메뉴 건너뛰기




Volumn 17, Issue 7, 2012, Pages 969-980

The chemical biology of S-nitrosothiols

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; GLUTATHIONE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; OXYGEN; PROTEIN; S NITROSOTHIOL; THIOL; TRANSITION ELEMENT;

EID: 84864579819     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4590     Document Type: Review
Times cited : (204)

References (108)
  • 1
    • 0028987969 scopus 로고
    • NO +, NO, and NO-donation by S-nitrosothiols: Implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation
    • Arnelle DR and Stamler JS. NO+, NO, and NO-donation by S-nitrosothiols: implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation. Arch Biochem Biophys 318: 279-285, 1995.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 5
    • 84970604344 scopus 로고
    • The spectra and equilibria of nitrosonium ion, nitroacidium ion, and nitrous acid in solutions of sulphuric, hydrochloric, and phosporic acids
    • Bayliss, NS and Watts DW. The spectra and equilibria of nitrosonium ion, nitroacidium ion, and nitrous acid in solutions of sulphuric, hydrochloric, and phosporic acids. Aust J Chem 9: 319-332, 1956.
    • (1956) Aust J Chem , vol.9 , pp. 319-332
    • Bayliss, N.S.1    Watts, D.W.2
  • 6
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • DOI 10.1126/science.1158265
    • Benhar M, Forrester MT, Hess DT, and Stamler JS. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320: 1050-1054, 2008. (Pubitemid 351929542)
    • (2008) Science , vol.320 , Issue.5879 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 8
    • 63849086054 scopus 로고    scopus 로고
    • Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide
    • Bosworth CA, Toledo JC, Zmijewski JW, Li Q, and Lancaster Jr. Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide. Proc Natl Acad Sci USA 106: 4671-4676, 2009.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4671-4676
    • Bosworth, C.A.1    Toledo, J.C.2    Zmijewski, J.W.3    Li, Q.4    Lancaster, J.R.5
  • 9
    • 77958046248 scopus 로고    scopus 로고
    • Differential mechanisms of inhibition of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by S-nitrosothiols and NO in cellular and cellfree conditions
    • Broniowska KA and Hogg N. Differential mechanisms of inhibition of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by S-nitrosothiols and NO in cellular and cellfree conditions. Am J Physiol Heart Circ Physiol 299: H1212-H1219, 2010.
    • (2010) Am J Physiol Heart Circ Physiol , vol.299
    • Broniowska, K.A.1    Hogg, N.2
  • 11
    • 33845961527 scopus 로고    scopus 로고
    • Requirement of transmembrane transport for S-nitrosocysteine-dependent modification of intracellular thiols
    • DOI 10.1074/jbc.M603248200
    • Broniowska KA, Zhang Y, and Hogg N. Requirement of transmembrane transport for S-nitrosocysteine-dependent modification of intracellular thiols. J Biol Chem 281: 33835-33841, 2006. (Pubitemid 46036595)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 33835-33841
    • Broniowska, K.A.1    Zhang, Y.2    Hogg, N.3
  • 14
    • 0032560621 scopus 로고    scopus 로고
    • Ionization-reactivity relationships for cysteine thiols in polypeptides
    • DOI 10.1021/bi973101r
    • Bulaj G, Kortemme T, and Goldenberg DP. Ionization-Reactivity Relationships for Cysteine Thiols in Polypeptides. Biochemistry 37: 8965-8972, 1998. (Pubitemid 28299665)
    • (1998) Biochemistry , vol.37 , Issue.25 , pp. 8965-8972
    • Bulaj, G.1    Kortemme, T.2    Goldenberg, D.P.3
  • 15
    • 0031567617 scopus 로고    scopus 로고
    • Transient-state and steady-state kinetics of the oxidation of aliphatic and aromatic thiols by horseradish peroxidase
    • DOI 10.1016/S0014-5793(97)00713-8, PII S0014579397007138
    • Burner U and Obinger C. Transient-state and steady-state kinetics of the oxidation of aliphatic and aromatic thiols by horseradish peroxidase. FEBS Lett 411: 269-274, 1997. (Pubitemid 27301468)
    • (1997) FEBS Letters , vol.411 , Issue.2-3 , pp. 269-274
    • Burner, U.1    Obinger, C.2
  • 16
    • 0346096863 scopus 로고    scopus 로고
    • Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin
    • Chan NL, Kavanaugh JS, Rogers PH, and Arnone A. Crystallographic analysis of the interaction of nitric oxide with quaternary-T human hemoglobin. Biochemistry 43: 118-132, 2004. (Pubitemid 38055947)
    • (2004) Biochemistry , vol.43 , Issue.1 , pp. 118-132
    • Chan, N.-L.1    Kavanaugh, J.S.2    Rogers, P.H.3    Arnone, A.4
  • 17
    • 0028970801 scopus 로고
    • The role of the reactions of.NO with superoxide and oxygen in biological systems: A kinetic approach
    • Czapski G and Goldstein S. The role of the reactions of.NO with superoxide and oxygen in biological systems: a kinetic approach. Free Radic Biol Med 19: 785-794, 1995.
