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Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor–Gs complex

44/44 checkable references clean · checked 2026-07-24

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

The 44 checked references that resolve

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Glucagon-Like Peptide-1 and Its Class B G Protein–Coupled Receptors: A Long March to Therapeutic Successes

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Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein

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Characterization of signal bias at the GLP-1 receptor induced by backbone modification of GLP-1

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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

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Differential Activation and Modulation of the Glucagon-Like Peptide-1 Receptor by Small Molecule Ligands

resolves10.1038/ncomms9918

Autocrine selection of a GLP-1R G-protein biased agonist with potent antidiabetic effects

resolves10.1042/BST0350713

Peptide binding at the GLP-1 receptor

resolves10.1021/jm500810s

Glucagon-like Peptide-1 (GLP-1) Analogs: Recent Advances, New Possibilities, and Therapeutic Implications

resolves10.1038/nature22327

Phase-plate cryo-EM structure of a class B GPCR–G-protein complex

resolves10.1073/pnas.1418377111

Volta potential phase plate for in-focus phase contrast transmission electron microscopy

resolves10.1038/ncomms16099

Cryo-EM structure of haemoglobin at 3.2 Å determined with the Volta phase plate

resolves10.1038/ncomms10534

Volta phase plate cryo-EM of the small protein complex Prx3

resolves10.1038/nature12393

Structure of the human glucagon class B G-protein-coupled receptor

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Structure of class B GPCR corticotropin-releasing factor receptor 1

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Crystal structure of the GLP-1 receptor bound to a peptide agonist

resolves10.1074/jbc.M708740200

Crystal Structure of the Ligand-bound Glucagon-like Peptide-1 Receptor Extracellular Domain

resolves10.1016/j.cell.2016.05.023

The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism

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Residues within the Transmembrane Domain of the Glucagon-Like Peptide-1 Receptor Involved in Ligand Binding and Receptor Activation: Modelling the Ligand-Bound Receptor

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The peptide agonist-binding site of the glucagon-like peptide-1 (GLP-1) receptor based on site-directed mutagenesis and knowledge-based modelling

resolves10.1074/jbc.M111.309328

Second Extracellular Loop of Human Glucagon-like Peptide-1 Receptor (GLP-1R) Has a Critical Role in GLP-1 Peptide Binding and Receptor Activation

resolves10.1016/j.bcp.2016.08.015

Key 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 receptor

resolves10.1074/jbc.M116.721977

Structural Determinants of Binding the Seven-transmembrane Domain of the Glucagon-like Peptide-1 Receptor (GLP-1R)

resolves10.1074/jbc.M114.612606

Ligand Binding Pocket Formed by Evolutionarily Conserved Residues in the Glucagon-like Peptide-1 (GLP-1) Receptor Core Domain

resolves10.1124/mol.115.101246

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 Structures

resolves10.1073/pnas.1221585110

Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations

resolves10.1016/j.cell.2016.09.021

Ligand-Dependent Modulation of G Protein Conformation Alters Drug Efficacy

resolves10.1038/nature22354

Single-molecule analysis of ligand efficacy in β2AR–G-protein activation

resolves10.1016/S0014-5793(98)01704-9

The N54 mutant of Gαs has a conditional dominant negative phenotype which suppresses hormone‐stimulated but not basal cAMP levels

resolves10.1016/S0021-9258(18)48416-5

The G226A mutant of Gs alpha highlights the requirement for dissociation of G protein subunits.

resolves10.1073/pnas.96.2.499

A G sα mutant designed to inhibit receptor signaling through G s

resolves10.1074/jbc.M201330200

A Highly Effective Dominant Negative αs Construct Containing Mutations That Affect Distinct Functions Inhibits Multiple Gs-coupled Receptor Signaling Pathways

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Automated electron microscope tomography using robust prediction of specimen movements

resolves10.1038/nmeth.4193

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Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2

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Coot: model-building tools for molecular graphics

resolves10.1107/S0907444909052925

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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MolProbity: all-atom structure validation for macromolecular crystallography

resolves10.2144/000114013

A Simple Method to Generate Stable Cell Lines for the Analysis of Transient Protein-Protein Interactions

resolves10.1021/jacs.6b08323

β-Arrestin-Biased Agonists of the GLP-1 Receptor from β-Amino Acid Residue Incorporation into GLP-1 Analogues

resolves10.1002/jcc.20084

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The relationship between muscarinic receptor occupancy and adenylate cyclase inhibition in the rabbit myocardium.

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