Secretin occupies a single protomer of the homodimeric secretin receptor complex: insights from photoaffinity labeling studies using dual sites of covalent attachment.
about
Refinement of the pharmacophore of an agonist ligand of the secretin receptor using conformationally constrained cyclic hexapeptides.Importance of each residue within secretin for receptor binding and biological activityRefinement of glucagon-like peptide 1 docking to its intact receptor using mid-region photolabile probes and molecular modeling.Molecular basis of secretin docking to its intact receptor using multiple photolabile probes distributed throughout the pharmacophoreLactam constraints provide insights into the receptor-bound conformation of secretin and stabilize a receptor antagonist.Site of action of a pentapeptide agonist at the glucagon-like peptide-1 receptor. Insight into a small molecule agonist-binding pocket.Ligand binding and activation of the secretin receptor, a prototypic family B G protein-coupled receptor.Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?Insights into the impact of phenolic residue incorporation at each position along secretin for receptor binding and biological activityStructural and functional insights into the juxtamembranous amino-terminal tail and extracellular loop regions of class B GPCRs.Lifting the lid on GPCRs: the role of extracellular loops.The role of the extracellular loops of the CGRP receptor, a family B GPCR.The activation of the CGRP receptor.Latest developments in molecular docking: 2010-2011 in review.Extracellular loops 1 and 3 and their associated transmembrane regions of the calcitonin receptor-like receptor are needed for CGRP receptor function.Analysis of Human Dopamine D3 Receptor Quaternary Structure.Spatial intensity distribution analysis quantifies the extent and regulation of homodimerization of the secretin receptor.Similarity between class A and class B G-protein-coupled receptors exemplified through calcitonin gene-related peptide receptor modelling and mutagenesis studies.
P2860
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P2860
Secretin occupies a single protomer of the homodimeric secretin receptor complex: insights from photoaffinity labeling studies using dual sites of covalent attachment.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին 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
Secretin occupies a single pro ...... sites of covalent attachment.
@ast
Secretin occupies a single pro ...... sites of covalent attachment.
@en
type
label
Secretin occupies a single pro ...... sites of covalent attachment.
@ast
Secretin occupies a single pro ...... sites of covalent attachment.
@en
prefLabel
Secretin occupies a single pro ...... sites of covalent attachment.
@ast
Secretin occupies a single pro ...... sites of covalent attachment.
@en
P2093
P2860
P356
P1476
Secretin occupies a single pro ...... sites of covalent attachment.
@en
P2093
Andrew Orry
Delia I Pinon
Laurence J Miller
Maoqing Dong
Patrick M Sexton
Polo C-H Lam
P2860
P304
P356
10.1074/JBC.M109.089730
P407
P577
2010-01-25T00:00:00Z