Negative allosteric modulation of the glucagon receptor by RAMP2
暂无分享,去创建一个
Naomi R. Latorraca | E. Isacoff | S. Marqusee | J. M. Mathiesen | B. Kobilka | D. Hilger | E. Montabana | Chris H. Habrian | Haoqing Wang | K. Krishna Kumar | Inga Tuneew | E. O’Brien
[1] Hideaki E. Kato,et al. Endogenous ligand recognition and structural transition of a human PTH receptor. , 2022, Molecular cell.
[2] P. Sexton,et al. A structural basis for amylin receptor phenotype , 2022, Science.
[3] S. Marqusee,et al. The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes , 2022, Nature Structural & Molecular Biology.
[4] Hideaki E. Kato,et al. Atypical structural snapshots of human cytomegalovirus GPCR interactions with host G proteins , 2022, Science advances.
[5] Shaoyong Lu,et al. Delineating the activation mechanism and conformational landscape of a class B G protein-coupled receptor glucagon receptor , 2022, Computational and structural biotechnology journal.
[6] U. Zabel,et al. Functional modulation of PTH1R activation and signalling by RAMP2 , 2021, bioRxiv.
[7] Oriol Vinyals,et al. Highly accurate protein structure prediction with AlphaFold , 2021, Nature.
[8] M. J. Robertson,et al. G-protein activation by a metabotropic glutamate receptor , 2021, Nature.
[9] D. Carling,et al. Receptor Activity-Modifying Protein 2 (RAMP2) alters glucagon receptor trafficking in hepatocytes with functional effects on receptor signalling , 2021, bioRxiv.
[10] G. Ladds,et al. RAMPs regulate signalling bias and internalisation of the GIPR , 2021, bioRxiv.
[11] David J. Fleet,et al. 3D Variability Analysis: Resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM. , 2021, Journal of structural biology.
[12] J. Javitch,et al. Agonist-induced formation of unproductive receptor-G12 complexes , 2020, Proceedings of the National Academy of Sciences.
[13] J. M. Mathiesen,et al. Structural insights into differences in G protein activation by family A and family B GPCRs , 2020, Science.
[14] I. Bahar,et al. Allosteric interactions in the parathyroid hormone GPCR–arrestin complex formation , 2020, Nature Chemical Biology.
[15] M. J. Robertson,et al. Structures of metabotropic GABAB receptor , 2020, Nature.
[16] 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.
[17] P. Sexton,et al. Structural basis of Gs and Gi recognition by the human glucagon receptor , 2020, Science.
[18] P. Sexton,et al. Toward a Structural Understanding of Class B GPCR Peptide Binding and Activation. , 2020, Molecular cell.
[19] Hideaki E. Kato,et al. Structure of the Neurotensin Receptor 1 in complex with β-arrestin 1 , 2020, Nature.
[20] David J. Fleet,et al. Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction , 2019, Nature Methods.
[21] A. Pioszak,et al. RAMPs as allosteric modulators of the calcitonin and calcitonin-like class B G protein-coupled receptors. , 2020, Advances in pharmacology.
[22] E. Isacoff,et al. Conformational pathway provides unique sensitivity to a synaptic mGluR , 2019, Nature Communications.
[23] Kelly K. Lee,et al. Bridging protein structure, dynamics, and function using hydrogen/deuterium‐exchange mass spectrometry , 2019, Protein science : a publication of the Protein Society.
[24] Robert M. Williams,et al. Perturbation of the interactions of calmodulin with GRK5 using a natural product chemical probe , 2019, Proceedings of the National Academy of Sciences.
[25] M. Uhlén,et al. Multiplexed analysis of the secretin-like GPCR-RAMP interactome , 2019, Science Advances.
[26] W. Baumeister,et al. Cryo-EM structure of the active, Gs-protein complexed, human CGRP receptor , 2018, Nature.
[27] Conrad C. Huang,et al. UCSF ChimeraX: Meeting modern challenges in visualization and analysis , 2018, Protein science : a publication of the Protein Society.
[28] Christopher J. Williams,et al. MolProbity: More and better reference data for improved all‐atom structure validation , 2018, Protein science : a publication of the Protein Society.
[29] T. Heise,et al. Pharmacokinetic and Pharmacodynamic Characteristics of Dasiglucagon, a Novel Soluble and Stable Glucagon Analog , 2017, Diabetes Care.
