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Volumn 93, Issue 2, 2005, Pages 319-325

The NO/cGMP pathway inhibits Rap I activation in human platelets via cGMP-dependent protein kinase I

Author keywords

cGMP; Kinase; Nitric oxide; Platelet physiology; Rap I

Indexed keywords

CYCLIC GMP; CYCLIC GMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE INHIBITOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANYLATE CYCLASE; INTEGRIN; NITRIC OXIDE; NITRIC OXIDE DONOR; NUCLEOTIDE BINDING PROTEIN; RAP PROTEIN;

EID: 13844276837     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH04-09-0582     Document Type: Article
Times cited : (53)

References (51)
  • 1
    • 0018099807 scopus 로고
    • Effect on platelet functions of derivatives of cyclic nucleotides
    • Pareti FI, Carrera D, Mannucci L, et al. Effect on platelet functions of derivatives of cyclic nucleotides. Thromb Haemost 1978; 39: 404-10.
    • (1978) Thromb. Haemost. , vol.39 , pp. 404-410
    • Pareti, F.I.1    Carrera, D.2    Mannucci, L.3
  • 2
    • 0025366847 scopus 로고
    • An L-arginine/nitric oxide pathway present in human platelets regulates aggregation
    • Radomski MW, Palmer RM, Moncada S. An L-arginine/nitric oxide pathway present in human platelets regulates aggregation. Proc Natl Acad Sci U S A 1990; 87: 5193-7.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 5193-5197
    • Radomski, M.W.1    Palmer, R.M.2    Moncada, S.3
  • 3
    • 0031048483 scopus 로고    scopus 로고
    • Identification of the NO synthase isoforms expressed in human neutrophil granulocytes, megakaryocytes and platelets
    • Wallerath T, Gath I, Aulitzky WE, et al. Identification of the NO synthase isoforms expressed in human neutrophil granulocytes, megakaryocytes and platelets. Thromb Haemost 1997; 77: 163-7.
    • (1997) Thromb. Haemost. , vol.77 , pp. 163-167
    • Wallerath, T.1    Gath, I.2    Aulitzky, W.E.3
  • 4
    • 0032407722 scopus 로고    scopus 로고
    • YC-1 potentiates nitric oxide- and carbon monoxide-induced cyclic GMP effects in human platelets
    • Friebe A, Müllershausen F, Smolenski A, et al. YC-1 potentiates nitric oxide- and carbon monoxide-induced cyclic GMP effects in human platelets. Mol Pharmacol 1998; 54: 962-7.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 962-967
    • Friebe, A.1    Müllershausen, F.2    Smolenski, A.3
  • 5
    • 0242552817 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinases and the cardiovascular system: Insights from genetically modified mice
    • Feil R, Lohmann SM, de Jonge H, et al. Cyclic GMP-dependent protein kinases and the cardiovascular system: insights from genetically modified mice. Circ Res 2003; 93: 907-16.
    • (2003) Circ. Res. , vol.93 , pp. 907-916
    • Feil, R.1    Lohmann, S.M.2    de Jonge, H.3
  • 6
    • 0242330206 scopus 로고    scopus 로고
    • Physiology and pathophysiology of vascular signaling controlled by guanosine 3′,5′-cyclic monophosphate-dependent protein kinase
    • [corrected]
    • Münzel T, Feil R, Mülsch A, et al. Physiology and pathophysiology of vascular signaling controlled by guanosine 3′,5′-cyclic monophosphate-dependent protein kinase [corrected]. Circulation 2003; 108: 2172-83.
    • (2003) Circulation , vol.108 , pp. 2172-2183
    • Münzel, T.1    Feil, R.2    Mülsch, A.3
  • 7
    • 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, et al. Defective nitrovasodilator-stimulated protein phosphorylation and calcium regulation in cGMP-dependent protein kinase-deficient human platelets of chronic myelocytic leukemia. J Biol Chem 1993; 268: 13526-31.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13526-13531
    • Eigenthaler, M.1    Ullrich, H.2    Geiger, J.3
  • 8
    • 0033583481 scopus 로고    scopus 로고
    • Increased adhesion and aggregation of platelets lacking cyclic guanosine 3′,5′-monophosphate kinase I
    • Massberg S, Sausbier M, Klatt P, et al. Increased adhesion and aggregation of platelets lacking cyclic guanosine 3′,5′-monophosphate kinase I. J Exp Med 1999; 189: 1255-64.
