Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing.
about
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 siteRole of the Extracellular and Intracellular Loops of Follicle-Stimulating Hormone Receptor in Its FunctionEvidence for Follicle-stimulating Hormone Receptor as a Functional TrimerTransitioning pharmacoperones to therapeutic use: in vivo proof-of-principle and design of high throughput screens.Rescue of defective G protein-coupled receptor function in vivo by intermolecular cooperation.Dominant negative effects of human follicle-stimulating hormone receptor expression-deficient mutants on wild-type receptor cell surface expression. Rescue of oligomerization-dependent defective receptor expression by using cognate decoys.The adapter protein APPL1 links FSH receptor to inositol 1,4,5-trisphosphate production and is implicated in intracellular Ca(2+) mobilizationDecreased degradation of internalized follicle-stimulating hormone caused by mutation of aspartic acid 6.30(550) in a protein kinase-CK2 consensus sequence in the third intracellular loop of human follicle-stimulating hormone receptor.Production, purification, and characterization of recombinant hFSH glycoforms for functional studies.Naturally Occurring Follicle-Stimulating Hormone Glycosylation Variants.Pharmacological chaperones for misfolded gonadotropin-releasing hormone receptorsTrafficking of the follitropin receptor.Revisiting and questioning functional rescue between dimerized LH receptor mutants.Mapping the follicle-stimulating hormone-induced signaling networks.Single-molecule analyses of fully functional fluorescent protein-tagged follitropin receptor reveal homodimerization and specific heterodimerization with lutropin receptor.Misfolding Ectodomain Mutations of the Lutropin Receptor Increase Efficacy of Hormone StimulationBioluminescence resonance energy transfer studies reveal constitutive dimerization of the human lutropin receptor and a lack of correlation between receptor activation and the propensity for dimerization.Mutations in G protein-coupled receptors that impact receptor trafficking and reproductive function.Structural determinants underlying constitutive dimerization of unoccupied human follitropin receptors.Are circulating gonadotropin isoforms naturally occurring biased agonists? Basic and therapeutic implications.The Follitropin Receptor: Matching Structure and Function.Development of Selective LH Receptor Agonists by Heterodimerization with a FSH Receptor Antagonist.Cells with stem cell characteristics in somatic compartments of the ovaryIntracellular Trafficking of Gonadotropin Receptors in Health and Disease.Evaluation of the oligosaccharide composition of commercial follicle stimulating hormone preparations.Synthesis and pharmacological evaluation of dimeric follicle-stimulating hormone receptor antagonists.
P2860
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P2860
Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing.
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Follice-stimulating hormone re ...... rminal proteolytic processing.
@ast
Follice-stimulating hormone re ...... rminal proteolytic processing.
@en
type
label
Follice-stimulating hormone re ...... rminal proteolytic processing.
@ast
Follice-stimulating hormone re ...... rminal proteolytic processing.
@en
prefLabel
Follice-stimulating hormone re ...... rminal proteolytic processing.
@ast
Follice-stimulating hormone re ...... rminal proteolytic processing.
@en
P2093
P2860
P356
P1433
P1476
Follice-stimulating hormone re ...... rminal proteolytic processing.
@en
P2093
Cheryl A Nechamen
James A Dias
Joseph E Mazurkiewicz
Marco Muda
Richard M Thomas
Stephen Palmer
P2860
P304
P356
10.1210/EN.2006-1672
P407
P577
2007-02-01T00:00:00Z