Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors. - Wikidata - wikimedia - TriplyDB

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

http://www.wikidata.org/entity/Q33952116

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GPCR oligomers in pharmacology and signaling Coordinated action of NSF and PKC regulates GABAB receptor signaling efficacy Different functional roles of T1R subunits in the heteromeric taste receptors Taste and pheromone perception in mammals and flies GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper Structure and functional interaction of the extracellular domain of human GABAB receptor GBR2 Structural mechanism of ligand activation in human GABAB receptor Oligomerization of the yeast alpha-factor receptor: implications for dominant negative effects of mutant receptors.Trans-activation between 7TM domains: implication in heterodimeric GABAB receptor activation Structure and ligand recognition of class C GPCRs Chaperoning G protein-coupled receptors: from cell biology to therapeutics Ligand-induced signal transduction within heterodimeric GABA(B) receptor.The GABAB receptor associates with regulators of G-protein signaling 4 protein in the mouse prefrontal cortex and hypothalamus Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors.The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes.The heptahelical domain of GABA(B2) is activated directly by CGP7930, a positive allosteric modulator of the GABA(B) receptor GABAB receptor subunit GB1 at the cell surface independently activates ERK1/2 through IGF-1R transactivation.The G protein-coupled receptor rhodopsin in the native membrane Allosteric signaling through an mGlu2 and 5-HT2A heteromeric receptor complex and its potential contribution to schizophrenia Methods used to study the oligomeric structure of G-protein-coupled receptors.Revealing protein oligomerization and densities in situ using spatial intensity distribution analysis.Escorts take the lead molecular chaperones as therapeutic targets Gamma-aminobutyric acid type B (GABA(B)) receptor internalization is regulated by the R2 subunit.Matching accessories.Role of the calcium-sensing receptor in parathyroid gland physiology.Functional homomers and heteromers of dopamine D2L and D3 receptors co-exist at the cell surface GABAB receptor complex as a potential target for tumor therapy Sushi domains confer distinct trafficking profiles on GABAB receptors.Common structural requirements for heptahelical domain function in class A and class C G protein-coupled receptors.How and why do GPCRs dimerize?Enhancement of the surface expression of G protein-coupled receptors.Modulation of cell surface GABA(B) receptors by desensitization, trafficking and regulated degradation.Pathophysiology of GPCR Homo- and Heterodimerization: Special Emphasis on Somatostatin Receptors Determination of the minimal functional ligand-binding domain of the GABAB1b receptor.Post-endocytotic Deubiquitination and Degradation of the Metabotropic γ-Aminobutyric Acid Receptor by the Ubiquitin-specific Protease 14.Direct detection of the interaction between recombinant soluble extracellular regions in the heterodimeric metabotropic gamma-aminobutyric acid receptor.Complex formation with the Type B gamma-aminobutyric acid receptor affects the expression and signal transduction of the extracellular calcium-sensing receptor. Studies with HEK-293 cells and neurons.Opsin oligomerization in a heterologous cell system.Coupling of GABAB receptor GABAB2 subunit to G proteins: evidence from Xenopus oocyte and baby hamster kidney cell expression system.Molecular determinants involved in the allosteric control of agonist affinity in the GABAB receptor by the GABAB2 subunit.

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Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

http://www.wikidata.org/entity/Q33952116

description

2001 nî lūn-bûn

@nan

2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

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2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

@ast

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

@en

type

label

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

@ast

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

@en

prefLabel

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

@ast

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

@en

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

P1476

Function of GB1 and GB2 subunits in G protein coupling of GABA(B) receptors.

@en

P2093

Jan LY

http://www.w3.org/2001/XMLSchema#string

Jan YN

http://www.w3.org/2001/XMLSchema#string

Margeta-Mitrovic M

http://www.w3.org/2001/XMLSchema#string

P2860

Heterodimerization is required for the formation of a functional GABA(B) receptor

The GABAB receptor interacts directly with the related transcription factors CREB2 and ATFx

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

Association of GABA(B) receptors and members of the 14-3-3 family of signaling proteins

The C-terminal domains of the GABA(b) receptor subunits mediate intracellular trafficking but are not required for receptor signaling.

Characterization of gamma-aminobutyric acid receptor GABAB(1e), a GABAB(1) splice variant encoding a truncated receptor.

A trafficking checkpoint controls GABA(B) receptor heterodimerization.

Mutant G protein alpha subunit activated by Gbeta gamma: a model for receptor activation?

Ligand-induced signal transduction within heterodimeric GABA(B) receptor.

Oligomerization of G-protein-coupled transmitter receptors.

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14649-14654

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scholarly article

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10.1073/PNAS.251554498

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25

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98

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2001-11-27T00:00:00Z

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11630779

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11724956

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64736

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