    • (1999) J. Exp. Med. , vol.189 , pp. 1255-1264
    • Massberg, S.1    Sausbier, M.2    Klatt, P.3
  • 9
    • 0037323858 scopus 로고    scopus 로고
    • The role of Rap1 in integrin-mediated cell adhesion
    • Bos JL, de Bruyn K, Enserink J, et al. The role of Rap1 in integrin-mediated cell adhesion. Biochem Soc Trans 2003; 31: 83-6.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 83-86
    • Bos, J.L.1    de Bruyn, K.2    Enserink, J.3
  • 10
    • 0142024483 scopus 로고    scopus 로고
    • Rap1 GTPase: Functions, regulation, and malignancy
    • Hattori M, Minato N. Rap1 GTPase: functions, regulation, and malignancy J Biochem (Tokyo) 2003; 134: 479-84.
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 479-484
    • Hattori, M.1    Minato, N.2
  • 12
    • 0038741814 scopus 로고    scopus 로고
    • Does Rap1 deserve a bad Rap?
    • Stork PJ. Does Rap1 deserve a bad Rap? Trends Biochem Sci 2003; 28: 267-75.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 267-275
    • Stork, P.J.1
  • 13
  • 14
    • 0026635746 scopus 로고
    • Generation of specific antibodies against the rap1A, rap1B and rap2 small GTP-binding proteins. Analysis of rap and ras proteins in membranes from mammalian cells
    • Klinz FJ, Seifert R, Schwaner I, et al. Generation of specific antibodies against the rap1A, rap1B and rap2 small GTP-binding proteins. Analysis of rap and ras proteins in membranes from mammalian cells. Eur J Biochem 1992; 207: 207-13.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 207-213
    • Klinz, F.J.1    Seifert, R.2    Schwaner, I.3
  • 15
    • 0028293483 scopus 로고
    • Structure and function of rap proteins in human platelets
    • Torti M, Lapetina EG. Structure and function of rap proteins in human platelets. Thromb Haemost 1994; 71: 533-43.
    • (1994) Thromb. Haemost. , vol.71 , pp. 533-543
    • Torti, M.1    Lapetina, E.G.2
  • 16
    • 0037067748 scopus 로고    scopus 로고
    • Relationships between Rap1b, affinity modulation of integrin alpha IIbbeta 3, and the actin cytoskeleton
    • Bertoni A, Tadokoro S, Eto K, et al. Relationships between Rap1b, affinity modulation of integrin alpha IIbbeta 3, and the actin cytoskeleton. J Biol Chem 2002; 277: 25715-21.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25715-25721
    • Bertoni, A.1    Tadokoro, S.2    Eto, K.3
  • 17
    • 0038266207 scopus 로고    scopus 로고
    • The small GTPase Rap1 is activated by turbulence and is involved in integrin [alpha] IIb[beta] 3-mediated cell adhesion in human megakaryocytes
    • de Bruyn KM, Zwartkruis FJ, de Rooij J, et al. The small GTPase Rap1 is activated by turbulence and is involved in integrin [alpha] IIb[beta] 3-mediated cell adhesion in human megakaryocytes. J Biol Chem 2003; 278: 22412-7.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22412-22417
    • de Bruyn, K.M.1    Zwartkruis, F.J.2    de Rooij, J.3
  • 18
    • 4644221351 scopus 로고    scopus 로고
    • Cal-DAG-GEFI integrates signaling for platelet aggregation and thrombus formation
    • Crittenden JR, Bergmeier W, Zhang Y, et al. Cal-DAG-GEFI integrates signaling for platelet aggregation and thrombus formation. Nat Med 2004; 10: 982-6.
