List of works - Laurence J Miller

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

scientific article

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.

scientific article

Changes in the plasma membrane in metabolic disease: impact of the membrane environment on G protein-coupled receptor structure and function

scientific article published on 10 July 2017

Development of a highly selective allosteric antagonist radioligand for the type 1 cholecystokinin receptor and elucidation of its molecular basis of binding

scientific article

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.

scientific article published on 28 January 2015

Glucagon-like peptide-1 receptor dimerization differentially regulates agonist signaling but does not affect small molecule allostery.

scientific article

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

scientific article

Minireview: Signal bias, allosterism, and polymorphic variation at the GLP-1R: implications for drug discovery

scientific article published on 17 July 2013

Molecular Mechanism of Action of Triazolobenzodiazepinone Agonists of the Type 1 Cholecystokinin Receptor. Possible Cooperativity across the Receptor Homodimeric Complex.

scientific article published on 10 December 2015

Molecular basis for benzodiazepine agonist action at the type 1 cholecystokinin receptor.

scientific article published on 10 June 2013

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

scientific article published on 21 February 2018

Polymorphism and ligand dependent changes in human glucagon-like peptide-1 receptor (GLP-1R) function: allosteric rescue of loss of function mutation.

scientific article

Recent advances in understanding GLP-1R (glucagon-like peptide-1 receptor) function.

scientific article published on February 2013

Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) differentially regulates orthosteric but not allosteric agonist binding and function.

scientific article published on 6 December 2011

Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activation

scientific article published on 6 December 2011

Structure and dynamics of the active Gs-coupled human secretin receptor

scientific article published on 18 August 2020

Structures of the human cholecystokinin 1 (CCK1) receptor bound to Gs and Gq mimetic proteins provide insight into mechanisms of G protein selectivity

scientific article published on 04 June 2021

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

scientific article

Use of Cysteine Trapping to Map Spatial Approximations between Residues Contributing to the Helix N-capping Motif of Secretin and Distinct Residues within Each of the Extracellular Loops of Its Receptor

scientific article published on 6 January 2016

List of works by Laurence J Miller

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

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.

Changes in the plasma membrane in metabolic disease: impact of the membrane environment on G protein-coupled receptor structure and function

Development of a highly selective allosteric antagonist radioligand for the type 1 cholecystokinin receptor and elucidation of its molecular basis of binding

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.

Glucagon-like peptide-1 receptor dimerization differentially regulates agonist signaling but does not affect small molecule allostery.

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

Minireview: Signal bias, allosterism, and polymorphic variation at the GLP-1R: implications for drug discovery

Molecular Mechanism of Action of Triazolobenzodiazepinone Agonists of the Type 1 Cholecystokinin Receptor. Possible Cooperativity across the Receptor Homodimeric Complex.

Molecular basis for benzodiazepine agonist action at the type 1 cholecystokinin receptor.

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

Polymorphism and ligand dependent changes in human glucagon-like peptide-1 receptor (GLP-1R) function: allosteric rescue of loss of function mutation.

Recent advances in understanding GLP-1R (glucagon-like peptide-1 receptor) function.

Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) differentially regulates orthosteric but not allosteric agonist binding and function.

Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activation

Structure and dynamics of the active Gs-coupled human secretin receptor

Structures of the human cholecystokinin 1 (CCK1) receptor bound to Gs and Gq mimetic proteins provide insight into mechanisms of G protein selectivity

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

Use of Cysteine Trapping to Map Spatial Approximations between Residues Contributing to the Helix N-capping Motif of Secretin and Distinct Residues within Each of the Extracellular Loops of Its Receptor