메뉴 건너뛰기




Volumn 72, Issue 5, 2006, Pages 608-615

Protein S-glutathionylation and platelet anti-aggregating activity of disulfiram

Author keywords

ADP induced platelet aggregation; Disulfiram; Human platelets; Protein thiols; S Glutathionylated proteins

Indexed keywords

DISULFIRAM; GLUTATHIONE; GLUTATHIONE DISULFIDE; THIOL DERIVATIVE;

EID: 33746752638     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.05.021     Document Type: Article
Times cited : (23)

References (61)
  • 1
    • 0026439016 scopus 로고
    • A review of the pharmacokinetics and pharmacodynamics of disulfiram and its metabolites
    • Johansson B. A review of the pharmacokinetics and pharmacodynamics of disulfiram and its metabolites. Acta Psychiatr Scand 369 (1992) 15-26
    • (1992) Acta Psychiatr Scand , vol.369 , pp. 15-26
    • Johansson, B.1
  • 3
    • 0032897832 scopus 로고    scopus 로고
    • Safety issues concerning the use of disulfiram in treating alcohol dependence
    • Chick J. Safety issues concerning the use of disulfiram in treating alcohol dependence. Drug Saf 20 (1999) 427-435
    • (1999) Drug Saf , vol.20 , pp. 427-435
    • Chick, J.1
  • 4
    • 0028126470 scopus 로고
    • Disulfiram-induced hepatitis. Report of four cases and review of the literature
    • Forns X., Caballeria J., Bruguera M., Salmeron J.M., Vilella A., Mas A., et al. Disulfiram-induced hepatitis. Report of four cases and review of the literature. J Hepatol 21 (1994) 853-857
    • (1994) J Hepatol , vol.21 , pp. 853-857
    • Forns, X.1    Caballeria, J.2    Bruguera, M.3    Salmeron, J.M.4    Vilella, A.5    Mas, A.6
  • 5
    • 4644235752 scopus 로고    scopus 로고
    • Disulfiram inhibits activating transcription factor/cyclic AMP-responsive element binding protein and human melanoma growth in a metal-dependent manner in vitro, in mice and in a patient with metastatic disease
    • Brar S.S., Grigg C., Wilson K.S., Holder Jr. W.D., Dreau D., Austin C., et al. Disulfiram inhibits activating transcription factor/cyclic AMP-responsive element binding protein and human melanoma growth in a metal-dependent manner in vitro, in mice and in a patient with metastatic disease. Mol Cancer Ther 3 (2004) 1049-1060
    • (2004) Mol Cancer Ther , vol.3 , pp. 1049-1060
    • Brar, S.S.1    Grigg, C.2    Wilson, K.S.3    Holder Jr., W.D.4    Dreau, D.5    Austin, C.6
  • 7
    • 0034616637 scopus 로고    scopus 로고
    • Blockage of drug resistance in vitro by disulfiram, a drug used to treat alcoholism
    • Loo T.W., and Clarke D.M. Blockage of drug resistance in vitro by disulfiram, a drug used to treat alcoholism. J Natl Cancer Inst 92 (2000) 898-902
    • (2000) J Natl Cancer Inst , vol.92 , pp. 898-902
    • Loo, T.W.1    Clarke, D.M.2
  • 8
    • 25144485047 scopus 로고    scopus 로고
    • Disulfiram metabolites permanently inactivate the human multidrug resistance P-glycoprotein
    • Loo T.W., Bartlett M.C., and Clarke D.M. Disulfiram metabolites permanently inactivate the human multidrug resistance P-glycoprotein. Mol Pharm 1 (2004) 426-433
