메뉴 건너뛰기




Volumn 64, Issue 3, 2011, Pages 289-297

In vitro inhibition of human and rat platelets by NO donors, nitrosoglutathione, sodium nitroprusside and SIN-1, through activation of cGMP-independent pathways

Author keywords

cGMP independent response; GSNO; Platelets; Protein sulfhydryl groups (PSH); SIN 1; Sodium nitroprusside

Indexed keywords

CYCLIC GMP; FIBRINOGEN RECEPTOR; LINSIDOMINE; NITRIC OXIDE; NITROPRUSSIDE SODIUM; S NITROSOGLUTATHIONE;

EID: 79960021199     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2011.03.014     Document Type: Article
Times cited : (13)

References (49)
  • 1
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • S. Moncada, R.M. Palmer, and E.A. Higgs Nitric oxide: physiology, pathophysiology, and pharmacology Pharmacol Rev 43 1991 109 142
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 2
    • 34247093334 scopus 로고    scopus 로고
    • Nitric oxide and the vascular endothelium
    • S. Moncada, and E.A. Higgs Nitric oxide and the vascular endothelium Handb Exp Pharmacol 176 Pt 1 2006 213 254
    • (2006) Handb Exp Pharmacol , vol.176 , Issue.PART 1 , pp. 213-254
    • Moncada, S.1    Higgs, E.A.2
  • 3
    • 0035504605 scopus 로고    scopus 로고
    • Taming platelets with cyclic nucleotides
    • DOI 10.1016/S0006-2952(01)00760-2, PII S0006295201007602
    • U.R. Schwarz, U. Walter, and M. Eigenthaler Taming platelets with cyclic nucleotides Biochem Pharmacol 62 2001 1153 1161 (Pubitemid 33055619)
    • (2001) Biochemical Pharmacology , vol.62 , Issue.9 , pp. 1153-1161
    • Schwarz, U.R.1    Walter, U.2    Eigenthaler, M.3
  • 5
    • 0031920694 scopus 로고    scopus 로고
    • Evidence for a cyclic GMP-independent mechanism in the anti-platelet action of S -nitrosoglutathione
    • DOI 10.1038/sj.bjp.0701821
    • M.P. Gordge, J.S. Hothersall, and A.A. Noronha-Dutra Evidence for a cyclic GMP-independent mechanism in the anti-platelet action of S-nitrosoglutathione Br J Pharmacol 124 1998 141 148 (Pubitemid 28210053)
    • (1998) British Journal of Pharmacology , vol.124 , Issue.1 , pp. 141-148
    • Gordge, M.P.1    Hothersall, J.S.2    Noronha-Dutra, A.A.3
  • 6
    • 0032955272 scopus 로고    scopus 로고
    • 2 synthesis in human blood platelets
    • DOI 10.1016/S0014-5793(98)01633-0, PII S0014579398016330
    • D. Tsikas, M. Ikic, K.S. Tewes, M. Raida, and J.C. Frolich Inhibition of platelet aggregation by S-nitroso-cysteine via cGMP-independent mechanisms: evidence of inhibition of thromboxane A2 synthesis in human blood platelets FEBS Lett 442 1999 162 166 (Pubitemid 29070826)
    • (1999) FEBS Letters , vol.442 , Issue.2-3 , pp. 162-166
    • Tsikas, D.1    Ikic, M.2    Tewes, K.S.3    Raida, M.4    Frolich, J.C.5
  • 7
    • 17144428125 scopus 로고    scopus 로고
    • A potential role for extracellular nitric oxide generation in cGMP-independent inhibition of human platelet aggregation: Biochemical and pharmacological considerations
    • DOI 10.1038/sj.bjp.0706110
    • M.S. Crane, A.G. Rossi, and I.L. Megson A potential role for extracellular nitric oxide generation in cGMP-independent inhibition of human platelet aggregation: biochemical and pharmacological considerations Br J Pharmacol 144 2005 849 859 (Pubitemid 40516124)
    • (2005) British Journal of Pharmacology , vol.144 , Issue.6 , pp. 849-859
    • Crane, M.S.1    Rossi, A.G.2    Megson, I.L.3
  • 8
    • 70350513336 scopus 로고    scopus 로고
