The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1.
about
Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RSMechanisms of action of glucagon-like peptide 1 in the pancreasCrystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domainCrystal Structure of Glucagon-like Peptide-1 in Complex with the Extracellular Domain of the Glucagon-like Peptide-1 ReceptorNMR Structure of the First Extracellular Domain of Corticotropin-releasing Factor Receptor 1 (ECD1-CRF-R1) Complexed with a High Affinity AgonistGlucagon-Like Peptide-1 and Its Class B G Protein-Coupled Receptors: A Long March to Therapeutic SuccessesGlucagon-like peptide-1 receptor ligand interactions: structural cross talk between ligands and the extracellular domainNovel small molecule glucagon-like peptide-1 receptor agonist stimulates insulin secretion in rodents and from human islets.The non-peptide GLP-1 receptor agonist WB4-24 blocks inflammatory nociception by stimulating β-endorphin release from spinal microglia.Site-specific PEGylation of exenatide analogues markedly improved their glucoregulatory activityGlucagon-like peptide-1 (GLP-1) analogs: recent advances, new possibilities, and therapeutic implications.Ligand binding pocket formed by evolutionarily conserved residues in the glucagon-like peptide-1 (GLP-1) receptor core domain.Evolutionarily conserved residues at glucagon-like peptide-1 (GLP-1) receptor core confer ligand-induced receptor activationAn Orally Active Allosteric GLP-1 Receptor Agonist Is Neuroprotective in Cellular and Rodent Models of Stroke.Class II G protein-coupled receptors and their ligands in neuronal function and protectionStructural and molecular conservation of glucagon-like Peptide-1 and its receptor confers selective ligand-receptor interaction.Suppression of food intake by glucagon-like peptide-1 receptor agonists: relative potencies and role of dipeptidyl peptidase-4Effects of Exendine-4 on The Differentiation of Insulin Producing Cells from Rat Adipose-Derived Mesenchymal Stem Cells.Insights into the structural basis of endogenous agonist activation of family B G protein-coupled receptorsStructural genomics and drug discovery.Implications of DPP4 modification of proteins that regulate stem/progenitor and more mature cell types.Allosteric modulators of class B G-protein-coupled receptorsDual role of the second extracellular loop of the cannabinoid receptor 1: ligand binding and receptor localization.Differences in the central anorectic effects of glucagon-like peptide-1 and exendin-4 in rats.The structure and function of the glucagon-like peptide-1 receptor and its ligandsPhysiology and emerging biochemistry of the glucagon-like peptide-1 receptor.Molecular Pharmacology of the Incretin Receptors.The major determinant of exendin-4/glucagon-like peptide 1 differential affinity at the rat glucagon-like peptide 1 receptor N-terminal domain is a hydrogen bond from SER-32 of exendin-4.A model for receptor-peptide binding at the glucagon-like peptide-1 (GLP-1) receptor through the analysis of truncated ligands and receptors.The effects of exendine-4 on insulin producing cell differentiation from rat bone marrow-derived mesenchymal stem cells.A hydrophobic site on the GLP-1 receptor extracellular domain orients the peptide ligand for signal transductionResidues within the transmembrane domain of the glucagon-like peptide-1 receptor involved in ligand binding and receptor activation: modelling the ligand-bound receptor.The positive charge at Lys-288 of the glucagon-like peptide-1 (GLP-1) receptor is important for binding the N-terminus of peptide agonists.Distinct structural and functional roles of conserved residues in the first extracellular domain of receptors for corticotropin-releasing factor and related G-protein-coupled receptors.PDGF Facilitates Direct Lineage Reprogramming of Hepatocytes to Functional β-Like Cells Induced by Pdx1 and Ngn3.
P2860
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P2860
The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
The isolated N-terminal domain ...... ch higher affinity than GLP-1.
@en
type
label
The isolated N-terminal domain ...... ch higher affinity than GLP-1.
@en
prefLabel
The isolated N-terminal domain ...... ch higher affinity than GLP-1.
@en
P2093
P2860
P356
P1476
The isolated N-terminal domain ...... ch higher affinity than GLP-1.
@en
P2093
Angela Willshaw
Antje Kuntzsch
Dan Donnelly
Rainer Rudolph
Rakel López de Maturana
P2860
P304
10195-10200
P356
10.1074/JBC.M212147200
P407
P577
2003-01-10T00:00:00Z