    • (1995) Free Radic Biol Med , vol.19 , pp. 785-794
    • Czapski, G.1    Goldstein, S.2
  • 18
    • 33744527052 scopus 로고    scopus 로고
    • Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite: Implications for the interaction of nitric oxide with mitochondria
    • DOI 10.1074/jbc.M512203200
    • Dahm CC, Moore K, and Murphy MP. Persistent Snitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite: implications for the interaction of nitric oxide with mitochondria. J Biol Chem 281: 10056-10065, 2006. (Pubitemid 43864540)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10056-10065
    • Dahm, C.C.1    Moore, K.2    Murphy, M.P.3
  • 19
    • 23944459059 scopus 로고    scopus 로고
    • Transfer of nitric oxide from nitrovasodilators to free thiols - Evidence of two distinct stages
    • DOI 10.1016/j.bbrc.2005.07.126, PII S0006291X05016025
    • Dasgupta TP and Aquart DV. Transfer of nitric oxide from nitrovasodilators to free thiols-evidence of two distinct stages. Biochem Biophys Res Commun 335: 730-733, 2005. (Pubitemid 41188259)
    • (2005) Biochemical and Biophysical Research Communications , vol.335 , Issue.3 , pp. 730-733
    • Dasgupta, T.P.1    Aquart, D.V.2
  • 20
    • 78049288138 scopus 로고    scopus 로고
    • Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation
    • Doulias PT, Greene JL, Greco TM, Tenopoulou M, Seeholzer SH, Dunbrack RL, and Ischiropoulos H. Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation. Proc Natl Acad Sci USA 107: 16958-16963, 2010.
    • (2010) Proc Natl Acad Sci USA , 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
  • 22
    • 0031024788 scopus 로고    scopus 로고
    • Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57
    • DOI 10.1021/bi961801a
    • Dyson HJ, Jeng MF, Tennant LL, Slaby I, Lindell M, Cui DS, Kuprin S, and Holmgren A. Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57GCxá. Biochemistry 36: 2622-2636, 1997. (Pubitemid 27106656)
    • (1997) Biochemistry , vol.36 , Issue.9 , pp. 2622-2636
    • Dyson, H.J.1    Jeng, M.-F.2    Tennant, L.L.3    Slaby, I.4    Lindell, M.5    Cui, D.-S.6    Kuprin, S.7    Holmgren, A.8
  • 23
    • 0033634643 scopus 로고    scopus 로고
    • Dexras1: A G protein specifically coupled to neuronal nitric oxide synthase via CAPON
    • Fang M, Jaffrey SR, Sawa A, Ye K, Luo X, and Snyder SH. Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON. Neuron 28: 183-193, 2000.