    • Nitric oxide inhibits platelet adhesion to collagen through cGMP-dependent and independent mechanisms: The potential role for S-nitrosylation
    • C. Irwin, W. Roberts, and K.M. Naseem Nitric oxide inhibits platelet adhesion to collagen through cGMP-dependent and independent mechanisms: the potential role for S-nitrosylation Platelets 20 2009 478 486
    • (2009) Platelets , vol.20 , pp. 478-486
    • Irwin, C.1    Roberts, W.2    Naseem, K.M.3
  • 9
    • 0034694667 scopus 로고    scopus 로고
    • Inhibition of human platelet aggregation by nitric oxide donor drugs: Relative contribution of cGMP-independent mechanisms
    • DOI 10.1006/bbrc.2000.3976
    • N. Sogo, K.S. Magid, C.A. Shaw, D.J. Webb, and I.L. Megson Inhibition of human platelet aggregation by nitric oxide donor drugs: relative contribution of cGMP-independent mechanisms Biochem Biophys Res Commun 279 2000 412 419 (Pubitemid 32036706)
    • (2000) Biochemical and Biophysical Research Communications , vol.279 , Issue.2 , pp. 412-419
    • Sogo, N.1    Magid, K.S.2    Shaw, C.A.3    Webb, D.J.4    Megson, I.L.5
  • 10
    • 0032570313 scopus 로고    scopus 로고
    • Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation
    • J.R. Pawloski, R.V. Swaminathan, and J.S. Stamler Cell-free and erythrocytic S-nitrosohemoglobin inhibits human platelet aggregation Circulation 97 1998 263 267 (Pubitemid 28067312)
    • (1998) Circulation , vol.97 , Issue.3 , pp. 263-267
    • Pawloski, J.R.1    Swaminathan, R.V.2    Stamler, J.S.3
  • 11
    • 0034704162 scopus 로고    scopus 로고
    • A redox site involved in integrin activation
    • DOI 10.1074/jbc.M007041200
    • B. Yan, and J.W. Smith A redox site involved in integrin activation J Biol Chem 275 2000 39964 39972 (Pubitemid 32064618)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 39964-39972
    • Yan, B.1    Smith, J.W.2
  • 12
    • 34047097300 scopus 로고    scopus 로고
    • Inhibition of ADP-induced platelet adhesion to immobilised fibrinogen by nitric oxide: Evidence for cGMP-independent mechanisms
    • DOI 10.1016/j.bcp.2007.01.017, PII S0006295207000299
    • N.G. Oberprieler, W. Roberts, A.M. Graham, S. Homer-Vanniasinkam, and K.M. Naseem Inhibition of ADP-induced platelet adhesion to immobilised fibrinogen by nitric oxide: evidence for cGMP-independent mechanisms Biochem Pharmacol 2007 1593 1601 (Pubitemid 46527540)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.10 , pp. 1593-1601
    • Oberprieler, N.G.1    Roberts, W.2    Graham, A.M.3    Homer-Vanniasinkam, S.4    Naseem, K.M.5
  • 13
    • 33751401894 scopus 로고    scopus 로고
    • Interactions between cell surface protein disulphide isomerase and S-nitrosoglutathione during nitric oxide delivery
    • DOI 10.1016/j.niox.2006.08.001, PII S1089860306003922
    • C.M. Shah, S.E. Bell, I.C. Locke, H.S. Chowdrey, and M.P. Gordge Interaction between cell surface protein disulphide isomerase and S-nitrosoglutathione during nitric oxide delivery Nitric Oxide 16 2007 135 142 (Pubitemid 44820891)
    • (2007) Nitric Oxide - Biology and Chemistry , vol.16 , Issue.1 , pp. 135-142
    • Shah, C.M.1    Bell, S.E.2    Locke, I.C.3    Chowdrey, H.S.4    Gordge, M.P.5
  • 15
    • 0025277355 scopus 로고
    • Properties of a novel nitric oxide-stimulated ADP-ribosyltransferase
    • DOI 10.1016/0003-9861(90)90493-I
    • B. Brune, and E.G. Lapetina Properties of a novel nitric oxide-stimulated ADP-ribosyltransferase Arch Biochem Biophys 279 1990 286 290 (Pubitemid 20177301)
