ArticleBiophysical journal2008
Stoichiometric pore mutations of the GABAAR reveal a pattern of hydrogen bonding with picrotoxin.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Picrotoxin Delineates Different Transport Configurations for Malate and γ Aminobutyric Acid through TaALMT1.Biology · 2022Article
- Physiological markers of rapid antidepressant effects of allopregnanolone.Journal of neuroendocrinology · 2022Review
- Insect RDL Receptor Models for Virtual Screening: Impact of the Template Conformational State in Pentameric Ligand-Gated Ion Channels.ACS omega · 2022Article
- Perspective on the Relationship between GABAA Receptor Activity and the Apparent Potency of an Inhibitor.Current neuropharmacology · 2022Article
- Identification of the Functional Binding Site for the Convulsant Tetramethylenedisulfotetramine in the Pore of theMolecular pharmacology · 2021Article
- Pharmacological and Biophysical Characteristics of Picrotoxin-Resistant, δSubunit-Containing GABAFrontiers in synaptic neuroscience · 2021Article
- Mild chronic perturbation of inhibition severely alters hippocampal function.Scientific reports · 2019Article
- Chemogenetic Isolation Reveals Synaptic Contribution of δ GABAThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Probing GABANeuropharmacology · 2018Article
- Side chain flexibility and the pore dimensions in the GABAA receptor.Journal of computer-aided molecular design · 2016Article
- Positive and Negative Allosteric Modulation of an α1β3γ2 γ-Aminobutyric Acid Type A (GABAA) Receptor by Binding to a Site in the Transmembrane Domain at the γ+-β- Interface.The Journal of biological chemistry · 2015Article
- Article
- Phenylalanine in the pore of the Erwinia ligand-gated ion channel modulates picrotoxinin potency but not receptor function.Biochemistry · 2014Article
- Methods for recording and measuring tonic GABAA receptor-mediated inhibition.Frontiers in neural circuits · 2013Review
- Mixed antagonistic effects of the ginkgolides at recombinant human ρ1 GABAC receptors.Neuropharmacology · 2012Article
- A single amino acid determines the toxicity of Ginkgo biloba extracts.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Influences on blockade by t-butylbicyclo-phosphoro-thionate of GABA(A) receptor spontaneous gating, agonist activation and desensitization.The Journal of physiology · 2012Article
- Cys-loop receptor channel blockers also block GLIC.Biophysical journal · 2011Article
- Binding sites for bilobalide, diltiazem, ginkgolide, and picrotoxinin at the 5-HT3 receptor.Molecular pharmacology · 2011Article
- Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Picrotoxin (PTX) is a noncompetitive antagonist of many ligand-gated ion channels, with a site of action believed to be within the ion-conducting pore. In the A-type gamma-aminobutyric acid receptor, a threonine residue in the second transmembrane domain is of particular importance for the binding of, and ultimate inhibition by, PTX. To better understand the relationship between this residue and the PTX molecule, we mutated this threonine residue to serine, valine, and tyrosine to change the structural and biochemical characteristics at this location. The known subunit stoichiometry of the A-type gamma-aminobutyric acid receptor allowed us to create receptors with anywhere from zero to five mutations. With an increasing number of mutated subunits, each amino acid substitution revealed a unique pattern of changes in PTX sensitivity, ultimately encompassing sensitivity shifts over several orders of magnitude. The electrophysiological data on PTX-mediated block, and supporting modeling and docking studies, provide evidence that an interaction between the PTX molecule and three adjacent uncharged polar amino acids at this position of the pore are crucial for PTX-mediated inhibition.
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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.