메뉴 건너뛰기




Volumn 18, Issue C, 1997, Pages 311-333

Signal Transduction by Cyclic Nucleotide-Dependent Protein Kinases in Platelets

(2)  Butt, Elke a   Walter, Ulrich a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0342860144     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(08)60419-1     Document Type: Article
Times cited : (4)

References (123)
  • 1
    • 0343956030 scopus 로고
    • Regulation of platelet cAMP formation
    • Longenecker G.L. (Ed), Academic Press, New York
    • Aktories K., and Jakobs K.H. Regulation of platelet cAMP formation. In: Longenecker G.L. (Ed). The Platelets: Physiology and Pharmacology (1985), Academic Press, New York 271-288
    • (1985) The Platelets: Physiology and Pharmacology , pp. 271-288
    • Aktories, K.1    Jakobs, K.H.2
  • 2
    • 0027474508 scopus 로고
    • Mutational analysis of the cAMP-dependent protein kinasemediated phosphorylation site of Rap lb
    • Altschuler D., and Lapetina E.G. Mutational analysis of the cAMP-dependent protein kinasemediated phosphorylation site of Rap lb. J. Biol. Chem. 268 (1993) 7527-7531
    • (1993) J. Biol. Chem. , vol.268 , pp. 7527-7531
    • Altschuler, D.1    Lapetina, E.G.2
  • 3
    • 0025734571 scopus 로고
    • Interaction of purified actin-binding protein with the platelet membrane glycoprotein lb-IX complex
    • Andrews R.K., and Fox J.E.B. Interaction of purified actin-binding protein with the platelet membrane glycoprotein lb-IX complex. J. Biol. Chem. 266 (1991) 7144-7147
    • (1991) J. Biol. Chem. , vol.266 , pp. 7144-7147
    • Andrews, R.K.1    Fox, J.E.B.2
  • 4
    • 0026687701 scopus 로고
    • Identification of a region in the cytoplasmic domain of the platelet membrane glycoprotein lb-IX complex that binds to purified actin-binding protein
    • Andrews R.K., and Fox J.E.B. Identification of a region in the cytoplasmic domain of the platelet membrane glycoprotein lb-IX complex that binds to purified actin-binding protein. J. Biol. Chem. 267 (1992) 18605-18611
    • (1992) J. Biol. Chem. , vol.267 , pp. 18605-18611
    • Andrews, R.K.1    Fox, J.E.B.2
  • 6
    • 0024253227 scopus 로고
    • Multiple isoenzymes of cyclic nucleotide phosphodiesterase
    • Beavo J.A. Multiple isoenzymes of cyclic nucleotide phosphodiesterase. Adv. Second Messenger Phosphoprotein Res. 22 (1988) 1-38
    • (1988) Adv. Second Messenger Phosphoprotein Res. , vol.22 , pp. 1-38
    • Beavo, J.A.1
  • 7
    • 0025215525 scopus 로고
    • Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors
    • Beavo J.A., and Reifsnyder D.H. Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors. Trends Pharmacol. Sci. 11 (1990) 150-155
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 150-155
    • Beavo, J.A.1    Reifsnyder, D.H.2
  • 8
    • 0026844552 scopus 로고
    • Regulation and function of cyclic nucleotides
    • Bentley J.K., and Beavo J.A. Regulation and function of cyclic nucleotides. Curr. Opin. Cell. Biol. 4 (1992) 233-240
    • (1992) Curr. Opin. Cell. Biol. , vol.4 , pp. 233-240
    • Bentley, J.K.1    Beavo, J.A.2
  • 10
    • 0027199485 scopus 로고
    • Signaling through G proteins and G protein-coupled receptors during platelet activation
    • Brass L.B., Hoxie J.A., and Manning D.R. Signaling through G proteins and G protein-coupled receptors during platelet activation. Thromb. Haemostas. 70 (1993) 217-223
    • (1993) Thromb. Haemostas. , vol.70 , pp. 217-223
    • Brass, L.B.1    Hoxie, J.A.2    Manning, D.R.3
  • 11
    • 0026735713 scopus 로고
    • Cyclic nucleotides and intracellular calcium homeostasis in human platelets
    • Brüne B., and Ullrich V. Cyclic nucleotides and intracellular calcium homeostasis in human platelets. Eur. J. Biochem. 207 (1992) 607-613
    • (1992) Eur. J. Biochem. , vol.207 , pp. 607-613
    • Brüne, B.1    Ullrich, V.2
  • 12
    • 0026566697 scopus 로고
    • The catalytic subunit of protein kinase A triggers activation of the type V cyclic GMP-dependent GMP-specific phosphodiesterases from guinea pig lung
    • Burns E., Rodger I.W., and Pyne N.J. The catalytic subunit of protein kinase A triggers activation of the type V cyclic GMP-dependent GMP-specific phosphodiesterases from guinea pig lung. Biochem. J. 283 (1992) 487-491
    • (1992) Biochem. J. , vol.283 , pp. 487-491
    • Burns, E.1    Rodger, I.W.2    Pyne, N.J.3
  • 13
    • 0026643018 scopus 로고
    • Analysis of the functional role of cGMP-dependent protein kinase in intact human platelets using a specific activator 8-para-chlorophenylthio-cGMP
    • Butt E., Nolte C., Schulz S., Beltman J., Beavo J.A., Jastorff B., and Walter U. Analysis of the functional role of cGMP-dependent protein kinase in intact human platelets using a specific activator 8-para-chlorophenylthio-cGMP. Biochem. Pharmacol. 43 (1992) 2591-2600
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 2591-2600
    • Butt, E.1    Nolte, C.2    Schulz, S.3    Beltman, J.4    Beavo, J.A.5    Jastorff, B.6    Walter, U.7
  • 15
    • 0028303913 scopus 로고
    • cAMP-and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion protein VASP in vitro and in intact human platelets
    • In: Biology of Nitric Oxides (Feelisch, M., Busse, R., & Moncada, S., Eds.). Portland Press, London
    • Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., and Walter U. cAMP-and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion protein VASP in vitro and in intact human platelets. J. Biol. Chem. 269 (1994) 14509-14517 In: Biology of Nitric Oxides (Feelisch, M., Busse, R., & Moncada, S., Eds.). Portland Press, London