    • (1990) Archives of Biochemistry and Biophysics , vol.279 , Issue.2 , pp. 286-290
    • Brune, B.1    Lapetina, E.G.2
  • 17
    • 0038299375 scopus 로고    scopus 로고
    • Inhaled NO inhibits platelet aggregation and elevates plasma but not intraplatelet cGMP in healthy human volunteers
    • M. Beghetti, C. Sparling, P.N. Cox, D. Stephens, and I. Adatia Inhaled NO inhibits platelet aggregation and elevates plasma but not intraplatelet cGMP in healthy human volunteers Am J Physiol 285 2003 H637 H642
    • (2003) Am J Physiol , vol.285
    • Beghetti, M.1    Sparling, C.2    Cox, P.N.3    Stephens, D.4    Adatia, I.5
  • 18
    • 0035999733 scopus 로고    scopus 로고
    • Nitric oxide donor drugs: Current status and future trends
    • DOI 10.1517/13543784.11.5.587
    • I.L. Megson, and D.J. Webb Nitric oxide donor drugs: current status and future trends Expert Opin Investig Drugs 11 2002 587 601 (Pubitemid 34520612)
    • (2002) Expert Opinion on Investigational Drugs , vol.11 , Issue.5 , pp. 587-601
    • Megson, I.L.1    Webb, D.J.2
  • 19
    • 0038170479 scopus 로고    scopus 로고
    • Inactivation of platelet glycoprotein IIb/IIIa receptor by nitric oxide donor 3-morpholino-sydnonimine
    • DOI 10.1097/00001721-200306000-00002
    • D. Keh, A. Thieme, I. Kürer, K.J. Falke, and H. Gerlach Inactivation of platelet glycoprotein IIb/IIIa receptor by nitric oxide donor 3-morpholino-sydnonimine Blood Coagul Fibrinolysis 14 2003 327 334 (Pubitemid 36688185)
    • (2003) Blood Coagulation and Fibrinolysis , vol.14 , Issue.4 , pp. 327-334
    • Keh, D.1    Thieme, A.2    Kurer, I.3    Falke, K.J.4    Gerlach, H.5
  • 20
    • 0026795885 scopus 로고
    • S-nitroso-glutathione inhibits platelet activation in vitro and in vivo
    • M.W. Radomski, D.D. Rees, A. Dutra, and S. Moncada S-nitroso-glutathione inhibits platelet activation in vitro and in vivo Br J Pharmacol 107 1992 745 749
    • (1992) Br J Pharmacol , vol.107 , pp. 745-749
    • Radomski, M.W.1    Rees, D.D.2    Dutra, A.3    Moncada, S.4
  • 21
    • 11844277081 scopus 로고    scopus 로고
    • Evidence for, and importance of, cGMP-independent mechanisms with NO and NO donors on blood vessels and platelets
    • DOI 10.2174/1570161052773933
    • J.C. Wanstall, K.L. Homer, and S.A. Doggrell Evidence for, and importance of, cGMP-independent mechanisms with NO and NO donors on blood vessels and platelets Curr Vasc Pharmacol 3 2005 41 53 (Pubitemid 40089526)
    • (2005) Current Vascular Pharmacology , vol.3 , Issue.1 , pp. 41-53
    • Wanstall, J.C.1    Homer, K.L.2    Doggrell, S.A.3
  • 22
    • 0346367328 scopus 로고
    • Aggregation of blood platelets by adenosine diphosphate and its reversal
    • G.V. Born Aggregation of blood platelets by adenosine diphosphate and its reversal Nature 194 1962 927 929
    • (1962) Nature , vol.194 , pp. 927-929
    • Born, G.V.1
  • 24
    • 38149106417 scopus 로고    scopus 로고
    • Administration of minor polar compound-enriched extra virgin olive oil decreases platelet aggregation and the plasma concentration of reduced homocysteine in rats
    • R. Priora, D. Summa, S. Frosali, A. Margaritis, D. Di Giuseppe, and C. Lapucci Administration of minor polar compound-enriched extra virgin olive oil decreases platelet aggregation and the plasma concentration of reduced homocysteine in rats J Nutr 138 2008 36 41
    • (2008) J Nutr , vol.138 , pp. 36-41
