Hydrophilic side chains in the third and seventh transmembrane helical domains of human A2A adenosine receptors are required for ligand recognition
about
Structure of an agonist-bound human A2A adenosine receptorA new drug design targeting the adenosinergic system for Huntington's diseaseStructure of the Adenosine A2A Receptor in Complex with ZM241385 and the Xanthines XAC and CaffeineNeoceptor concept based on molecular complementarity in GPCRs: a mutant adenosine A(3) receptor with selectively enhanced affinity for amine-modified nucleosidesChemogenomic analysis of G-protein coupled receptors and their ligands deciphers locks and keys governing diverse aspects of signallingStructural and energetic effects of A2A adenosine receptor mutations on agonist and antagonist bindingEvaluation of homology modeling of G-protein-coupled receptors in light of the A(2A) adenosine receptor crystallographic structure.Ligand-dependent activation and deactivation of the human adenosine A(2A) receptor.Identification by site-directed mutagenesis of residues involved in ligand recognition and activation of the human A3 adenosine receptor.Thermostabilisation of an agonist-bound conformation of the human adenosine A(2A) receptor.Arginine 199 and leucine 208 have key roles in the control of adenosine A2A receptor signalling function.Molecular Architecture of G Protein-Coupled Receptors.A mutational analysis of residues essential for ligand recognition at the human P2Y1 receptor.Mutagenesis reveals structure-activity parallels between human A2A adenosine receptors and biogenic amine G protein-coupled receptors.Co-evolving stability and conformational homogeneity of the human adenosine A2a receptor.Ligand binding and subtype selectivity of the human A(2A) adenosine receptor: identification and characterization of essential amino acid residues.Loss of constitutive activity is correlated with increased thermostability of the human adenosine A2A receptor.GPCR Conformations: Implications for Rational Drug Design.
P2860
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P2860
Hydrophilic side chains in the third and seventh transmembrane helical domains of human A2A adenosine receptors are required for ligand recognition
description
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1996
@ast
im September 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1996/09/01)
@sk
vědecký článek publikovaný v roce 1996
@cs
wetenschappelijk artikel (gepubliceerd op 1996/09/01)
@nl
наукова стаття, опублікована у вересні 1996
@uk
научни чланак (објављен 1996/09/01)
@sr
name
Hydrophilic side chains in the ...... equired for ligand recognition
@ast
Hydrophilic side chains in the ...... equired for ligand recognition
@en
Hydrophilic side chains in the ...... equired for ligand recognition
@nl
type
label
Hydrophilic side chains in the ...... equired for ligand recognition
@ast
Hydrophilic side chains in the ...... equired for ligand recognition
@en
Hydrophilic side chains in the ...... equired for ligand recognition
@nl
prefLabel
Hydrophilic side chains in the ...... equired for ligand recognition
@ast
Hydrophilic side chains in the ...... equired for ligand recognition
@en
Hydrophilic side chains in the ...... equired for ligand recognition
@nl
P2093
P2860
P1476
Hydrophilic side chains in the ...... equired for ligand recognition
@en
P2093
P2860
P304
P407
P577
1996-09-01T00:00:00Z