 32:520-528
    • (2007) Trends Biochem Sci , vol.32 , pp. 520-528
    • Tasaki, T.1    Kwon, Y.T.2
  • 191
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas JA, Poland B, Honzatko R (1995) Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 319:1-9
    • (1995) Arch Biochem Biophys , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 192
    • 0000902631 scopus 로고
    • Selectivity: A key to synthetic efficiency
    • Trost BM (1983) Selectivity: a key to synthetic efficiency. Science 219:245-250
    • (1983) Science , vol.219 , pp. 245-250
    • Trost, B.M.1
  • 193
    • 0033152455 scopus 로고    scopus 로고
    • Investigations of S-transnitrosylation reactions between low-and high-molecular-weight S-nitroso compounds and their thiols by high-performance liquid chromatography and gas chromatography-mass spectrometry
    • Tsikas D, Sandmann J, Rossa S, Gutzki FM, Frölich JC (1999) Investigations of S-transnitrosylation reactions between low-and high-molecular-weight S-nitroso compounds and their thiols by high-performance liquid chromatography and gas chromatography-mass spectrometry. Anal Biochem 270:231-241
    • (1999) Anal Biochem , vol.270 , pp. 231-241
    • Tsikas, D.1    Sandmann, J.2    Rossa, S.3    Gutzki, F.M.4    Frölich, J.C.5
  • 195
    • 0032706865 scopus 로고    scopus 로고
    • Nitrosation of 1, 2-phenylenediamine by peroxynitrite/CO2: Evidence for a free radical mechanism
    • Uppu RM, PryorWA (1999) Nitrosation of 1, 2-phenylenediamine by peroxynitrite/CO2: evidence for a free radical mechanism. J Am Chem Soc 121:9738-9739
    • (1999) J Am Chem Soc , vol.121 , pp. 9738-9739
    • Uppu, R.M.1    Pryor, W.A.2
  • 197
    • 15144349362 scopus 로고    scopus 로고
    • Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide
    • Van der Vliet A, Hoen PA, Wong PS, Bast A, Cross CE (1998) Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide. J Biol Chem 273:30255-30262
    • (1998) J Biol Chem , vol.273 , pp. 30255-30262
    • Van Der Vliet, A.1    Hoen, P.A.2    Wong, P.S.3    Bast, A.4    Cross, C.E.5
  • 198
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • Van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H (2003) Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423:773-777
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 199
    • 77950805698 scopus 로고    scopus 로고
    • Hydrogen sulfide: The third gasotransmitter in biology and medicine
    • Wang R (2010) Hydrogen sulfide: the third gasotransmitter in biology and medicine. Antioxid Redox Signal 12:1061-1064
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1061-1064
    • Wang, R.1
  • 200
    • 52449112301 scopus 로고    scopus 로고
    • Fast reductive ligation of S-nitrosothiols
    • Wang H, Xian M (2008) Fast reductive ligation of S-nitrosothiols. Angew Chem Int Ed Engl 47:6598-6601
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 6598-6601
    • Wang, H.1    Xian, M.2
  • 201
    • 79851509433 scopus 로고    scopus 로고
    • Chemical methods to detect S-nitrosation
    • Wang H, XianM(2011) Chemical methods to detect S-nitrosation. Curr Opin Chem Biol 15:32-37
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 32-37
    • Wang, H.1    Xian, M.2
  • 202
    • 0035797915 scopus 로고    scopus 로고
    • An unusually low pKa for Cys-282 in the active site of human muscle creatine kinase
    • Wang P-F, McLeish MJ, Kneen MM, Lee G, Kenyon GL (2001) An unusually low pKa for Cys-282 in the active site of human muscle creatine kinase. Biochemistry 40:11698-11705
    • (2001) Biochemistry , vol.40 , pp. 11698-11705
    • Wang, P.-F.1    McLeish, M.J.2    Kneen, M.M.3    Lee, G.4    Kenyon, G.L.5
  • 203
    • 45549108466 scopus 로고    scopus 로고
    • Disparate proteome reactivity profiles of carbon electrophiles
    • Weerapana E, Simon GM, Cravatt BF (2008) Disparate proteome reactivity profiles of carbon electrophiles. Nat Chem Biol 4:405-407
    • (2008) Nat Chem Biol , vol.4 , pp. 405-407
    • Weerapana, E.1    Simon, G.M.2    Cravatt, B.F.3
  • 204
