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Proteomic analysis of integrin alphaIIbbeta3 outside-in signaling reveals Src-kinase-independent phosphorylation of Dok-1 and Dok-3 leading to SHIP-1 interactions
Journal of Thrombosis and Haemostasis, 10/06/09
Senis YA et al. – This study provides new insights into the molecular mechanism regulating alphaIIbbeta3–mediated platelet spreading on fibrinogen. The novel platelet adapter Dok–3 and the structurally related Dok–1 are tyrosine phosphorylated in an Src kinase–independent manner downstream of alphaIIbbeta3 in human platelets, leading to an interaction with Grb2 and SHIP–1.
Today in Basic Science/Genetics...keeping you current
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Functional membrane androgen receptors in colon tumors trigger pro-apoptotic responses in vitro and reduce drastically tumor incidence in vivo
Molecular Cancer, 12/08/09
Dual effects of TGF-beta on ERalpha-mediated estrogenic transcriptional activity in breast cancer
Molecular Cancer, 12/08/09
Activation of hedgehog signaling is not a frequent event in ovarian cancers
Molecular Cancer, 12/08/09
Today in Coagulation/Bleeding Dz...keeping you current
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A modified thrombin generation test for investigating very low levels of factor VIII activity in hemophilia A
International Journal of Hematology, 12/08/09
Risk factors for thrombophilia in young adults presenting with thrombosis
International Journal of Hematology, 12/08/09
Diagnosis of platelet-type von Willebrand disease by flow cytometry
Haematologica, 12/08/09
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