New Binding Sites, New Opportunities for GPCR Drug Discovery.
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Shuguang Yuan | Horst Vogel | Thamani Dahoun | Shuguang Yuan | H. Vogel | T. Dahoun | H. C. S. Chan | Yi Li | H.C. Stephen Chan | Yi Li | H. C. S. Chan | Shuguang Yuan
[1] Nicole J. Yang,et al. Getting across the cell membrane: an overview for small molecules, peptides, and proteins. , 2015, Methods in molecular biology.
[2] Naomi R. Latorraca,et al. Structure of the μ Opioid Receptor-Gi Protein Complex , 2018, Nature.
[3] S. Filipek,et al. W246(6.48) opens a gate for a continuous intrinsic water pathway during activation of the adenosine A2A receptor. , 2014, Angewandte Chemie.
[4] A. Goldman,et al. G protein-coupled receptors show unusual patterns of intrinsic unfolding. , 2005, Protein engineering, design & selection : PEDS.
[5] Shuguang Yuan,et al. Lipid Receptor S1P1 Activation Scheme Concluded from Microsecond All-Atom Molecular Dynamics Simulations , 2013, PLoS Comput. Biol..
[6] G. Bottegoni,et al. Structure of the complement C5a receptor bound to the extra-helical antagonist NDT9513727 , 2018, Nature.
[7] Bryan L Roth,et al. Discovery of new GPCR ligands to illuminate new biology. , 2017, Nature chemical biology.
[8] Qi Wu,et al. COACH-D: improved protein–ligand binding sites prediction with refined ligand-binding poses through molecular docking , 2018, Nucleic Acids Res..
[9] A. J. Venkatakrishnan,et al. Universal allosteric mechanism for Gα activation by GPCRs , 2015, Nature.
[10] J. Simms,et al. Lifting the lid on GPCRs: the role of extracellular loops , 2011, British journal of pharmacology.
[11] R. Stevens,et al. Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions , 2012, Science.
[12] J. Wess,et al. Activation and allosteric modulation of a muscarinic acetylcholine receptor , 2013, Nature.
[13] F. Cordes,et al. Proline-induced distortions of transmembrane helices. , 2002, Journal of molecular biology.
[14] A. Kruse,et al. Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist , 2011, Nature.
[15] Hugh Rosen,et al. Crystal Structure of a Lipid G Protein–Coupled Receptor , 2012, Science.
[16] Richard M. Jackson,et al. Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites , 2005, Bioinform..
[17] B. Honig,et al. On the nature of cavities on protein surfaces: Application to the identification of drug‐binding sites , 2006, Proteins.
[18] Christofer S Tautermann,et al. GPCR structures in drug design, emerging opportunities with new structures. , 2014, Bioorganic & medicinal chemistry letters.
[19] J. García-Nafría,et al. Cryo-EM structure of the serotonin 5-HT1B receptor coupled to heterotrimeric Go , 2018, Nature.
[20] Gianni De Fabritiis,et al. DeepSite: protein‐binding site predictor using 3D‐convolutional neural networks , 2017, Bioinform..
[21] José Xavier-Neto,et al. KVFinder: steered identification of protein cavities as a PyMOL plugin , 2014, BMC Bioinformatics.
[22] Enrico Guarnera,et al. Allosteric sites: remote control in regulation of protein activity. , 2016, Current opinion in structural biology.
[23] Shuguang Yuan,et al. The role of water and sodium ions in the activation of the μ-opioid receptor. , 2013, Angewandte Chemie.
[24] R. Stevens,et al. Chemical Diversity in the G Protein-Coupled Receptor Superfamily. , 2018, Trends in pharmacological sciences.
[25] David Hoksza,et al. Improving protein-ligand binding site prediction accuracy by classification of inner pocket points using local features , 2015, Journal of Cheminformatics.
[26] M. Raida,et al. NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin. , 2011, Biochimica et biophysica acta.
[27] Dahlia R. Weiss,et al. Structure-based discovery of selective positive allosteric modulators of antagonists for the M2 muscarinic acetylcholine receptor , 2018, Proceedings of the National Academy of Sciences.
[28] Ruben Abagyan,et al. Structure of CC Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists , 2016, Nature.
[29] T. Kawabata. Detection of multiscale pockets on protein surfaces using mathematical morphology , 2010, Proteins.
[30] Gebhard F. X. Schertler,et al. The 2.1 Å Resolution Structure of Cyanopindolol-Bound β1-Adrenoceptor Identifies an Intramembrane Na+ Ion that Stabilises the Ligand-Free Receptor , 2014, PloS one.
[31] David E. Gloriam,et al. Pharmacogenomics of GPCR Drug Targets , 2018, Cell.