    • (2004) Nat. Med. , vol.10 , pp. 982-986
    • Crittenden, J.R.1    Bergmeier, W.2    Zhang, Y.3
  • 19
    • 0031014969 scopus 로고    scopus 로고
    • Rapid Ca2+-mediated activation of Rap1 in human platelets
    • Franke B, Akkerman JW, Bos JL. Rapid Ca2+-mediated activation of Rap1 in human platelets. Embo J 1997; 16: 252-9.
    • (1997) Embo J. , vol.16 , pp. 252-259
    • Franke, B.1    Akkerman, J.W.2    Bos, J.L.3
  • 20
    • 0033967470 scopus 로고    scopus 로고
    • Sequential regulation of the small GTPase Rap1 in human platelets
    • Franke B, van Triest M, de Bruijn KM, et al. Sequential regulation of the small GTPase Rap1 in human platelets. Mol Cell Biol 2000; 20: 779-85.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 779-785
    • Franke, B.1    van Triest, M.2    de Bruijn, K.M.3
  • 21
    • 0037023134 scopus 로고    scopus 로고
    • A Gi-dependent pathway is required for activation of the small GTPase Rap1 B in human platelets
    • Lova P, Paganini S, Sinigaglia E et al. A Gi-dependent pathway is required for activation of the small GTPase Rap1 B in human platelets. J Biol Chem 2002; 277: 12009-15.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12009-12015
    • Lova, P.1    Paganini, S.2    Sinigaglia, E.3
  • 22
    • 0037189528 scopus 로고    scopus 로고
    • Activation of Rap1B by G(i) family members in platelets
    • Woulfe D, Jiang H, Mortensen R, et al. Activation of Rap1B by G(i) family members in platelets. J Biol Chem 2002; 277: 23382-90.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23382-23390
    • Woulfe, D.1    Jiang, H.2    Mortensen, R.3
  • 23
    • 0037441754 scopus 로고    scopus 로고
    • Identification of P2Y12-dependent and -independent mechanisms of glycoprotein VI-mediated Rap1 activation in platelets
    • Larson MK, Chen H, Kahn ML, et al. Identification of P2Y12-dependent and -independent mechanisms of glycoprotein VI-mediated Rap1 activation in platelets. Blood 2003; 101: 1409-15.
    • (2003) Blood , vol.101 , pp. 1409-1415
    • Larson, M.K.1    Chen, H.2    Kahn, M.L.3
  • 24
    • 0037414793 scopus 로고    scopus 로고
    • A selective role for phosphatidylinositol 3,4,5-trisphosphate in the Gi-dependent activation of platelet Rap1B
    • Lova P, Paganini S, Hirsch E, et al. A selective role for phosphatidylinositol 3,4,5-trisphosphate in the Gi-dependent activation of platelet Rap1B. J Biol Chem 2003; 278: 131-8.
    • (2003) J. Biol. Chem. , vol.278 , pp. 131-138
    • Lova, P.1    Paganini, S.2    Hirsch, E.3
  • 25
    • 0024467006 scopus 로고
    • Phosphorylation of smg p21, a ras p21-like GTP-binding protein, by cyclic AMP-dependent protein kinase in a cell-free system and in response to prostaglandin E1 in intact human platelets
    • Kawata M, Kikuchi A, Hoshijima M, et al. Phosphorylation of smg p21, a ras p21-like GTP-binding protein, by cyclic AMP-dependent protein kinase in a cell-free system and in response to prostaglandin E1 in intact human platelets. J Biol Chem 1989; 264: 15688-95.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15688-15695
    • Kawata, M.1    Kikuchi, A.2    Hoshijima, M.3
  • 26
    • 0026602309 scopus 로고
    • Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase
    • Miura Y, Kaibuchi K, Itoh T, et al. Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase. FEBS Lett 1992; 297: 171-4.
