The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
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Receptor 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 receptorHuman GLP-1 receptor transmembrane domain structure in complex with allosteric modulators.Genetically 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)Receptor activity-modifying protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin receptors to Gs.An intrinsic agonist mechanism for activation of glucagon-like peptide-1 receptor by its extracellular domain.Characterization of signal bias at the GLP-1 receptor induced by backbone modification of GLP-1.Functional selectivity at G-protein coupled receptors: Advancing cannabinoid receptors as drug targets.Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein.Phase-plate cryo-EM structure of a class B GPCR-G-protein complex.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.β-Arrestin-Biased Agonists of the GLP-1 Receptor from β-Amino Acid Residue Incorporation into GLP-1 Analogues.Crystal Structure of an LSD-Bound Human Serotonin Receptor.Biased signalling: from simple switches to allosteric microprocessors.Glucagon receptor as a drug target: A witches' brew of eye of newt (peptides) and toe of frog (receptors).Extracellular loops 2 and 3 of the calcitonin receptor selectively modify agonist binding and efficacy.Crystal structure of the GLP-1 receptor bound to a peptide agonist.Conditional and Reversible Activation of Class A and B G Protein-Coupled Receptors Using Tethered Pharmacology.Targeting GLP-1 receptor trafficking to improve agonist efficacy.Cryo-EM structure of the active, G-protein complexed, human CGRP receptor
P2860
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P2860
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
description
2016 nî lūn-bûn
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2016 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2016 թվականի հունիսին հրատարակված գիտական հոդված
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2016年の論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年論文
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2016年论文
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name
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@ast
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
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The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
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type
label
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@ast
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@en
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@nl
prefLabel
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@ast
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@en
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@nl
P2093
P2860
P50
P3181
P1433
P1476
The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism
@en
P2093
Cassandra Koole
Christopher A Reynolds
Emilia E Savage
Kavita Pabreja
Kevin J Smith
Laurence J Miller
Rohan Sridhar
P2860
P304
P3181
P356
10.1016/J.CELL.2016.05.023
P407
P50
P577
2016-06-01T00:00:00Z