ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011
Single-channel and structural foundations of neuronal α7 acetylcholine receptor potentiation.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 71 citations in OpenAlex.
- Symmetry-adapted Markov state models of closing, opening, and desensitizing in α 7 nicotinic acetylcholine receptors.Nature communications · 2024Article
- Novel interplay between agonist and calcium binding sites modulates drug potentiation of α7 acetylcholine receptor.Cellular and molecular life sciences : CMLS · 2024Article
- Article
- Cannabidiol as a modulator of α7 nicotinic receptors.Cellular and molecular life sciences : CMLS · 2022Article
- Differential interactions of resting, activated, and desensitized states of the α7 nicotinic acetylcholine receptor with lipidic modulators.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Alkaloid ligands enable function of homomeric human α10 nicotinic acetylcholine receptors.Frontiers in pharmacology · 2022Article
- Deepening the understanding of CNVs on chromosome 15q11-13 by using hiPSCs: An overview.Frontiers in cell and developmental biology · 2022Review
- Homomeric and Heteromeric α7 Nicotinic Acetylcholine Receptors in Health and Some Central Nervous System Diseases.Membranes · 2021Review
- Article
- The role of nicotinic cholinergic neurotransmission in delusional thinking.NPJ schizophrenia · 2020Review
- Functional Tolerance to Cysteine Mutations in Human α7 Nicotinic Acetylcholine Receptors.ACS chemical neuroscience · 2020Article
- Article
- Molecular Modulation of Human α7 Nicotinic Receptor by Amyloid-β Peptides.Frontiers in cellular neuroscience · 2019Article
- A human-specific, truncated α7 nicotinic receptor subunit assembles with full-length α7 and forms functional receptors with different stoichiometries.The Journal of biological chemistry · 2018Article
- Molecular function of the novel α7β2 nicotinic receptor.Cellular and molecular life sciences : CMLS · 2018Article
- Nicotinic acetylcholine receptors at the single-channel level.British journal of pharmacology · 2018Review
- The dual-gate model for pentameric ligand-gated ion channels activation and desensitization.The Journal of physiology · 2018Review
- Shared and unique aspects of ligand- and voltage-gated ion-channel gating.The Journal of physiology · 2018Article
- Molecular function of α7 nicotinic receptors as drug targets.The Journal of physiology · 2018Review
- An allosteric link connecting the lipid-protein interface to the gating of the nicotinic acetylcholine receptor.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Potentiation of neuronal nicotinic acetylcholine receptors by exogenous ligands is a promising strategy for treatment of neurological disorders including Alzheimer's disease and schizophrenia. To gain insight into molecular mechanisms underlying potentiation, we examined ACh-induced single-channel currents through the human neuronal α7 acetylcholine receptor in the presence of the α7-specific potentiator PNU-120596 (PNU). Compared to the unusually brief single-channel opening episodes elicited by agonist alone, channel opening episodes in the presence of agonist and PNU are dramatically prolonged. Dwell time analysis reveals that PNU introduces two novel components into open time histograms, indicating at least two degrees of PNU-induced potentiation. Openings of the longest potentiated class coalesce into clusters whose frequency and duration change over a narrow range of PNU concentration. At PNU concentrations approaching saturation, these clusters last up to several minutes, prolonging the submillisecond α7 opening episodes by several orders of magnitude. Mutations known to reduce PNU potentiation at the whole-cell level still give rise to multisecond-long single-channel clusters. However mutation of five residues lining a cavity within each subunit's transmembrane domain abolishes PNU potentiation, defining minimal structural determinants of PNU potentiation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.