(Q52530481)

2 May 2018

title

Regulation of a common, low-affinity binding site for primary prostanoids on bovine aortic endothelial cells. (English)

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2 May 2018

author name string

G Rimon

series ordinal

1

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2 May 2018

M Rubin

series ordinal

2

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2 May 2018

publication date

1 April 1998

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2 May 2018

Biochimica et Biophysica Acta

published in

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2 May 2018

volume

1380

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2 May 2018

issue

2

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2 May 2018

page(s)

289-296

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2 May 2018

A common low-affinity binding site for primary prostanoids on bovine aortic endothelial cells

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A common binding site for primary prostanoids in vascular smooth muscles: a definitive discrimination of the binding for thromboxane A2/prostaglandin H2 receptor agonist from its antagonist

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Phosphorylation/dephosphorylation of the beta-adrenergic receptor regulates its functional coupling to adenylate cyclase and subcellular distribution

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Desensitization of the isolated beta 2-adrenergic receptor by beta-adrenergic receptor kinase, cAMP-dependent protein kinase, and protein kinase C occurs via distinct molecular mechanisms

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Cloning of the rat and human prostaglandin F2 alpha receptors and the expression of the rat prostaglandin F2 alpha receptor

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Cloning and expression of the EP3-subtype of human receptors for prostaglandin E2

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Local amplification of platelet function by 8-Epi prostaglandin F2alpha is not mediated by thromboxane receptor isoforms

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Cloning and expression of three isoforms of the human EP3 prostanoid receptor

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Cloning and expression of a cDNA for the human prostacyclin receptor.

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Agonist-induced phosphorylation of human platelet TXA2/PGH2 receptors

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Regulation of response to thromboxane A2 in CHRF-288 megakaryocytic cells

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Dual regulation of PLA2 and PGI2 production by G proteins in bovine aortic endothelial cells

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Desensitization of adenylate cyclase responses following exposure to IP prostanoid receptor agonists. Homologous and heterologous desensitization exhibit the same time course

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Identifiers

DOI

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2 May 2018

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2 May 2018