Common activation mechanism of class A GPCRs

Adhikari, 2016, Protein residue contacts and prediction methods, Methods in Molecular Biology, 1415, 463, 10.1007/978-1-4939-3572-7_24

Alhadeff, 2018, Exploring the free-energy landscape of GPCR activation, PNAS, 115, 10327, 10.1073/pnas.1810316115

Allen, 2011, Strategies to discover unexpected targets for drugs active at G protein-coupled receptors, Annual Review of Pharmacology and Toxicology, 51, 117, 10.1146/annurev-pharmtox-010510-100553

Amberger, 2011, A new face and new challenges for online mendelian inheritance in man (OMIM), Human Mutation, 32, 564, 10.1002/humu.21466

Ballesteros, 1995, [19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors, Methods in Neurosciences, 25, 366, 10.1016/S1043-9471(05)80049-7

Beard, 2013, Applying physics-based scoring to calculate free energies of binding for single amino acid mutations in protein-protein complexes, PLOS ONE, 8, 10.1371/journal.pone.0082849

Bhattacharya, 2014, Differences in allosteric communication pipelines in the inactive and active states of a GPCR, Biophysical Journal, 107, 422, 10.1016/j.bpj.2014.06.015

Bockaert, 1999, Molecular tinkering of G protein-coupled receptors: an evolutionary success, The EMBO Journal, 18, 1723, 10.1093/emboj/18.7.1723

Caffrey, 2009, Crystallizing membrane proteins using lipidic mesophases, Nature Protocols, 4, 706, 10.1038/nprot.2009.31

Capra, 2007, Predicting functionally important residues from sequence conservation, Bioinformatics, 23, 1875, 10.1093/bioinformatics/btm270

Carpenter, 2016, Structure of the adenosine A(2A) receptor bound to an engineered G protein, Nature, 536, 104, 10.1038/nature18966

Chaturvedi, 2018, Emerging paradigm of intracellular targeting of G Protein-Coupled receptors, Trends in Biochemical Sciences, 43, 533, 10.1016/j.tibs.2018.04.003

Che, 2018, Structure of the Nanobody-Stabilized active state of the kappa opioid receptor, Cell, 172, 55, 10.1016/j.cell.2017.12.011

Chen, 2019, Human substance P receptor binding mode of the antagonist drug aprepitant by NMR and crystallography, Nature Communications, 10, 10.1038/s41467-019-08568-5

Cheng, 2018, Single-particle cryo-EM-How did it get here and where will it go, Science, 361, 876, 10.1126/science.aat4346

Cherezov, 2004, A robotic system for crystallizing membrane and soluble proteins in lipidic mesophases, Acta Crystallographica Section D Biological Crystallography, 60, 1795, 10.1107/S0907444904019109

Cherezov, 2007, High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor, Science, 318, 1258, 10.1126/science.1150577

Choe, 2011, Crystal structure of metarhodopsin II, Nature, 471, 651, 10.1038/nature09789

Christopoulos, 2014, Advances in G protein-coupled receptor allostery: from function to structure, Molecular Pharmacology, 86, 463, 10.1124/mol.114.094342

Christopoulos, 2002, G protein-coupled receptor allosterism and complexing, Pharmacological Reviews, 54, 323, 10.1124/pr.54.2.323

Ciancetta, 2015, Advances in computational techniques to study GPCR-Ligand recognition, Trends in Pharmacological Sciences, 36, 878, 10.1016/j.tips.2015.08.006

Cooke, 2015, Structures of G protein-coupled receptors reveal new opportunities for drug discovery, Drug Discovery Today, 20, 1355, 10.1016/j.drudis.2015.08.003

Crooks, 2004, WebLogo: a sequence logo generator, Genome Research, 14, 1188, 10.1101/gr.849004

Dalton, 2015, Quantifying conformational changes in GPCRs: glimpse of a common functional mechanism, BMC Bioinformatics, 16, 10.1186/s12859-015-0567-3

DeVree, 2016, Allosteric coupling from G protein to the agonist-binding pocket in GPCRs, Nature, 535, 182, 10.1038/nature18324

Draper-Joyce, 2018, Structure of the adenosine-bound human Adenosine A1 receptor–Gi complex, Nature, 558, 559, 10.1038/s41586-018-0236-6

Dror, 2011, Activation mechanism of the β2-adrenergic receptor, PNAS, 108, 18684, 10.1073/pnas.1110499108

