| scholarly article | Q13442814 |
| P50 | author | Stefano Costanzi | Q37381929 |
| P2093 | author name string | Marvin C Gershengorn | |
| Irina G Tikhonova | |||
| Chi Shing Sum | |||
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| P433 | issue | 6 | |
| P407 | language of work or name | English | Q1860 |
| P1104 | number of pages | 8 | |
| P304 | page(s) | 3529-3536 | |
| P577 | publication date | 2008-12-08 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Two arginine-glutamate ionic locks near the extracellular surface of FFAR1 gate receptor activation | |
| P478 | volume | 284 |
| Q24338456 | A novel antidiabetic drug, fasiglifam/TAK-875, acts as an ago-allosteric modulator of FFAR1 |
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| Q35080498 | Extracellular loop 2 of the free fatty acid receptor 2 mediates allosterism of a phenylacetamide ago-allosteric modulator |
| Q39192856 | Free Fatty Acid Receptor 1 (FFAR1) as an Emerging Therapeutic Target for Type 2 Diabetes Mellitus: Recent Progress and Prevailing Challenges |
| Q36327956 | Free fatty acid receptors: emerging targets for treatment of diabetes and its complications |
| Q35766268 | Free fatty acid receptors: structural models and elucidation of ligand binding interactions |
| Q41883243 | From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs). |
| Q24301044 | High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875 |
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| Q94486019 | In vivo pharmacokinetic study and oral glucose tolerance test of sulfoxide analogs of GPR40 agonist TAK-875 |
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| Q35592107 | Signaling-sensitive amino acids surround the allosteric ligand binding site of the thyrotropin receptor |
| Q27865233 | The action and mode of binding of thiazolidinedione ligands at free fatty acid receptor 1 |
| Q35550563 | The extracellular loop 2 (ECL2) of the human histamine H4 receptor substantially contributes to ligand binding and constitutive activity |
| Q34181416 | Third extracellular loop (EC3)-N terminus interaction is important for seven-transmembrane domain receptor function: implications for an activation microswitch region |
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