ReviewMolecular pharmacology2025
Voltage sensors.
Review in Molecular pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- The four voltage-sensing domains of T-type calcium channels activate near the resting membrane potential.Nature communications · 2026Article
- Differential negative dominance by KCNA2 variants associated with global developmental delay suggests KCNA2 haploinsufficiency in humans.The Journal of physiology · 2026Article
- Two-step voltage-sensor activation of the human KNature communications · 2026Article
- Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2025Review
- A rich conformational palette underlies human CaNature communications · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Widely distributed in all kingdoms of life, voltage sensors in the membrane serve important functions via their movements driven by changes in voltage across the membrane (membrane potential). A voltage sensor domain contains 4 transmembrane segments (S1-S4). The S1-S3 helices form a hydrophobic constriction site (HCS, also known as the gating charge transfer center) that spans roughly one-third of the membrane thickness. Flanked by aqueous vestibules connected to the extracellular solution above the HCS or cytoplasmic solution below the HCS, the HCS forms a gating pore for the S4 segment bearing multiple basic residues. Membrane potential changes cause S4 to move through the HCS in a 3
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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.