Dror, 2011, Pathway and mechanism of drug binding to G-protein-coupled receptors, PNAS, 108, 13118, 10.1073/pnas.1104614108

Dror, 2013, Structural basis for modulation of a G-protein-coupled receptor by allosteric drugs, Nature, 503, 295, 10.1038/nature12595

Dror, 2015, SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins, Science, 348, 1361, 10.1126/science.aaa5264

Du, 2019, Assembly of a GPCR-G protein complex, Cell, 177, 1232, 10.1016/j.cell.2019.04.022

Eddy, 2018, Allosteric coupling of drug binding and intracellular signaling in the A2A adenosine receptor, Cell, 172, 68, 10.1016/j.cell.2017.12.004

Eldridge, 1997, Empirical scoring functions: I. the development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes, Journal of Computer-Aided Molecular Design, 11, 425, 10.1023/a:1007996124545

Erdélyi, 2015, Mutation in the V2 vasopressin receptor gene, AVPR2, causes nephrogenic syndrome of inappropriate diuresis, Kidney International, 88, 1070, 10.1038/ki.2015.181

Fenalti, 2014, Molecular control of δ-opioid receptor signalling, Nature, 506, 191, 10.1038/nature12944

Feng, 2017, Computational design of ligand-binding membrane receptors with high selectivity, Nature Chemical Biology, 13, 715, 10.1038/nchembio.2371

Filipek, 2019, Molecular switches in GPCRs, Current Opinion in Structural Biology, 55, 114, 10.1016/j.sbi.2019.03.017

Flock, 2015, Universal allosteric mechanism for gα activation by GPCRs, Nature, 524, 173, 10.1038/nature14663

Flock, 2017, Selectivity determinants of GPCR-G-protein binding, Nature, 545, 317, 10.1038/nature22070

Fredriksson, 2003, The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints, Molecular Pharmacology, 63, 1256, 10.1124/mol.63.6.1256

Furness, 2016, Ligand-Dependent modulation of G protein conformation alters drug efficacy, Cell, 167, 739, 10.1016/j.cell.2016.09.021

Gainetdinov, 2004, Desensitization of G protein-coupled receptors and neuronal functions, Annual Review of Neuroscience, 27, 107, 10.1146/annurev.neuro.27.070203.144206

García-Nafría, 2018, Cryo-EM structure of the serotonin 5-HT1B receptor coupled to heterotrimeric Go, Nature, 558, 620, 10.1038/s41586-018-0241-9

Ghosh, 2015, Methodological advances: the unsung heroes of the GPCR structural revolution, Nature Reviews Molecular Cell Biology, 16, 69, 10.1038/nrm3933

Gilchrist, 2007, Modulating G-protein-coupled receptors: from traditional pharmacology to allosterics, Trends in Pharmacological Sciences, 28, 431, 10.1016/j.tips.2007.06.012

Glukhova, 2018, Rules of engagement: gpcrs and G proteins, ACS Pharmacology & Translational Science, 1, 73, 10.1021/acsptsci.8b00026

Gregorio, 2017, Single-molecule analysis of ligand efficacy in β2AR-G-protein activation, Nature, 547, 68, 10.1038/nature22354

Haga, 2012, Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist, Nature, 482, 547, 10.1038/nature10753

Halls, 2018, Genetically encoded FRET biosensors to illuminate compartmentalised GPCR signalling, Trends in Pharmacological Sciences, 39, 148, 10.1016/j.tips.2017.09.005

Han, 2012, Leu128(3.43) (l128) and Val247(6.40) (V247) of CXCR1 are critical amino acid residues for g protein coupling and receptor activation, PLOS ONE, 7, 10.1371/journal.pone.0042765

Hauser, 2017, Trends in GPCR drug discovery: new agents, targets and indications, Nature Reviews Drug Discovery, 16, 829, 10.1038/nrd.2017.178

Hauser, 2018, Pharmacogenomics of GPCR drug targets, Cell, 172, 41, 10.1016/j.cell.2017.11.033

Hofmann, 2009, A G protein-coupled receptor at work: the rhodopsin model, Trends in Biochemical Sciences, 34, 540, 10.1016/j.tibs.2009.07.005

