Mutational analysis of the human vasoactive intestinal peptide receptor subtype VPAC(2): role of basic residues in the second transmembrane helix
about
A Hydrogen-Bonded Polar Network in the Core of the Glucagon-Like Peptide-1 Receptor Is a Fulcrum for Biased Agonism: Lessons from Class B Crystal StructuresMapping spatial approximations between the amino terminus of secretin and each of the extracellular loops of its receptor using cysteine trapping.Use of Cysteine Trapping to Map Spatial Approximations between Residues Contributing to the Helix N-capping Motif of Secretin and Distinct Residues within Each of the Extracellular Loops of Its Receptor.Structural and functional insights into the juxtamembranous amino-terminal tail and extracellular loop regions of class B GPCRs.The peptide agonist-binding site of the glucagon-like peptide-1 (GLP-1) receptor based on site-directed mutagenesis and knowledge-based modelling.Mechanisms involved in VPAC receptors activation and regulation: lessons from pharmacological and mutagenesis studiesHigh affinity binding of the peptide agonist TIP-39 to the parathyroid hormone 2 (PTH2) receptor requires the hydroxyl group of Tyr-318 on transmembrane helix 5.Residues within the transmembrane domain of the glucagon-like peptide-1 receptor involved in ligand binding and receptor activation: modelling the ligand-bound receptor.Mutational analysis of the glucagon receptor: similarities with the vasoactive intestinal peptide (VIP)/pituitary adenylate cyclase-activating peptide (PACAP)/secretin receptors for recognition of the ligand's third residue.
P2860
Q27345100-BF58132B-0695-46A2-860C-E8E4B05EDD69Q36430829-C8CEE05A-C9D5-4234-B72C-78A87E208415Q36650346-AAD48DD4-1ADB-49CC-9924-FBE6825DE296Q37635253-91B40170-D384-4CC9-945E-FB3DA1CC898AQ40284076-FB4A2BEC-251E-4070-9DFF-E26B1048FF7CQ41645695-49411837-6815-41ED-9D21-C5077DD5FB54Q41830097-4E607417-9572-436F-85F5-BCE03FE5DE15Q42289659-2A3320A9-34BB-4EE6-915B-34616F61E847Q42918169-849F88F1-5255-47BB-8754-8BEBD0B91B04
P2860
Mutational analysis of the human vasoactive intestinal peptide receptor subtype VPAC(2): role of basic residues in the second transmembrane helix
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
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
Mutational analysis of the hum ...... the second transmembrane helix
@ast
Mutational analysis of the hum ...... the second transmembrane helix
@en
Mutational analysis of the hum ...... the second transmembrane helix
@nl
type
label
Mutational analysis of the hum ...... the second transmembrane helix
@ast
Mutational analysis of the hum ...... the second transmembrane helix
@en
Mutational analysis of the hum ...... the second transmembrane helix
@nl
prefLabel
Mutational analysis of the hum ...... the second transmembrane helix
@ast
Mutational analysis of the hum ...... the second transmembrane helix
@en
Mutational analysis of the hum ...... the second transmembrane helix
@nl
P2093
P2860
P356
P1476
Mutational analysis of the hum ...... the second transmembrane helix
@en
P2093
M Waelbroeck
P Robberecht
P Vertongen
R M Solano
P2860
P304
P356
10.1038/SJ.BJP.0704195
P407
P577
2001-08-01T00:00:00Z