About: A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor

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About: A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 1995 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Juli 1995 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q58451438-AAE207D3-3142-487F-9649-F2F1198531A1
publication date	1995-07-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58451438-605413C7-2176-41F5-A95A-67C85A456EEF
language of work or name	English
cites work	wds:Q58451438-1299841C-2122-40E8-BA06-70E8413C1C46 wds:Q58451438-30627D50-2BDB-4310-B718-FC926993B640 wds:Q58451438-33DAB607-FA1F-46ED-B787-093AE528E8CD wds:Q58451438-449157E0-4819-454A-B9B1-E74EC04BE542 wds:Q58451438-625924A3-8ACD-4D5F-A803-1F4151EA937C wds:Q58451438-7D2714CB-0586-4E86-BCDF-A0B5DB78A947 wds:Q58451438-A3F399D4-F310-43C8-B24B-5615B98B4F21 wds:Q58451438-A8DF34AF-A943-4598-BD64-247A56D96397 wds:Q58451438-B2E1DAC4-0BCE-4933-A92B-667C748A58DE wds:Q58451438-BFBFE17A-D9DA-45FF-B0A1-1F88B7F65EE6 wds:Q58451438-C66686BB-2B9D-4855-BFB1-7AD1780BBAEC wds:Q58451438-CAFEFCEC-742D-4E7E-93EF-265F28C54E89 wds:Q58451438-ED6E62AC-D4BA-49D5-83A8-B28330C991A4 wds:Q58451438-F57F80AE-7620-4CDB-9E40-1BB9BD92C86E wds:Q58451438-FCB1C5C9-1CD3-40DE-B69B-DFDABB4F2B9E
cites work	The cytoplasmic tail of the G-protein-coupled receptor for parathyroid hormone and parathyroid hormone-related protein contains positive and negative signals for endocytosis LIGAND: A versatile computerized approach for characterization of ligand-binding systems Aromatic-aromatic interaction: a mechanism of protein structure stabilization Sequence alignment of the G-protein coupled receptor superfamily In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors Generation and role of calcium signal in adrenal glomerulosa cells Differentiation between binding sites for angiotensin II and nonpeptide antagonists on the angiotensin II type 1 receptors Rapid and efficient site-specific mutagenesis without phenotypic selection Projection structure of rhodopsin Isolation of a cDNA encoding the vascular type-1 angiotensin II receptor. Modeling of G-protein-coupled receptors: application to dopamine, adrenaline, serotonin, acetylcholine, and mammalian opsin receptors Mutation of Asp74 of the rat angiotensin II receptor confers changes in antagonist affinities and abolishes G-protein coupling. The biology of angiotensin II receptors. Structure of G-protein-linked receptors Competitive Binding Activity of Angiotensin II Analogues in an Adrenal Cortex Radioligand-Receptor Assay
author name string	wds:Q58451438-476B0BB6-D5FF-453E-B9CA-FA417BA17A20 wds:Q58451438-645CD189-A198-4DC8-B335-C318071D01C9 wds:Q58451438-A0D03E08-23A3-4CF1-98DF-783C2B5A3423 wds:Q58451438-D9DB5446-18D1-4934-80E8-673692C39825
author name string	K J Catt L Hunyady A J Baukal M Bor
rdfs:label	A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor (en) A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor (nl)
skos:prefLabel	A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor (en) A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor (nl)
name	A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor (en) A Conserved NPLFY Sequence Contributes to Agonist Binding and Signal Transduction but Is Not an Internalization Signal for the Type 1 Angiotensin II Receptor (nl)
author	wds:Q58451438-38A01D26-5A30-4BB3-9E97-BD91B46444FC
author	Tamas Balla
title	wds:Q58451438-7F224D2E-1852-4D3D-989E-BF5C91727774
title	A conserved NPLFY sequence contributes to agonist binding and signal transduction but is not an internalization signal for the type 1 angiotensin II receptor (en)
page(s)	wds:Q58451438-D3604644-7EBD-4BD1-A497-3141E8DCC7B7
page(s)	16602-16609
instance of	wds:Q58451438-B54C7DC3-F10B-44BB-83DF-5AAC87B4B1FF
instance of	scholarly article
PubMed ID	wds:Q58451438-312B67D5-3F7D-4572-8113-1D6E4028AC34
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7622467
PubMed ID	7622467
published in	wds:Q58451438-B7693CDF-4E4A-424F-9069-0453D073294A
published in	Journal of Biological Chemistry
issue	wds:Q58451438-98B88AE7-4722-4B5B-B15D-C9663491E033
volume	wds:Q58451438-2D1F6640-7CA4-4769-BB5E-A43B2F787AB1
issue	28
volume	270
number of pages	wds:Q58451438-599C7597-F9E7-4206-9665-7F631C99BCE6
number of pages	8 (xsd:decimal)
DOI	wds:Q58451438-063DEC2B-AD43-47AA-8C81-7A9B34561198
DOI	http://dx.doi.org/10.1074/JBC.270.28.16602
DOI	10.1074/JBC.270.28.16602
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58451438
is cites work of	Visualization of the calcitonin receptor-like receptor and its receptor activity-modifying proteins during internalization and recycling Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface Regulatory mechanisms that modulate signalling by G-protein-coupled receptors Cross-talk between the insulin and angiotensin signaling systems A receptor-G protein coupling-independent step in the internalization of the thyrotropin-releasing hormone receptor Conserved helix 7 tyrosine acts as a multistate conformational switch in the 5HT2C receptor. Identification of a novel "locked-on" phenotype and double revertant mutations. The Role of a Conserved Region of the Second Intracellular Loop in AT1 Angiotensin Receptor Activation and Signaling Functional role of the NPxxY motif in internalization of the type 2 vasopressin receptor in LLC-PK1 cells Sequestration of the delta opioid receptor. Role of the C terminus in agonist-mediated internalization Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor from the silkmoth, Bombyx mori. Significance of the carboxyl terminus in receptor internalization. Role of G protein-coupled receptor kinase 2 and arrestins in beta-adrenergic receptor internalization. The Functional Microdomain in Transmembrane Helices 2 and 7 Regulates Expression, Activation, and Coupling Pathways of the Gonadotropin-releasing Hormone Receptor Chapter 14 Molecular pharmacology and modeling of vasopressin receptors Mechanisms and functions of AT(1) angiotensin receptor internalization The angiotensin II type 1 receptor and receptor-associated proteins Identification of potential tyrosine-containing endocytic motifs in the carboxyl-tail and seventh transmembrane domain of the neurokinin 1 receptor Selective Interaction of ARF1 with the Carboxy-Terminal Tail Domain of the 5-HT2A Receptor Model of the whole rat AT1 receptor and the ligand-binding site. Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif Motif mutation of bradykinin B2 receptor second intracellular loop and proximal C terminus is critical for signal transduction, internalization, and resensitization. Identification of a putative nuclear localization sequence within ANG II AT(1A) receptor associated with nuclear activation. Constitutive activation of the angiotensin II type 1 receptor alters the spatial proximity of transmembrane 7 to the ligand-binding pocket

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