    • (1994) J. Biol. Chem. , vol.269 , pp. 14509-14517
    • Butt, E.1    Abel, K.2    Krieger, M.3    Palm, D.4    Hoppe, V.5    Hoppe, J.6    Walter, U.7
  • 16
    • 0024386997 scopus 로고
    • In situ phosphorylation of platelet actin-binding protein by cAMP-dependent protein kinase stabilizes it against proteolysis by calpain
    • Chen M., and Stracher A. In situ phosphorylation of platelet actin-binding protein by cAMP-dependent protein kinase stabilizes it against proteolysis by calpain. J. Biol. Chem. 264 (1989) 14282-14289
    • (1989) J. Biol. Chem. , vol.264 , pp. 14282-14289
    • Chen, M.1    Stracher, A.2
  • 19
    • 0025782740 scopus 로고
    • Direct activation of cardiac pacemaker channels by intracellular cAMP
    • DiFrancesco D., and Tortora P. Direct activation of cardiac pacemaker channels by intracellular cAMP. Nature 351 (1991) 145-147
    • (1991) Nature , vol.351 , pp. 145-147
    • DiFrancesco, D.1    Tortora, P.2
  • 20
    • 0026546129 scopus 로고
    • Concentration and regulation of cyclic nucleotides, cyclic nucleotide-dependent protein kinases and one of their major substrates in human platelets
    • Eigenthaler M., Nolte C., Halbrügge M., and Walter U. Concentration and regulation of cyclic nucleotides, cyclic nucleotide-dependent protein kinases and one of their major substrates in human platelets. Eur. J. Biochem. 205 (1992) 471-481
    • (1992) Eur. J. Biochem. , vol.205 , pp. 471-481
    • Eigenthaler, M.1    Nolte, C.2    Halbrügge, M.3    Walter, U.4
  • 21
    • 0027525491 scopus 로고
    • Defective nitrovasodilator-stimulated protein phosphorylation and calcium regulation in cGMP-dependent protein kinase deficient human platelets of chronic myelocytic leukemia
    • Eigenthaler M., Ullrich H., Geiger J., Horstrup K., Hönig-Liedl P., Wiebecke D., and Walter U. Defective nitrovasodilator-stimulated protein phosphorylation and calcium regulation in cGMP-dependent protein kinase deficient human platelets of chronic myelocytic leukemia. J. Biol. Chem. 268 (1993) 13526-13531
    • (1993) J. Biol. Chem. , vol.268 , pp. 13526-13531
    • Eigenthaler, M.1    Ullrich, H.2    Geiger, J.3    Horstrup, K.4    Hönig-Liedl, P.5    Wiebecke, D.6    Walter, U.7
  • 22
    • 77956730233 scopus 로고
    • Endothelial-cell-dependent protein phosphorylation and inhibition of the fMLP-induced calcium response in human neutrophils
    • Moncada S., Feelich M., Busse R., and Higgs E.A. (Eds), Portland Press, London
    • Eigenthaler M., Klippel E., Nolte C., and Walter U. Endothelial-cell-dependent protein phosphorylation and inhibition of the fMLP-induced calcium response in human neutrophils. In: Moncada S., Feelich M., Busse R., and Higgs E.A. (Eds). The Biology of Nitric Oxide, 4, Enzymology, Biochemistry and Immunology (1994), Portland Press, London 179-182
    • (1994) The Biology of Nitric Oxide, 4, Enzymology, Biochemistry and Immunology , pp. 179-182
    • Eigenthaler, M.1    Klippel, E.2    Nolte, C.3    Walter, U.4
  • 23
    • 0023113639 scopus 로고
    • Activation of adenylate cyclase in human platelet membranes by guanosine 5′-[βτ-imido]triphosphate is inhibited by cyclic AMP-dependent phosphorylation
    • Farndale R.W., Wong S.K.F., and Martin B.R. Activation of adenylate cyclase in human platelet membranes by guanosine 5′-[βτ-imido]triphosphate is inhibited by cyclic AMP-dependent phosphorylation. Biochem. J. 242 (1987) 637-643
    • (1987) Biochem. J. , vol.242 , pp. 637-643
    • Farndale, R.W.1    Wong, S.K.F.2    Martin, B.R.3
  • 24
    • 0025224154 scopus 로고
    • Rap 1B, a cAMP-dependent protein kinase substrate, associates with the platelet cytoskeleton
    • Fisher T.H., Gatling M.N., Lacal J.C., and White II G.C. Rap 1B, a cAMP-dependent protein kinase substrate, associates with the platelet cytoskeleton. J. Biol. Chem. 265 (1990) 19405-19408
    • (1990) J. Biol. Chem. , vol.265 , pp. 19405-19408
    • Fisher, T.H.1    Gatling, M.N.2    Lacal, J.C.3    White II, G.C.4
  • 25
    • 0024336047 scopus 로고
    • Cyclic AMP-dependent phosphorylation of glycoprotein lb inhibits collagen-induced polymerization of actin in platelets
    • Fox J.E.B., and Berndt M.C. Cyclic AMP-dependent phosphorylation of glycoprotein lb inhibits collagen-induced polymerization of actin in platelets. J. Biol. Chem. 264 (1989) 9520-9526
    • (1989) J. Biol. Chem. , vol.264 , pp. 9520-9526
    • Fox, J.E.B.1    Berndt, M.C.2
  • 26
    • 0023205608 scopus 로고
    • ß as one of the major proteins phosphorylated during exposure of intact platelets to agents that activate cyclic AMP-dependent protein kinase
    • ß as one of the major proteins phosphorylated during exposure of intact platelets to agents that activate cyclic AMP-dependent protein kinase. J. Biol. Chem. 262 (1987) 12627-12631
    • (1987) J. Biol. Chem. , vol.262 , pp. 12627-12631
    • Fox, J.E.B.1    Reynolds, C.C.2    Johnson, M.M.3
  • 27
    • 0026570503 scopus 로고
    • Role of cGMP and cGMP-dependent protein kinase in nitrovasodilator inhibition of agonist-evoked calcium elevation in human platelets
    • Geiger J., Nolte C., Butt E., Sage S.O., and Walter U. Role of cGMP and cGMP-dependent protein kinase in nitrovasodilator inhibition of agonist-evoked calcium elevation in human platelets. Proc. Natl. Acad. Sci. USA 89 (1992) 1031-1035
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1031-1035