    • (1992) FEBS Lett. , vol.297 , pp. 171-174
    • Miura, Y.1    Kaibuchi, K.2    Itoh, T.3
  • 27
    • 0028910849 scopus 로고
    • Platelet rap1B phosphorylation is a sensitive marker for the action of cyclic AMP- and cyclic GMP-increasing platelet inhibitors and vasodilators
    • Grunberg B, Kruse HJ, Negrescu EV, et al. Platelet rap1B phosphorylation is a sensitive marker for the action of cyclic AMP- and cyclic GMP-increasing platelet inhibitors and vasodilators. J Cardiovasc Pharmacol 1995; 25: 545-51.
    • (1995) J. Cardiovasc. Pharmacol. , vol.25 , pp. 545-551
    • Grunberg, B.1    Kruse, H.J.2    Negrescu, E.V.3
  • 28
    • 0032493663 scopus 로고    scopus 로고
    • Analysis and regulation of vasodilator-stimulated phosphoprotein serine 239 phosphorylation in vitro and in intact cells using a phosphospecific monoclonal antibody
    • Smolenski A, Bachmann C, Reinhard K, et al. Analysis and regulation of vasodilator-stimulated phosphoprotein serine 239 phosphorylation in vitro and in intact cells using a phosphospecific monoclonal antibody. J Biol Chem 1998; 273: 20029-35.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20029-20035
    • Smolenski, A.1    Bachmann, C.2    Reinhard, K.3
  • 29
    • 0034682801 scopus 로고    scopus 로고
    • Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I
    • Smolenski A, Poller W, Walter U, et al. Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I. J Biol Chem 2000; 275: 25723-32.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25723-25732
    • Smolenski, A.1    Poller, W.2    Walter, U.3
  • 30
    • 0031866842 scopus 로고    scopus 로고
    • The use of nitric oxide donors in pharmacological studies
    • Feelisch M. The use of nitric oxide donors in pharmacological studies. Naunyn Schmiedebergs Arch Pharmacol 1998; 358: 113-22.
    • (1998) Naunyn. Schmiedebergs. Arch. Pharmacol. , vol.358 , pp. 113-122
    • Feelisch, M.1
  • 31
    • 0029928061 scopus 로고    scopus 로고
    • cGMP mediates the vascular and platelet actions of nitric oxide: Confirmation using an inhibitor of the soluble guanylyl cyclase
    • Moro MA, Russel RJ, Cellek S, et al. cGMP mediates the vascular and platelet actions of nitric oxide: confirmation using an inhibitor of the soluble guanylyl cyclase. Proc Natl Acad Sci U S A 1996; 93: 1480-5.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1480-1485
    • Moro, M.A.1    Russel, R.J.2    Cellek, S.3
  • 33
    • 0034911702 scopus 로고    scopus 로고
    • ADP receptors of platelets and their inhibition
    • Gachet C. ADP receptors of platelets and their inhibition. Thromb Haemost 2001; 86: 222-32.
    • (2001) Thromb. Haemost. , vol.86 , pp. 222-232
    • Gachet, C.1
  • 34
    • 0035793347 scopus 로고    scopus 로고
    • Inhibition of platelet function by administration of MRS2179, a P2Y1 receptor antagonist
    • Baurand A, Raboisson P, Freund M, et al. Inhibition of platelet function by administration of MRS2179, a P2Y1 receptor antagonist. Eur J Pharmacol 2001; 412: 213-21.
    • (2001) Eur. J. Pharmacol. , vol.412 , pp. 213-221
    • Baurand, A.1    Raboisson, P.2    Freund, M.3
  • 35
    • 0033603292 scopus 로고    scopus 로고
    • Deficient platelet-derived nitric oxide and enhanced hemostasis in mice lacking the NOSIII gene
    • Freedman JE, Sauter R, Battinelli EM, et al. Deficient platelet-derived nitric oxide and enhanced hemostasis in mice lacking the NOSIII gene. Circ Res 1999; 84: 1416-21.
