Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes.
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Structure of an agonist-bound human A2A adenosine receptorThe structural basis for agonist and partial agonist action on a β(1)-adrenergic receptorStructure of the human histamine H1 receptor complex with doxepinDiversity and modularity of G protein-coupled receptor structuresConserved Binding Mode of Human β 2 Adrenergic Receptor Inverse Agonists and Antagonist Revealed by X-ray CrystallographyStructure of the nociceptin/orphanin FQ receptor in complex with a peptide mimeticUnderstanding functional residues of the cannabinoid CB1.Function-specific virtual screening for GPCR ligands using a combined scoring methodPredicting novel binding modes of agonists to β adrenergic receptors using all-atom molecular dynamics simulationsModeling of human prokineticin receptors: interactions with novel small-molecule binders and potential off-target drugsThe role of experimental and computational structural approaches in 7TM drug discovery.Compound activity prediction using models of binding pockets or ligand properties in 3D.Structure-based discovery of novel chemotypes for adenosine A(2A) receptor antagonists.GPCR 3D homology models for ligand screening: lessons learned from blind predictions of adenosine A2a receptor complex.Structure-function of the G protein-coupled receptor superfamily.Structure-based discovery of A2A adenosine receptor ligands.Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-10 microm size X-ray synchrotron beam.Seven transmembrane receptors as shapeshifting proteins: the impact of allosteric modulation and functional selectivity on new drug discovery.Do crystal structures obviate the need for theoretical models of GPCRs for structure-based virtual screening?Ligand-induced modulation of the free-energy landscape of G protein-coupled receptors explored by adaptive biasing techniquesThe flexible pocketome engine for structural chemogenomics.ALiBERO: evolving a team of complementary pocket conformations rather than a single leader.Gastrin-releasing peptide/neuromedin B receptor antagonists PD176252, PD168368, and related analogs are potent agonists of human formyl-peptide receptors.Conformation guides molecular efficacy in docking screens of activated β-2 adrenergic G protein coupled receptorDevelopment of 7TM receptor-ligand complex models using ligand-biased, semi-empirical helix-bundle repacking in torsion space: application to the agonist interaction of the human dopamine D2 receptor.Structure-based ligand discovery targeting orthosteric and allosteric pockets of dopamine receptors.Effect of intracellular loop 3 on intrinsic dynamics of human β2-adrenergic receptor.In silico analysis of the binding of agonists and blockers to the β2-adrenergic receptor.Pocketome: an encyclopedia of small-molecule binding sites in 4DEvaluation of molecular modeling of agonist binding in light of the crystallographic structure of an agonist-bound A₂A adenosine receptor.Molecular mechanism of serotonin transporter inhibition elucidated by a new flexible docking protocol.Involvement of α2- and β2-adrenoceptors on breast cancer cell proliferation and tumour growth regulationStructural basis for selectivity and diversity in angiotensin II receptorsThe GPCR Network: a large-scale collaboration to determine human GPCR structure and function.Molecular interactions between fenoterol stereoisomers and derivatives and the β₂-adrenergic receptor binding site studied by docking and molecular dynamics simulations.Chemotype-selective modes of action of κ-opioid receptor agonists.Challenges and advances in computational docking: 2009 in review.The importance of interactions with helix 5 in determining the efficacy of β-adrenoceptor ligands.X-ray structural information of GPCRs in drug design: what are the limitations and where do we go?Ligand-dependent perturbation of the conformational ensemble for the GPCR β2 adrenergic receptor revealed by HDX.
P2860
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P2860
Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Analysis of full and partial a ...... ecific conformational changes.
@ast
Analysis of full and partial a ...... ecific conformational changes.
@en
type
label
Analysis of full and partial a ...... ecific conformational changes.
@ast
Analysis of full and partial a ...... ecific conformational changes.
@en
prefLabel
Analysis of full and partial a ...... ecific conformational changes.
@ast
Analysis of full and partial a ...... ecific conformational changes.
@en
P2093
P2860
P356
P1476
Analysis of full and partial a ...... ecific conformational changes.
@en
P2093
Christopher B Roth
Kimberly A Reynolds
Mark Yeager
Michael A Hanson
Vadim Cherezov
P2860
P304
P356
10.1002/JMR.949
P577
2009-07-01T00:00:00Z