ArticleProceedings of the National Academy of Sciences of the United States of America2014
Stoichiometry and specific assembly of Best ion channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Architectural and biochemical advances in understanding microbial COThe Plant journal : for cell and molecular biology · 2026Review
- Bestrophin-like protein 4 is involved in photosynthetic acclimation to light fluctuations in Chlamydomonas.Plant physiology · 2024Article
- Quantitative Single-Molecule Analysis of Ryanodine Receptor 2 Subunit Assembly in Cardiac and Neuronal Tissues.Analytical chemistry · 2024Article
- New horizons for building pyrenoid-based CO2-concentrating mechanisms in plants to improve yields.Plant physiology · 2022Review
- Chloride Channels and Transporters: Roles beyond Classical Cellular Homeostatic pH or Ion Balance in Cancers.Cancers · 2022Review
- Transmembrane topology and oligomeric nature of an astrocytic membrane protein, MLC1.Open biology · 2021Article
- Chloride - The Underrated Ion in Nociceptors.Frontiers in neuroscience · 2020Review
- Functional analyses of heteromeric human PIEZO1 Channels.PloS one · 2018Article
- Organelle-specific single-molecule imaging of α4β2 nicotinic receptors reveals the effect of nicotine on receptor assembly and cell-surface trafficking.The Journal of biological chemistry · 2017Article
- Real-Time Sensing of Single-Ligand Delivery with Nanoaperture-Integrated Microfluidic Devices.ACS omega · 2017Article
- Detecting stoichiometry of macromolecular complexes in live cells using FRET.Nature communications · 2016Article
- A New Splice Variant of Large Conductance Ca2+-activated K+ (BK) Channel α Subunit Alters Human Chondrocyte Function.The Journal of biological chemistry · 2016Article
- Autosomal Recessive Bestrophinopathy Is Not Associated With the Loss of Bestrophin-1 Anion Channel Function in a Patient With a Novel BEST1 Mutation.Investigative ophthalmology & visual science · 2015Article
- Regulation of vascular tone and arterial blood pressure: role of chloride transport in vascular smooth muscle.Pflugers Archiv : European journal of physiology · 2015Review
- Single-Molecule Pull-Down FRET to Dissect the Mechanisms of Biomolecular Machines.Methods in enzymology · 2015Article
- Article
- The bestrophin- and TMEM16A-associated Ca(2+)- activated Cl(–) channels in vascular smooth muscles.Channels (Austin, Tex.) · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Human Bestrophin 1 (hBest1) is a calcium-activated chloride channel that regulates neuronal excitability, synaptic activity, and retinal homeostasis. Mutations in hBest1 cause the autosomal-dominant Best macular dystrophy (BMD). Because hBest1 mutations cause BMD, but a knockout does not, we wondered if hBest1 mutants exert a dominant negative effect through interaction with other calcium-activated chloride channels, such as hBest2, 3, or 4, or transmembrane member 16A (TMEM16A), a member of another channel family. The subunit architecture of Best channels is debated, and their ability to form heteromeric channel assemblies is unclear. Using single-molecule subunit analysis, we find that each of hBest1, 2, 3, and 4 forms a homotetrameric channel. Despite considerable conservation among hBests, hBest1 has little or no interaction with other hBests or mTMEM16A. We identify the domain responsible for assembly specificity. This domain also plays a role in channel function. Our results indicate that Best channels preferentially self-assemble into homotetramers.
Indexed as
Identifiers
What OpenQuestion holds
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.