    • (1999) Circ. Res. , vol.84 , pp. 1416-1421
    • Freedman, J.E.1    Sauter, R.2    Battinelli, E.M.3
  • 36
    • 0037152279 scopus 로고    scopus 로고
    • Role of platelet endothelial form of nitric oxide synthase in collagen-platelet interaction: Regulation by phophorylation
    • Chiang TM, Woo-Rasberry V, Cole F. Role of platelet endothelial form of nitric oxide synthase in collagen-platelet interaction: regulation by phophorylation. Biochim Biophys Acta 2002; 1592: 169-74.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 169-174
    • Chiang, T.M.1    Woo-Rasberry, V.2    Cole, F.3
  • 37
    • 0242690438 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) regulates the insulin-induced activation of the nitric oxide synthase in human platelets
    • Fleming I, Schulz C, Fichtlscherer B, et al. AMP-activated protein kinase (AMPK) regulates the insulin-induced activation of the nitric oxide synthase in human platelets. Thromb Haemost 2003; 90: 863-71.
    • (2003) Thromb. Haemost. , vol.90 , pp. 863-871
    • Fleming, I.1    Schulz, C.2    Fichtlscherer, B.3
  • 38
    • 0037428145 scopus 로고    scopus 로고
    • A stimulatory role for cGMP-dependent protein kinase in platelet activation
    • Li Z, Xi X, Gu M, et al. A stimulatory role for cGMP-dependent protein kinase in platelet activation. Cell 2003; 112: 77-86.
    • (2003) Cell , vol.112 , pp. 77-86
    • Li, Z.1    Xi, X.2    Gu, M.3
  • 39
    • 0038142355 scopus 로고    scopus 로고
    • A predominant role for cAMP-dependent protein kinase in the cGMP-induced phosphorylation of vasodilator-stimulated phosphoprotein and platelet inhibition in humans
    • Li Z, Ajdic J, Eigenthaler M, et al. A predominant role for cAMP-dependent protein kinase in the cGMP-induced phosphorylation of vasodilator-stimulated phosphoprotein and platelet inhibition in humans. Blood 2003; 101: 4423-9.
    • (2003) Blood , vol.101 , pp. 4423-4429
    • Li, Z.1    Ajdic, J.2    Eigenthaler, M.3
  • 40
    • 1642411578 scopus 로고    scopus 로고
    • Potent inhibition of human platelets by cGMP analogs independent of cGMP-dependent protein kinase
    • Gambaryan S, Geiger J, Schwarz UR, et al. Potent inhibition of human platelets by cGMP analogs independent of cGMP-dependent protein kinase. Blood 2004; 103: 2593-600.
    • (2004) Blood , vol.103 , pp. 2593-2600
    • Gambaryan, S.1    Geiger, J.2    Schwarz, U.R.3
  • 41
    • 1642278417 scopus 로고    scopus 로고
    • GPIb-dependent platelet activation is dependent on Src kinases but not MAP kinase or cGMP-dependent kinase
    • Marshall SJ, Senis YA, Auger JM, et al. GPIb-dependent platelet activation is dependent on Src kinases but not MAP kinase or cGMP-dependent kinase. Blood 2004; 103: 2601-9.
    • (2004) Blood , vol.103 , pp. 2601-2609
    • Marshall, S.J.1    Senis, Y.A.2    Auger, J.M.3
  • 42
    • 4444257333 scopus 로고    scopus 로고
    • Reciprocal cross-talk between P2Y1 and P2Y12 receptors at the level of calcium signaling in human platelets
    • Hardy AR, Jones ML, Mundell SJ, et al. Reciprocal cross-talk between P2Y1 and P2Y12 receptors at the level of calcium signaling in human platelets. Blood 2004; 104: 1745-52.
    • (2004) Blood , vol.104 , pp. 1745-1752
    • Hardy, A.R.1    Jones, M.L.2    Mundell, S.J.3
  • 43
    • 0036683714 scopus 로고    scopus 로고
    • Inhibition of platelet P2Y12 and alpha2A receptor signaling by cGMP-dependent protein kinase
    • Aktas B, Honig-Liedl P, Walter U, et al. Inhibition of platelet P2Y12 and alpha2A receptor signaling by cGMP-dependent protein kinase. Biochem Pharmacol 2002; 64: 433-9.