    • Geiger, J.1    Nolte, C.2    Butt, E.3    Sage, S.O.4    Walter, U.5
  • 28
    • 0027950792 scopus 로고
    • Regulation of calcium mobilization and calcium entry in human platelets by endothelium-derived factors
    • Geiger J., Nolte C., and Walter U. Regulation of calcium mobilization and calcium entry in human platelets by endothelium-derived factors. Am. J. Physiol. 267 (1994) C236-C244
    • (1994) Am. J. Physiol. , vol.267
    • Geiger, J.1    Nolte, C.2    Walter, U.3
  • 32
    • 0025925359 scopus 로고
    • c-src, phospholipase C, inositol-lipid, and diacylglycerol kinases with the cytoskeletons of thrombin-stimulated platelets
    • c-src, phospholipase C, inositol-lipid, and diacylglycerol kinases with the cytoskeletons of thrombin-stimulated platelets. J. Biol. Chem. 266 (1991) 15705-15709
    • (1991) J. Biol. Chem. , vol.266 , pp. 15705-15709
    • Grondin, P.1    Plantavid, M.2    Sultan, C.3    Breton, M.4    Mauco, G.5    Chap, H.6
  • 33
    • 0026584177 scopus 로고
    • Calcium pump isoforms: Diversity, selectivity and plasticity
    • Grover A.K., and Khan I. Calcium pump isoforms: Diversity, selectivity and plasticity. Calcium 13 (1992) 9-17
    • (1992) Calcium , vol.13 , pp. 9-17
    • Grover, A.K.1    Khan, I.2
  • 34
    • 0024445576 scopus 로고
    • Purification of a vasodilator-regulated phosphoprotein from human platelets
    • Halbrügge M., and Walter U. Purification of a vasodilator-regulated phosphoprotein from human platelets. Eur. J. Biochem. 185 (1989) 41-50
    • (1989) Eur. J. Biochem. , vol.185 , pp. 41-50
    • Halbrügge, M.1    Walter, U.2
  • 35
    • 0002689846 scopus 로고
    • The regulation of platelet functions by protein kinases
    • Huang C.-K., and Sha'afi R.I. (Eds), CRC Press, Boca Raton, FL
    • Halbrügge M., and Walter U. The regulation of platelet functions by protein kinases. In: Huang C.-K., and Sha'afi R.I. (Eds). Protein Kinases in Blood Cell Function (1993), CRC Press, Boca Raton, FL 245-298
    • (1993) Protein Kinases in Blood Cell Function , pp. 245-298
    • Halbrügge, M.1    Walter, U.2
  • 36
    • 0025250142 scopus 로고
    • Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP-and cAMP-elevating vasodilators
    • Halbrügge M., Friedrich C., Eigenthaler M., Schanzenbächer P., and Walter U. Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP-and cAMP-elevating vasodilators. J. Biol. Chem. 265 (1990) 3088-3093
    • (1990) J. Biol. Chem. , vol.265 , pp. 3088-3093
    • Halbrügge, M.1    Friedrich, C.2    Eigenthaler, M.3    Schanzenbächer, P.4    Walter, U.5
  • 38
    • 0343163542 scopus 로고
    • Signal transduction in platelet activation
    • Verstraete M., Vermylen J., Lijnen R., and Arnout J. (Eds), Leuven University Press, Leuven
    • Haslam R.J. Signal transduction in platelet activation. In: Verstraete M., Vermylen J., Lijnen R., and Arnout J. (Eds). Thrombosis and Haemostasis (1987), Leuven University Press, Leuven 147-174
    • (1987) Thrombosis and Haemostasis , pp. 147-174
    • Haslam, R.J.1
  • 39
    • 0025909632 scopus 로고
    • Enhancement of the actions of smg p21 GDP/GTP exchange protein by the protein kinase A-catalyzed phosphorylation of smg p21
    • Hata Y., Kaibuchi K., Kawamura S., Hiroyoshi M., Shirataki H., and Takai Y. Enhancement of the actions of smg p21 GDP/GTP exchange protein by the protein kinase A-catalyzed phosphorylation of smg p21. J. Biol. Chem. 266 (1991) 6571-6577
    • (1991) J. Biol. Chem. , vol.266 , pp. 6571-6577
    • Hata, Y.1    Kaibuchi, K.2    Kawamura, S.3    Hiroyoshi, M.4    Shirataki, H.5    Takai, Y.6
  • 40
    • 0019466838 scopus 로고
    • Regulation of human platelet myosin light chain kinase by the catalytic subunit of cyclic AMP-dependent protein kinase
    • Hathaway D.R., Eaton C.R., and Adelstein R.S. Regulation of human platelet myosin light chain kinase by the catalytic subunit of cyclic AMP-dependent protein kinase. Nature 291 (1981) 252-254
    • (1981) Nature , vol.291 , pp. 252-254
    • Hathaway, D.R.1    Eaton, C.R.2    Adelstein, R.S.3
  • 41
    • 0025952666 scopus 로고
    • Caldesmon phosphorylation in intact human platelets by cAMP-dependent protein kinase and protein kinase C
    • Hettasch J.M., and Sellers J. Caldesmon phosphorylation in intact human platelets by cAMP-dependent protein kinase and protein kinase C. J. Biol. Chem. 266 (1991) 11876-11881
    • (1991) J. Biol. Chem. , vol.266 , pp. 11876-11881
    • Hettasch, J.M.1    Sellers, J.2
  • 42
    • 0028146120 scopus 로고
    • Phosphorylation of local adhesion vasodilator-stimulated phosphoprotein at Ser 157 in intact human platelets correlates with fibrinogen receptor inhibition
    • Hontrup K., Jablonka B., Hönig-Liedl P., Just M., Kochsiek K., and Walter U. Phosphorylation of local adhesion vasodilator-stimulated phosphoprotein at Ser 157 in intact human platelets correlates with fibrinogen receptor inhibition. Eur. J. Biochem. 225 (1994) 21-27
    • (1994) Eur. J. Biochem. , vol.225 , pp. 21-27
    • Hontrup, K.1    Jablonka, B.2    Hönig-Liedl, P.3    Just, M.4    Kochsiek, K.5    Walter, U.6
  • 43
    • 0026597050 scopus 로고
    • c-src to the cytoskeleton during platelet aggregation
    • c-src to the cytoskeleton during platelet aggregation. EMBO J. 11 (1992) 855-861
    • (1992) EMBO J. , vol.11 , pp. 855-861
    • Horvath, A.R.1    Muszbek, L.2    Kellie, S.3
  • 44
    • 0024230866 scopus 로고