    • Priora, R.1    Summa, D.2    Frosali, S.3    Margaritis, A.4    Di Giuseppe, D.5    Lapucci, C.6
  • 26
    • 0036900275 scopus 로고    scopus 로고
    • Inhibition of rat platelet aggregation by the diazeniumdiolate nitric oxide donor MAHMA NONOate
    • DOI 10.1038/sj.bjp.0704971
    • K.L. Homer, and J.C. Wanstall Inhibition of rat platelet aggregation by the diazeniumdiolate nitric oxide donor MAHMA NONOate Br J Pharmacol 137 2002 1071 1081 (Pubitemid 35440748)
    • (2002) British Journal of Pharmacology , vol.137 , Issue.7 , pp. 1071-1081
    • Homer, K.L.1    Wanstall, J.C.2
  • 27
    • 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
    • R. Rossi, L. Lusini, F. Giannerini, D. Giustarini, G. Lungarella, and P. Di Simplicio A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols Anal Biochem 254 1997 215 220 (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
  • 28
    • 77955866737 scopus 로고    scopus 로고
    • Regulation of redox forms of plasma thiols by albumin in multiple sclerosis after fasting and methionine loading test
    • D. Di Giuseppe, M. Ulivelli, S. Bartalini, S. Battistini, A. Cerase, and S. Passero Regulation of redox forms of plasma thiols by albumin in multiple sclerosis after fasting and methionine loading test Amino Acids 38 2010 1461 1471
    • (2010) Amino Acids , vol.38 , pp. 1461-1471
    • Di Giuseppe, D.1    Ulivelli, M.2    Bartalini, S.3    Battistini, S.4    Cerase, A.5    Passero, S.6
  • 29
    • 79551523391 scopus 로고    scopus 로고
    • A structurally driven analysis of thiol reactivity in mammalian albumins
    • doi:10.1002/bip.21577
    • Spiga O, Summa D, Cirri S, Bernini A, Venditti V, De Chiara M, et al. A structurally driven analysis of thiol reactivity in mammalian albumins. Biopolymers, in press DOI:10.1002/bip.21577.
    • Biopolymers
    • Spiga, O.1    Summa, D.2    Cirri, S.3    Bernini, A.4    Venditti, V.5    De Chiara, M.6
  • 30
    • 0030780657 scopus 로고    scopus 로고
    • The in vitro and in vivo pharmacological profiles of a platelet glycoprotein IIb/IIIa antagonist, NSL-9403
    • J. Katada, Y. Takiguchi, M. Muramatsu, T. Fujiyoshi, and I. Uno The in vitro and in vivo pharmacological profiles of a platelet glycoprotein IIb/IIIa antagonist, NSL-9403 Thromb Res 88 1997 27 40
    • (1997) Thromb Res , vol.88 , pp. 27-40
    • Katada, J.1    Takiguchi, Y.2    Muramatsu, M.3    Fujiyoshi, T.4    Uno, I.5
  • 31
    • 0027283778 scopus 로고
    • Platelet aggregation and fibrinogen binding in human, rhesus monkey, guinea-pig, hamster and rat blood: Activation by ADP and a thrombin receptor peptide and inhibition by glycoprotein IIb/IIIa antagonists
    • N.S. Cook, H.G. Zerwes, C. Tapparelli, M. Powling, J. Singh, and R. Metternich Platelet aggregation and fibrinogen binding in human, rhesus monkey, guinea-pig, hamster and rat blood: activation by ADP and a thrombin receptor peptide and inhibition by glycoprotein IIb/IIIa antagonists Thromb Haemost 70 1993 531 539 (Pubitemid 23254689)
    • (1993) Thrombosis and Haemostasis , vol.70 , Issue.3 , pp. 531-539
    • Cook, N.S.1    Zerwes, H.-G.2    Tapparelli, C.3    Powling, M.4    Singh, J.5    Metternich, R.6    Hagenbach, A.7
  • 32
    • 0038048505 scopus 로고    scopus 로고
    • Characterization of platelet aggregation in whole blood of laboratory animals by a screen filtration pressure method
    • DOI 10.1080/0953710031000118885
