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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 StructuresAn arginyl in the N-terminus of the V1a vasopressin receptor is part of the conformational switch controlling activation by agonistThe Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased AgonismA key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors.Understanding the molecular functions of the second extracellular loop (ECL2) of the calcitonin gene-related peptide (CGRP) receptor using a comprehensive mutagenesis approach.Receptor activity-modifying protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin receptors to Gs.Ligand binding and activation of the CGRP receptor.Allosteric ligands of the glucagon-like peptide 1 receptor (GLP-1R) differentially modulate endogenous and exogenous peptide responses in a pathway-selective manner: implications for drug screening.Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activationSecond extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) differentially regulates orthosteric but not allosteric agonist binding and function.Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.Polymorphism and ligand dependent changes in human glucagon-like peptide-1 receptor (GLP-1R) function: allosteric rescue of loss of function mutation.An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology.Modulating receptor function through RAMPs: can they represent drug targets in themselves?Receptor activity modifying proteins and their potential as drug targets.Lifting the lid on GPCRs: the role of extracellular loops.RAMPs and CGRP receptors.RAMPs as drug targets.Membrane proteins by accident or design.The second intracellular loop of the calcitonin gene-related peptide receptor provides molecular determinants for signal transduction and cell surface expression.Structure-function analysis of RAMP1-RAMP3 chimeras.Systematic analysis of the entire second extracellular loop of the V(1a) vasopressin receptor: key residues, conserved throughout a G-protein-coupled receptor family, identified.Characterization of the structure of RAMP1 by mutagenesis and molecular modeling.Evidence that interaction between conserved residues in transmembrane helices 2, 3, and 7 are crucial for human VPAC1 receptor activation.Structure-function analysis of RAMP1 by alanine mutagenesis.Homology modeling of GPCRs.Improving virtual screening of G protein-coupled receptors via ligand-directed modeling.Relative Antagonism of Mutants of the CGRP Receptor Extracellular Loop 2 Domain (ECL2) Using a Truncated Competitive Antagonist (CGRP8-37): Evidence for the Dual Involvement of ECL2 in the Two-Domain Binding Model.Differential impact of amino acid substitutions on critical residues of the human glucagon-like peptide-1 receptor involved in peptide activity and small-molecule allostery.Relative domain folding and stability of a membrane transport protein.Photoaffinity Cross-Linking and Unnatural Amino Acid Mutagenesis Reveal Insights into Calcitonin Gene-Related Peptide Binding to the Calcitonin Receptor-like Receptor/Receptor Activity-Modifying Protein 1 (CLR/RAMP1) ComplexLigand Binding and Activation of the CGRP ReceptorDiverse Functional Motifs within the Three Intracellular Loops of the CGRP1Receptor†Functional characterisation of G protein-coupled receptors
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description
researcher ORCID ID = 0000-0002-4675-0902
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wetenschapper
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name
John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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John Simms
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P1153
7006574415
P31
P496
0000-0002-4675-0902