    • (2000) Neuron , vol.28 , pp. 183-193
    • Fang, M.1    Jaffrey, S.R.2    Sawa, A.3    Ye, K.4    Luo, X.5    Snyder, S.H.6
  • 24
    • 0036846736 scopus 로고    scopus 로고
    • Concomitant S-, N-, and heme-nitros(yl)ation in biological tissues and fluids: Implications for the fate of NO in vivo
    • DOI 10.1096/fj.02-0363com
    • Feelisch M, Rassaf T, Mnaimneh S, Singh N, Bryan NS, Jourd'heuil D, and Kelm M. Concomitant S-, N-, and hemenitros (yl)ation in biological tissues and fluids: implications for the fate of NO in vivo. FASEB J 16: 1775-1785, 2002. (Pubitemid 35340358)
    • (2002) FASEB Journal , vol.16 , Issue.13 , pp. 1775-1785
    • Feelisch, M.1    Rassaf, T.2    Mnaimneh, S.3    Singh, N.4    Bryan, N.S.5    Jourd'Heuil, D.6    Kelm, M.7
  • 26
    • 76049119067 scopus 로고    scopus 로고
    • A nitric oxide/cysteine interaction mediates the activation of soluble guanylate cyclase
    • Fernhoff NB, Derbyshire ER, and Marletta MA. A nitric oxide/cysteine interaction mediates the activation of soluble guanylate cyclase. Proc Natl Acad Sci USA 106: 21602-21607, 2009.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21602-21607
    • Fernhoff, N.B.1    Derbyshire, E.R.2    Marletta, M.A.3
  • 28
  • 30
    • 0027268548 scopus 로고
    • Creatine kinase: The reactive cysteine is required for synergism but is nonessential for catalysis
    • Furter R, Furter-Graves EM, and Wallimann T. Creatine kinase: the reactive cysteine is required for synergism but is nonessential for catalysis. Biochemistry 32: 7022-7029, 1993. (Pubitemid 23221637)
    • (1993) Biochemistry , vol.32 , Issue.27 , pp. 7022-7029
    • Furter, R.1    Furter-Graves, E.M.2    Wallimann, T.3
  • 32
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert HF. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 63: 69-172, 1990.
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 33
    • 33746085196 scopus 로고    scopus 로고
    • Methodological vexation about thiol oxidation versus S-nitrosation-A commentary on "An ascorbate-dependent artifact that interferes with the interpretation of the biotin-switch assay"
    • DOI 10.1016/j.freeradbiomed.2006.05.025, PII S0891584906003546
    • Gladwin MT, Wang X, and Hogg N. Methodological vexation about thiol oxidation versus S-nitrosation-A commentary on "An ascorbate-dependent artifact that interferes with the interpretation of the biotin-switch assay". Free Radic Biol Med 41: 557-561, 2006. (Pubitemid 44080518)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.4 , pp. 557-561
    • Gladwin, M.T.1    Wang, X.2    Hogg, N.3
  • 35
    • 0029558489 scopus 로고
    • Kinetics of nitric oxide autoxidation in aqueous solution in the absence and presence of various reductants. The nature of the oxidizing intermediates
    • DOI 10.1021/ja00154a007
    • Goldstein S and Czapski G. Kinetics of nitric oxide autoxidation in aqueous solution in the absence and presence of various reductants. The nature of the oxidizing intermediates. J Am Chem Soc 117: 12078-12084, 1995. (Pubitemid 26026977)
    • (1995) Journal of the American Chemical Society , vol.117 , Issue.49 , pp. 12078-12084
    • Goldstein, S.1    Czapski, G.2
  • 36
    • 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 and Czapski G. 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.
