About: Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor

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About: Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1986 (ast) 1986年學術文章 (zh) vědecký článek publikovaný v roce 1986 (cs) наукова стаття, опублікована в травні 1986 (uk) 1986 թվականի մայիսին հրատարակված գիտական հոդված (hy) 1986 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في مايو 1986) (ar) vedecký článok (publikovaný 1986/05/01) (sk) article publié dans les Proceedings of the National Academy of Sciences of the United States of America (fr) wetenschappelijk artikel (gepubliceerd op 1986/05/01) (nl) scientific journal article (en) im Mai 1986 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28646192-DAA2E0F1-4E1B-4AAB-9ABB-B9A7C4BD7E5B
publication date	1986-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28646192-3F622B13-43CF-44DD-AEB8-79E5A80B0E5F
language of work or name	English
cites work	wds:Q28646192-0DF0C1C5-9596-41DF-904C-9A0474A59015 wds:Q28646192-1D162E70-66E5-415B-A2C6-FC780A131C81 wds:Q28646192-1F04BF86-7379-4288-BF3B-2D5AD8AF9C63 wds:Q28646192-258815E5-FB19-47FB-945C-1F5D8D91B82A wds:Q28646192-2C1E63A4-3749-499A-A840-909A1D7B28C1 wds:Q28646192-318FDD33-A1C1-4BDD-B7E3-397FF4D26B25 wds:Q28646192-41B3C0E0-6613-462C-B566-2ECBA8951868 wds:Q28646192-50D52A98-2E1B-4DF1-8FA4-0313CA01C16F wds:Q28646192-5C34FA5A-39D0-4487-BA61-C262A742DD95 wds:Q28646192-5DB9DCFD-1BAB-42F5-8443-6CBA66A8ECF8 wds:Q28646192-76162886-5B5B-4D30-996F-44994437157E wds:Q28646192-7680BF74-7906-466C-822D-A8E5FE9D1283 wds:Q28646192-76B73C4D-21B9-438E-A9C5-95967C10FCED wds:Q28646192-7E389195-F182-4CBC-9FCA-9CF8A619D251 wds:Q28646192-848C6C02-1E84-4475-926F-313F8624097A wds:Q28646192-8D292A8B-5139-44D2-A10C-E34426D152CB wds:Q28646192-8FA35A04-3AA5-45E8-BC92-FEC6B8B30BAF wds:Q28646192-901AE30B-4CB5-4AC6-BC48-6D2F46CEDD16 wds:Q28646192-95A41D2A-AF9D-4D30-A98F-776672DA005C wds:Q28646192-AA4ACF07-D005-4041-AD83-3A5C3BA779E8 wds:Q28646192-AA947D50-8EA7-4158-81B2-3103D5BB2B27 wds:Q28646192-AC6DA1F8-E6BC-4B76-BE9B-059A2AC58588 wds:Q28646192-CB4027D0-A96E-406F-A2DD-9871FADBDDCE wds:Q28646192-D41A60A1-3DC8-4C35-B742-9500DF501307 wds:Q28646192-DE4186D9-E8F6-497E-B8F8-9659B78DEAB5 wds:Q28646192-E0A3F58A-D54A-4F46-B5E2-05567C441DC9 wds:Q28646192-E6F4848B-611F-4BE1-952F-DCBAAC99F1F5 wds:Q28646192-F7887E33-074C-44AF-8826-98171DA71E4F
cites work	A rapid, sensitive, and specific method for the determination of protein in dilute solution Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Rapid internalization of the transferrin receptor in K562 cells is triggered by ligand binding or treatment with a phorbol ester Association of phorbol ester-induced hyperphosphorylation and reversible regulation of transferrin membrane receptors in HL60 cells Rhodopsin kinase activity in the mammalian pineal gland and other tissues. Mammalian .beta.2-adrenergic receptor: purification and characterization Resolution of high and low affinity epidermal growth factor receptors. Inhibition of high affinity component by low temperature, cycloheximide, and phorbol esters Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors Direct Demonstration of Impaired Functionality of a Purified Desensitized β-Adrenergic Receptor in a Reconstituted System Light dependent phosphorylation of rhodopsin by ATP. Phosphorylation of frog photoreceptor membranes induced by light Molecular mechanisms of receptor desensitization using the beta-adrenergic receptor-coupled adenylate cyclase system as a model Catecholamine-specific desensitization of adenylate cyclase. Evidence for a multistep process Agonist-induced desensitization of the beta-adrenergic receptor-linked adenylate cyclase. Phosphorylation of the mammalian beta-adrenergic receptor by cyclic AMP-dependent protein kinase. Regulation of the rate of receptor phosphorylation and dephosphorylation by agonist occupancy and effects on coupling of the receptor to the stimulator Desensitization of turkey erythrocyte adenylate cyclase. Beta-adrenergic receptor phosphorylation is correlated with attenuation of adenylate cyclase activity GTP binding protein: properties and lack of activation by phosphorylated rhodopsin. Homologous desensitization of adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor 31 Calcium-activated, phospholipid-dependent protein kinase (protein kinase C) from rat brain Catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase is associated with phosphorylation of the beta-adrenergic receptor Adenylate cyclase-coupled beta-adrenergic receptors: structure and mechanisms of activation and desensitization Kinase-negative mutants of S49 mouse lymphoma cells carry a trans-dominant mutation affecting expression of cAMP-dependent protein kinase Catecholamine-induced desensitization involves an uncoupling of beta-adrenergic receptors and adenylate cyclase Desensitization of the turkey erythrocyte beta-adrenergic receptor in a cell-free system. Evidence that multiple protein kinases can phosphorylate and desensitize the receptor Cell-free desensitization of catecholamine-sensitive adenylate cyclase. Agonist- and cAMP-promoted alterations in turkey erythrocyte beta-adrenergic receptors Light-stimulated phosphorylation of bovine visual pigments by adenosine triphosphate Phosphorylation of rhodopsin: most rhodopsin molecules are not phosphorylated.
author name string	wds:Q28646192-63C17F3B-CD3E-4063-B665-EC85721100E7 wds:Q28646192-7540B6B7-53D4-4350-A2E6-41D7C0D19DD0
OpenCitations bibliographic resource ID	wds:Q28646192-9659272D-525E-4B18-911F-D0747B085F07
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1714530
author name string	R. H. Strasser J. L. Benovic
OpenCitations bibliographic resource ID	1714530
rdfs:label	Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (en) Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (nl) Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (ast)
skos:prefLabel	Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (en) Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (nl) Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (ast)
name	Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (en) Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (nl) Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (ast)
author	wds:Q28646192-3D7DAD3E-98F2-4CFE-BAD2-39C359FB1E73 wds:Q28646192-A61BAEF7-3BE9-4E5E-9847-380FFC856675
author	Robert Lefkowitz Marc Caron
title	wds:Q28646192-78EF1822-D3FE-469E-B77F-F4586D29E914
title	Beta-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist-occupied form of the receptor (en)
page(s)	wds:Q28646192-AD61584E-D052-4A8F-921D-CF42F00C18DF
page(s)	2797–2801
instance of	wds:Q28646192-19B63F4D-C589-4852-9E53-E2A224582954
instance of	scholarly article
main subject	wds:Q28646192-9D6D0045-172E-4185-9E4A-6DF6768EEAEE

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