ArticleProceedings of the National Academy of Sciences of the United States of America2003
Conformation-dependent hydrophobic photolabeling of the nicotinic receptor: electrophysiology-coordinated photochemistry and mass spectrometry.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 51 citations in OpenAlex.
- Photoaffinity labeling of nicotinic receptors: diversity of drug binding sites!Journal of molecular neuroscience : MN · 2014Review
- Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions.PLoS biology · 2013Article
- Validation of membrane protein topology models by oxidative labeling and mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- The energetic consequences of loop 9 gating motions in acetylcholine receptor-channels.The Journal of physiology · 2012Article
- Effects of lipid-analog detergent solubilization on the functionality and lipidic cubic phase mobility of the Torpedo californica nicotinic acetylcholine receptor.The Journal of membrane biology · 2011Article
- Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
- Allosteric activation mechanism of the cys-loop receptors.Acta pharmacologica Sinica · 2009Review
- Structural rearrangements in loop F of the GABA receptor signal ligand binding, not channel activation.Biophysical journal · 2009Article
- Structural mechanisms underlying benzodiazepine modulation of the GABA(A) receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Photo-activated azi-etomidate, a general anesthetic photolabel, irreversibly enhances gating and desensitization of gamma-aminobutyric acid type A receptors.Anesthesiology · 2008Article
- Nanosecond-timescale conformational dynamics of the human alpha7 nicotinic acetylcholine receptor.Biophysical journal · 2007Article
- Targeted molecular dynamics study of C-loop closure and channel gating in nicotinic receptors.PLoS computational biology · 2006Article
- Modulating inhibitory ligand-gated ion channels.The AAPS journal · 2006Review
- Cholesterol interacts with transmembrane alpha-helices M1, M3, and M4 of the Torpedo nicotinic acetylcholine receptor: photolabeling studies using [3H]Azicholesterol.Biochemistry · 2006Article
- Time-resolved measurement of state-specific P2X2 ion channel cytosolic gating motions.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We characterized the differential accessibility of the nicotinic acetylcholine receptor alpha1 subunit in the open, closed, and desensitized states by using electrophysiology-coordinated photolabeling by several lipophilic probes followed by mass spectrometric analysis. Voltage-clamped oocytes expressing receptors were preincubated with one of the lipophilic probes and were continually exposed to acetylcholine; UV irradiation was applied during 500-ms pulses to + 40 or to -140 mV (which produced closed or approximately 50% open receptors, respectively). In the open state, there was specific probe incorporation within the N-terminal domain at residues that align with the beta8-beta9 loop of the acetylcholine-binding protein. In the closed state, probe incorporation was identified at several sites of the N-terminal domain within the conserved cysteine loop (residues 128-142), the cytoplasmic loop (M3-M4), and M4. The labeling pattern in the M4 region is consistent with previous results, further defining the lipid-exposed face of this transmembrane alpha-helix. These results show regions within the N-terminal domain that are involved in gating-dependent conformational shifts, confirm that the cysteine loop resides at or near the protein-membrane interface, and show that segments of the M3-M4 loop are near to the lipid bilayer.
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