A Fluorescence Resonance Energy Transfer-based M2 Muscarinic Receptor Sensor Reveals Rapid Kinetics of Allosteric Modulation-Reference-Cited by-同舟云学术

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A Fluorescence Resonance Energy Transfer-based M2 Muscarinic Receptor Sensor Reveals Rapid Kinetics of Allosteric Modulation

Published:2010-03 Issue:12 Volume:285 Page:8793-8800
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Maier-Peuschel Monika,Frölich Nadine,Dees Christian,Hommers Leif G.,Hoffmann Carsten,Nikolaev Viacheslav O.,Lohse Martin J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference43 articles.

1. Structure-Function Studies of Allosteric Agonism at M2Muscarinic Acetylcholine Receptors

2. Allosteric site in M2 acetylcholine receptors: evidence for a major conformational change upon binding of an orthosteric agonist instead of an antagonist

3. Critical Amino Acid Residues of the Common Allosteric Site on the M2 Muscarinic Acetylcholine Receptor: More Similarities than Differences between the Structurally Divergent Agents Gallamine and Bis(ammonio)alkane-Type Hexamethylene-bis-[dimethyl-(3-phthalimidopropyl)ammonium]dibromide

4. Ligands for the common allosteric site of acetylcholine M2-receptors: development and application

5. Atypical Muscarinic Allosteric Modulation: Cooperativity between Modulators and Their Atypical Binding Topology in Muscarinic M2and M2/M5Chimeric Receptors

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5. Novel Xanomeline-Containing Bitopic Ligands of Muscarinic Acetylcholine Receptors: Design, Synthesis and FRET Investigation;Molecules;2023-03-06

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