[32] D. Montange,et al. Impact of ticagrelor on P2Y1 and P2Y12 localization and on cholesterol levels in platelet plasma membrane , 2018, Platelets.
[33] Arthur Christopoulos,et al. Crystal structures of the M1 and M4 muscarinic acetylcholine receptors , 2016, Nature.
[34] H. Brückmann,et al. Polypharmacology of dopamine receptor ligands , 2016, Progress in Neurobiology.
[35] Bas Vroling,et al. GPCRdb: an information system for G protein-coupled receptors , 2015, Nucleic Acids Res..
[36] S. Hill,et al. Multiple GPCR conformations and signalling pathways: implications for antagonist affinity estimates , 2007, Trends in pharmacological sciences.
[37] M. Sturlese,et al. Exploring Protein-Peptide Recognition Pathways Using a Supervised Molecular Dynamics Approach. , 2017, Structure.
[38] Sujata Sharma,et al. Structural basis for the cooperative allosteric activation of the free fatty acid receptor GPR40 , 2017, Nature Structural &Molecular Biology.
[39] Naomi R. Latorraca,et al. Structure of the mu-opioid receptor-Giprotein complex. , 2018 .
[40] S. Vermeire,et al. Randomised clinical trial: vercirnon, an oral CCR9 antagonist, vs. placebo as induction therapy in active Crohn's disease , 2015, Alimentary pharmacology & therapeutics.
[41] K. Lindorff-Larsen,et al. Role of protein dynamics in transmembrane receptor signalling. , 2018, Current opinion in structural biology.
[42] Yang Zhang,et al. Protein-ligand binding site recognition using complementary binding-specific substructure comparison and sequence profile alignment , 2013, Bioinform..
[43] Ruben Abagyan,et al. Pocketome: an encyclopedia of small-molecule binding sites in 4D , 2011, Nucleic Acids Res..
[44] Hongbo Zhu,et al. MSPocket: an orientation-independent algorithm for the detection of ligand binding pockets , 2011, Bioinform..
[45] Dario Ghersi,et al. EASYMIFS and SITEHOUND: a toolkit for the identification of ligand-binding sites in protein structures , 2009, Bioinform..
[46] David Ryan Koes,et al. PocketQuery: protein–protein interaction inhibitor starting points from protein–protein interaction structure , 2012, Nucleic Acids Res..
[47] Hualiang Jiang,et al. Two disparate ligand-binding sites in the human P2Y1 receptor , 2015, Nature.
[48] Nagasuma Chandra,et al. PocketDepth: a new depth based algorithm for identification of ligand binding sites in proteins. , 2008, Journal of structural biology.
[49] George Papadatos,et al. The ChEMBL database in 2017 , 2016, Nucleic Acids Res..
[50] Min Liu,et al. bSiteFinder, an improved protein-binding sites prediction server based on structural alignment: more accurate and less time-consuming , 2016, Journal of Cheminformatics.
[51] Naomi R. Latorraca,et al. Mechanism of intracellular allosteric β2AR antagonist revealed by X-ray crystal structure , 2017, Nature.
[52] K. Palczewski,et al. Designing Safer Analgesics via μ-Opioid Receptor Pathways. , 2017, Trends in pharmacological sciences.
[53] Patrik Johansson,et al. Structural insight into allosteric modulation of protease-activated receptor 2 , 2017, Nature.
[54] A. Pioszak,et al. Structural insights into ligand recognition and selectivity for classes A, B, and C GPCRs. , 2015, European journal of pharmacology.
[55] Thomas A. Halgren,et al. Identifying and Characterizing Binding Sites and Assessing Druggability , 2009, J. Chem. Inf. Model..
[56] Yen-Jen Oyang,et al. MEDock: a web server for efficient prediction of ligand binding sites based on a novel optimization algorithm , 2005, Nucleic Acids Res..
[57] Yu Li,et al. Identification of cavities on protein surface using multiple computational approaches for drug binding site prediction , 2011, Bioinform..
[58] Chaok Seok,et al. GalaxySite: ligand-binding-site prediction by using molecular docking , 2014, Nucleic Acids Res..
[59] A. T. Nguyen,et al. New paradigms in adenosine receptor pharmacology: allostery, oligomerization and biased agonism , 2018, British journal of pharmacology.
[60] S. Rasmussen,et al. Allosteric coupling from G protein to the agonist binding pocket in GPCRs , 2016, Nature.
[61] Vadim Cherezov,et al. Allosteric sodium in class A GPCR signaling. , 2014, Trends in biochemical sciences.
[62] Guangyu Wu,et al. A Single Lys Residue on the First Intracellular Loop Modulates the Endoplasmic Reticulum Export and Cell-Surface Expression of α2A-Adrenergic Receptor , 2012, PloS one.