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn CC, Hampton MB (2008) Thiol chemistry and specificity in redox signaling. Free Radic Biol Med 45:549-561
    • (2008) Free Radic Biol Med , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 205
    • 0346850874 scopus 로고    scopus 로고
    • Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence
    • Woo HA, Kang SW, Kim HK, Yang KS, Chae HZ, Rhee SG (2003) Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence. J Biol Chem 278:47361-47364
    • (2003) J Biol Chem , vol.278 , pp. 47361-47364
    • Woo, H.A.1    Kang, S.W.2    Kim, H.K.3    Yang, K.S.4    Chae, H.Z.5    Rhee, S.G.6
  • 206
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood ZA, Poole LB, Karplus PA (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300:650-653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 207
    • 71549143840 scopus 로고    scopus 로고
    • Disulfides as redox switches: From molecular mechanisms to functional significance
    • Wouters MA, Fan SW, Haworth NL (2010) Disulfides as redox switches: from molecular mechanisms to functional significance. Antioxid Redox Signal 12:53-91
    • (2010) Antioxid Redox Signal , vol.12 , pp. 53-91
    • Wouters, M.A.1    Fan, S.W.2    Haworth, N.L.3
  • 209
    • 0034733112 scopus 로고    scopus 로고
    • Regioselective intramolecular oxidation of phenols and anisoles by dioxiranes generated in situ
    • Yang D, Wong M-K, Yan Z (2000) Regioselective intramolecular oxidation of phenols and anisoles by dioxiranes generated in situ. J Org Chem 65:4179-4184
    • (2000) J Org Chem , vol.65 , pp. 4179-4184
    • Yang, D.1    Wong, M.-K.2    Yan, Z.3
  • 210
    • 33646505308 scopus 로고    scopus 로고
    • A highly selective fluorescent probe for the detection and imaging of peroxynitrite in living cells
    • Yang D, Wang H-L, Sun Z-N, Chung N-W, Shen J-G (2006) A highly selective fluorescent probe for the detection and imaging of peroxynitrite in living cells. J Am Chem Soc 128:6004-6005
    • (2006) J Am Chem Soc , vol.128 , pp. 6004-6005
    • Yang, D.1    Wang, H.-L.2    Sun, Z.-N.3    Chung, N.-W.4    Shen, J.-G.5
  • 211
    • 62749100714 scopus 로고    scopus 로고
    • A rhodamine-hydroxamic acid-based fluorescent probe for hypochlorous acid and its applications to biological imagings
    • Yang ZYK, Cho HJ, Lee J, Shin I, Tae J (2009) A rhodamine-hydroxamic acid-based fluorescent probe for hypochlorous acid and its applications to biological imagings. Org Lett 11:859-861
    • (2009) Org Lett , vol.11 , pp. 859-861
    • Yang, Z.Y.K.1    Cho, H.J.2    Lee, J.3    Shin, I.4    Tae, J.5
  • 212
    • 0016803949 scopus 로고
    • The conversion of glyceraldehyde-3-phosphate dehydrogenase to an acylphosphatase by trinitroglycerin and inactivation of this activity by azide and ascorbate
    • You KS, Benitez LV, McConachie WA, Allison WS (1975) The conversion of glyceraldehyde-3-phosphate dehydrogenase to an acylphosphatase by trinitroglycerin and inactivation of this activity by azide and ascorbate. Biochem Biophys Acta 384:317-330
    • (1975) Biochem Biophys Acta , vol.384 , pp. 317-330
    • You, K.S.1    Benitez, L.V.2    McConachie, W.A.3    Allison, W.S.4
  • 213
    • 77956596119 scopus 로고    scopus 로고
    • Reductive ligation mediated onestep disulfide formation of S-nitrosothiols
    • Zhang J, Li S, Zhang D, Wang H, Whorton AR, Xian M (2010) Reductive ligation mediated onestep disulfide formation of S-nitrosothiols. Org Lett 12:4208-4211
    • (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
  • 214
    • 59949094333 scopus 로고    scopus 로고
    • Fluorogenic and chromogenic rhodamine spirolactam based probe for nitric oxide by spiro ring opening reaction
    • Zheng H, Shang G-H, Yang S-Y, Gao X, Xu J-G (2008) Fluorogenic and chromogenic rhodamine spirolactam based probe for nitric oxide by spiro ring opening reaction. Org Lett 10:2357-2360
    • (2008) Org Lett , vol.10 , pp. 2357-2360
    • Zheng, H.1    Shang, G.-H.2    Yang, S.-Y.3    Gao, X.4    Xu, J.-G.5


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