    • (2004) Mol Pharm , vol.1 , pp. 426-433
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 11
    • 0142148099 scopus 로고    scopus 로고
    • Inhibition of invasion and angiogenesis by zinc-chelating agent disulfiram
    • Shiah S.G., Kao Y.R., Wu F., and Wu C.W. Inhibition of invasion and angiogenesis by zinc-chelating agent disulfiram. Mol Pharmacol 64 (2003) 1076-1084
    • (2003) Mol Pharmacol , vol.64 , pp. 1076-1084
    • Shiah, S.G.1    Kao, Y.R.2    Wu, F.3    Wu, C.W.4
  • 12
    • 0037457481 scopus 로고    scopus 로고
    • Disulfiram-mediated inhibition of NF-nB activity enhances cytotoxicity of 5-fluorouracil in colorectal cancer cell lines
    • Wang W., McLeod H.L., and Cassidy J. Disulfiram-mediated inhibition of NF-nB activity enhances cytotoxicity of 5-fluorouracil in colorectal cancer cell lines. Int J Cancer 104 (2003) 504-511
    • (2003) Int J Cancer , vol.104 , pp. 504-511
    • Wang, W.1    McLeod, H.L.2    Cassidy, J.3
  • 13
    • 0034308085 scopus 로고    scopus 로고
    • Role of disulfiram in the in vitro inhibition of rat liver mitochondrial aldehyde dehydrogenase
    • Shen M.L., Lipsky J.J., and Naylor S. Role of disulfiram in the in vitro inhibition of rat liver mitochondrial aldehyde dehydrogenase. Biochem Pharmacol 60 (2000) 947-953
    • (2000) Biochem Pharmacol , vol.60 , pp. 947-953
    • Shen, M.L.1    Lipsky, J.J.2    Naylor, S.3
  • 14
    • 0035283181 scopus 로고    scopus 로고
    • Determination of in vivo adducts of disulfiram with mitochondrial aldehyde dehydrogenase
    • Shen M.L., Johnson K.L., Mays D.C., Lipsky J.J., and Naylor S. Determination of in vivo adducts of disulfiram with mitochondrial aldehyde dehydrogenase. Biochem Pharmacol 61 (2001) 537-545
    • (2001) Biochem Pharmacol , vol.61 , pp. 537-545
    • Shen, M.L.1    Johnson, K.L.2    Mays, D.C.3    Lipsky, J.J.4    Naylor, S.5
  • 15
    • 0343376119 scopus 로고    scopus 로고
    • Mechanism of dithiocarbamate inhibition of apoptosis: thiol oxidation by dithiocarbamate disulfides directly inhibits processing of the caspase-3 proenzyme
    • Nobel C.S., Burgess D.H., Zhivotovsky B., Burkitt M.J., Orrenius S., and Slater A.F. Mechanism of dithiocarbamate inhibition of apoptosis: thiol oxidation by dithiocarbamate disulfides directly inhibits processing of the caspase-3 proenzyme. Chem Res Toxicol 10 (1997) 636-643
    • (1997) Chem Res Toxicol , vol.10 , pp. 636-643
    • Nobel, C.S.1    Burgess, D.H.2    Zhivotovsky, B.3    Burkitt, M.J.4    Orrenius, S.5    Slater, A.F.6
  • 17
  • 18
    • 22044453218 scopus 로고    scopus 로고
    • PKC sulfhydryl targeting by disulfiram produces divergent isozymic regulatory responses that accord with the cancer preventive activity of the thiuramdisulfide
    • Chu F., and O'Brian C.A. PKC sulfhydryl targeting by disulfiram produces divergent isozymic regulatory responses that accord with the cancer preventive activity of the thiuramdisulfide. Antioxid Redox Signal 7 (2005) 855-862
    • (2005) Antioxid Redox Signal , vol.7 , pp. 855-862
    • Chu, F.1    O'Brian, C.A.2
