Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Phosphorylated human platelet proteins

Figure 11.1 Autoradiography of a two-dimensional separation of phosphorylated human platelet proteins after labeling with [ P] in the pH range 3-10. Figure 11.1 Autoradiography of a two-dimensional separation of phosphorylated human platelet proteins after labeling with [ P] in the pH range 3-10.
Connolly, T., Laiving, W. and Majerus, P. (1986). Protein kinase C phosphorylates human platelet inositol trisphosphate 5 -phosphomonesterase increasing the phosphatase activity. Cell 46, 951-958... [Pg.230]

Immler, D. Gremm, D. Kirsch, D. Spengler, B. Presek, R Meyer, H. E. 1998. Identification of phosphorylated proteins from thrombin-activated human platelets isolated by two-dimensional gel electrophoresis by electrospray ionization-tandem mass spectrometry (ESI-MS/MS) and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS). Electrophoresis, 19,1015-1023. [Pg.217]

Differential analysis of phosphorylated proteins in resting and thrombin-stimulated human platelets. Anal. Bioanal. Chem. 376, 973-993. [Pg.156]

All PKG substrates identified so far in human platelets interact directly or indirectly with the actin filament and the cytoskeleton of the cell and are involved in the negative regulation of platelet activation after phosphorylation by PKG. The proteomic approach in combination with functional studies is a very successful tool for studying phosphorylation-dependent effects in platelets. Ongoing proteome studies will now focus on membrane proteins for new therapeutic targets to develop antithrombotic drugs. [Pg.218]

Butt, E., Abel, K., Krieger, M., Palm, D., Hoppe, V., Hoppe, J., Walter, U. (1994). cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. J. Biol. Chem. [Pg.220]

Kotlyarov, A., Laass, K., Gaestel, M. (2001). Heat shock protein 27 is a substrate of cGM P-dependent protein kinase in intact human platelets phosphorylation-induced actin polymerization caused by HSP27 mutants. / Biol. Chem. 276, 7108-7113. [Pg.220]

Defective nitrovasodilator-stimulated protein phosphorylation and calcium regulation in cGM P-dependent protein kinase-defident human platelets of chronic myelocytic leukemia. Biol. [Pg.220]

Kawamoto, S., Bengue,A. R., Sellers,). R., Adelstein, R. S. (1989). In situ phosphorylation of human platelet myosin heavy and light chains by protein kinase C. [Pg.221]

Marcus, K., Moebius, )., Meyer, H. E. (2003). Differential analysis of phosphorylated proteins in resting and thrombin-stimulated human platelets. Anal. Bioanal. Chem. 276, 973-993. [Pg.221]

Siess, W., Winegar, D.A., and Lapetina, E.G. (1990). Rapl-B is phosphorylated by protein kinase A in intact human platelets. Biochem Biophys Res Commun 170 944—950. [Pg.64]

Bsbinska A, Ehrlich YH, Komecki E. Activation of human platelets by protein kinase C antibody rede for surface phosphorylation in homeostasis AmJPhysiol 1996 271 H2134-44... [Pg.75]

Borsch-Haubold AG, Kramer RM, Watson SP. Cytosolic phospholipase Aj is phosphorylated in collagen- and thrombin-stimulated human platelets independent of protein kinase C and mitogen-activated protein kinase. JBiol Chem 270 25885-25892,1995. [Pg.219]

INAZU T, TANIGUCHI T, YANAGI S, YaMAMURA H. Protein-tyrosine phosphorylation and aggregation of intact human platelets by vansalate with HjOj. Biochem Biophys Res Commun 170 259-263,1990. [Pg.225]

LAPETINA eg, LACAL JC, Reep BR, Molina Y, Vedia L. a ras-related protein is phosphorylated and translocated by agonists that increase cAMP levels in human platelets. ProcNatl Acad Sci USA 86 3131-3134, 1989. [Pg.227]

HOSHIJIMA M, KIKUCHI A, KAWATA M, OHMORIT, HASHIMOTO E, YAMAMURA H, et al (1988) Phosphorylation by cyclic AMP-dependent protein kinase of a human platelet Nfr 22,000 GTP-binding protein (smg p21) having the same putative effector domain as the ras gene products Biochemical A Bio ysical Research Communications, 157,851-860. [Pg.248]

Horstrup, K., Jablonka, B., Honig-Liedl, P., Just, M., Kochsiek, K., and Walter, U. (1994). Phosphorylation of the focal adhesion protein VASP at Ser 157 in intact human platelets correlates with fibrinogen receptor inhibition. Eur. ]. Biochem. 225, 21-27. [Pg.67]


See other pages where Phosphorylated human platelet proteins is mentioned: [Pg.182]    [Pg.238]    [Pg.238]    [Pg.239]    [Pg.239]    [Pg.24]    [Pg.209]    [Pg.216]    [Pg.216]    [Pg.51]    [Pg.57]    [Pg.90]    [Pg.129]    [Pg.200]    [Pg.209]    [Pg.257]    [Pg.301]    [Pg.302]    [Pg.432]    [Pg.445]    [Pg.454]    [Pg.20]    [Pg.155]    [Pg.218]    [Pg.372]    [Pg.78]    [Pg.214]    [Pg.1258]    [Pg.263]   


SEARCH



Phosphorylated protein

© 2024 chempedia.info