    • Phosphorylation by cyclic AMP-dependent protein kinase of a human platelet Mr 22,000 GTP-binding protein (smg p21) having the same putative effector domain as the ras gene products
    • Hoshijima M., Kikuchi A., Kawata M., Ohmori T., Hashimoto E., Yamamura H., and Takai Y. Phosphorylation by cyclic AMP-dependent protein kinase of a human platelet Mr 22,000 GTP-binding protein (smg p21) having the same putative effector domain as the ras gene products. Biochem. Biophys. Res. Comm. 157 (1988) 851-860
    • (1988) Biochem. Biophys. Res. Comm. , vol.157 , pp. 851-860
    • Hoshijima, M.1    Kikuchi, A.2    Kawata, M.3    Ohmori, T.4    Hashimoto, E.5    Yamamura, H.6    Takai, Y.7
  • 45
    • 77956715116 scopus 로고
    • Correlation of nitrovasodilator-induced VASP phosphorylation and inhibition of fibrinogen receptor activation in human platelets
    • Moncada S., Feelisch M., Busse R., and Higgs E.A. (Eds), Portland Press, London
    • Jablonka B., Horstrup K., Hönig-Liedl P., Just M., Kochsiek K., and Walter U. Correlation of nitrovasodilator-induced VASP phosphorylation and inhibition of fibrinogen receptor activation in human platelets. In: Moncada S., Feelisch M., Busse R., and Higgs E.A. (Eds). The Biology of Nitric Oxide, 3, Physiological and Clinical Aspects (1994), Portland Press, London 179-182
    • (1994) The Biology of Nitric Oxide, 3, Physiological and Clinical Aspects , pp. 179-182
    • Jablonka, B.1    Horstrup, K.2    Hönig-Liedl, P.3    Just, M.4    Kochsiek, K.5    Walter, U.6
  • 46
    • 0026570943 scopus 로고
    • Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries
    • Jiang H., Colbran J.L., Francis S.H., and Corbin J.D. Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries. J. Biol. Chem. 267 (1992) 1015-1019
    • (1992) J. Biol. Chem. , vol.267 , pp. 1015-1019
    • Jiang, H.1    Colbran, J.L.2    Francis, S.H.3    Corbin, J.D.4
  • 47
    • 0026533648 scopus 로고
    • Cyclic GMP increases the rate of the calcium extrusion pump in intact human platelets but has no direct effect on the dense tubular calcium accumulation system
    • Johansson J.S., and Haynes D.H. Cyclic GMP increases the rate of the calcium extrusion pump in intact human platelets but has no direct effect on the dense tubular calcium accumulation system. Biochim. Biophys. Acta. 1105 (1992) 40-50
    • (1992) Biochim. Biophys. Acta. , vol.1105 , pp. 40-50
    • Johansson, J.S.1    Haynes, D.H.2
  • 49
    • 0027378338 scopus 로고
    • Phosphorylation of the inositol trisphosphate receptor in isolated rat hepatocytes
    • Joseph S.K., and Ryan S.V. Phosphorylation of the inositol trisphosphate receptor in isolated rat hepatocytes. J. Biol. Chem. 268 (1993) 23059-23065
    • (1993) J. Biol. Chem. , vol.268 , pp. 23059-23065
    • Joseph, S.K.1    Ryan, S.V.2
  • 51
    • 0026065274 scopus 로고
    • The cyclic nucleotide-gated channels of vertebrate photoreceptors and olfactory epithelium
    • Kaupp U.B. The cyclic nucleotide-gated channels of vertebrate photoreceptors and olfactory epithelium. Trends Neurosci. 14 (1991) 150-157
    • (1991) Trends Neurosci. , vol.14 , pp. 150-157
    • Kaupp, U.B.1
  • 52
    • 0026610741 scopus 로고
    • 2+ in vertebrate photoreceptor excitation and adaptation
    • 2+ in vertebrate photoreceptor excitation and adaptation. Annu. Rev. Physiol. 54 (1992) 153-175
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 153-175
    • Kaupp, U.B.1    Koch, K.-W.2
  • 55
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly P., and Krebs E.G. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J. Biol. Chem. 266 (1991) 15555-15558
    • (1991) J. Biol. Chem. , vol.266 , pp. 15555-15558
    • Kennelly, P.1    Krebs, E.G.2
  • 56
    • 0025748703 scopus 로고
    • Guanylyl cyclases, a growing number of signal-transducing enzymes
    • Koesling D., Böhme E., and Schultz G. Guanylyl cyclases, a growing number of signal-transducing enzymes. FASEB J. 5 (1991) 2785-2791
    • (1991) FASEB J. , vol.5 , pp. 2785-2791
    • Koesling, D.1    Böhme, E.2    Schultz, G.3
  • 57
    • 0025765005 scopus 로고
    • The adenylyl cyclase family
    • Krupinski J. The adenylyl cyclase family. Mol. Cell. Biochem. 104 (1991) 73-79
    • (1991) Mol. Cell. Biochem. , vol.104 , pp. 73-79
    • Krupinski, J.1
  • 58
    • 0001558427 scopus 로고
    • A ras-related protein is phosphorylated and translocated by agonists that increase cAMP levels in human platelets
    • Lapetina E.G., Lacal J.C., Reep B.R., and Molina y Vedia L. A ras-related protein is phosphorylated and translocated by agonists that increase cAMP levels in human platelets. Proc. Natl. Acad. Sci. USA 86 (1989) 3131-3134
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3131-3134
    • Lapetina, E.G.1    Lacal, J.C.2    Reep, B.R.3    Molina y Vedia, L.4
  • 59
    • 0027194487 scopus 로고
    • G protein-coupled receptor kinases
    • Lefkowitz R.J. G protein-coupled receptor kinases. Cell 74 (1993) 409-412
    • (1993) Cell , vol.74 , pp. 409-412
    • Lefkowitz, R.J.1
  • 60
    • 0025778245 scopus 로고
    • S-Nitrosocysteine inhibition of human platelet secretion is correlated with increases in platelet cGMP levels
    • Liebermann E.H., O'Neill S., and Mendelsohn M.E. S-Nitrosocysteine inhibition of human platelet secretion is correlated with increases in platelet cGMP levels. Circ. Res. 68 (1991) 1722-1728
    • (1991) Circ. Res. , vol.68 , pp. 1722-1728
    • Liebermann, E.H.1    O'Neill, S.2    Mendelsohn, M.E.3
