A tyrosine residue on the TSH receptor stabilizes multimer formation

A tyrosine residue on the TSH receptor stabilizes multimer formation

Item
http://www.wikidata.org/entity/Q30436858
Structural-Functional Features of the Thyrotropin Receptor: A Class A G-Protein-Coupled Receptor at WorkTransmembrane domains of attraction on the TSH receptor.Dominant negative effect of mutated thyroid stimulating hormone receptor (P556L) causes hypothyroidism in C.RF-Tshr(hyt/wild) mice.Evidence that the thyroid-stimulating hormone (TSH) receptor transmembrane domain influences kinetics of TSH binding to the receptor ectodomain.Crystal structure of a TSH receptor monoclonal antibody: insight into Graves' disease pathogenesis.Novel insights on thyroid-stimulating hormone receptor signal transduction.Development of Selective LH Receptor Agonists by Heterodimerization with a FSH Receptor Antagonist.Immunohistochemical mapping and transcript expression of the GPA2/GPB5 receptor in tissues of the adult mosquito, Aedes aegypti.
P2860

A tyrosine residue on the TSH receptor stabilizes multimer formation

Item
http://www.wikidata.org/entity/Q30436858
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
A tyrosine residue on the TSH receptor stabilizes multimer formation
@ast
A tyrosine residue on the TSH receptor stabilizes multimer formation
@en
type
label
A tyrosine residue on the TSH receptor stabilizes multimer formation
@ast
A tyrosine residue on the TSH receptor stabilizes multimer formation
@en
prefLabel
A tyrosine residue on the TSH receptor stabilizes multimer formation
@ast
A tyrosine residue on the TSH receptor stabilizes multimer formation
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
A tyrosine residue on the TSH receptor stabilizes multimer formation
@en
P2093
P2860
P304
P31
P356
10.1371/JOURNAL.PONE.0009449
P407
P433
P478
P577
P5875
P698
P932