Fluorescence Studies of the Acetylcholine Receptor: Structure and Dynamics in Membranes and Cells
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Summary
A series of biophysical studies on the AChR protein is reviewed, with particular focus on the interactions of the macromolecule with its lipid microenvironment, and the application of site-specific labeling and steady-state fluorescence spectroscopy to probe the location of A ChR membrane-embedded domains.
- Type
- article
- Published
- 2001-12-01
- Cited by
- 8
- References
- 12
- OpenAlex
- https://openalex.org/W525846
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:41440382
Keywords
Chemistry
References
- Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
- Blocker protection in the pore of a voltage-gated K+ channel and its structural implications
- Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
- Physical state of bulk and protein-associated lipid in nicotinic acetylcholine receptor-rich membrane studied by laurdan generalized polarization and fluorescence energy transfer.
- Nicotinic acetylcholine receptor channels are influenced by the physical state of their membrane environment.
- Spatial structure of the M2 transmembrane segment of the nicotinic acetylcholine receptor α‐subunit
- A minimum number of lipids are required to support the functional properties of the nicotinic acetylcholine receptor.
- The Nicotinic Acetylcholine Receptor
Cited by
- FRET-based luminescence sensors for carbohydrates and glycoproteins analysis
- Interferences in Fluo-3 based ion-flux assays for ligand-gated-ion channels
- Identification of threonine 422 in transmembrane domain alpha M4 of the nicotinic acetylcholine receptor as a possible site of interaction with hydrocortisone.
- Phospholipid phase transitions in homogeneous nanometer scale bilayer discs
- U18666A, a cholesterol‐inhibition agent, modulates human neuronal nicotinic acetylcholine receptors heterologously expressed in SH‐EP1 cell line
- Structural basis for lipid modulation of nicotinic acetylcholine receptor function.
- Lipid matters: nicotinic acetylcholine receptor-lipid interactions (Review)
- Cholesterol modulates the organization of the gammaM4 transmembrane domain of the muscle nicotinic acetylcholine receptor.
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