    • (1996) J Am Chem Soc , vol.118 , pp. 3419-3425
    • Goldstein, S.1    Czapski, G.2
  • 37
    • 0031029150 scopus 로고    scopus 로고
    • A novel reaction mechanism for the formation of S-nitrosothiol in vivo
    • DOI 10.1074/jbc.272.5.2841
    • Gow AJ, Buerk DG, and Ischiropoulos H. A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J Biol Chem 272: 2841-2845, 1997. (Pubitemid 27053331)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.5 , pp. 2841-2845
    • Gow, A.J.1    Buerk, D.G.2    Ischiropoulos, H.3
  • 41
    • 19644378636 scopus 로고    scopus 로고
    • Allosteric inhibition of PTP1B activity by selective modification of a non-active site cysteine residue
    • DOI 10.1021/bi047417s
    • Hansen SK, Cancilla MT, Shiau TP, Kung J, Chen T, and Erlanson DA. Allosteric Inhibition of PTP1B Activity by Selective Modification of a Non-Active Site Cysteine ResidueGCxa ́. Biochemistry 44: 7704-7712, 2005. (Pubitemid 40740754)
    • (2005) Biochemistry , vol.44 , Issue.21 , pp. 7704-7712
    • Hansen, S.K.1    Cancilla, M.T.2    Shiau, T.P.3    Kung, J.4    Chen, T.5    Erlanson, D.A.6
  • 44
    • 0033179843 scopus 로고    scopus 로고
    • The kinetics of S-transnitrosation - A reversible second-order reaction
    • DOI 10.1006/abio.1999.4199
    • Hogg N. The kinetics of S-Transnitrosation-a reversible second-order reaction. Anal Biochem 272: 257-262, 1999. (Pubitemid 29364991)
    • (1999) Analytical Biochemistry , vol.272 , Issue.2 , pp. 257-262
    • Hogg, N.1
  • 45
    • 0029927487 scopus 로고    scopus 로고
    • The role of glutathione in the transport and catabolism of nitric oxide
    • DOI 10.1016/0014-5793(96)00086-5
    • Hogg N, Singh RJ, and Kalyanaraman B. The role of glutathione in the transport and catabolism of nitric oxide. FEBS Lett 382: 223-228, 1996. (Pubitemid 26091436)
    • (1996) FEBS Letters , vol.382 , Issue.3 , pp. 223-228
    • Hogg, N.1    Singh, R.J.2    Kalyanaraman, B.3
  • 46
    • 77954142212 scopus 로고    scopus 로고
    • Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP)
    • Huang B and Chen C. Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP). Free Radic Biol Med 49: 447-456, 2010.
    • (2010) Free Radic Biol Med , vol.49 , pp. 447-456
    • Huang, B.1    Chen, C.2
  • 47
    • 33645528748 scopus 로고    scopus 로고
    • Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the beta subunit of hemoglobin
    • Huang KT, Azarov I, Basu S, Huang J, and Kim-Shapiro DB. Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the beta subunit of hemoglobin. Blood 107: 2602-2604, 2006.
    • (2006) Blood , vol.107 , pp. 2602-2604
    • Huang, K.T.1    Azarov, I.2    Basu, S.3    Huang, J.4    Kim-Shapiro, D.B.5
  • 48
    • 0019322058 scopus 로고
    • Possible involvement of S-nitrosothiols in the activation of guanylate cyclase by nitroso compounds
    • Ignarro LJ, Edwards JC, Gruetter DY, Barry BK, and Gruetter CA. Possible involvement of S-nitrosothiols in the activation of guanylate cyclase by nitroso compounds. FEBS Lett 110: 275-278, 1980.
    • (1980) FEBS Lett , vol.110 , pp. 275-278
    • Ignarro, L.J.1    Edwards, J.C.2    Gruetter, D.Y.3    Barry, B.K.4    Gruetter, C.A.5
  • 51
  • 53
    • 0032522535 scopus 로고    scopus 로고
    • S-nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
    • Jensen DE, Belka GK, and Du Bois GC. S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme. Biochem J 331: 659-668, 1998. (Pubitemid 28182185)
    • (1998) Biochemical Journal , vol.331 , Issue.2 , pp. 659-668
    • Jensen, D.E.1    Belka, G.K.2    Du Bois, G.C.3
  • 54
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • DOI 10.1038/380221a0
    • Jia L, Bonaventura C, Bonaventura J, and Stamler JS. Snitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 380: 221-226, 1996. (Pubitemid 26090643)
    • (1996) Nature , vol.380 , Issue.6571 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 56
    • 0038182543 scopus 로고    scopus 로고
    • Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide: Evidence for a free radical mechanism
    • DOI 10.1074/jbc.M300203200
    • Jourd'heuil, D, Jourd'heuil FL, and Feelisch M. 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. (Pubitemid 36799683)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 15720-15726
    • Jourd'heuil, D.1    Jourd'heuil, F.L.2    Feelisch, M.3
  • 57
    • 0034709457 scopus 로고    scopus 로고
    • S-Nitrosothiol Formation in Blood of Lipopolysaccharide-Treated Rats
    • Jourd'heuil, D, Gray L, and Grisham MB. S-Nitrosothiol Formation in Blood of Lipopolysaccharide-Treated Rats. Biochem Biophys Res Commun 273: 22-26, 2000.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 22-26
    • Jourd'heuil, D.1    Gray, L.2    Grisham, M.B.3
  • 58
    • 74049084627 scopus 로고    scopus 로고
    • The reaction between nitric oxide, glutathione and oxygen in the presence and absence of protein: How are S-nitrosothiols formed?
