ArticleNature2014
Structure and insights into the function of a Ca(2+)-activated Cl(-) channel.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 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
142 citing papers in PubMed, 213 citations in OpenAlex.
- An All-Optical Approach to Probe Chloride Transport with a Bright ChlorON.bioRxiv : the preprint server for biology · 2026Article
- Evaluation of the Toxicity and Efficacy of an Adeno-Associated Viral Vector ExpressingHuman gene therapy · 2026Article
- Glial-neuronal crosstalk via GABA signaling: mechanistic insights into neuropsychiatric and neurological pathophysiology.Molecular psychiatry · 2026Review
- Allele-specific suppression of pathogenic bestrophin-1 transcripts by CRISPR/Cas9-mediated genome editing.Genome medicine · 2026Article
- Review
- Gene Therapy Strategies for the Treatment of Bestrophinopathies.International journal of molecular sciences · 2025Review
- Novel BEST1 Variant Characterization in a Large French Cohort in Light of Updated Bestrophin-1 Structure-Function Correlation.Investigative ophthalmology & visual science · 2025Article
- Design and Biological Evaluation of hBest1-Containing Bilayer Nanostructures.Molecules (Basel, Switzerland) · 2025Article
- Clinical and Genetic Features of Autosomal Recessive Bestrophinopathy: A Case Series from a Vietnamese Cohort.Biomedicines · 2025Article
- Structure of the human TWIK-2 potassium channel and its inhibition by pimozide.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryo-EM structures of mouse bestrophin 1 channel in closed and partially open conformations.Molecules and cells · 2025Article
- The pentameric chloride channel BEST1 is activated by extracellular GABA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClJournal of chemical theory and computation · 2025Article
- A quantitative analysis of bestrophin 1 cellular localization in mouse cerebral cortex.Acta physiologica (Oxford, England) · 2025Article
- Neurotransmitter-bound bestrophin channel structures reveal small molecule drug targeting sites for disease treatment.Nature communications · 2024Article
- GAD65 tunes the functions of Best1 as a GABA receptor and a neurotransmitter conducting channel.Nature communications · 2024Article
- Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClbioRxiv : the preprint server for biology · 2024Article
- Knockdown of best1 Gene in Zebrafish Caused Abnormal Neuronal and Skeletal Development - A Subtype of Craniovertebral Junction Malformation?Neurospine · 2024Article
- Cryo-EM structures of pannexin 1 and 3 reveal differences among pannexin isoforms.Nature communications · 2024Article
- Atomic structure of the open SARS-CoV-2 E viroporin.Science advances · 2023Article
82 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Bestrophin calcium-activated chloride channels (CaCCs) regulate the flow of chloride and other monovalent anions across cellular membranes in response to intracellular calcium (Ca(2+)) levels. Mutations in bestrophin 1 (BEST1) cause certain eye diseases. Here we present X-ray structures of chicken BEST1-Fab complexes, at 2.85 Å resolution, with permeant anions and Ca(2+). Representing, to our knowledge, the first structure of a CaCC, the eukaryotic BEST1 channel, which recapitulates CaCC function in liposomes, is formed from a pentameric assembly of subunits. Ca(2+) binds to the channel's large cytosolic region. A single ion pore, approximately 95 Å in length, is located along the central axis and contains at least 15 binding sites for anions. A hydrophobic neck within the pore probably forms the gate. Phenylalanine residues within it may coordinate permeating anions via anion-π interactions. Conformational changes observed near the 'Ca(2+) clasp' hint at the mechanism of Ca(2+)-dependent gating. Disease-causing mutations are prevalent within the gating apparatus.
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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.