Role of platelet endothelial form of nitric oxide synthase in collagen-platelet interaction: regulation by phosphorylation. (Q44179123)

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13 December 2019

title

Role of platelet endothelial form of nitric oxide synthase in collagen-platelet interaction: regulation by phosphorylation (English)

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13 December 2019

0 references

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Thomas M Chiang

1

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13 December 2019

Virginia Woo-Rasberry

series ordinal

2

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13 December 2019

Flecia Cole

series ordinal

3

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13 December 2019

publication date

1 October 2002

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Biochimica et Biophysica Acta

13 December 2019

published in

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13 December 2019

volume

1592

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13 December 2019

issue

2

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13 December 2019

page(s)

169-174

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Collagen-mediated platelet aggregation. Effects of collagen modification involving the protein and carbohydrate moieties

13 December 2019

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The membrane glycoprotein Ia-IIa (VLA-2) complex mediates the Mg++-dependent adhesion of platelets to collagen

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Glycoprotein VI is the collagen receptor in platelets which underlies tyrosine phosphorylation of the Fc receptor gamma-chain

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Role of the recombinant protein of the platelet receptor for type I collagen in the release of nitric oxide during platelet aggregation

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Role of nitric oxide synthase in collagen-platelet interaction: involvement of platelet nonintegrin collagen receptor nitrotyrosylation

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Oxygen-free radicals and nitric oxide are involved in the thrombus growth produced by iontophoresis of ADP

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Nitric oxide modulates the activity of the hemoproteins prostaglandin I2 synthase and thromboxane A2 synthase

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Aggregation of Blood Platelets by Adenosine Diphosphate and its Reversal

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Upregulation of nitric oxide synthase in cultured human keratinocytes after ultraviolet B and bradykinin.

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Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1

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AMP-activated protein kinase phosphorylation of endothelial NO synthase

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Phosphorylation of Thr(495) regulates Ca(2+)/calmodulin-dependent endothelial nitric oxide synthase activity.

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Phosphorylation-dephosphorylation states at different sites affect phosphoprotein phosphatase 1 activity

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The Akt kinase signals directly to endothelial nitric oxide synthase

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12379480%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

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