    • Keszler A, Zhang Y, and Hogg N. The 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, 2009.
    • (2009) Free Radic Biol Med , vol.48 , pp. 55-64
    • Keszler, A.1    Zhang, Y.2    Hogg, N.3
  • 59
    • 0028237777 scopus 로고
    • Cell-free hemoglobin reverses the endotoxin-mediated hyporesponsivity of rat aortic rings to alpha adrenergic agents
    • KilbournRG, JolyG,Cashon B,DeAngelo J, and Bonaventura J. Cell-free hemoglobin reverses the endotoxin-mediated hyporesponsivity of rat aortic rings to alpha.-adrenergic agents. Biochem Biophys Res Commun 199: 155-162, 1994.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 155-162
    • Kilbourn, R.G.1    Joly, G.2    Cashon, B.3    Deangelo, J.4    Bonaventura, J.5
  • 60
    • 29344465714 scopus 로고    scopus 로고
    • Medicine: Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2
    • DOI 10.1126/science.1119407
    • Kim SF, Huri DA, and Snyder SH. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science 310: 1966-1970, 2005. (Pubitemid 43005992)
    • (2005) Science , vol.310 , Issue.5756 , pp. 1966-1970
    • Kim, S.F.1    Huri, D.A.2    Snyder, S.H.3
  • 61
    • 14044254798 scopus 로고    scopus 로고
    • Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation
    • DOI 10.1089/ars.2005.7.385
    • Kobayashi M and Yamamoto M. Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation. Antioxid Redox Signal 7: 385-394, 2005. (Pubitemid 40279806)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.3-4 , pp. 385-394
    • Kobayashi, M.1    Yamamoto, M.2
  • 62
    • 12544257904 scopus 로고    scopus 로고
    • Myeloperoxidase potentiates nitric oxide-mediated nitrosation
    • Lakshmi VM, Nauseef WM, and Zenser TV. Myeloperoxidase potentiates nitric oxide-mediated nitrosation. J Biol Chem 280: 1746-1753, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 1746-1753
    • Lakshmi, V.M.1    Nauseef, W.M.2    Zenser, T.V.3
  • 63
    • 0025117611 scopus 로고
    • EPR demonstration of ironnitrosyl complex formation by cytotoxic activated macrophages
    • Lancaster JR Jr. and Hibbs JB Jr. EPR demonstration of ironnitrosyl complex formation by cytotoxic activated macrophages. Proc Natl Acad Sci USA 87: 1223-1227, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1223-1227
    • Lancaster Jr., J.R.1    Hibbs Jr., J.B.2
  • 64
    • 47049113679 scopus 로고    scopus 로고
    • Protein cysteine thiol nitrosation: Maker or marker of reactive nitrogen species-induced nonerythroid cellular signaling?
    • DOI 10.1016/j.niox.2008.04.028, PII S1089860308000803
    • Lancaster JR Jr. Protein cysteine thiol nitrosation: maker or marker of reactive nitrogen species-induced nonerythroid cellular signaling? Nitric Oxide 19: 68-72, 2008. (Pubitemid 351970244)
    • (2008) Nitric Oxide - Biology and Chemistry , vol.19 , Issue.2 , pp. 68-72
    • Lancaster Jr., J.R.1
  • 65
    • 21244501313 scopus 로고    scopus 로고
    • Identification of Stereoselective Transporters for S-Nitroso-L-cysteine: Role of LAT1 and LAT2 in biological activity of S-nitrosothiols
    • Li S and Whorton AR. Identification of Stereoselective Transporters for S-Nitroso-L-cysteine: role of LAT1 and LAT2 in biological activity of S-nitrosothiols. J Biol Chem 280: 20102-20110, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 20102-20110
    • Li, S.1    Whorton, A.R.2
  • 67
