Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. - Wikidata - wikimedia - TriplyDB

Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation.

Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation.

http://www.wikidata.org/entity/Q34142522

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GPCR oligomers in pharmacology and signaling Adenosine A(2A) receptors assemble into higher-order oligomers at the plasma membrane Dopamine D2 receptors form higher order oligomers at physiological expression levels Emerging roles for the FSH receptor adapter protein APPL1 and overlap of a putative 14-3-3τ interaction domain with a canonical G-protein interaction site Identification of three residues essential for 5-hydroxytryptamine 2A-metabotropic glutamate 2 (5-HT2A·mGlu2) receptor heteromerization and its psychoactive behavioral function The impact of GPCR structures on pharmacology and structure-based drug design Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes Computational approaches for modeling GPCR dimerization Opioid receptors: toward separation of analgesic from undesirable effects Crystal structure of oligomeric β1-adrenergic G protein–coupled receptors in ligand-free basal state Membrane-Mediated Oligomerization of G Protein Coupled Receptors and Its Implications for GPCR Function mu opioid and CB1 cannabinoid receptor interactions: reciprocal inhibition of receptor signaling and neuritogenesis Functional characterization of G-protein-coupled receptors: a bioinformatics approach.Divergent positive selection in rhodopsin from lake and riverine cichlid fishes.Activation of G protein-coupled receptors: beyond two-state models and tertiary conformational changes.G protein-coupled receptor heterocomplexes in neuropsychiatric disorders.Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at Work Transmembrane domains of attraction on the TSH receptor.Transmembrane domain IV of the Gallus gallus VT2 vasotocin receptor is essential for forming a heterodimer with the corticotrophin releasing hormone receptor Complex patterns of divergence among green-sensitive (RH2a) African cichlid opsins revealed by Clade model analyses Membrane driven spatial organization of GPCRs.Structure-function of the G protein-coupled receptor superfamily.Requirements and ontology for a G protein-coupled receptor oligomerization knowledge base.Rhodopsin and the others: a historical perspective on structural studies of G protein-coupled receptors.Modeling activated states of GPCRs: the rhodopsin template.Not just an oil slick: how the energetics of protein-membrane interactions impacts the function and organization of transmembrane proteins.Increasingly accurate dynamic molecular models of G-protein coupled receptor oligomers: Panacea or Pandora's box for novel drug discovery?Dynamic models of G-protein coupled receptor dimers: indications of asymmetry in the rhodopsin dimer from molecular dynamics simulations in a POPC bilayer.Importance of lipid-exposed residues in transmembrane segment four for family B calcitonin receptor homo-dimerization.Interactions between intracellular domains as key determinants of the quaternary structure and function of receptor heteromers.Making structural sense of dimerization interfaces of delta opioid receptor homodimers.Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling.Ligand-dependent conformations and dynamics of the serotonin 5-HT(2A) receptor determine its activation and membrane-driven oligomerization properties Fluorescent protein complementation assays: new tools to study G protein-coupled receptor oligomerization and GPCR-mediated signaling.Mechanism of activation of protein kinase JAK2 by the growth hormone receptor.Glucagon-like peptide-1 receptor dimerization differentially regulates agonist signaling but does not affect small molecule allostery.Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.Rhodopsin self-associates in asolectin liposomes.Dynamic Regulation of Quaternary Organization of the M1 Muscarinic Receptor by Subtype-selective Antagonist Drugs.G-protein coupled receptor 83 (GPR83) signaling determined by constitutive and zinc(II)-induced activity.

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Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation.

http://www.wikidata.org/entity/Q34142522

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2005 nî lūn-bûn

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2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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Crosstalk in G protein-coupled ...... nterface determine activation.

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Crosstalk in G protein-coupled ...... nterface determine activation.

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Crosstalk in G protein-coupled ...... nterface determine activation.

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Crosstalk in G protein-coupled ...... nterface determine activation.

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Crosstalk in G protein-coupled ...... nterface determine activation.

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Proceedings of the National Academy of Sciences of the United States of America

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Crosstalk in G protein-coupled ...... nterface determine activation.

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Harel Weinstein

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Jonathan A Javitch

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Lei Shi

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Marta Filizola

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Wen Guo

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P2860

G-protein-coupled receptor heterodimerization modulates receptor function

Heteromeric association creates a P2Y-like adenosine receptor

Crystal structure of rhodopsin: A G protein-coupled receptor

Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor

Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+.

VMD: visual molecular dynamics

Heterodimerization of mu and delta opioid receptors: A role in opiate synergy

Allosteric interactions between GB1 and GB2 subunits are required for optimal GABA(B) receptor function

A single subunit (GB2) is required for G-protein activation by the heterodimeric GABA(B) receptor

The fourth transmembrane segment of the dopamine D2 receptor: accessibility in the binding-site crevice and position in the transmembrane bundle

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G protein-coupled receptor

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