  • 19
    • 0031825806 scopus 로고    scopus 로고
    • Dithiocarbamate toxicity toward thymocytes involves their copper-catalyzed conversion to thiuram disulfides, which oxidize glutathione in a redox cycle without the release of reactive oxygen species
    • Burkitt M.J., Bishop H.S., Milne L., Tsang S.Y., Provan G.J., Nobel C.S., et al. Dithiocarbamate toxicity toward thymocytes involves their copper-catalyzed conversion to thiuram disulfides, which oxidize glutathione in a redox cycle without the release of reactive oxygen species. Arch Biochem Biophys 353 (1998) 73-84
    • (1998) Arch Biochem Biophys , vol.353 , pp. 73-84
    • Burkitt, M.J.1    Bishop, H.S.2    Milne, L.3    Tsang, S.Y.4    Provan, G.J.5    Nobel, C.S.6
  • 20
    • 0035794002 scopus 로고    scopus 로고
    • Oxidative stress and c-Jun-amino-terminal kinase activation involved in apoptosis of primary astrocytes induced by disulfiram-Cu(2+) complex
    • Chen S.H., Liu S.H., Liang Y.C., Lin J.K., and Lin-Shiau S.Y. Oxidative stress and c-Jun-amino-terminal kinase activation involved in apoptosis of primary astrocytes induced by disulfiram-Cu(2+) complex. Eur J Pharmacol 414 (2001) 177-188
    • (2001) Eur J Pharmacol , vol.414 , pp. 177-188
    • Chen, S.H.1    Liu, S.H.2    Liang, Y.C.3    Lin, J.K.4    Lin-Shiau, S.Y.5
  • 21
    • 0028815621 scopus 로고
    • Dithiocarbamates induce apoptosis in thymocytes by raising the intracellular level of redox-active copper
    • Nobel C.S., Kimland M., Lind B., Orrenius S., and Slater A.F. Dithiocarbamates induce apoptosis in thymocytes by raising the intracellular level of redox-active copper. J Biol Chem 270 (1995) 26202-26208
    • (1995) J Biol Chem , vol.270 , pp. 26202-26208
    • Nobel, C.S.1    Kimland, M.2    Lind, B.3    Orrenius, S.4    Slater, A.F.5
  • 22
    • 0030795773 scopus 로고    scopus 로고
    • Effect of membrane-permeable sulfhydryl reagents and depletion of glutathione on calcium mobilisation in human platelets
    • van Gorp R.M., van Dam-Mieras M.C., Hornstra G., and Heemskerk J.W. Effect of membrane-permeable sulfhydryl reagents and depletion of glutathione on calcium mobilisation in human platelets. Biochem Pharmacol 53 (1997) 1533-1542
    • (1997) Biochem Pharmacol , vol.53 , pp. 1533-1542
    • van Gorp, R.M.1    van Dam-Mieras, M.C.2    Hornstra, G.3    Heemskerk, J.W.4
  • 23
    • 18844427352 scopus 로고    scopus 로고
    • S-Glutathionylation in human platelets by a thiol-disulphide exchange-independent mechanism
    • Dalle-Donne I., Giustarini D., Colombo R., Milzani A., and Rossi R. S-Glutathionylation in human platelets by a thiol-disulphide exchange-independent mechanism. Free Radic Biol Med 38 (2005) 1501-1510
    • (2005) Free Radic Biol Med , vol.38 , pp. 1501-1510
    • Dalle-Donne, I.1    Giustarini, D.2    Colombo, R.3    Milzani, A.4    Rossi, R.5
  • 24
    • 0037435609 scopus 로고    scopus 로고
    • Redox control of platelet aggregation
    • Essex D.W., and Li M. Redox control of platelet aggregation. Biochemistry 42 (2003) 129-136
    • (2003) Biochemistry , vol.42 , pp. 129-136