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • DOI 10.1038/35068596
    • Liu L, Hausladen A, Zeng M, Que L, Heitman J, and Stamler JS. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410: 490-494, 2001. (Pubitemid 32240051)
    • (2001) Nature , vol.410 , Issue.6827 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 69
    • 0027934013 scopus 로고
    • Human glutathione transferase catalysis of the formation of S-nitrosoglutathione from organic nitrites plus glutathione
    • DOI 10.1016/0014-5793(94)00904-X
    • Meyer DJ, Kramer H, and Ketterer B. Human glutathione transferase catalysis of the formation of S-nitrosoglutathione from organic nitrites plus glutathione. FEBS Lett 351: 427-428, 1994. (Pubitemid 24285350)
    • (1994) FEBS Letters , vol.351 , Issue.3 , pp. 427-428
    • Meyer, D.J.1
  • 70
    • 0028308730 scopus 로고
    • Kinetics and equilibria of S-nitrosothiol-thiol exchange between glutathione, cysteine, penicillamines and serum albumin
    • DOI 10.1016/0014-5793(94)00429-3
    • Meyer DJ, Kramer H, Ozer N, Coles B, and Ketterer B. Kinetics and equilibria of S-nitrosothiol-thiol exchange between glutathione, cysteine, penicillamines and serum albumin. FEBS Lett 345: 177-180, 1994. (Pubitemid 24188920)
    • (1994) FEBS Letters , vol.345 , Issue.2-3 , pp. 177-180
    • Meyer, D.J.1
  • 71
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the Snitrosation of the caspase-3 active site cysteine
    • Mitchell DA and Marletta MA. Thioredoxin catalyzes the Snitrosation of the caspase-3 active site cysteine. Nat Chem Biol 1: 154-158, 2005.
    • (2005) Nat Chem Biol , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marletta, M.A.2
  • 75
    • 84952172818 scopus 로고
    • Organic thionitrites and related substances
    • Oae S and Shinhama K. Organic thionitrites and related substances. Org Prep Proc Int 15: 165-198, 1983.
    • (1983) Org Prep Proc Int , vol.15 , pp. 165-198
    • Oae, S.1    Shinhama, K.2
  • 77
    • 0033016469 scopus 로고    scopus 로고
    • Biochemical characterization of human S-nitrosohemoglobin: Effects on oxygen binding and and transnitrosation
    • Patel RP, Hogg N, Spencer NY, Kalyanaraman B, Matalon S, and Darley-Usmar VM. Biochemical characterization of human S-nitrosohemoglobin: effects on oxygen binding and and transnitrosation. J Biol Chem 274: 15487-15492, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 15487-15492
    • Patel, R.P.1    Hogg, N.2    Spencer, N.Y.3    Kalyanaraman, B.4    Matalon, S.5    Darley-Usmar, V.M.6
  • 78
    • 0005693463 scopus 로고
    • Oxidation of thiols by nitric oxide and nitrogen dioxide: Synthetic utility and toxicological implications
    • Pryor WA, Church DF, Govindan CK, and Crank G. Oxidation of thiols by nitric oxide and nitrogen dioxide: synthetic utility and toxicological implications. J Org Chem 47: 159-161, 1982.
    • (1982) J Org Chem , vol.47 , pp. 159-161
    • Pryor, W.A.1    Church, D.F.2    Govindan, C.K.3    Crank, G.4
  • 82
    • 67349161335 scopus 로고    scopus 로고
    • Activation and inhibition of soluble gunylyl cyclase by Snitrosocysteine: Involvement of amino acid transport system L
    • Riego JA, Broniowska KA, Kettenhofen NJ, and Hogg N. Activation and inhibition of soluble gunylyl cyclase by Snitrosocysteine: involvement of amino acid transport system L. Free Radic Biol Med 47: 269-274, 2009.