Hollingsworth, 2019, Cryptic pocket formation underlies allosteric modulator selectivity at Muscarinic GPCRs, Nature Communications, 10, 10.1038/s41467-019-11062-7

Holst, 2010, A conserved aromatic lock for the tryptophan rotameric switch in TM-VI of seven-transmembrane receptors, Journal of Biological Chemistry, 285, 3973, 10.1074/jbc.M109.064725

Hori, 2018, Na+-mimicking ligands stabilize the inactive state of leukotriene B4 receptor BLT1, Nature Chemical Biology, 14, 262, 10.1038/nchembio.2547

Huang, 2015, Structural insights into µ-opioid receptor activation, Nature, 524, 315, 10.1038/nature14886

Hulme, 2013, GPCR activation: a mutagenic spotlight on crystal structures, Trends in Pharmacological Sciences, 34, 67, 10.1016/j.tips.2012.11.002

Hunyady, 2003, Agonist induction and conformational selection during activation of a G-protein-coupled receptor, Trends in Pharmacological Sciences, 24, 81, 10.1016/S0165-6147(02)00050-0

Ilyaskina, 2018, Lifetime of muscarinic receptor-G-protein complexes determines coupling efficiency and G-protein subtype selectivity, PNAS, 115, 5016, 10.1073/pnas.1715751115

Inoue, 2019, Illuminating G-Protein-Coupling selectivity of GPCRs, Cell, 177, 1933, 10.1016/j.cell.2019.04.044

Irannejad, 2013, Conformational biosensors reveal GPCR signalling from endosomes, Nature, 495, 534, 10.1038/nature12000

Isberg, 2015, Generic GPCR residue numbers - aligning topology maps while minding the gaps, Trends in Pharmacological Sciences, 36, 22, 10.1016/j.tips.2014.11.001

Isberg, 2016, GPCRdb: an information system for G protein-coupled receptors, Nucleic Acids Research, 44, D356, 10.1093/nar/gkv1178

Ishchenko, 2017, Structural insights into the extracellular recognition of the human serotonin 2B receptor by an antibody, PNAS, 114, 8223, 10.1073/pnas.1700891114

Isogai, 2016, Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor, Nature, 530, 237, 10.1038/nature16577

Isom, 2015, Buried ionizable networks are an ancient hallmark of G protein-coupled receptor activation, PNAS, 112, 5702, 10.1073/pnas.1417888112

Jaakola, 2008, The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist, Science, 322, 1211, 10.1126/science.1164772

Jacobson, 2014, Computational studies to predict or explain G protein coupled receptor polypharmacology, Trends in Pharmacological Sciences, 35, 658, 10.1016/j.tips.2014.10.009

Jaeger, 2019, Structural basis for allosteric ligand recognition in the human CC chemokine receptor 7, Cell, 178, 1222, 10.1016/j.cell.2019.07.028

Jones, 1991, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallographica Section a Foundations of Crystallography, 47, 110, 10.1107/S0108767390010224

Kang, 2015, Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser, Nature, 523, 561, 10.1038/nature14656

Kang, 2018, Cryo-EM structure of human rhodopsin bound to an inhibitory G protein, Nature, 558, 553, 10.1038/s41586-018-0215-y

Kato, 2019, Conformational transitions of a neurotensin receptor 1-Gi1 complex, Nature, 572, 80, 10.1038/s41586-019-1337-6

Katritch, 2012, Diversity and modularity of G protein-coupled receptor structures, Trends in Pharmacological Sciences, 33, 17, 10.1016/j.tips.2011.09.003

Katritch, 2013, Structure-function of the G protein-coupled receptor superfamily, Annual Review of Pharmacology and Toxicology, 53, 531, 10.1146/annurev-pharmtox-032112-135923

Katritch, 2014, Allosteric sodium in class A GPCR signaling, Trends in Biochemical Sciences, 39, 233, 10.1016/j.tibs.2014.03.002

Kayikci, 2018, Visualization and analysis of non-covalent contacts using the protein contacts atlas, Nature Structural & Molecular Biology, 25, 185, 10.1038/s41594-017-0019-z

Kleywegt, 2004, The Uppsala Electron-Density server, Acta Crystallographica Section D Biological Crystallography, 60, 2240, 10.1107/S0907444904013253

Kobilka, 2008, New G-protein-coupled receptor crystal structures: insights and limitations, Trends in Pharmacological Sciences, 29, 79, 10.1016/j.tips.2007.11.009

