ArticleCommunications biology2025
Preferential allosteric modulation of Otop1 channels by small molecule compounds.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Mechanistic insights into taste modulation ofFood chemistry: X · 2026Article
- Functional characterization of the bovine sour taste receptor Otopetrin 1 (OTOP1) in response to dietary and ruminal acids.Biochemistry and biophysics reports · 2026Article
- Structure-guided discovery of Otopetrin 1 inhibitors reveals druggable binding sites at the intrasubunit interface.Nature 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
11 authors.
Funding
Abstract
The Otopetrin (Otop) proteins, comprising Otop1-3, are proton-gated proton channels with key biological functions. Otop1 acts as a receptor for sour and ammonium salt tastes in mammals, but its gating mechanisms and pharmacology remain poorly understood. Here, we report the functional characterization of three small molecule positive allosteric modulators of Otop1-MFaN, HIMOP, and B2FAMP-that enhance proton gating in a pH-dependent manner, potentiating Otop1 activity under weak acidic but not strong acidic conditions. HIMOP also uniquely enhances Otop1's alkali gating. These modulators preferentially target Otop1, sparing Otop2 and Otop3, and other ion channels. MFaN activates Otop1 while preserving its core biophysical and pharmacological properties by associating with key residues on the channel's S5-6 and S11-12 loops, including a crucial arginine (R554) essential for Zn
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.