|
Volumn 136, Issue 7, 2002, Pages 1042-1048
|
Two tyrosine residues in the first transmembrane helix of the human vasoactive intestinal peptide receptors play a role in supporting the active conformation
a a a a a a a |
Author keywords
Receptor point mutations; VIP
|
Indexed keywords
ADENYLATE CYCLASE;
TYROSINE;
VASOACTIVE INTESTINAL POLYPEPTIDE;
VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR;
VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1;
VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 2;
ASPARAGINE;
G PROTEIN COUPLED RECEPTOR;
HISTIDINE;
NEUROPEPTIDE;
PHENYLALANINE;
ANIMAL;
ARTICLE;
CHEMISTRY;
CHO CELL;
HAMSTER;
HUMAN;
METABOLISM;
MUTATION;
PROTEIN CONFORMATION;
ALPHA HELIX;
ANIMAL CELL;
BINDING SITE;
DRUG EFFECT;
ENZYME ACTIVITY;
NONHUMAN;
PEPTIDE SYNTHESIS;
POINT MUTATION;
PRIORITY JOURNAL;
PROTEIN FAMILY;
RECEPTOR AFFINITY;
RESIDUE ANALYSIS;
SIGNAL TRANSDUCTION;
ADENYLATE CYCLASE;
ANIMALS;
CHO CELLS;
CRICETINAE;
HUMANS;
MUTATION;
PROTEIN CONFORMATION;
RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE;
RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE, TYPE II;
RECEPTORS, VASOACTIVE INTESTINAL POLYPEPTIDE, TYPE I;
TYROSINE;
VASOACTIVE INTESTINAL PEPTIDE;
ANIMAL;
HAMSTERS;
HUMAN;
SUPPORT, NON-U.S. GOV'T;
|
EID: 0036024240
PISSN: 00071188
EISSN: None
Source Type: Journal
DOI: 10.1038/sj.bjp.0704802 Document Type: Article |
Times cited : (7)
|
References (18)
|