    • Essex, D.W.1    Li, M.2
  • 26
    • 12244311183 scopus 로고    scopus 로고
    • Reversible S-glutathionylation of Cys(374) regulates actin filament formation by inducing structural changes in the actin molecule
    • Dalle-Donne I., Giustarini D., Rossi R., Colombo R., and Milzani A. Reversible S-glutathionylation of Cys(374) regulates actin filament formation by inducing structural changes in the actin molecule. Free Radic Biol Med 34 (2003) 23-32
    • (2003) Free Radic Biol Med , vol.34 , pp. 23-32
    • Dalle-Donne, I.1    Giustarini, D.2    Rossi, R.3    Colombo, R.4    Milzani, A.5
  • 27
    • 0021969361 scopus 로고
    • Effect of GSH depletion by 1-chloro-2,4-dinitrobenzene on human platelet aggregation, arachidonic acid oxidative metabolism and cytoskeletal proteins
    • Bosia A., Spangenberg P., Ghigo D., Heller R., Losche W., Pescarmona G.P., et al. Effect of GSH depletion by 1-chloro-2,4-dinitrobenzene on human platelet aggregation, arachidonic acid oxidative metabolism and cytoskeletal proteins. Thromb Res 37 (1985) 423-434
    • (1985) Thromb Res , vol.37 , pp. 423-434
    • Bosia, A.1    Spangenberg, P.2    Ghigo, D.3    Heller, R.4    Losche, W.5    Pescarmona, G.P.6
  • 28
    • 0023221336 scopus 로고
    • Extracts of feverfew may inhibit platelet behaviour via neutralization of sulphydryl groups
    • Heptinstall S., Groenewegen W.A., Spangenberg P., and Losche W. Extracts of feverfew may inhibit platelet behaviour via neutralization of sulphydryl groups. J Pharm Pharmacol 39 (1987) 459-465
    • (1987) J Pharm Pharmacol , vol.39 , pp. 459-465
    • Heptinstall, S.1    Groenewegen, W.A.2    Spangenberg, P.3    Losche, W.4
  • 29
    • 0025304714 scopus 로고
    • Helenalin and 11alpha,13-dihydrohelenalin, two constituents from Arnica montana L., inhibit human platelet function via thiol-dependent pathways
    • Schroder H., Losche W., Strobach H., Leven W., Willuhn G., Till U., et al. Helenalin and 11alpha,13-dihydrohelenalin, two constituents from Arnica montana L., inhibit human platelet function via thiol-dependent pathways. Thromb Res 57 (1990) 839-845
    • (1990) Thromb Res , vol.57 , pp. 839-845
    • Schroder, H.1    Losche, W.2    Strobach, H.3    Leven, W.4    Willuhn, G.5    Till, U.6
  • 31
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P., and Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 267 (2000) 4928-4944
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 32
    • 14044272119 scopus 로고    scopus 로고
    • S-Glutathionylation: from redox regulation of protein functions to human diseases
    • Giustarini D., Rossi R., Milzani A., Colombo R., and Dalle-Donne I. S-Glutathionylation: from redox regulation of protein functions to human diseases. J Cell Mol Med 8 (2004) 201-212
    • (2004) J Cell Mol Med , vol.8 , pp. 201-212
    • Giustarini, D.1    Rossi, R.2    Milzani, A.3    Colombo, R.4    Dalle-Donne, I.5
  • 33
    • 18844411597 scopus 로고    scopus 로고
    • Is there a role for S-glutathionylation of proteins in human disease?