[63] H Weinstein,et al. Prokink: a protocol for numerical evaluation of helix distortions by proline. , 2000, Protein engineering.
[64] David E. Gloriam,et al. 5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology , 2018, Cell.
[65] J. Cheong,et al. The N‐terminal region of the dopamine D2 receptor, a rhodopsin‐like GPCR, regulates correct integration into the plasma membrane and endocytic routes , 2012, British journal of pharmacology.
[66] K. Palczewski,et al. Exploring a new ligand binding site of G protein-coupled receptors† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc01680a , 2018, Chemical science.
[67] Kathryn E. Livingston,et al. Allostery at opioid receptors: modulation with small molecule ligands , 2018, British journal of pharmacology.
[68] Naomi R. Latorraca,et al. Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors , 2017, Cell.
[69] R. Dey,et al. Regulation, Signaling, and Physiological Functions of G-Proteins. , 2016, Journal of molecular biology.
[70] Jonathan S. Mason,et al. Structures of G protein-coupled receptors reveal new opportunities for drug discovery. , 2015, Drug discovery today.
[71] Charged Extracellular Residues, Conserved throughout a G-protein-coupled Receptor Family, Are Required for Ligand Binding, Receptor Activation, and Cell-surface Expression* , 2006, Journal of Biological Chemistry.
[72] Stefano Moro,et al. Supervised Molecular Dynamics (SuMD) as a Helpful Tool To Depict GPCR-Ligand Recognition Pathway in a Nanosecond Time Scale , 2014, J. Chem. Inf. Model..
[73] Ali Jazayeri,et al. Intracellular allosteric antagonism of the CCR9 receptor , 2016, Nature.
[74] Alexander S. Hauser,et al. GPCRdb in 2018: adding GPCR structure models and ligands , 2017, Nucleic Acids Res..
[75] Mona Singh,et al. Predicting Protein Ligand Binding Sites by Combining Evolutionary Sequence Conservation and 3D Structure , 2009, PLoS Comput. Biol..
[76] Anthony Ivetac,et al. High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875 , 2014, Nature.
[77] Bryan L. Roth,et al. Molecular control of δ-opioid receptor signalling , 2014, Nature.
[78] A. J. Venkatakrishnan,et al. Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region , 2016, Nature.
[79] David E. Gloriam,et al. Trends in GPCR drug discovery: new agents, targets and indications , 2017, Nature Reviews Drug Discovery.
[80] A Keith Dunker,et al. Intrinsically Disordered Proteins Link Alternative Splicing and Post-translational Modifications to Complex Cell Signaling and Regulation. , 2018, Journal of molecular biology.
[81] Chris de Graaf,et al. Generic GPCR residue numbers - aligning topology maps while minding the gaps. , 2015, Trends in pharmacological sciences.
[82] S. Yokoyama,et al. Na+-mimicking ligands stabilize the inactive state of leukotriene B4 receptor BLT1. , 2018, Nature chemical biology.
[83] Vadim Cherezov,et al. Diversity and modularity of G protein-coupled receptor structures. , 2012, Trends in pharmacological sciences.
[84] Arthur Christopoulos,et al. Structure of the adenosine-bound human adenosine A1 receptor–Gi complex , 2018, Nature.
[85] O. Kuybeda,et al. Cryo-EM structure of human rhodopsin bound to an inhibitory G protein , 2018, Nature.
[86] Arthur Christopoulos,et al. Muscarinic acetylcholine receptors: novel opportunities for drug development , 2014, Nature Reviews Drug Discovery.
[87] Xiliang Zheng,et al. Pocket-Based Drug Design: Exploring Pocket Space , 2012, The AAPS Journal.
[88] Tilman Flock,et al. Structured and disordered facets of the GPCR fold. , 2014, Current opinion in structural biology.
[89] S. C. Wolff,et al. Charged residues in the C-terminus of the P2Y1 receptor constitute a basolateral-sorting signal , 2010, Journal of Cell Science.
[90] Michael J. E. Sternberg,et al. 3DLigandSite: predicting ligand-binding sites using similar structures , 2010, Nucleic Acids Res..
[91] M. Congreve,et al. Applying Structure-Based Drug Design Approaches to Allosteric Modulators of GPCRs. , 2017, Trends in pharmacological sciences.
[92] R. Lewis,et al. Extracellular Surface Residues of the α1B-Adrenoceptor Critical for G Protein–Coupled Receptor Function , 2015, Molecular Pharmacology.
[93] Albert C. Pan,et al. Structure and Dynamics of the M3 Muscarinic Acetylcholine Receptor , 2012, Nature.
[94] R. Stevens,et al. The Molecular Mechanism of P2Y1 Receptor Activation , 2016, Angewandte Chemie.