Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing. - Wikidata - wikimedia - TriplyDB

Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing.

Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing.

http://www.wikidata.org/entity/Q35040371

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 site Role of the Extracellular and Intracellular Loops of Follicle-Stimulating Hormone Receptor in Its Function Evidence for Follicle-stimulating Hormone Receptor as a Functional Trimer Transitioning 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+) mobilization Decreased 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 receptors Trafficking 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 Stimulation Bioluminescence 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 ovary Intracellular 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.

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P2860

Follice-stimulating hormone receptor forms oligomers and shows evidence of carboxyl-terminal proteolytic processing.

http://www.wikidata.org/entity/Q35040371

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

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2007年論文

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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.

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Follice-stimulating hormone re ...... rminal proteolytic processing.

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type

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Follice-stimulating hormone re ...... rminal proteolytic processing.

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Follice-stimulating hormone re ...... rminal proteolytic processing.

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Follice-stimulating hormone re ...... rminal proteolytic processing.

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Follice-stimulating hormone re ...... rminal proteolytic processing.

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Follice-stimulating hormone re ...... rminal proteolytic processing.

@en

P2093

Cheryl A Nechamen

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

James A Dias

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

Joseph E Mazurkiewicz

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

Marco Muda

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Richard M Thomas

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Stephen Palmer

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P2860

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

Structure of human follicle-stimulating hormone in complex with its receptor

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors.

Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not re

Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer

Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer

Dimerization and phosphorylation of thyrotropin-releasing hormone receptors are modulated by agonist stimulation

Postendocytotic trafficking of the follicle-stimulating hormone (FSH)-FSH receptor complex

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1987-1995

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scholarly article

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10.1210/EN.2006-1672

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5

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148

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2007-02-01T00:00:00Z

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6533084

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17272391

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