ArticleeLife2019
TMEM266 is a functional voltage sensor regulated by extracellular Zn
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Voltage sensors.Molecular pharmacology · 2025Review
- Primary aldosteronism: molecular medicine meets public health.Nature reviews. Nephrology · 2023Review
- Voltage-Gated Proton Channels in the Tree of Life.Biomolecules · 2023Review
- Unexpected expansion of the voltage-gated proton channel family.The FEBS journal · 2023Article
- Retrotransposon insertions associated with risk of neurologic and psychiatric diseases.EMBO reports · 2023Article
- Multiple mechanisms contribute to fluorometry signals from the voltage-gated proton channel.Communications biology · 2022Article
- Discovery and characterization of HeLife · 2021Article
- Article
- Voltage-gated proton channels from fungi highlight role of peripheral regions in channel activation.Communications biology · 2021Article
- Serious neonatal morbidities are associated with differences in DNA methylation among very preterm infants.Clinical epigenetics · 2020Article
- Hydrophobic gasket mutation produces gating pore currents in closed human voltage-gated proton channels.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 2 countries.
Funding
Abstract
Voltage-activated ion channels contain S1-S4 domains that sense membrane voltage and control opening of ion-selective pores, a mechanism that is crucial for electrical signaling. Related S1-S4 domains have been identified in voltage-sensitive phosphatases and voltage-activated proton channels, both of which lack associated pore domains. hTMEM266 is a protein of unknown function that is predicted to contain an S1-S4 domain, along with partially structured cytoplasmic termini. Here we show that hTMEM266 forms oligomers, undergoes both rapid (µs) and slow (ms) structural rearrangements in response to changes in voltage, and contains a Zn
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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.