    • Dalle-Donne I., Rossi R., Giustarini D., Colombo R., and Milzani A. Is there a role for S-glutathionylation of proteins in human disease?. IUBMB Life 57 (2005) 189-192
    • (2005) IUBMB Life , vol.57 , pp. 189-192
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3    Colombo, R.4    Milzani, A.5
  • 34
    • 0028890599 scopus 로고
    • The effects of disulfiram on the hippocampus and cerebellum of the rat brain: a study on oxidative stress
    • Delmaestro E., and Trombetta L.D. The effects of disulfiram on the hippocampus and cerebellum of the rat brain: a study on oxidative stress. Toxicol Lett 75 (1995) 235-243
    • (1995) Toxicol Lett , vol.75 , pp. 235-243
    • Delmaestro, E.1    Trombetta, L.D.2
  • 37
    • 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
    • Giustarini D., Campoccia G., Fanetti G., Rossi R., Giannerini F., Lusini L., et al. 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
    • (2000) Arch Biochem Biophys , vol.380 , pp. 1-10
    • Giustarini, D.1    Campoccia, G.2    Fanetti, G.3    Rossi, R.4    Giannerini, F.5    Lusini, L.6
  • 38
    • 0020529711 scopus 로고
    • The role of the GSH-disulfide status in the reversible and irreversible aggregation of human platelets
    • Bosia A., Spangenberg P., Losche W., Arese P., and Till U. The role of the GSH-disulfide status in the reversible and irreversible aggregation of human platelets. Thromb Res 30 (1983) 137-142
    • (1983) Thromb Res , vol.30 , pp. 137-142
    • Bosia, A.1    Spangenberg, P.2    Losche, W.3    Arese, P.4    Till, U.5
  • 39
    • 0023612856 scopus 로고
    • Changes in the distribution and organization of platelet actin induced by diamide and its functional consequences
    • Spangenberg P., Till U., Gschmeissner S., and Crawford N. Changes in the distribution and organization of platelet actin induced by diamide and its functional consequences. Br J Haematol 67 (1987) 443-450
    • (1987) Br J Haematol , vol.67 , pp. 443-450
    • Spangenberg, P.1    Till, U.2    Gschmeissner, S.3    Crawford, N.4
  • 40
    • 0024602320 scopus 로고
    • The influence of glutathione depleting agents on human platelet function
    • Hill T.D., White J.C., and Rao G.H.R. The influence of glutathione depleting agents on human platelet function. Thromb Res 53 (1989) 457-465
    • (1989) Thromb Res , vol.53 , pp. 457-465
    • Hill, T.D.1    White, J.C.2    Rao, G.H.R.3
  • 41
    • 4444282377 scopus 로고    scopus 로고
    • Platelet surface glutathione reductase-like activity
    • Essex D.W., Li M., Feinman R.D., and Miller A. Platelet surface glutathione reductase-like activity. Blood 104 (2004) 1383-1385
    • (2004) Blood , vol.104 , pp. 1383-1385
    • Essex, D.W.1    Li, M.2    Feinman, R.D.3    Miller, A.4
  • 42
    • 3042824871 scopus 로고    scopus 로고
    • The role of thiols and disulfides in platelet function
    • Essex D.W. The role of thiols and disulfides in platelet function. Antioxid Redox Signal 6 (2004) 736-746
    • (2004) Antioxid Redox Signal , vol.6 , pp. 736-746
    • Essex, D.W.1
  • 43
    • 0034956503 scopus 로고    scopus 로고
    • Association of quinone-induced platelet anti-aggregation with cytotoxicity
    • Kim S.R., Lee J.Y., Lee M.Y., Chung S.M., Bae O.N., and Chung J.H. Association of quinone-induced platelet anti-aggregation with cytotoxicity. Toxicol Sci 62 (2001) 176-182
    • (2001) Toxicol Sci , vol.62 , pp. 176-182
    • Kim, S.R.1    Lee, J.Y.2    Lee, M.Y.3    Chung, S.M.4    Bae, O.N.5    Chung, J.H.6
  • 44
    • 0035572870 scopus 로고    scopus 로고
    • Long-term smoking causes nitroglycerin resistance in platelets by depletion of intraplatelet glutathione
