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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 StructuresCrystal structure of the human OX2 orexin receptor bound to the insomnia drug suvorexantThe Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased AgonismReceptor Activity-modifying Protein-directed G Protein Signaling Specificity for the Calcitonin Gene-related Peptide Family of ReceptorsKey interactions by conserved polar amino acids located at the transmembrane helical boundaries in Class B GPCRs modulate activation, effector specificity and biased signalling in the glucagon-like peptide-1 receptorGenetically encoded photocross-linkers determine the biological binding site of exendin-4 peptide in the N-terminal domain of the intact human glucagon-like peptide-1 receptor (GLP-1R)Ligand-induced modulation of the free-energy landscape of G protein-coupled receptors explored by adaptive biasing techniquesUnderstanding the molecular functions of the second extracellular loop (ECL2) of the calcitonin gene-related peptide (CGRP) receptor using a comprehensive mutagenesis approach.Advances in the Development and Application of Computational Methodologies for Structural Modeling of G-Protein Coupled Receptors.Life in blue: copper resistance mechanisms of bacteria and archaea used in industrial biomining of minerals.The quorum-sensing regulator ComA from Bacillus subtilis activates transcription using topologically distinct DNA motifsThe mode of agonist binding to a G protein-coupled receptor switches the effect that voltage changes have on signaling.Receptor activity-modifying protein-directed G protein signaling specificity for the calcitonin gene-related peptide family of receptors.High 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.Computational modeling, docking and molecular dynamics of the transcriptional activator ComA bound to a newly-identified functional DNA binding site.Identification of a novel allosteric GLP-1R antagonist HTL26119 using structure- based drug design
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description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Juan Carlos Mobarec
@ast
Juan Carlos Mobarec
@en
Juan Carlos Mobarec
@es
Juan Carlos Mobarec
@nl
Juan Carlos Mobarec
@sl
type
label
Juan Carlos Mobarec
@ast
Juan Carlos Mobarec
@en
Juan Carlos Mobarec
@es
Juan Carlos Mobarec
@nl
Juan Carlos Mobarec
@sl
prefLabel
Juan Carlos Mobarec
@ast
Juan Carlos Mobarec
@en
Juan Carlos Mobarec
@es
Juan Carlos Mobarec
@nl
Juan Carlos Mobarec
@sl
P106
P21
P31
P496
0000-0001-9482-4294