Koehl, 2018, Structure of the µ-opioid receptor-Gi protein complex, Nature, 558, 547, 10.1038/s41586-018-0219-7

Kohlhoff, 2014, Cloud-based simulations on google exacycle reveal ligand modulation of GPCR activation pathways, Nature Chemistry, 6, 15, 10.1038/nchem.1821

Kolakowski, 1994, GCRDb: a G-protein-coupled receptor database, Receptors & Channels, 2, 1

Komolov, 2017, Structural and functional analysis of a β2-Adrenergic Receptor Complex with GRK5, Cell, 169, 407, 10.1016/j.cell.2017.03.047

Kooistra, 2016, Function-specific virtual screening for GPCR ligands using a combined scoring method, Scientific Reports, 6, 10.1038/srep28288

Krautwurst, 1998, Identification of ligands for olfactory receptors by functional expression of a receptor library, Cell, 95, 917, 10.1016/S0092-8674(00)81716-X

Kruse, 2013, Activation and allosteric modulation of a muscarinic acetylcholine receptor, Nature, 504, 101, 10.1038/nature12735

Kufareva, 2011, Status of GPCR modeling and docking as reflected by community-wide GPCR dock 2010 assessment, Structure, 19, 1108, 10.1016/j.str.2011.05.012

Kufareva, 2013, A novel approach to quantify G-protein-coupled receptor dimerization equilibrium using bioluminescence resonance energy transfer, Methods in Molecular Biology, 1013, 93, 10.1007/978-1-62703-426-5_7

Kufareva, 2014, Advances in GPCR modeling evaluated by the GPCR dock 2013 assessment: meeting new challenges, Structure, 22, 1120, 10.1016/j.str.2014.06.012

Kufareva, 2014, Stoichiometry and geometry of the CXC chemokine receptor 4 complex with CXC ligand 12: Molecular modeling and experimental validation, PNAS, 111, E5363, 10.1073/pnas.1417037111

Kufareva, 2012, Homology Modeling: Methods and Protocols, 231

Lagerström, 2008, Structural diversity of G protein-coupled receptors and significance for drug discovery, Nature Reviews Drug Discovery, 7, 339, 10.1038/nrd2518

Lamichhane, 2015, Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β2ar, PNAS, 112, 14254, 10.1073/pnas.1519626112

Lan, 2012, Sensitive and high resolution localization and tracking of membrane proteins in live cells with BRET, Traffic, 13, 1450, 10.1111/j.1600-0854.2012.01401.x

Lans, 2015, Helix 3 acts as a conformational hinge in class A GPCR activation: an analysis of interhelical interaction energies in crystal structures, Journal of Structural Biology, 192, 545, 10.1016/j.jsb.2015.10.019

Latorraca, 2017, GPCR dynamics: structures in motion, Chemical Reviews, 117, 139, 10.1021/acs.chemrev.6b00177

Latorraca, 2018, Molecular mechanism of GPCR-mediated arrestin activation, Nature, 557, 452, 10.1038/s41586-018-0077-3

Leach, 2007, Allosteric GPCR modulators: taking advantage of permissive receptor pharmacology, Trends in Pharmacological Sciences, 28, 382, 10.1016/j.tips.2007.06.004

Lee, 2016, The conformational signature of β-arrestin2 predicts its trafficking and signalling functions, Nature, 531, 665, 10.1038/nature17154

Li, 2004, Structure of bovine rhodopsin in a trigonal crystal form, Journal of Molecular Biology, 343, 1409, 10.1016/j.jmb.2004.08.090

Liang, 2017, Phase-plate cryo-EM structure of a class B GPCR-G-protein complex, Nature, 546, 118, 10.1038/nature22327

Liu, 2012, Structural basis for allosteric regulation of GPCRs by sodium ions, Science, 337, 232, 10.1126/science.1219218

Liu, 2013, Serial femtosecond crystallography of G protein-coupled receptors, Science, 342, 1521, 10.1126/science.1244142

Liu, 2017, Mechanism of intracellular allosteric β2AR antagonist revealed by X-ray crystal structure, Nature, 548, 480, 10.1038/nature23652

Liu, 2019, Structural insights into the process of GPCR-G protein complex formation, Cell, 177, 1243, 10.1016/j.cell.2019.04.021

