About: -mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity

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rdf:type	Item
description	artículu científicu espublizáu en 1994 (ast) vědecký článek publikovaný v roce 1994 (cs) 1994 թուականի Օգոստոսին հրատարակուած գիտական յօդուած (hyw) 1994 թվականի օգոստոսին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в серпні 1994 (uk) vedecký článok (publikovaný 1994/08/12) (sk) مقالة علمية (نشرت في 12-8-1994) (ar) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en) im August 1994 veröffentlichter wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1994/08/12) (nl)
publication date	wds:Q28569235-AEBE7742-F92F-4E95-81EA-373A56EFC25A
publication date	1994-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28569235-56BCB478-ACCF-4018-AAA6-82B2970DB847
language of work or name	English
author name string	wds:Q28569235-146A50FC-0308-4338-AE5A-AD1FEEE898EC wds:Q28569235-1B75BD68-DABB-464E-98DA-B4D9A5256EF7 wds:Q28569235-25404136-86B6-4D29-8457-505590B383EA wds:Q28569235-40236C73-14ED-45B1-98BC-EA4EE86BF8D3 wds:Q28569235-A89140E9-6AC8-4F1E-B29B-235DEFB52B78 wds:Q28569235-C0CE780B-49D4-46E6-9104-072809820AA9 wds:Q28569235-E7AA0246-6DFD-4295-A01B-E70C4ED22534
author name string	Surratt CK Moriwaki A Uhl GR Johnson PS Wang JB Seidleck BK Blaschak CJ
rdfs:label	-mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (en) -mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (nl) -mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (ast)
skos:prefLabel	-mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (en) -mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (nl) -mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (ast)
name	-mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (en) -mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (nl) -mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (ast)
title	wds:Q28569235-020D1A97-BCBE-45C3-AB4A-22008697535A
title	-mu opiate receptor. Charged transmembrane domain amino acids are critical for agonist recognition and intrinsic activity (en)
page(s)	wds:Q28569235-36294904-B412-4D20-9331-DFA852C3F5E3
page(s)	20548-20553
instance of	wds:Q28569235-CFDEBD28-B6B5-4444-A695-D8013433B061
instance of	scholarly article
main subject	wds:Q28569235-78B33F0A-C046-42E0-ACA1-640D3607DC69
main subject	transmembrane protein
PubMed ID	wds:Q28569235-5555E8ED-70CB-4C21-97C8-744ABE57E347
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8051154
PubMed ID	8051154
published in	wds:Q28569235-39BD15B6-D511-4C7B-B146-26963E25719E
published in	Journal of Biological Chemistry
issue	wds:Q28569235-9AFAF909-85D8-4682-A7F6-2A2087D461F2
volume	wds:Q28569235-A41B59A5-08CF-4856-A7E1-2A4FA683FF4E
issue	32
volume	269
number of pages	wds:Q28569235-62445AB2-0913-4C32-9DFE-A83087CEA32D
number of pages	6 (xsd:decimal)
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28569235
is cites work of	Ultrastructural relationship between the mu opioid receptor and its interacting protein, GPR177, in striatal neurons Insights into subtype selectivity of opioid agonists by ligand-based and structure-based methods Structure of the human κ-opioid receptor in complex with JDTic mu-Opioid receptors are localized to extrasynaptic plasma membranes of GABAergic neurons and their targets in the rat nucleus accumbens Construction of a sequence motif characteristic of aminergic G protein-coupled receptors Recent advances in molecular recognition and signal transduction of active peptides: receptors for opioid peptides Neuropharmacology of the naturally occurring kappa-opioid hallucinogen salvinorin A High- and low-affinity sites for sodium in δ-OR-Gi1α (Cys (351)-Ile (351)) fusion protein stably expressed in HEK293 cells; functional significance and correlation with biophysical state of plasma membrane. Exploring molecular mechanisms of ligand recognition by opioid receptors with metadynamics Structural Determinants for the Binding of Morphinan Agonists to the μ-Opioid Receptor μ Opioid receptor: novel antagonists and structural modeling Structural basis for μ-opioid receptor binding and activation Molecular modeling study of the differential ligand-receptor interaction at the mu, delta and kappa opioid receptors Opiate receptor knockout mice define mu receptor roles in endogenous nociceptive responses and morphine-induced analgesia Mutation of a conserved serine in TM4 of opioid receptors confers full agonistic properties to classical antagonists Homology modeling of opioid receptor-ligand complexes using experimental constraints Structural organization of G-protein-coupled receptors Mu opioids and their receptors: evolution of a concept Ultrastructural evidence for prominent distribution of the mu-opioid receptor at extrasynaptic sites on noradrenergic dendrites in the rat nucleus locus coeruleus. mu Opiate receptor immunoreactivity in rat central nervous system. Opioid tolerance development: a pharmacokinetic/pharmacodynamic perspective Salvinorin A analogs as probes in opioid pharmacology Application of the message-address concept to the docking of naltrexone and selective naltrexone-derived opioid antagonists into opioid receptor models Opioid receptor three-dimensional structures from distance geometry calculations with hydrogen bonding constraints Molecular recognition of opioid receptor ligands Studies on mu and delta opioid receptor selectivity utilizing chimeric and site-mutagenized receptors Allosteric modulation model of the mu opioid receptor by herkinorin, a potent not alkaloidal agonist Structure modeling of the chemokine receptor CCR5: implications for ligand binding and selectivity Ultrastructural immunocytochemical localization of mu-opioid receptors in rat nucleus accumbens: extrasynaptic plasmalemmal distribution and association with Leu5-enkephalin Ultrastructural evidence for co-localization of corticotropin-releasing factor receptor and mu-opioid receptor in the rat nucleus locus coeruleus Morphine-induced trafficking of a mu-opioid receptor interacting protein in rat locus coeruleus neurons Computational study of the heterodimerization between mu and delta receptors. Mu opioid receptor knockdown in the substantia nigra/ventral tegmental area by synthetic small interfering RNA blocks the rewarding and locomotor effects of heroin Increased response to morphine in mice lacking protein kinase C epsilon Conformationally constrained opioid ligands: the Dmt-Aba and Dmt-Aia versus Dmt-Tic scaffold Inactivation of the purified bovine mu opioid receptor by sulfhydryl reagents Synthetic Studies of Neoclerodane Diterpenes from Salvia divinorum: Identification of a Potent and Centrally Acting μ Opioid Analgesic with Reduced Abuse Liability. Computational design of environmental sensors for the potent opioid fentanyl. Fentanyl Family at the Mu-Opioid Receptor: Uniform Assessment of Binding and Computational Analysis Physiology, signaling, and pharmacology of opioid receptors and their ligands in the gastrointestinal tract: current concepts and future perspectives How mu-Opioid Receptor Recognizes Fentanyl

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