Cholesterol modulates the organization of the gammaM4 transmembrane domain of the muscle nicotinic acetylcholine receptor.
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Summary
The presence of a cholesterol-rich, ordered POPC phase drives the organization of peptide-enriched patches, in which the gammaM4 peptide occupies approximately 30% of the patch area.
- Type
- article
- Published
- 2004-04-01
- Cited by
- 52
- References
- 73
- Access
- Open access
- OpenAlex
- https://openalex.org/W2150437316
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:18958886
Keywords
POPC, Chemistry, Peptide, Biophysics, Lipid bilayer
References
- Fluorescence Studies of the Acetylcholine Receptor: Structure and Dynamics in Membranes and Cells
- The Physical Chemistry of Lipids
- Principles and Applications
- Resonance Energy Transfer: Theory and Data
- Molecular Fluorescence: Principles and Applications
- Kinetic enzymic method for automated determination of total cholesterol in serum.
- The steroid promegestone is a noncompetitive antagonist of the Torpedo nicotinic acetylcholine receptor that interacts with the lipid-protein interface.
- Diffusion-controlled reactions in two-dimensional fluids: discussion of measurements of lateral diffusion of lipids in biological membranes
- Translational diffusion of acetylcholine receptor (monomeric and dimeric forms) of Torpedo marmorata reconstituted into phospholipid bilayers studied by fluorescence recovery after photobleaching.
- Transverse location of the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene in model lipid bilayer membrane systems by resonance excitation energy transfer.
- Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins.
- Fluorescence energy transfer in two dimensions. A numeric solution for random and nonrandom distributions.
- The time resolved emission spectra of peptide conformers measured by pulsed laser excitation.
- Stabilization of acetylcholine receptor secondary structure by cholesterol and negatively charged phospholipids in membranes.
- Toward understanding tryptophan fluorescence in proteins.
- Two dimensional diffusion theory: Cylindrical diffusion model applied to fluorescence quenching
- Average membrane penetration depth of tryptophan residues of the nicotinic acetylcholine receptor by the parallax method.
- FTIR analysis of nicotinic acetylcholine receptor secondary structure in reconstituted membranes.
- Fluorescence depolarization by electronic energy transfer in donor–acceptor pairs of like and unlike chromophores
- Liquid-crystalline phases of cholesterol/lipid bilayers as revealed by the fluorescence of trans-parinaric acid.
Cited by
- Structure and dynamics of the gammaM4 transmembrane domain of the acetylcholine receptor in lipid bilayers: insights into receptor assembly and function.
- Organization and dynamics of SNARE proteins in the presynaptic membrane
- FRET analysis of domain formation and properties in complex membrane systems.
- Membrane lipid domains and rafts: current applications of fluorescence lifetime spectroscopy and imaging.
- Distinct γ2 Subunit Domains Mediate Clustering and Synaptic Function of Postsynaptic GABAA Receptors and Gephyrin
- Interaction of the indole class of vacuolar H(+)-ATPase inhibitors with lipid bilayers.
- Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
- The photophysics of a Rhodamine head labeled phospholipid in the identification and characterization of membrane lipid phases.
- Fluorescence and molecular dynamics studies of the acetylcholine receptor γM4 transmembrane peptide in reconstituted systems
- Membrane‐bound peptides from V‐ATPase subunit a do not interact with an indole‐type inhibitor
- U18666A, a cholesterol‐inhibition agent, modulates human neuronal nicotinic acetylcholine receptors heterologously expressed in SH‐EP1 cell line
- Fluorescent sterols as tools in membrane biophysics and cell biology.
- Structural basis for lipid modulation of nicotinic acetylcholine receptor function.
- Alpha-helical transmembrane peptides: a "divide and conquer" approach to membrane proteins.
- Membrane microheterogeneity: Förster resonance energy transfer characterization of lateral membrane domains
- How protein transmembrane segments sense the lipid environment.
- Organization and dynamics of Fas transmembrane domain in raft membranes and modulation by ceramide.
- Is there a preferential interaction between cholesterol and tryptophan residues in membrane proteins?
- Partition profile of the nicotinic acetylcholine receptor in lipid domains upon reconstitution[S]
- Molecular simulation of the effect of cholesterol on lipid-mediated protein-protein interactions.
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