Liu, 2019, Mechanism of β2AR regulation by an intracellular positive allosteric modulator, Science, 364, 1283, 10.1126/science.aaw8981

Livingston, 2018, Measuring ligand efficacy at the mu-opioid receptor using a conformational biosensor, eLife, 7, 10.7554/eLife.32499

Lu, 2019, Small molecule allosteric modulators of G-Protein-Coupled receptors: drug-target interactions, Journal of Medicinal Chemistry, 62, 24, 10.1021/acs.jmedchem.7b01844

Lyu, 2019, Ultra-large library docking for discovering new chemotypes, Nature, 566, 224, 10.1038/s41586-019-0917-9

Madabushi, 2004, Evolutionary trace of G protein-coupled receptors reveals clusters of residues that determine global and class-specific functions, Journal of Biological Chemistry, 279, 8126, 10.1074/jbc.M312671200

Manglik, 2012, Crystal structure of the µ-opioid receptor bound to a morphinan antagonist, Nature, 485, 321, 10.1038/nature10954

Manglik, 2015, Structural insights into the dynamic process of β2-Adrenergic receptor signaling, Cell, 161, 1101, 10.1016/j.cell.2015.04.043

Marsden, 2004, SAD--a normalized structural alignment database: improving sequence-structure alignments, Bioinformatics, 20, 2333, 10.1093/bioinformatics/bth244

Martí-Solano, 2014, A dynamic view of molecular switch behavior at serotonin receptors: implications for functional selectivity, PLOS ONE, 9, 10.1371/journal.pone.0109312

Massink, 2015, Sodium ion binding pocket mutations and adenosine A2A receptor function, Molecular Pharmacology, 87, 305, 10.1124/mol.114.095737

Masuho, 2015, Distinct profiles of functional discrimination among G proteins determine the actions of G protein-coupled receptors, Science Signaling, 8, 10.1126/scisignal.aab4068

Masureel, 2018, Structural insights into binding specificity, efficacy and Bias of a β2AR partial agonist, Nature Chemical Biology, 14, 1059, 10.1038/s41589-018-0145-x

May, 2007, Allosteric modulation of G protein-coupled receptors, Annual Review of Pharmacology and Toxicology, 47, 1, 10.1146/annurev.pharmtox.47.120505.105159

McCorvy, 2018, Structure-inspired design of β-arrestin-biased ligands for aminergic GPCRs, Nature Chemical Biology, 14, 126, 10.1038/nchembio.2527

Miao, 2013, Activation and dynamic network of the M2 muscarinic receptor, PNAS, 110, 10982, 10.1073/pnas.1309755110

Miao, 2016, Accelerated structure-based design of chemically diverse allosteric modulators of a muscarinic G protein-coupled receptor, PNAS, 113, E5675, 10.1073/pnas.1612353113

Mirny, 1999, Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function, Journal of Molecular Biology, 291, 177, 10.1006/jmbi.1999.2911

Munk, 2019, An online resource for GPCR structure determination and analysis, Nature Methods, 16, 151, 10.1038/s41592-018-0302-x

Nagiri, 2019, Crystal structure of human endothelin ETBb receptor in complex with peptide inverse agonist IRL2500, Communications Biology, 2, 10.1038/s42003-019-0482-7

Napier, 2015, Mutational analysis of the Rhodopsin gene in sector retinitis pigmentosa, Ophthalmic Genetics, 36, 239, 10.3109/13816810.2014.958862

Nehmé, 2017, Mini-G proteins: novel tools for studying GPCRs in their active conformation, PLOS ONE, 12, 10.1371/journal.pone.0175642

Ngo, 2017, Orphan receptor ligand discovery by pickpocketing pharmacological neighbors, Nature Chemical Biology, 13, 235, 10.1038/nchembio.2266

Nygaard, 2009, Ligand binding and micro-switches in 7tm receptor structures, Trends in Pharmacological Sciences, 30, 249, 10.1016/j.tips.2009.02.006

Nygaard, 2013, The dynamic process of β(2)-adrenergic receptor activation, Cell, 152, 532, 10.1016/j.cell.2013.01.008

Okada, 2001, Activation of rhodopsin: new insights from structural and biochemical studies, Trends in Biochemical Sciences, 26, 318, 10.1016/S0968-0004(01)01799-6

Okashah, 2019, Variable G protein determinants of GPCR coupling selectivity, PNAS, 116, 12054, 10.1073/pnas.1905993116

