Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
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Structure and mechanism for recognition of peptide hormones by Class B G-protein-coupled receptorsCrystal structure of the incretin-bound extracellular domain of a G protein-coupled receptorCrystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domainMolecular recognition of parathyroid hormone by its G protein-coupled receptorNMR Structure of the First Extracellular Domain of Corticotropin-releasing Factor Receptor 1 (ECD1-CRF-R1) Complexed with a High Affinity AgonistReceptors for PTH and PTHrP: their biological importance and functional propertiesN-terminal splice variants of the type I PACAP receptor: isolation, characterization and ligand binding/selectivity determinantsThe human secretin receptor gene: genomic organization and promoter characterizationIdentification of key residues for interaction of vasoactive intestinal peptide with human VPAC1 and VPAC2 receptors and development of a highly selective VPAC1 receptor agonist. Alanine scanning and molecular modeling of the peptideVPAC receptors for VIP and PACAPMolecular pharmacology of the secretin receptorA segment of five amino acids in the second extracellular loop of the cholecystokinin-B receptor is essential for selectivity of the peptide agonist gastrinAntibodies against specific extracellular epitopes of the glucagon receptor block glucagon bindingMolecular basis of glucagon-like peptide 1 docking to its intact receptor studied with carboxyl-terminal photolabile probesSecretin occupies a single protomer of the homodimeric secretin receptor complex: insights from photoaffinity labeling studies using dual sites of covalent attachment.Spatial approximations between residues 6 and 12 in the amino-terminal region of glucagon-like peptide 1 and its receptor: a region critical for biological activity.Human VPAC1 receptor selectivity filter. Identification of a critical domain for restricting secretin binding.Cloning and characterization of the signal transduction of four splice variants of the human pituitary adenylate cyclase activating polypeptide receptor. Evidence for dual coupling to adenylate cyclase and phospholipase C.Alternative splicing in the N-terminal extracellular domain of the pituitary adenylate cyclase-activating polypeptide (PACAP) receptor modulates receptor selectivity and relative potencies of PACAP-27 and PACAP-38 in phospholipase C activation.Combined administration of secretin and oxytocin inhibits chronic colitis and associated activation of forebrain neurons.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.Lactam constraints provide insights into the receptor-bound conformation of secretin and stabilize a receptor antagonist.Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activationEvolutionarily conserved residues at glucagon-like peptide-1 (GLP-1) receptor core confer ligand-induced receptor activationLigand 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?Consequences of splice variation on Secretin family G protein-coupled receptor functionStructural and molecular conservation of glucagon-like Peptide-1 and its receptor confers selective ligand-receptor interaction.Insights into the structural basis of endogenous agonist activation of family B G protein-coupled receptorsEvidence for cooperative signal triggering at the extracellular loops of the TSH receptorSecretin receptor oligomers form intracellularly during maturation through receptor core domains.Deletions of the N-terminal regions of the human melanocortin receptors.Molecular basis for agonist selectivity and activation of the orphan bombesin receptor subtype 3 receptor.Allosteric modulators of class B G-protein-coupled receptorsJuxtamembranous region of the amino terminus of the family B G protein-coupled calcitonin receptor plays a critical role in small-molecule agonist action.Molecular basis for the selectivity of the mammalian bombesin peptide, neuromedin B, for its receptorDual role of the second extracellular loop of the cannabinoid receptor 1: ligand binding and receptor localization.Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding.Extragastrointestinal functions and transcriptional regulation of secretin and secretin receptors.
P2860
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P2860
Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Critical contributions of amin ...... Studies of chimeric receptors
@ast
Critical contributions of amin ...... Studies of chimeric receptors
@en
Critical contributions of amin ...... Studies of chimeric receptors
@nl
type
label
Critical contributions of amin ...... Studies of chimeric receptors
@ast
Critical contributions of amin ...... Studies of chimeric receptors
@en
Critical contributions of amin ...... Studies of chimeric receptors
@nl
prefLabel
Critical contributions of amin ...... Studies of chimeric receptors
@ast
Critical contributions of amin ...... Studies of chimeric receptors
@en
Critical contributions of amin ...... Studies of chimeric receptors
@nl
P2093
P2860
P356
P1476
Critical contributions of amin ...... Studies of chimeric receptors
@en
P2093
L J Miller
M H Holtmann
P2860
P304
P356
10.1074/JBC.270.24.14394
P407
P577
1995-06-16T00:00:00Z