  • 63
    • 0023679813 scopus 로고
    • Phosphorylation results in activation of a cAMP phosphodiesterase in human platelets
    • Macphee C.H., Reifsnyder D.H., Moore T.A., Lerea K.M., and Beavo J.A. Phosphorylation results in activation of a cAMP phosphodiesterase in human platelets. J. Biol. Chem. 263 (1988) 10353-10358
    • (1988) J. Biol. Chem. , vol.263 , pp. 10353-10358
    • Macphee, C.H.1    Reifsnyder, D.H.2    Moore, T.A.3    Lerea, K.M.4    Beavo, J.A.5
  • 64
    • 0027416021 scopus 로고
    • Thromboregulation: Multicellular modulation of platelet reactivity in hemostasis and thrombosis
    • Marcus A.J., and Safier L.B. Thromboregulation: Multicellular modulation of platelet reactivity in hemostasis and thrombosis. FASEB J. 7 (1993) 516-522
    • (1993) FASEB J. , vol.7 , pp. 516-522
    • Marcus, A.J.1    Safier, L.B.2
  • 65
    • 0025314048 scopus 로고
    • Molecular basis of the synergistic inhibition of platelet function by nitrovasodilators and activators of adenylate cyclase: Inhibition of cAMP breakdown by cGMP
    • Maurice D.H., and Haslam R.J. Molecular basis of the synergistic inhibition of platelet function by nitrovasodilators and activators of adenylate cyclase: Inhibition of cAMP breakdown by cGMP. Mol. Pharmacol. 37 (1990) 671-681
    • (1990) Mol. Pharmacol. , vol.37 , pp. 671-681
    • Maurice, D.H.1    Haslam, R.J.2
  • 67
    • 0026145549 scopus 로고
    • Cyclic AMP second messenger systems
    • McKnight G.S. Cyclic AMP second messenger systems. Curr. Opin. Cell. Biol. 3 (1991) 213-217
    • (1991) Curr. Opin. Cell. Biol. , vol.3 , pp. 213-217
    • McKnight, G.S.1
  • 68
    • 77956721113 scopus 로고
    • cAMP-dependent protein kinase: subunit diversity and functional role in gene expression
    • Jeserich G., Althaus H.H., and Waehnelt T.V. (Eds), Springer-Verlag, Heidelberg NATO ASI series H
    • Meinecke M., Büchler W., Fischer L., Lohmann S.M., and Walter U. cAMP-dependent protein kinase: subunit diversity and functional role in gene expression. In: Jeserich G., Althaus H.H., and Waehnelt T.V. (Eds). Cellular and Molecular Biology of Myelination 43 (1990), Springer-Verlag, Heidelberg 201-215 NATO ASI series H
    • (1990) Cellular and Molecular Biology of Myelination , vol.43 , pp. 201-215
    • Meinecke, M.1    Büchler, W.2    Fischer, L.3    Lohmann, S.M.4    Walter, U.5
  • 69
    • 0027953816 scopus 로고
    • Human cGMP-dependent protein kinase overexpression increases phosphorylation of an endogenous focal contact associated protein VASP without altering the thrombin-evoked calcium response
    • Meinecke M., Geiger J., Butt E., Jahnsen T., Chakraborty T., Walter U., Jarchau T., and Lohmann S.M. Human cGMP-dependent protein kinase overexpression increases phosphorylation of an endogenous focal contact associated protein VASP without altering the thrombin-evoked calcium response. Mol. Pharmacol. 46 (1994) 283-290
    • (1994) Mol. Pharmacol. , vol.46 , pp. 283-290
    • Meinecke, M.1    Geiger, J.2    Butt, E.3    Jahnsen, T.4    Chakraborty, T.5    Walter, U.6    Jarchau, T.7    Lohmann, S.M.8
  • 70
    • 0025001733 scopus 로고
    • Inhibition of fibrinogen binding to human platelets by S-nitroso-N-acetylcysteine
    • Mendelsohn M.E., O'Neil S., George D., and Loscalzo J. Inhibition of fibrinogen binding to human platelets by S-nitroso-N-acetylcysteine. J. Biol. Chem. 265 (1990) 19028-19034
    • (1990) J. Biol. Chem. , vol.265 , pp. 19028-19034
    • Mendelsohn, M.E.1    O'Neil, S.2    George, D.3    Loscalzo, J.4
  • 71
    • 0026602309 scopus 로고
    • Phosphorylation of smg p21/rap 1B p21 by cyclic GMP-dependent protein kinase
    • Miura Y., Kaibuchi K., Itoh T., Corbin J., Francis S.H., and Takai Y. Phosphorylation of smg p21/rap 1B p21 by cyclic GMP-dependent protein kinase. FEBS Lett. 297 (1992) 171-174
    • (1992) FEBS Lett. , vol.297 , pp. 171-174
    • Miura, Y.1    Kaibuchi, K.2    Itoh, T.3    Corbin, J.4    Francis, S.H.5    Takai, Y.6
  • 72
    • 0026008409 scopus 로고
    • Differential modulation of tissue function and therapeutic potential of selective inhibitors of cyclic nucleotide phosphodiesterase isoenzymes
    • Nicholson C.D., Challiss R.A.J., and Shahid M. Differential modulation of tissue function and therapeutic potential of selective inhibitors of cyclic nucleotide phosphodiesterase isoenzymes. Trends Pharmacol. Sci. 12 (1991) 19-27
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 19-27
    • Nicholson, C.D.1    Challiss, R.A.J.2    Shahid, M.3
  • 74
    • 0021268721 scopus 로고
    • Phosphorylation of mammalian myosin light chain kinase by catalytic subunit of cAMP-dependent protein kinase and by cGMP-dependent protein kinase
    • Nishikawa M., de Lanerolle P., Lincoln T., and Adelstein R.S. Phosphorylation of mammalian myosin light chain kinase by catalytic subunit of cAMP-dependent protein kinase and by cGMP-dependent protein kinase. J. Biol. Chem. 259 (1984) 8429-8436
    • (1984) J. Biol. Chem. , vol.259 , pp. 8429-8436
    • Nishikawa, M.1    de Lanerolle, P.2    Lincoln, T.3    Adelstein, R.S.4
  • 75
    • 0025910262 scopus 로고
    • Comparison of vasodilatory prostaglandins with respect to cAMP-mediated phosphorylation of a target substrate in intact human platelets
    • Nolte C., Eigenthaler M., Schanzenbächer P., and Walter U. Comparison of vasodilatory prostaglandins with respect to cAMP-mediated phosphorylation of a target substrate in intact human platelets. Biochem. Pharmacol. 42 (1991) 253-262