Onaran, 2014, What is biased efficacy? defining the relationship between intrinsic efficacy and free energy coupling, Trends in Pharmacological Sciences, 35, 639, 10.1016/j.tips.2014.09.010

Ortiz Zacarías, 2018, Intracellular receptor modulation: novel approach to target GPCRs, Trends in Pharmacological Sciences, 39, 547, 10.1016/j.tips.2018.03.002

Oswald, 2016, Intracellular allosteric antagonism of the CCR9 receptor, Nature, 540, 462, 10.1038/nature20606

Pándy-Szekeres, 2018, GPCRdb in 2018: adding GPCR structure models and ligands, Nucleic Acids Research, 46, D440, 10.1093/nar/gkx1109

Pardon, 2014, A general protocol for the generation of nanobodies for structural biology, Nature Protocols, 9, 674, 10.1038/nprot.2014.039

Pasel, 2000, Functional characterization of the molecular defects causing nephrogenic diabetes insipidus in eight families, Journal of Clinical Endocrinology & Metabolism, 85, 1703, 10.1210/jc.85.4.1703

Peng, 2018, 5-HT2C receptor structures reveal the structural basis of GPCR polypharmacology, Cell, 172, 719, 10.1016/j.cell.2018.01.001

Popov, 2018, Computational design of thermostabilizing point mutations for G protein-coupled receptors, eLife, 7, 10.7554/eLife.34729

Ragnarsson, 2019, Mutations in the NPxxY motif stabilize pharmacologically distinct conformational states of the α1B- and β2-adrenoceptors, Science Signaling, 12, 10.1126/scisignal.aas9485

Rana, 2001, Genetic variations and polymorphisms of G protein-coupled receptors: functional and therapeutic implications, Annual Review of Pharmacology and Toxicology, 41, 593, 10.1146/annurev.pharmtox.41.1.593

Rasmussen, 2011, Crystal structure of the β2 adrenergic receptor-Gs protein complex, Nature, 477, 549, 10.1038/nature10361

Rasmussen, 2011, Structure of a nanobody-stabilized active state of the β(2) adrenoceptor, Nature, 469, 175, 10.1038/nature09648

Renaud, 2018, Cryo-EM in drug discovery: achievements, limitations and prospects, Nature Reviews Drug Discovery, 17, 471, 10.1038/nrd.2018.77

Robertson, 2018, Structure of the complement C5a receptor bound to the extra-helical antagonist NDT9513727, Nature, 553, 111, 10.1038/nature25025

Rodriguez, 2010, Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors, PNAS, 107, 7787, 10.1073/pnas.0914877107

Rosenbaum, 2007, GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function, Science, 318, 1266, 10.1126/science.1150609

Rosenbaum, 2009, The structure and function of G-protein-coupled receptors, Nature, 459, 356, 10.1038/nature08144

Roth, 2008, Stabilization of the human beta2-adrenergic receptor TM4-TM3-TM5 Helix interface by mutagenesis of Glu122(3.41), a critical residue in GPCR structure, Journal of Molecular Biology, 376, 1305, 10.1016/j.jmb.2007.12.028

Roth, 2017, Discovery of new GPCR ligands to illuminate new biology, Nature Chemical Biology, 13, 1143, 10.1038/nchembio.2490

Sandhu, 2019, Conformational plasticity of the intracellular cavity of GPCR-G-protein complexes leads to G-protein promiscuity and selectivity, PNAS, 116, 11956, 10.1073/pnas.1820944116

Schmid, 2017, Bias factor and therapeutic window correlate to predict safer opioid analgesics, Cell, 171, 1165, 10.1016/j.cell.2017.10.035

Schöneberg, 2007, Learning from the past: evolution of GPCR functions, Trends in Pharmacological Sciences, 28, 117, 10.1016/j.tips.2007.01.001

Schönegge, 2017, Evolutionary action and structural basis of the allosteric switch controlling β2AR functional selectivity, Nature Communications, 8, 10.1038/s41467-017-02257-x

Shao, 2019, Structure of an allosteric modulator bound to the CB1 cannabinoid receptor, Nature Chemical Biology, 15, 1199, 10.1038/s41589-019-0387-2

Shihoya, 2017, X-ray structures of endothelin ETB receptor bound to clinical antagonist bosentan and its analog, Nature Structural & Molecular Biology, 24, 758, 10.1038/nsmb.3450