    • (2009) Free Radic Biol Med , vol.47 , pp. 269-274
    • Riego, J.A.1    Broniowska, K.A.2    Kettenhofen, N.J.3    Hogg, N.4
  • 83
    • 0031574042 scopus 로고    scopus 로고
    • A method to study kinetics of transnitrosation with nitrosoglutathione: Reactions with hemoglobin and other thiols
    • DOI 10.1006/abio.1997.2424
    • Rossi R, Lusini L, Giannerini F, Giustarini D, Lungarella G, and Di Simplicio P. A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols. Anal Biochem 254: 215-220, 1997. (Pubitemid 28021082)
    • (1997) Analytical Biochemistry , vol.254 , Issue.2 , pp. 215-220
    • Rossi, R.1    Lusini, L.2    Giannerini, F.3    Giustarini, D.4    Lungarella, G.5    Simplicio, P.D.6
  • 84
    • 31344470089 scopus 로고    scopus 로고
    • Modification of amino acid residues in human serum albumin by myeloperoxidase
    • DOI 10.1016/j.freeradbiomed.2005.09.007, PII S0891584905005253
    • Salavej P, Spalteholz H, and Arnhold J. Modification of amino acid residues in human serum albumin by myeloperoxidase. Free Radic Biol Med 40: 516-525, 2006. (Pubitemid 43139687)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.3 , pp. 516-525
    • Salavej, P.1    Spalteholz, H.2    Arnhold, J.3
  • 88
    • 15744403464 scopus 로고    scopus 로고
    • Characterization of the S-denitrosation activity of protein disulfide isomerase
    • DOI 10.1074/jbc.M408080200
    • Sliskovic I, Raturi A, and Mutus B. Characterization of the S-denitrosation activity of protein disulfide isomerase. J Biol Chem 280: 8733-8741, 2005. (Pubitemid 40409560)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 90
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: Translocation, regulation, and a consensus motif
    • Stamler JS, Toone EJ, Lipton SA, and Sucher NJ. (S)NO signals: translocation, regulation, and a consensus motif. Neuron 18: 691-696, 1997.
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 91
    • 0033214985 scopus 로고    scopus 로고
    • Mechanism of S nitrosothiol formation and degradation mediated by Copper Ions
    • Stubauer G, Giuffre A, and Sarti P. Mechanism of SNitrosothiol Formation and Degradation Mediated by Copper Ions. J Biol Chem 274: 28128-28133, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 28128-28133
    • Stubauer, G.1    Giuffre, A.2    Sarti, P.3
  • 92
    • 36348964192 scopus 로고    scopus 로고
    • Preconditioning results in S-nitrosylation of proteins involved in regulation of mitochondrial energetics and calcium transport
    • DOI 10.1161/CIRCRESAHA.107.155879
    • Sun J, Morgan M, Shen RF, Steenbergen C, and Murphy E. Preconditioning results in S-nitrosylation of proteins involved in regulation of mitochondrial energetics and calcium transport. Circ Res 101: 1155-1163, 2007. (Pubitemid 350146442)
    • (2007) Circulation Research , vol.101 , Issue.11 , pp. 1155-1163
    • Sun, J.1    Morgan, M.2    Shen, R.-F.3    Steenbergen, C.4    Murphy, E.5
  • 93
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite: A potential additional mechanism of nitric oxide- dependent toxicity
    • DOI 10.1074/jbc.272.12.7617
    • van der Vliet A, Eiserich JP, Halliwell B, and Cross CE. Formation of reactive nitrogen species during peroxidasecatalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J Biol Chem 272: 7617-7625, 1997. (Pubitemid 27137309)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.12 , pp. 7617-7625
    • Van Der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 94
    • 0001124088 scopus 로고
    • On the stability of the dinitrosyl-iron-cysteine complex, a candidate for the endothelium-derived relaxation factor
    • Vanin AF. On the stability of the dinitrosyl-iron-cysteine complex, a candidate for the endothelium-derived relaxation factor. Biochemistry (Mosc) 60: 225-230, 1995.