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 253-262
    • Nolte, C.1    Eigenthaler, M.2    Schanzenbächer, P.3    Walter, U.4
  • 76
    • 0026315448 scopus 로고
    • Endothelial cell-dependent phosphorylation of a platelet protein mediated by cAMP-and cGMP-elevating factors
    • Nolte C., Eigenthaler M., Schanzenbächer P., and Walter U. Endothelial cell-dependent phosphorylation of a platelet protein mediated by cAMP-and cGMP-elevating factors. J. Biol. Chem. 266 (1991) 14808-14812
    • (1991) J. Biol. Chem. , vol.266 , pp. 14808-14812
    • Nolte, C.1    Eigenthaler, M.2    Schanzenbächer, P.3    Walter, U.4
  • 77
    • 0024477926 scopus 로고
    • ++ by inositol 1,4,5-trisphosphate in platelet membrane vesicles is not dependent on cAMP dependent protein kinase
    • ++ by inositol 1,4,5-trisphosphate in platelet membrane vesicles is not dependent on cAMP dependent protein kinase. Biochem. J. 157 (1989) 715-721
    • (1989) Biochem. J. , vol.157 , pp. 715-721
    • O'Rourke, F.A.1    Zavioco, G.B.2    Feinstein, M.B.3
  • 78
    • 0025608896 scopus 로고
    • Cyclic AMP agonists induce the phosphorylation of phospholipase C-τ and of a 76 kDa protein coprecipitated by anti-(phospholipase C-τ) monoclonal antibodies in BALB/ C-3T3 cells
    • Olashaw N.E., Rhee S.G., and Pledger W.J. Cyclic AMP agonists induce the phosphorylation of phospholipase C-τ and of a 76 kDa protein coprecipitated by anti-(phospholipase C-τ) monoclonal antibodies in BALB/ C-3T3 cells. Biochem. J. 272 (1990) 297-303
    • (1990) Biochem. J. , vol.272 , pp. 297-303
    • Olashaw, N.E.1    Rhee, S.G.2    Pledger, W.J.3
  • 79
    • 0026556562 scopus 로고
    • Inhibition of CD3-linked phospholipase C by phorbol ester and by cAMP is associated with decreased phosphotyrosine and increased phosphoserine contents of PLC-τl
    • Park D.J., Min H.K., and Rhee S.G. Inhibition of CD3-linked phospholipase C by phorbol ester and by cAMP is associated with decreased phosphotyrosine and increased phosphoserine contents of PLC-τl. J. Biol. Chem. 267 (1992) 1496-1501
    • (1992) J. Biol. Chem. , vol.267 , pp. 1496-1501
    • Park, D.J.1    Min, H.K.2    Rhee, S.G.3
  • 80
    • 0028002180 scopus 로고
    • Endothelium-dependent phosphorylation of the vasodilator stimulated protein in platelets during coronary passage
    • Pohl U., Nolte C., Bunse A., Eigenthaler M., and Walter U. Endothelium-dependent phosphorylation of the vasodilator stimulated protein in platelets during coronary passage. Am. J. Physiol. 266 (1994) H606-H612
    • (1994) Am. J. Physiol. , vol.266
    • Pohl, U.1    Nolte, C.2    Bunse, A.3    Eigenthaler, M.4    Walter, U.5
  • 82
    • 0023568115 scopus 로고
    • The role of nitric oxide and cGMP in platelet adhesion to vascular endothelium
    • Radomski M.W., Palmer R.M.J., and Moncada S. The role of nitric oxide and cGMP in platelet adhesion to vascular endothelium. Biochem. Biophys. Res. Commun. 148 (1987) 1482-1489
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 1482-1489
    • Radomski, M.W.1    Palmer, R.M.J.2    Moncada, S.3
  • 84
    • 0026563095 scopus 로고
    • The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts
    • Reinhard M., Halbrügge M., Scheer U., Wiegand C., Jockusch B., and Walter U. The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 11 (1992) 2063-2070
    • (1992) EMBO J. , vol.11 , pp. 2063-2070
    • Reinhard, M.1    Halbrügge, M.2    Scheer, U.3    Wiegand, C.4    Jockusch, B.5    Walter, U.6
  • 86
    • 0025267690 scopus 로고
    • Calcium signaling in human platelets
    • Rink T., and Sage S.O. Calcium signaling in human platelets. Annu. Rev. Physiol. 52 (1990) 431-449
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 431-449
    • Rink, T.1    Sage, S.O.2
  • 87
    • 0027241856 scopus 로고
    • The pathogenesis of atherosclerosis: A perspective for the 1990s
    • Ross R. The pathogenesis of atherosclerosis: A perspective for the 1990s. Nature 362 (1993) 801-809
    • (1993) Nature , vol.362 , pp. 801-809
    • Ross, R.1
  • 88
    • 0026059204 scopus 로고
    • Characterization of Sp-5,6-dichloro-l-ß-D-ribofuranosyl-benzimidazole-3′,5′-monophosphorothioate (Sp-5,6 DCl-cBiMPS) as a potent and specific activator of cAMP-dependent protein kinase in cell extracts and intact cells
    • Sandberg M., Butt E., Nolte C., Fischer L., Halbrügge M., Beltman J., Jahnsen T., Genieser H.-G., Jastorff B., and Walter U. Characterization of Sp-5,6-dichloro-l-ß-D-ribofuranosyl-benzimidazole-3′,5′-monophosphorothioate (Sp-5,6 DCl-cBiMPS) as a potent and specific activator of cAMP-dependent protein kinase in cell extracts and intact cells. Biochem. J. 279 (1991) 521-527
    • (1991) Biochem. J. , vol.279 , pp. 521-527
    • Sandberg, M.1    Butt, E.2    Nolte, C.3    Fischer, L.4    Halbrügge, M.5    Beltman, J.6    Jahnsen, T.7    Genieser, H.-G.8    Jastorff, B.9    Walter, U.10
  • 89
    • 0027284439 scopus 로고
    • The nitric oxide and cGMP signal transduction system, regulation and mechanism of action
    • Schmidt H.H.H.W., Lohmann S.M., and Walter U. The nitric oxide and cGMP signal transduction system, regulation and mechanism of action. Biochim. Biophys. Acta 1178 (1993) 153-175
    • (1993) Biochim. Biophys. Acta , vol.1178 , pp. 153-175
    • Schmidt, H.H.H.W.1    Lohmann, S.M.2    Walter, U.3
  • 90
    • 0025173097 scopus 로고
    • Developmental mechanism underlying pathology of arteries