Shimada, 2019, GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures, Nature Reviews Drug Discovery, 18, 59, 10.1038/nrd.2018.180

Smart, 2018, Validation of ligands in macromolecular structures determined by X-ray crystallography, Acta Crystallographica Section D Structural Biology, 74, 228, 10.1107/S2059798318002541

Smit, 2007, Pharmacogenomic and structural analysis of constitutive g protein-coupled receptor activity, Annual Review of Pharmacology and Toxicology, 47, 53, 10.1146/annurev.pharmtox.47.120505.105126

Smith, 2018, Biased signalling: from simple switches to allosteric microprocessors, Nature Reviews Drug Discovery, 17, 243, 10.1038/nrd.2017.229

Solt, 2017, Insight into partial agonism by observing multiple equilibria for ligand-bound and Gs-mimetic nanobody-bound β1-adrenergic receptor, Nature Communications, 8, 10.1038/s41467-017-02008-y

Sounier, 2015, Propagation of conformational changes during μ-opioid receptor activation, Nature, 524, 375, 10.1038/nature14680

Spehr, 2009, Olfactory receptors: g protein-coupled receptors and beyond, Journal of Neurochemistry, 109, 1570, 10.1111/j.1471-4159.2009.06085.x

Stauch, 2018, Serial femtosecond crystallography of G Protein-Coupled receptors, Annual Review of Biophysics, 47, 377, 10.1146/annurev-biophys-070317-033239

Staus, 2016, Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation, Nature, 535, 448, 10.1038/nature18636

Sung, 2016, Intramolecular allosteric communication in dopamine D2 receptor revealed by evolutionary amino acid covariation, PNAS, 113, 3539, 10.1073/pnas.1516579113

Tan, 2018, Biased ligands of G Protein-Coupled receptors (GPCRs): Structure–Functional Selectivity Relationships (SFSRs) and Therapeutic Potential, Journal of Medicinal Chemistry, 61, 9841, 10.1021/acs.jmedchem.8b00435

Tao, 2006, Inactivating mutations of G protein-coupled receptors and diseases: structure-function insights and therapeutic implications, Pharmacology & Therapeutics, 111, 949, 10.1016/j.pharmthera.2006.02.008

Tao, 2008, Constitutive activation of G protein-coupled receptors and diseases: insights into mechanisms of activation and therapeutics, Pharmacology & Therapeutics, 120, 129, 10.1016/j.pharmthera.2008.07.005

Tehan, 2014, Unifying family A GPCR theories of activation, Pharmacology & Therapeutics, 143, 51, 10.1016/j.pharmthera.2014.02.004

Thal, 2018, Structural insights into G-protein-coupled receptor allostery, Nature, 559, 45, 10.1038/s41586-018-0259-z

The UniProt Consortium, 2017, UniProt: the universal protein knowledgebase, Nucleic Acids Research, 45, D158, 10.1093/nar/gkw1099

Thompson, 2014, G protein-coupled receptor mutations and human genetic disease, Methods in Molecular Biology, 1175, 153, 10.1007/978-1-4939-0956-8_8

Tian, 2017, Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics, Chemical Reviews, 117, 186, 10.1021/acs.chemrev.6b00084

Trzaskowski, 2012, Action of molecular switches in GPCRs--theoretical and experimental studies, Current Medicinal Chemistry, 19, 1090, 10.2174/092986712799320556

Tsai, 2018, Crystal structure of rhodopsin in complex with a mini-Go sheds light on the principles of G protein selectivity, Science Advances, 4, 10.1126/sciadv.aat7052

Van Eps, 2018, Gi-and Gs-coupled GPCRs show different modes of G-protein binding, PNAS, 115, 2383, 10.1073/pnas.1721896115

Vass, 2018, Chemical Diversity in the G Protein-Coupled Receptor Superfamily, Trends in Pharmacological Sciences, 39, 494, 10.1016/j.tips.2018.02.004

Vassart, 2011, G protein-coupled receptors: mutations and endocrine diseases, Nature Reviews Endocrinology, 7, 362, 10.1038/nrendo.2011.20

Venkatakrishnan, 2013, Molecular signatures of G-protein-coupled receptors, Nature, 494, 185, 10.1038/nature11896

Venkatakrishnan, 2016, Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region, Nature, 536, 484, 10.1038/nature19107