    • Haramaki N., Ikeda H., Takajo Y., Katoh A., Kanaya S., Shintani S., et al. Long-term smoking causes nitroglycerin resistance in platelets by depletion of intraplatelet glutathione. Arterioscler Thromb Vasc Biol 21 (2001) 1852-1856
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 1852-1856
    • Haramaki, N.1    Ikeda, H.2    Takajo, Y.3    Katoh, A.4    Kanaya, S.5    Shintani, S.6
  • 45
    • 0035499992 scopus 로고    scopus 로고
    • Augmented oxidative stress of platelets in chronic smokers Mechanisms of impaired platelet-derived nitric oxide bioactivity and augmented platelet aggregability
    • Takajo Y., Ikeda H., Haramaki N., Murohara T., and Imaizumi T. Augmented oxidative stress of platelets in chronic smokers Mechanisms of impaired platelet-derived nitric oxide bioactivity and augmented platelet aggregability. J Am Coll Cardiol 38 (2001) 1320-1327
    • (2001) J Am Coll Cardiol , vol.38 , pp. 1320-1327
    • Takajo, Y.1    Ikeda, H.2    Haramaki, N.3    Murohara, T.4    Imaizumi, T.5
  • 46
    • 0037271306 scopus 로고    scopus 로고
    • Scientific and therapeutic advances in antiplatelet therapy
    • Bhatt D.L., and Topol E.J. Scientific and therapeutic advances in antiplatelet therapy. Nat Rev Drug Discov 2 (2003) 15-28
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 15-28
    • Bhatt, D.L.1    Topol, E.J.2
  • 47
    • 4644368365 scopus 로고    scopus 로고
    • Signalling through the platelet glycoprotein Ib-V-IX complex
    • Canobbio I., Balduini C., and Torti M. Signalling through the platelet glycoprotein Ib-V-IX complex. Cell Signal 16 (2004) 1329-1344
    • (2004) Cell Signal , vol.16 , pp. 1329-1344
    • Canobbio, I.1    Balduini, C.2    Torti, M.3
  • 48
    • 24644441719 scopus 로고    scopus 로고
    • Intracellular signaling in platelets
    • Abrams C.S. Intracellular signaling in platelets. Curr Opin Hematol 12 (2005) 401-405
    • (2005) Curr Opin Hematol , vol.12 , pp. 401-405
    • Abrams, C.S.1
  • 49
    • 0034702868 scopus 로고    scopus 로고
    • Oxidant-induced S-glutathiolation inactivates protein kinase C-α: a potential mechanism of PKC isozyme regulation
    • Ward N.E., Stewart J.R., Ioannides C.G., and O'Brian C.A. Oxidant-induced S-glutathiolation inactivates protein kinase C-α: a potential mechanism of PKC isozyme regulation. Biochemistry 39 (2000) 10319-10329
    • (2000) Biochemistry , vol.39 , pp. 10319-10329
    • Ward, N.E.1    Stewart, J.R.2    Ioannides, C.G.3    O'Brian, C.A.4
  • 50
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • Eaton P., Byers H.L., Leeds N., Ward M.A., and Shattock M.J. Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 277 (2002) 9806-9811
    • (2002) J Biol Chem , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 51
    • 0036280012 scopus 로고    scopus 로고
    • Regulation of protein kinase C isozyme activity by S-glutathiolation
    • Ward N.E., Chu F., and O'Brian C.A. Regulation of protein kinase C isozyme activity by S-glutathiolation. Meth Enzymol 353 (2002) 89-100
    • (2002) Meth Enzymol , vol.353 , pp. 89-100
    • Ward, N.E.1    Chu, F.2    O'Brian, C.A.3
  • 52
    • 14044252389 scopus 로고    scopus 로고
    • Cellular protein kinase C isozyme regulation by exogenously delivered physiological disulfides-implications of oxidative protein kinase C regulation to cancer prevention
    • Chu F., Chen L.H., and O'Brian C.A. Cellular protein kinase C isozyme regulation by exogenously delivered physiological disulfides-implications of oxidative protein kinase C regulation to cancer prevention. Carcinogenesis 25 (2004) 585-596
    • (2004) Carcinogenesis , vol.25 , pp. 585-596
    • Chu, F.1    Chen, L.H.2    O'Brian, C.A.3
  • 53
    • 14844302394 scopus 로고    scopus 로고
    • Functional interaction of protein kinase Cα with the tyrosine kinases Syk and Src in human platelets