    • Schwartz S.M., Heimark R.L., and Majesky M.W. Developmental mechanism underlying pathology of arteries. Physiol. Rev. 70 (1990) 1177-1209
    • (1990) Physiol. Rev. , vol.70 , pp. 1177-1209
    • Schwartz, S.M.1    Heimark, R.L.2    Majesky, M.W.3
  • 91
    • 77956930245 scopus 로고
    • Regulation of contractile activity
    • Boyer P.D., and Krebs E.G. (Eds), Academic Press, New York
    • Sellers J.R., and Adelstein R.S. Regulation of contractile activity. In: Boyer P.D., and Krebs E.G. (Eds). The Enzymes, 3rd ed. 18 (1987), Academic Press, New York 381-418
    • (1987) The Enzymes, 3rd ed. , vol.18 , pp. 381-418
    • Sellers, J.R.1    Adelstein, R.S.2
  • 93
    • 0024532116 scopus 로고
    • Molecular mechanisms of platelet activation
    • Siess W. Molecular mechanisms of platelet activation. Physiol. Rev. 69 (1989) 58-178
    • (1989) Physiol. Rev. , vol.69 , pp. 58-178
    • Siess, W.1
  • 94
    • 0027419168 scopus 로고
    • Phosphorylation of rap 1B by protein kinase A is not involved in platelet inhibition by cyclic AMP
    • Siess W., and Grünberg B. Phosphorylation of rap 1B by protein kinase A is not involved in platelet inhibition by cyclic AMP. Cell. Signal. 5 (1993) 209-214
    • (1993) Cell. Signal. , vol.5 , pp. 209-214
    • Siess, W.1    Grünberg, B.2
  • 95
    • 0025153076 scopus 로고
    • Functional relationship between cyclic AMP-dependent protein phosphorylation and platelet inhibition
    • Siess W., and Lapetina E.G. Functional relationship between cyclic AMP-dependent protein phosphorylation and platelet inhibition. Biochem. J. 271 (1990) 815-819
    • (1990) Biochem. J. , vol.271 , pp. 815-819
    • Siess, W.1    Lapetina, E.G.2
  • 96
    • 0025120593 scopus 로고
    • Rap-lb is phosphorylated by protein kinase A in intact human platelets
    • Siess W., Winegar D.A., and Lapetina E.G. Rap-lb is phosphorylated by protein kinase A in intact human platelets. Biochem. Biophys. Res. Comm. 170 (1990) 944-950
    • (1990) Biochem. Biophys. Res. Comm. , vol.170 , pp. 944-950
    • Siess, W.1    Winegar, D.A.2    Lapetina, E.G.3
  • 97
    • 0038860948 scopus 로고
    • Purification of acalmodulin-binding protein from chicken gizzard that interacts with F-actin
    • Sobue K., Muramoto Y., Fujita M., and Kakiuchi S. Purification of acalmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc. Natl. Acad. Sci. USA 78 (1981) 5652-5655
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5652-5655
    • Sobue, K.1    Muramoto, Y.2    Fujita, M.3    Kakiuchi, S.4
  • 99
    • 0000559009 scopus 로고
    • Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium
    • Suppattapone S., Danoff S.K., Theibert A., Joseph S., Steiner J., and Snyder S.H. Cyclic AMP-dependent phosphorylation of a brain inositol trisphosphate receptor decreases its release of calcium. Proc. Natl. Acad. Sci. USA 85 (1988) 8747-8750
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8747-8750
    • Suppattapone, S.1    Danoff, S.K.2    Theibert, A.3    Joseph, S.4    Steiner, J.5    Snyder, S.H.6
  • 101
    • 0026709998 scopus 로고
    • Control of nonmuscle myosins by phosphorylation
    • Tan J.L., Ravid S., and Spudich J.A. Control of nonmuscle myosins by phosphorylation. Annu. Rev. Biochem. 61 (1992) 721-759
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 721-759
    • Tan, J.L.1    Ravid, S.2    Spudich, J.A.3
  • 102
    • 0027326801 scopus 로고
    • Photoaffinity labelling of cyclic GMP-binding proteins in human platelets
    • Tang K.M., Sherwood J.L., and Haslam J.R. Photoaffinity labelling of cyclic GMP-binding proteins in human platelets. Biochem. J. 294 (1993) 329-333
    • (1993) Biochem. J. , vol.294 , pp. 329-333
    • Tang, K.M.1    Sherwood, J.L.2    Haslam, J.R.3
  • 104
    • 0025330489 scopus 로고
    • cAMP-dependent protein kinase: Framework for a diverse family of regulator enzymes
    • Taylor S.S., Buechler J.A., and Yonemoto W. cAMP-dependent protein kinase: Framework for a diverse family of regulator enzymes. Annu. Rev. Biochem. 59 (1990) 971-1005
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 971-1005
    • Taylor, S.S.1    Buechler, J.A.2    Yonemoto, W.3
  • 105
    • 0025143899 scopus 로고
    • Substrate-and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP
    • Thomas M.K., Francis S.H., and Corbin J.D. Substrate-and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP. J. Biol. Chem. 265 (1990) 14971-14978
    • (1990) J. Biol. Chem. , vol.265 , pp. 14971-14978
    • Thomas, M.K.1    Francis, S.H.2    Corbin, J.D.3
  • 107
    • 0026611069 scopus 로고
    • ras GTPase activating protein in the regulation of phospholipase C-τ1 in human platelets
    • ras GTPase activating protein in the regulation of phospholipase C-τ1 in human platelets. Proc. Natl. Acad. Sci. USA 89 (1992) 7796-7800
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7796-7800
    • Torti, M.1    Lapetina, E.G.2
  • 109
    • 0026581931 scopus 로고
    • Interaction of the low-molecular-mass, guanine-nucleotide-binding protein with the actin-binding protein and its modulation by the cAMP-dependent protein kinase in bovine platelets
    • Ueda M., Oho C., Takisawa H., and Ogihara S. Interaction of the low-molecular-mass, guanine-nucleotide-binding protein with the actin-binding protein and its modulation by the cAMP-dependent protein kinase in bovine platelets. Eur. J. Biochem. 203 (1992) 347-352
    • (1992) Eur. J. Biochem. , vol.203 , pp. 347-352