    • T. Sudo, H. Ito, and Y. Kimura Characterization of platelet aggregation in whole blood of laboratory animals by a screen filtration pressure method Platelets 14 2003 239 246 (Pubitemid 36791844)
    • (2003) Platelets , vol.14 , Issue.4 , pp. 239-246
    • Sudo, T.1    Ito, H.2    Kimura, Y.3
  • 33
    • 0034209724 scopus 로고    scopus 로고
    • Modification of creatine kinase by S-nitrosothiols: S-nitrosation vs. S-thiolation
    • DOI 10.1016/S0891-5849(00)00281-1, PII S0891584900002811
    • E.A. Konorev, B. Kalyanaraman, and N. Hogg Modification of creatine kinase by S-nitrosothiols: S-nitrosation vs. S-thiolation Free Radic Biol Med 28 2000 1671 1678 (Pubitemid 30628471)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.11 , pp. 1671-1678
    • Konorev, E.A.1    Kalyanaraman, B.2    Hogg, N.3
  • 35
    • 79151482021 scopus 로고    scopus 로고
    • The role of protein sulfhydryl groups and protein disulfides of the platelet surface in aggregation processes involving thiol exchange reactions
    • A. Margaritis, R. Priora, S. Frosali, D. Di Giuseppe, D. Summa, and L. Coppo The role of protein sulfhydryl groups and protein disulfides of the platelet surface in aggregation processes involving thiol exchange reactions Pharmacol Res 63 2011 77 84
    • (2011) Pharmacol Res , vol.63 , pp. 77-84
    • Margaritis, A.1    Priora, R.2    Frosali, S.3    Di Giuseppe, D.4    Summa, D.5    Coppo, L.6
  • 37
    • 0019489007 scopus 로고
    • Evidence that regulation of hepatic guanylate cyclase activity involves interactions between catalytic site -SH groups and both substrate and activator
    • DOI 10.1016/0003-9861(81)90125-9
    • L.J. Ignarro, P.J. Kadowitz, and W.H. Baricos Evidence that regulation of hepatic guanylate cyclase activity involves interactions between catalytic sites -SH groups and both substrate and activator Arch Biochem Biophys 208 1981 75 86 (Pubitemid 11043395)
    • (1981) Archives of Biochemistry and Biophysics , vol.208 , Issue.1 , pp. 75-86
    • Ignarro, L.J.1    Kadowitz, P.J.2    Baricos, W.H.3
  • 38
    • 0029743817 scopus 로고    scopus 로고
    • Redox modulation of L-type calcium channels in ferret ventricular myocytes: Dual mechanism regulation by nitric oxide and S-nitrosothiols
    • D.L. Campbell, J.S. Stamler, and H.C. Strauss Redox modulation of L-type calcium channel in ferret ventricular myocytes. Dual mechanism regulation by nitric oxide and S-nitrosothiols J Gen Physiol 108 1996 277 293 (Pubitemid 26332539)
    • (1996) Journal of General Physiology , vol.108 , Issue.4 , pp. 277-293
    • Campbell, D.L.1    Stamler, J.S.2    Strauss, H.C.3
  • 40
    • 64549119138 scopus 로고    scopus 로고
    • Redox control of platelet function
    • D.W. Essex Redox control of platelet function Antioxid Redox Signal 11 2009 1191 1225
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1191-1225
    • Essex, D.W.1
  • 41
    • 33750985704 scopus 로고    scopus 로고
    • Allosteric disulfide bonds in thrombosis and thrombolysis
    • DOI 10.1111/j.1538-7836.2006.02236.x
    • V.M. Chen, and P.J. Hogg Allosteric disulfide bonds in thrombosis and thrombolysis J Thromb Haemost 4 2006 2533 2541 (Pubitemid 44741542)
    • (2006) Journal of Thrombosis and Haemostasis , vol.4 , Issue.12 , pp. 2533-2541
    • Chen, V.M.1    Hogg, P.J.2
  • 42
    • 7244238089 scopus 로고    scopus 로고
    • KCl cotransport mediates abnormal sulfhydryl-dependent volume regulation in sickle reticulocytes
    • DOI 10.1182/blood-2004-01-0112