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 433-439
    • Aktas, B.1    Honig-Liedl, P.2    Walter, U.3
  • 44
    • 0027419168 scopus 로고
    • Phosphorylation of rap1B by protein kinase A is not involved in platelet inhibition by cyclic AMP
    • Siess W, Grunberg B. Phosphorylation of rap1B by protein kinase A is not involved in platelet inhibition by cyclic AMP. Cell Signal 1993; 5: 209-14.
    • (1993) Cell Signal. , vol.5 , pp. 209-214
    • Siess, W.1    Grunberg, B.2
  • 45
    • 9144259249 scopus 로고    scopus 로고
    • Enhanced in vivo platelet adhesion in vasodilator-stimulated phosphoprotein (VASP)-deficient mice
    • Massberg S, Gruner S, Konrad I, et al. Enhanced in vivo platelet adhesion in vasodilator-stimulated phosphoprotein (VASP)-deficient mice. Blood 2004; 103: 136-42.
    • (2004) Blood , vol.103 , pp. 136-142
    • Massberg, S.1    Gruner, S.2    Konrad, I.3
  • 46
    • 0039207312 scopus 로고    scopus 로고
    • The vasodilator-stimulated phosphoprotein (VASP) is involved in cGMP- and cAMP-mediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function
    • Aszodi A, Pfeifer A, Ahmad M, et al. The vasodilator-stimulated phosphoprotein (VASP) is involved in cGMP- and cAMP-mediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function. Embo J 1999; 18: 37-48.
    • (1999) Embo J. , vol.18 , pp. 37-48
    • Aszodi, A.1    Pfeifer, A.2    Ahmad, M.3
  • 47
    • 0033529302 scopus 로고    scopus 로고
    • Megakaryocyte hyperplasia and enhanced agonist-induced platelet activation in vasodilator-stimulated phosphoprotein knockout mice
    • Hauser W, Knobeloch KP, Eigenthaler M, et al. Megakaryocyte hyperplasia and enhanced agonist-induced platelet activation in vasodilator-stimulated phosphoprotein knockout mice. Proc Natl Acad Sci U S A 1999; 96: 8120-5.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8120-8125
    • Hauser, W.1    Knobeloch, K.P.2    Eigenthaler, M.3
  • 48
    • 5044241734 scopus 로고    scopus 로고
    • RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion
    • Lafuente EM, van Puijenbroek AA, Krause M, et al. RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion. Dev Cell 2004; 7: 585-95.
    • (2004) Dev. Cell , vol.7 , pp. 585-595
    • Lafuente, E.M.1    van Puijenbroek, A.A.2    Krause, M.3
  • 49
    • 0037416169 scopus 로고    scopus 로고
    • Direct activation of PDE5 by cGMP: Long-term effects within NO/cGMP signaling
    • Müllershausen F, Friebe A, Feil R, et al. Direct activation of PDE5 by cGMP: long-term effects within NO/cGMP signaling. J Cell Biol 2003; 160: 719-27.
    • (2003) J. Cell Biol. , vol.160 , pp. 719-727
    • Müllershausen, F.1    Friebe, A.2    Feil, R.3
  • 50
    • 0038521306 scopus 로고    scopus 로고
    • Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146
    • Butt E, Gambaryan S, Gottfert N, et al. Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146. J Biol Chem 2003; 278: 15601-7.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15601-15607
    • Butt, E.1    Gambaryan, S.2    Gottfert, N.3
  • 51
    • 0035831438 scopus 로고    scopus 로고
    • Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: Phosphorylation-induced actin polymerization caused by HSP27 mutants
    • Butt E, Immler D, Meyer HE, et al. Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: phosphorylation-induced actin polymerization caused by HSP27 mutants. J Biol Chem 2001; 276: 7108-13.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7108-7113
    • Butt, E.1    Immler, D.2    Meyer, H.E.3


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