Venkatakrishnan, 2019, Diverse GPCRs exhibit conserved water networks for stabilization and activation, PNAS, 116, 3288, 10.1073/pnas.1809251116

Verdonk, 2003, Improved protein-ligand docking using GOLD, Proteins: Structure, Function, and Bioinformatics, 52, 609, 10.1002/prot.10465

Vickery, 2018, Intracellular Transfer of Na+ in an Active-State G-Protein-Coupled Receptor, Structure, 26, 171, 10.1016/j.str.2017.11.013

Wang, 2017, Accurate de novo prediction of protein contact map by ultra-deep learning model, PLOS Computational Biology, 13, 10.1371/journal.pcbi.1005324

Warne, 2009, Development and crystallization of a minimal thermostabilised G protein-coupled receptor, Protein Expression and Purification, 65, 204, 10.1016/j.pep.2009.01.014

Weierstall, 2014, Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography, Nature Communications, 5, 10.1038/ncomms4309

Weis, 2018, The molecular basis of G Protein-Coupled receptor activation, Annual Review of Biochemistry, 87, 897, 10.1146/annurev-biochem-060614-033910

Wescott, 2016, Signal transmission through the CXC chemokine receptor 4 (CXCR4) transmembrane helices, PNAS, 113, 9928, 10.1073/pnas.1601278113

Whalen, 2011, Therapeutic potential of β-arrestin- and G protein-biased agonists, Trends in Molecular Medicine, 17, 126, 10.1016/j.molmed.2010.11.004

White, 2018, Structural connection between activation microswitch and allosteric sodium site in GPCR signaling, Structure, 26, 259, 10.1016/j.str.2017.12.013

Wingler, 2019, Angiotensin analogs with divergent Bias stabilize distinct receptor conformations, Cell, 176, 468, 10.1016/j.cell.2018.12.005

Wootten, 2016, The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonism, Cell, 165, 1632, 10.1016/j.cell.2016.05.023

Wootten, 2018, Mechanisms of signalling and biased agonism in G protein-coupled receptors, Nature Reviews Molecular Cell Biology, 19, 638, 10.1038/s41580-018-0049-3

Wu, 2012, Structure of the human κ-opioid receptor in complex with JDTic, Nature, 485, 327, 10.1038/nature10939

Wu, 2019, Protein Allostery in Drug Discovery, 225, 10.1007/978-981-13-8719-7_10

Yang, 2018, Allosteric mechanisms underlie GPCR signaling to SH3-domain proteins through arrestin, Nature Chemical Biology, 14, 876, 10.1038/s41589-018-0115-3

Yao, 2009, The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex, PNAS, 106, 9501, 10.1073/pnas.0811437106

Ye, 2016, Activation of the A2A adenosine G-protein-coupled receptor by conformational selection, Nature, 533, 265, 10.1038/nature17668

Ye, 2018, Mechanistic insights into allosteric regulation of the A2AAdenosine G protein-coupled receptor by physiological cations, Nature Communications, 9, 10.1038/s41467-018-03314-9

Yuan, 2013, The role of water and sodium ions in the activation of the μ-opioid receptor, Angewandte Chemie International Edition, 52, 10112, 10.1002/anie.201302244

Yuan, 2014, Activation of G-protein-coupled receptors correlates with the formation of a continuous internal water pathway, Nature Communications, 5, 10.1038/ncomms5733

Yuan, 2016, A gating mechanism of the serotonin 5-HT3 receptor, Structure, 24, 816, 10.1016/j.str.2016.03.019

Zerbino, 2018, Ensembl 2018, Nucleic Acids Research, 46, D754, 10.1093/nar/gkx1098

Zhang, 2015, Structure of the angiotensin receptor revealed by serial femtosecond crystallography, Cell, 161, 833, 10.1016/j.cell.2015.04.011

Zhang, 2017, Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein, Nature, 546, 248, 10.1038/nature22394

Zheng, 2016, Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists, Nature, 540, 458, 10.1038/nature20605

Zhou, 2017, Identification of phosphorylation codes for arrestin recruitment by G protein-coupled receptors, Cell, 170, 457, 10.1016/j.cell.2017.07.002

Zhou Q. 2019. RRCS (Residue-residue contact score). GitHub. 2f9a555. https://github.com/zhaolabSHT/RRCS.