    • C.H. Joiner, R.K. Retting, M. Jiang, and R.S. Franco KCl cotransport mediates abnormal sulfhydryl-dependent volume regulation in sickle reticulocytes Blood 104 2004 2954 2960 (Pubitemid 39434987)
    • (2004) Blood , vol.104 , Issue.9 , pp. 2954-2960
    • Joiner, C.H.1    Rettig, R.K.2    Jiang, M.3    Franco, R.S.4
  • 43
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide
    • A. Zai, M.A. Rudd, A.W. Scribner, and J. Loscalzo Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide J Clin Invest 103 1999 393 399 (Pubitemid 29069989)
    • (1999) Journal of Clinical Investigation , vol.103 , Issue.3 , pp. 393-399
    • Zai, A.1    Rudd, M.A.2    Scribner, A.W.3    Loscalzo, J.4
  • 45
    • 15744403464 scopus 로고    scopus 로고
    • Characterization of the S-denitrosation activity of protein disulfide isomerase
    • DOI 10.1074/jbc.M408080200
    • I. Sliskovic, A. Raturi, and B. Mutus Characterization of the S-denitrosation activity of protein disulfide isomerase J Biol Chem 280 2005 8733 8741 (Pubitemid 40409560)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 46
    • 33644946470 scopus 로고    scopus 로고
    • Thiol oxidation inhibits nitric oxide-mediated pulmonary artery relaxation and guanylate cyclase stimulation
    • C.G. Mingone, S.A. Gupte, N. Ali, R.A. Oeckler, and M.S. Wolin Thiol oxidation inhibits nitric oxide-mediated pulmonary artery relaxation and guanylate cyclase stimulation Am J Physiol Lung Cell Mol Physiol 290 2007 L549 L557
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.290
    • Mingone, C.G.1    Gupte, S.A.2    Ali, N.3    Oeckler, R.A.4    Wolin, M.S.5
  • 47
    • 0034254350 scopus 로고    scopus 로고
    • Minor thiols cysteine and cysteinylglycine regulate the competition between glutathione and protein SH groups in human platelets subjected to oxidative stress
    • DOI 10.1006/abbi.2000.1847
    • D. Giustarini, G. Campoccia, G. Fanetti, R. Rossi, F. Giannerini, and L. Lusini Minor thiols cysteine and cysteinylglycine regulate the competition between glutathione and protein SH groups in human platelets subjected to oxidative stress Arch Biochem Biophys 380 2000 1 10 (Pubitemid 30616764)
    • (2000) Archives of Biochemistry and Biophysics , vol.380 , Issue.1 , pp. 1-10
    • Giustarini, D.1    Campoccia, G.2    Fanetti, G.3    Rossi, R.4    Giannerini, F.5    Lusini, L.6    Di Simplicio, P.7
  • 48
    • 73449114553 scopus 로고    scopus 로고
    • The control of S-thiolation by cysteine via gamma-glutamyltranspeptidase and thiol exchanges in erythrocytes and plasma of diamide-treated rats
    • R. Priora, L. Coppo, A. Margaritis, D. Di Giuseppe, S. Frosali, and D. Summa The control of S-thiolation by cysteine via gamma-glutamyltranspeptidase and thiol exchanges in erythrocytes and plasma of diamide-treated rats Toxicol Appl Pharmacol 242 2010 333 343
    • (2010) Toxicol Appl Pharmacol , vol.242 , pp. 333-343
    • Priora, R.1    Coppo, L.2    Margaritis, A.3    Di Giuseppe, D.4    Frosali, S.5    Summa, D.6
  • 49
    • 0026572110 scopus 로고
    • Reversible activation of soluble guanylate cyclase by oxidizing agents
    • X.-B. Wu, B. Brune, F. von Appen, and V. Ullrich Reversible activation of soluble guanylate cyclase by oxidizing agents Arch Biochem Biophys 294 1992 75 82
    • (1992) Arch Biochem Biophys , vol.294 , pp. 75-82
    • Wu, X.-B.1    Brune, B.2    Von Appen, F.3    Ullrich, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.