[30] R. Stevens,et al. Extending the Structural View of Class B GPCRs. , 2017, Trends in biochemical sciences.
[31] S. Bloom,et al. RAMP2 Influences Glucagon Receptor Pharmacology via Trafficking and Signaling , 2017, Endocrinology.
[32] Jonathan A. Javitch,et al. Single-molecule analysis of ligand efficacy in β2AR-G protein activation , 2017, Nature.
[33] Arthur Christopoulos,et al. Phase-plate cryo-EM structure of a class B GPCR-G protein complex , 2017, Nature.
[34] M. Tschöp,et al. The New Biology and Pharmacology of Glucagon. , 2017, Physiological reviews.
[35] David J. Fleet,et al. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.
[36] P. Sexton,et al. Allostery and Biased Agonism at Class B G Protein-Coupled Receptors. , 2017, Chemical reviews.
[37] R. Riek,et al. Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics , 2016, Angewandte Chemie.
[38] B. Kobilka,et al. Structure and dynamics of GPCR signaling complexes , 2017, Nature Structural & Molecular Biology.
[39] L. Bankir,et al. Glucagon actions on the kidney revisited: possible role in potassium homeostasis. , 2016, American journal of physiology. Renal physiology.
[40] Mingyao Liu,et al. Differential Requirement of the Extracellular Domain in Activation of Class B G Protein-coupled Receptors* , 2016, The Journal of Biological Chemistry.
[41] Daniel S. Terry,et al. Single-molecule imaging of non-equilibrium molecular ensembles on the millisecond timescale , 2016, Nature Methods.
[42] G. Ladds,et al. Modulation of Glucagon Receptor Pharmacology by Receptor Activity-modifying Protein-2 (RAMP2)* , 2015, The Journal of Biological Chemistry.
[43] E. Isacoff,et al. Conformational dynamics of a class C G protein-coupled receptor , 2015, Nature.
[44] J. M. Mathiesen,et al. A cAMP Biosensor-Based High-Throughput Screening Assay for Identification of Gs-Coupled GPCR Ligands and Phosphodiesterase Inhibitors , 2015, Journal of biomolecular screening.
[45] G. von Heijne,et al. Tissue-based map of the human proteome , 2015, Science.
[46] Chris de Graaf,et al. Structure of the human glucagon class B G-protein-coupled receptor , 2013, Nature.
[47] H. Lindmark,et al. Receptor activity modifying proteins (RAMPs) interact with the VPAC2 receptor and CRF1 receptors and modulate their function , 2013, British journal of pharmacology.
[48] Luís M. S. Loura. Simple Estimation of Förster Resonance Energy Transfer (FRET) Orientation Factor Distribution in Membranes , 2012, International journal of molecular sciences.
[49] I. Hötzel,et al. Molecular basis for negative regulation of the glucagon receptor , 2012, Proceedings of the National Academy of Sciences.
[50] N. Lee,et al. Dual mode of glucagon receptor internalization: role of PKCα, GRKs and β-arrestins. , 2011, Experimental cell research.
[51] Nathaniel Echols,et al. The Phenix software for automated determination of macromolecular structures. , 2011, Methods.
[52] S. Rasmussen,et al. Crystal Structure of the β2Adrenergic Receptor-Gs protein complex , 2011, Nature.
[53] H. Xu,et al. Molecular recognition of parathyroid hormone by its G protein-coupled receptor , 2008, Proceedings of the National Academy of Sciences.
[54] Gilad Haran,et al. Noise reduction in single-molecule fluorescence trajectories of folding proteins , 2004 .
[55] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[56] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[57] A. E. Hirsh,et al. Coevolution of gene expression among interacting proteins , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[58] D. Drucker,et al. International Union of Pharmacology. XXXV. The Glucagon Receptor Family , 2003, Pharmacological Reviews.
[59] P. Sexton,et al. Novel Receptor Partners and Function of Receptor Activity-modifying Proteins* , 2003, The Journal of Biological Chemistry.
[60] R. B. Merrifield,et al. Identification of an essential serine residue in glucagon: implication for an active site triad. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[61] R. B. Merrifield,et al. Biological activities of des-His1[Glu9]glucagon amide, a glucagon antagonist , 1989, Peptides.