Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation

[1]  C. Langmead,et al.  Differential GLP-1R Binding and Activation by Peptide and Non-peptide Agonists. , 2020, Molecular cell.

[2]  J. M. Mathiesen,et al.  Structural insights into differences in G protein activation by family A and family B GPCRs , 2020, Science.

[3]  P. Sexton,et al.  Structure and Dynamics of Adrenomedullin Receptors AM1 and AM2 Reveal Key Mechanisms in the Control of Receptor Phenotype by Receptor Activity-Modifying Proteins. , 2020, ACS pharmacology & translational science.

[4]  P. Sexton,et al.  Structural basis of Gs and Gi recognition by the human glucagon receptor , 2020, Science.

[5]  P. Sexton,et al.  Toward a Structural Understanding of Class B GPCR Peptide Binding and Activation. , 2020, Molecular cell.

[6]  P. Sexton,et al.  Molecular Basis for Hormone Recognition and Activation of Corticotropin-Releasing Factor Receptors. , 2020, Molecular cell.

[7]  P. Sexton,et al.  Activation of the GLP-1 receptor by a non-peptidic agonist , 2020, Nature.

[8]  S. Raunser,et al.  SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM , 2019, Communications Biology.

[9]  Tomoyuki Watanabe,et al.  Structure and dynamics of the active human parathyroid hormone receptor-1 , 2019, Science.

[10]  W. Baumeister,et al.  Cryo-EM structure of the active, Gs-protein complexed, human CGRP receptor , 2018, Nature.

[11]  Arthur Christopoulos,et al.  Dominant Negative G Proteins Enhance Formation and Purification of Agonist-GPCR-G Protein Complexes for Structure Determination. , 2018, ACS pharmacology & translational science.

[12]  G. Rutter,et al.  Targeting GLP-1 receptor trafficking to improve agonist efficacy , 2018, Nature Communications.

[13]  Yiming Yu,et al.  shinyCircos: an R/Shiny application for interactive creation of Circos plot , 2018, Bioinform..

[14]  W. Baumeister,et al.  Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor–Gs complex , 2018, Nature.

[15]  Conrad C. Huang,et al.  UCSF ChimeraX: Meeting modern challenges in visualization and analysis , 2018, Protein science : a publication of the Protein Society.

[16]  J. Wess,et al.  Lack of beta-arrestin signaling in the absence of active G proteins , 2018, Nature Communications.

[17]  P. Sexton,et al.  Characterization of signal bias at the GLP‐1 receptor induced by backbone modification of GLP‐1 , 2017, Biochemical pharmacology.

[18]  Arthur Christopoulos,et al.  Phase-plate cryo-EM structure of a class B GPCR-G protein complex , 2017, Nature.

[19]  D. Agard,et al.  MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy , 2017, Nature Methods.

[20]  P. Sexton,et al.  Allostery and Biased Agonism at Class B G Protein-Coupled Receptors. , 2017, Chemical reviews.

[21]  R. Sunahara,et al.  Mechanistic insights into GPCR-G protein interactions. , 2016, Current opinion in structural biology.

[22]  P. Sexton,et al.  β-Arrestin-Biased Agonists of the GLP-1 Receptor from β-Amino Acid Residue Incorporation into GLP-1 Analogues. , 2016, Journal of the American Chemical Society.

[23]  P. Sexton,et al.  Ligand-Dependent Modulation of G Protein Conformation Alters Drug Efficacy , 2016, Cell.

[24]  P. Sexton,et al.  Glucagon-Like Peptide-1 and Its Class B G Protein–Coupled Receptors: A Long March to Therapeutic Successes , 2016, Pharmacological Reviews.

[25]  S. Rasmussen,et al.  Allosteric coupling from G protein to the agonist binding pocket in GPCRs , 2016, Nature.

[26]  P. Sexton,et al.  The Extracellular Surface of the GLP-1 Receptor Is a Molecular Trigger for Biased Agonism , 2016, Cell.

[27]  Itay Mayrose,et al.  ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules , 2016, Nucleic Acids Res..

[28]  Frank Noé,et al.  HTMD: High-Throughput Molecular Dynamics for Molecular Discovery. , 2016, Journal of chemical theory and computation.

[29]  P. Sexton,et al.  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 , 2016, Molecular Pharmacology.