    • Pula G., Crosby D., Baker J., and Poole A.W. Functional interaction of protein kinase Cα with the tyrosine kinases Syk and Src in human platelets. J Biol Chem 280 (2005) 7194-7205
    • (2005) J Biol Chem , vol.280 , pp. 7194-7205
    • Pula, G.1    Crosby, D.2    Baker, J.3    Poole, A.W.4
  • 54
    • 0032493295 scopus 로고    scopus 로고
    • Coactivation of two different G protein-coupled receptors is essential for ADP-induced platelet aggregation
    • Jin J., and Kunapuli S.P. Coactivation of two different G protein-coupled receptors is essential for ADP-induced platelet aggregation. Proc Natl Acad Sci USA 95 (1998) 8070-8074
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8070-8074
    • Jin, J.1    Kunapuli, S.P.2
  • 55
    • 0037588974 scopus 로고    scopus 로고
    • Inactivation of the human P2Y12 receptor by thiol reagents requires interaction with both extracellular cysteine residues, Cys17 and Cys270
    • Ding Z., Kim S., Dorsam R.T., Jin J., and Kunapuli S.P. Inactivation of the human P2Y12 receptor by thiol reagents requires interaction with both extracellular cysteine residues, Cys17 and Cys270. Blood 101 (2003) 3908-3914
    • (2003) Blood , vol.101 , pp. 3908-3914
    • Ding, Z.1    Kim, S.2    Dorsam, R.T.3    Jin, J.4    Kunapuli, S.P.5
  • 57
    • 0032168873 scopus 로고    scopus 로고
    • The antiplatelet effects of ticlopidine and clopidogrel
    • Sharis P.J., Cannon C.P., and Loscalzo J. The antiplatelet effects of ticlopidine and clopidogrel. Ann Intern Med 129 (1998) 394-405
    • (1998) Ann Intern Med , vol.129 , pp. 394-405
    • Sharis, P.J.1    Cannon, C.P.2    Loscalzo, J.3
  • 58
    • 18044378766 scopus 로고    scopus 로고
    • 12 adenosine diphosphate-receptor antagonists for the prevention of atherothrombosis
    • 12 adenosine diphosphate-receptor antagonists for the prevention of atherothrombosis. Semin Thromb Hemost 31 (2005) 174-183
    • (2005) Semin Thromb Hemost , vol.31 , pp. 174-183
    • Savi, P.1    Herbert, J.M.2
  • 59
    • 0034068625 scopus 로고    scopus 로고
    • The in vivo pharmacological profile of CS-747, a novel antiplatelet agent with platelet ADP receptor antagonist properties
    • Sugidachi A., Asai F., Ogawa T., Inoue T., and Koike H. The in vivo pharmacological profile of CS-747, a novel antiplatelet agent with platelet ADP receptor antagonist properties. Br J Pharmacol 129 (2000) 1439-1446
    • (2000) Br J Pharmacol , vol.129 , pp. 1439-1446
    • Sugidachi, A.1    Asai, F.2    Ogawa, T.3    Inoue, T.4    Koike, H.5
  • 60
    • 18044398749 scopus 로고    scopus 로고
    • Pharmacology of CS-747 (prasugrel, LY640315), a novel, potent antiplatelet agent with in vivo P2Y12 receptor antagonist activity
    • Niitsu Y., Jakubowski J.A., Sugidachi A., and Asai F. Pharmacology of CS-747 (prasugrel, LY640315), a novel, potent antiplatelet agent with in vivo P2Y12 receptor antagonist activity. Semin Thromb Hemost 31 (2005) 184-194
    • (2005) Semin Thromb Hemost , vol.31 , pp. 184-194
    • Niitsu, Y.1    Jakubowski, J.A.2    Sugidachi, A.3    Asai, F.4
  • 61
    • 21644448736 scopus 로고    scopus 로고
    • 12 antagonist, to clopidogrel in percutaneous coronary intervention; results of the Joint Utilization of Medications to Block Platelets Optimally (JUMBO)-TIMI 26 Trial
    • 12 antagonist, to clopidogrel in percutaneous coronary intervention; results of the Joint Utilization of Medications to Block Platelets Optimally (JUMBO)-TIMI 26 Trial. Circulation 111 (2005) 3366-3373
    • (2005) Circulation , vol.111 , pp. 3366-3373
    • Wiviott, S.D.1    Antman, E.M.2    Winters, K.J.3    Weerakkody, G.4    Behounek, B.D.5    Carney, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.