    • Ueda, M.1    Oho, C.2    Takisawa, H.3    Ogihara, S.4
  • 110
    • 0026014052 scopus 로고
    • Protein kinase C and cyclic AMP regulate reversible exposure of binding sites for fibrinogen on the glycoprotein IIb-IIIa complex of human platelets
    • Van Willigen G., and Akkerman J.W.N. Protein kinase C and cyclic AMP regulate reversible exposure of binding sites for fibrinogen on the glycoprotein IIb-IIIa complex of human platelets. Biochem. J. 273 (1991) 115-120
    • (1991) Biochem. J. , vol.273 , pp. 115-120
    • Van Willigen, G.1    Akkerman, J.W.N.2
  • 111
    • 0025334367 scopus 로고
    • Regulatory functions of the vascular endothelium
    • Vane J.R., Äangard E.E., and Botting R.M. Regulatory functions of the vascular endothelium. N. Engl. J. Med. 323 (1990) 27-36
    • (1990) N. Engl. J. Med. , vol.323 , pp. 27-36
    • Vane, J.R.1    Äangard, E.E.2    Botting, R.M.3
  • 112
    • 0024533108 scopus 로고
    • Cyclic nucleotide-elevating vasodilators inhibit platelet aggregation at an early step of the activation cascade
    • Waldmann R., and Walter U. Cyclic nucleotide-elevating vasodilators inhibit platelet aggregation at an early step of the activation cascade. Eur. J. Pharmacol. 159 (1989) 317-320
    • (1989) Eur. J. Pharmacol. , vol.159 , pp. 317-320
    • Waldmann, R.1    Walter, U.2
  • 113
    • 0022501109 scopus 로고
    • Demonstration of cGMP-dependent protein kinase and cGMP-dependent protein kinase phosphorylation in cell-free extracts of platelets
    • Waldmann R., Bauer S., Göbel C., Hofmann F., Jakobs K.H., and Walter U. Demonstration of cGMP-dependent protein kinase and cGMP-dependent protein kinase phosphorylation in cell-free extracts of platelets. Eur. J. Biochem. 158 (1986) 203-210
    • (1986) Eur. J. Biochem. , vol.158 , pp. 203-210
    • Waldmann, R.1    Bauer, S.2    Göbel, C.3    Hofmann, F.4    Jakobs, K.H.5    Walter, U.6
  • 114
    • 0023265447 scopus 로고
    • Vasodilator-stimulated protein phosphorylation in platelets is mediated by cAMP-and cGMP-dependent protein kinases
    • Waldmann R., Nieberding M., and Walter U. Vasodilator-stimulated protein phosphorylation in platelets is mediated by cAMP-and cGMP-dependent protein kinases. Eur. J. Biochem. 167 (1987) 441-448
    • (1987) Eur. J. Biochem. , vol.167 , pp. 441-448
    • Waldmann, R.1    Nieberding, M.2    Walter, U.3
  • 115
    • 0021305910 scopus 로고
    • Cyclic cGMP-regulated enzymes and their possible physiological functions
    • Walter U. Cyclic cGMP-regulated enzymes and their possible physiological functions. Adv. Cyclic Nucleotide Protein Phosphorylation Res. 17 (1984) 249-258
    • (1984) Adv. Cyclic Nucleotide Protein Phosphorylation Res. , vol.17 , pp. 249-258
    • Walter, U.1
  • 116
    • 0024848484 scopus 로고
    • Physiological role of cGMP and cGMP-dependent protein kinase in the cardiovascular system
    • Walter U. Physiological role of cGMP and cGMP-dependent protein kinase in the cardiovascular system. Rev. Physiol. Biochem. Pharmacol. 113 (1989) 41-88
    • (1989) Rev. Physiol. Biochem. Pharmacol. , vol.113 , pp. 41-88
    • Walter, U.1
  • 119
    • 0027397638 scopus 로고
    • Platelet endothelium interactions
    • Ware J.A., and Heistad D.D. Platelet endothelium interactions. N. Engl. J. Med. 328 (1993) 628-635
    • (1993) N. Engl. J. Med. , vol.328 , pp. 628-635
    • Ware, J.A.1    Heistad, D.D.2
  • 120
    • 0021751461 scopus 로고
    • The rapid formation of inositol phosphates in human platelets by thrombin is inhibited by prostacyclin
    • Watson S.P., McConnell R.T., and Lapetina E.G. The rapid formation of inositol phosphates in human platelets by thrombin is inhibited by prostacyclin. J. Biol. Chem. 259 (1984) 13199-13203
    • (1984) J. Biol. Chem. , vol.259 , pp. 13199-13203
    • Watson, S.P.1    McConnell, R.T.2    Lapetina, E.G.3
  • 121
    • 0024496215 scopus 로고
    • Inhibition by cyclic AMP of guanosine nucleotide-induced activation of phosphoinositide-induced activation of phosphoinositide-specific phospholipase C in human platelets
    • Yada Y., Nagao S., Okano Y., and Nozawa Y. Inhibition by cyclic AMP of guanosine nucleotide-induced activation of phosphoinositide-induced activation of phosphoinositide-specific phospholipase C in human platelets. FEBS Lett. 242 (1989) 368-372
    • (1989) FEBS Lett. , vol.242 , pp. 368-372
    • Yada, Y.1    Nagao, S.2    Okano, Y.3    Nozawa, Y.4
  • 122
    • 0023851867 scopus 로고
    • Phosphorylation of platelet actin binding protein protects against proteolysis by calcium dependent sulfhydryl proteases
    • Zhang Z., Lawrence J., and Stracher A. Phosphorylation of platelet actin binding protein protects against proteolysis by calcium dependent sulfhydryl proteases. Biochem. Biophys. Res. Comm. 151 (1988) 355-360
    • (1988) Biochem. Biophys. Res. Comm. , vol.151 , pp. 355-360
    • Zhang, Z.1    Lawrence, J.2    Stracher, A.3
  • 123
    • 0026774568 scopus 로고
    • Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed platelets
    • Zhang J., Fry M.J., Waterfield M.D., Jaken S., Liao L., Fox J.E.B., and Rittenhouse S.E. Activated phosphoinositide 3-kinase associates with membrane skeleton in thrombin-exposed platelets. J. Biol. Chem. 267 (1992) 4686-4692
    • (1992) J. Biol. Chem. , vol.267 , pp. 4686-4692
    • Zhang, J.1    Fry, M.J.2    Waterfield, M.D.3    Jaken, S.4    Liao, L.5    Fox, J.E.B.6    Rittenhouse, S.E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.