[30]  Kai Zhang,et al.  Gctf: Real-time CTF determination and correction , 2015, bioRxiv.

[31]  Jing Huang,et al.  CHARMM36 all‐atom additive protein force field: Validation based on comparison to NMR data , 2013, J. Comput. Chem..

[32]  Chris de Graaf,et al.  Structure of the human glucagon class B G-protein-coupled receptor , 2013, Nature.

[33]  P. Sexton,et al.  Differential Activation and Modulation of the Glucagon-Like Peptide-1 Receptor by Small Molecule Ligands , 2013, Molecular Pharmacology.

[34]  Arthur Christopoulos,et al.  Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations , 2013, Proceedings of the National Academy of Sciences.

[35]  Bruck Taddese,et al.  Similarity between class A and class B G-protein-coupled receptors exemplified through calcitonin gene-related peptide receptor modelling and mutagenesis studies , 2013, Journal of The Royal Society Interface.

[36]  Björn Sommer,et al.  Membrane Packing Problems: A short Review on computational Membrane Modeling Methods and Tools , 2013, Computational and structural biotechnology journal.

[37]  Klaus Schulten,et al.  Cryo-electron microscopy modeling by the molecular dynamics flexible fitting method. , 2012, Biopolymers.

[38]  D. Donnelly,et al.  The structure and function of the glucagon‐like peptide‐1 receptor and its ligands , 2012, British journal of pharmacology.

[39]  Arthur Christopoulos,et al.  A simple method for quantifying functional selectivity and agonist bias. , 2012, ACS chemical neuroscience.

[40]  Kuntal Pal,et al.  Structure and mechanism for recognition of peptide hormones by Class B G-protein-coupled receptors , 2012, Acta Pharmacologica Sinica.

[41]  R. DiMarchi,et al.  Functional association of the N‐terminal residues with the central region in glucagon‐related peptides , 2011, Journal of peptide science : an official publication of the European Peptide Society.

[42]  P. Sexton,et al.  Polymorphism and Ligand Dependent Changes in Human Glucagon-Like Peptide-1 Receptor (GLP-1R) Function: Allosteric Rescue of Loss of Function Mutation , 2011, Molecular Pharmacology.

[43]  Jan H. Jensen,et al.  PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pKa Predictions. , 2011, Journal of chemical theory and computation.

[44]  P. Sexton,et al.  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 , 2010, Molecular Pharmacology.

[45]  M. Rooman,et al.  Evidence that Interaction between Conserved Residues in Transmembrane Helices 2, 3, and 7 Are Crucial for Human VPAC1 Receptor Activation , 2010, Molecular Pharmacology.

[46]  Z. Luthey-Schulten,et al.  Dynamical networks in tRNA:protein complexes , 2009, Proceedings of the National Academy of Sciences.

[47]  Wen Jiang,et al.  EMAN2: an extensible image processing suite for electron microscopy. , 2007, Journal of structural biology.

[48]  Andrei L. Lomize,et al.  OPM: Orientations of Proteins in Membranes database , 2006, Bioinform..

[49]  Conrad C. Huang,et al.  UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..

[50]  Nathan A. Baker,et al.  PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations , 2004, Nucleic Acids Res..

[51]  D. Donnelly,et al.  A model for receptor–peptide binding at the glucagon‐like peptide‐1 (GLP‐1) receptor through the analysis of truncated ligands and receptors , 2003, British journal of pharmacology.

[52]  M E J Newman,et al.  Community structure in social and biological networks , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[53]  J. Holst,et al.  Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity , 1998, Diabetologia.

[54]  C. Montrose‐Rafizadeh,et al.  High Potency Antagonists of the Pancreatic Glucagon-like Peptide-1 Receptor* , 1997, The Journal of Biological Chemistry.

[55]  K Schulten,et al.  VMD: visual molecular dynamics. , 1996, Journal of molecular graphics.

[56]  T. Darden,et al.  A smooth particle mesh Ewald method , 1995 .

[57]  B. Brooks,et al.  Langevin dynamics of peptides: The frictional dependence of isomerization rates of N‐acetylalanyl‐N′‐methylamide , 1992, Biopolymers.

[58]  H. Berendsen,et al.  Molecular dynamics with coupling to an external bath , 1984 .

[59]  W. L. Jorgensen,et al.  Comparison of simple potential functions for simulating liquid water , 1983 .