    • (1995) Biochemistry (Mosc) , vol.60 , pp. 225-230
    • Vanin, A.F.1
  • 95
    • 0032111181 scopus 로고    scopus 로고
    • Dinitrosyl iron complexes and S-nitrosothiols are two possible forms for stabilization and transport of nitric oxide in biological systems
    • Vanin AF. Dinitrosyl iron complexes and S-nitrosothiols are two possible forms for stabilization and transport of nitric oxide in biological systems. Biochemistry (Mosc) 63: 782-793, 1998. (Pubitemid 128588107)
    • (1998) Biochemistry (Moscow) , vol.63 , Issue.7 , pp. 782-793
    • Vanin, A.F.1
  • 96
    • 0031417313 scopus 로고    scopus 로고
    • Iron catalyzes both decomposition and synthesis of S-nitrosothiols: Optical and electron paramagnetic resonance studies
    • DOI 10.1006/niox.1997.0122
    • Vanin AF, Malenkova IV, and Serezhenkov VA. Iron catalyzes both decomposition and synthesis of S-nitrosothiols: optical and electron paramagnetic resonance studies. Nitric Oxide 1: 191-203, 1997. (Pubitemid 28079396)
    • (1997) Nitric Oxide - Biology and Chemistry , vol.1 , Issue.3 , pp. 191-203
    • Vanin, A.F.1    Malenkova, I.V.2    Serezhenkov, V.A.3
  • 97
    • 33748743427 scopus 로고    scopus 로고
    • Measurement of nitric oxide levels in the red cell: Validation of tri-iodide-based chemiluminescence with acid-sulfanilamide pretreatment
    • DOI 10.1074/jbc.M603953200
    • Wang X, Bryan NS, MacArthur PH, Rodriguez J, Gladwin MT, and Feelisch M. Measurement of nitric oxide levels in the red cell: validation of tri-iodide-based chemiluminescence with acid-sulfanilamide pretreatment. J Biol Chem 281: 26994-27002, 2006. (Pubitemid 44401728)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.37 , pp. 26994-27002
    • Wang, X.1    Bryan, N.S.2    MacArthur, P.H.3    Rodriguez, J.4    Gladwin, M.T.5    Feelisch, M.6
  • 98
    • 0002489906 scopus 로고    scopus 로고
    • Kinetics of nitric oxide reaction in liquid and gas phase
    • Edited By Feelisch M, Stamler JS. New York: John Wiley & Sons Ltd
    • Wink DA, Beckman JS, and Ford PC. Kinetics of nitric oxide reaction in liquid and gas phase. In: Methods in Nitric Oxide Research, edited by Feelisch M, Stamler JS. New York: John Wiley & Sons Ltd., 1996, pp. 29-37.
    • (1996) Methods in Nitric Oxide Research , pp. 29-37
    • Wink, D.A.1    Beckman, J.S.2    Ford, P.C.3
  • 100
    • 0032848295 scopus 로고    scopus 로고
    • Biochemical characterization of S-nitrosohemoglobin: Mechanisms underlying synthesis, NO release and biological activity
    • Wolzt M, MacAllister RJ, Davis D, Feelisch M, Moncada S, Vallance P, and Hobbs AJ. Biochemical characterization of S-nitrosohemoglobin: mechanisms underlying synthesis, NO release and biological activity. J Biol Chem 274: 28983-28990, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 28983-28990
    • Wolzt, M.1    MacAllister, R.J.2    Davis, D.3    Feelisch, M.4    Moncada, S.5    Vallance, P.6    Hobbs, A.J.7
  • 104
    • 0036591864 scopus 로고    scopus 로고
    • Mixing artifacts from the bolus addition of nitric oxide to oxymyoglobin: Implications for S-nitrosothiol formation
    • DOI 10.1016/S0891-5849(02)00829-8, PII S0891584902008298
    • Zhang Y and Hogg N. Mixing artifacts from bolus addition of nitric oxide to oxymyoglobin: implications for Snitrosohtiol formation. Free Radic Biol Med 32: 1212-1219, 2002. (Pubitemid 34603358)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.11 , pp. 1212-1219
    • Zhang, Y.1    Hogg, N.2
  • 107
    • 14644423288 scopus 로고    scopus 로고
    • Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins
    • DOI 10.1016/j.freeradbiomed.2004.12.012
    • Zhang Y, Keszler A, Broniowska KA, and Hogg N. Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins. Free Radic Biol Med 38: 874-881, 2005. (Pubitemid 40321079)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.7 , pp. 874-881
    • Zhang, Y.1    Keszler, A.2    Broniowska, K.A.3    Hogg, N.4
  • 108
    • 32244434531 scopus 로고    scopus 로고
    • .: The structure of the SNO moiety in "S-nitrosohemoglobin", a possible NO reservoir and transporter
    • DOI 10.1021/ja057097f
    • Zhao YL and Houk KN. Thionitroxides, RSNHO: the structure of the SNO moiety in "S-Nitrosohemoglobin", a possible NO reservoir and transporter. J Am Chem Soc 128: 1422-1423, 2006. (Pubitemid 43214834)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.5 , pp. 1422-1423
    • Zhao, Y.-L.1    Houk, K.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.