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Biophysical Journal, ISSN 0006-3495, 02/2016, Volume 110, Issue 3, pp. 395a - 395a
Journal Article
Political Science Quarterly, ISSN 0032-3195, 06/2012, Volume 127, Issue 2, pp. 315 - 316
Journal Article
Methods in molecular biology (Clifton, N.J.), ISSN 1064-3745, 2010, Volume 654, pp. 141 - 168
G protein-coupled receptors (GPCRs) constitute a highly diverse and ubiquitous family of integral membrane proteins, transmitting signals inside the cells in... 
Fluorescence Recovery After Photobleaching | Membrane Proteins - chemistry | Crystallography | Receptors, G-Protein-Coupled - chemistry | Index Medicus
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2018, Volume 115, Issue 50, p. 12733
brane to intracellular binding sites for partners such as G proteins and arrestins. This signaling process is related to dynamic equilibria in conformational... 
Proteins | Signaling | Adenosine | Nuclear magnetic resonance--NMR | Spectrum analysis | Proteomics | Activation | Qualitative analysis | Receptor mechanisms | Intracellular | Binding sites
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 02/2015, Volume 40, Issue 2, p. 79
  Traditionally, G protein-coupled receptor (GPCR) activity has been characterized by ligand properties including affinity (...), potency (...), efficacy... 
Molecules | Membranes | Protein folding | Glycoproteins | T cell receptors
Journal Article
Journal Article
Advances in Health Sciences Education, ISSN 1382-4996, 03/2019, Volume 24, Issue 1, pp. 141 - 150
Journal Article
Science, ISSN 0036-8075, 2/2012, Volume 335, Issue 6070, pp. 851 - 855
Journal Article
Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6091, pp. 232 - 236
Pharmacological responses of G protein-coupled receptors (GPCRs) can be fine-tuned by allosteric modulators. Structural studies of such effects have been... 
Molecules | Receptors | Sodium | Molecular structure | REPORTS | Lipids | Ligands | Cell membranes | Cholesterols | Water channels | Crystal structure | ANGSTROM CRYSTAL-STRUCTURE | COMPLEX | ANTAGONIST | OPIOID RECEPTOR | MULTIDISCIPLINARY SCIENCES | RHODOPSIN | PROTEIN-COUPLED RECEPTORS | ADENOSINE A(2A) RECEPTOR | ALPHA-2-ADRENERGIC RECEPTORS | MODULATION | MUSCARINIC ACETYLCHOLINE-RECEPTOR | Allosteric Regulation | Humans | Crystallography, X-Ray | Adenosine A2 Receptor Agonists - metabolism | Recombinant Fusion Proteins - metabolism | Cholesterol - chemistry | Adenosine A2 Receptor Antagonists - metabolism | Lipids - chemistry | Lipid Bilayers | Sodium - analysis | HEK293 Cells | Protein Engineering | Water - chemistry | Triazines - metabolism | Protein Structure, Secondary | Models, Molecular | Receptor, Adenosine A2A - metabolism | Recombinant Fusion Proteins - chemistry | Triazoles - metabolism | Hydrogen Bonding | Receptor, Adenosine A2A - chemistry | Protein Conformation | Cytochrome b Group - chemistry | Escherichia coli Proteins - chemistry | Chemistry | G proteins | Chemical properties | Research | Receptor-mediated endocytosis | Proteins | Ions | Adenosine | Pharmacology | Index Medicus | Binding | Control | Stabilization | Strategy | Channels | BASIC BIOLOGICAL SCIENCES | STABILIZATION | CLATHRATES | RESOLUTION | ADENOSINE | REGULATIONS | 60 APPLIED LIFE SCIENCES | RESIDUES | SODIUM IONS | LIPIDS | WATER
Journal Article
Science, ISSN 0036-8075, 9/2013, Volume 341, Issue 6152, pp. 1387 - 1390
Journal Article