Evidence map›Paper›PMID 37053086›Full record

ArticleeLife2023

Zinc activation of OTOP proton channels identifies structural elements of the gating apparatus.

Bochuan Teng, Joshua P Kaplan, Ziyu Liang, Kevin Saejin Chyung, Marcel P Goldschen-Ohm, Emily R Liman

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Molecular and structural basis of the dual regulation of the polycystin-2 ion channel by small-molecule ligands.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Transcendent Aspects of Proton Channels.Annual review of physiology · 2024
    Review
  9. Article
  10. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Bochuan Teng *Section of Neurobiology, Department of Biological Sciences, University of Southern California, Los Angeles, United States.ORCID 0000-0001-7918-484X
Joshua P Kaplan *Section of Neurobiology, Department of Biological Sciences, University of Southern California, Los Angeles, United States.ORCID 0000-0001-5064-2130
Ziyu LiangSection of Neurobiology, Department of Biological Sciences, University of Southern California, Los Angeles, United States.
Kevin Saejin ChyungSection of Neurobiology, Department of Biological Sciences, University of Southern California, Los Angeles, United States.
Marcel P Goldschen-OhmUniversity of Texas at Austin, Department of Neuroscience, Austin, United States.ORCID 0000-0003-1466-9808
Emily R LimanSection of Neurobiology, Department of Biological Sciences, University of Southern California, Los Angeles, United States.ORCID 0000-0003-4765-5496
University of Southern California · USThe University of Texas at Austin · US

Funding

Cellular Physiology of Otopetrin Proton ChannelsR01GM131234 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LIMAN, EMILY R. · 2019 to 2022
$1.4M
Mechanisms of stepwise activation and drug-modulation in ligand-gated ion channels.R01GM148591 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI GOLDSCHEN-OHM, MARCEL PAZ · 2022 to 2025
$1.3M
NIGMS NIH HHS R01 GM131234NIGMS NIH HHS R01 GM148591
6 · The paper itself

Abstract

Otopetrin proteins (OTOPs) form proton-selective ion channels that are expressed in diverse cell types where they mediate detection of acids or regulation of pH. In vertebrates there are three family members: OTOP1 is required for formation of otoconia in the vestibular system and it forms the receptor for sour taste, while the functions of OTOP2 and OTOP3 are not yet known. Importantly, the gating mechanisms of any of the OTOP channels are not well understood. Here, we show that zinc (Zn

Indexed as

ProtonsZincAcidsAnimalsMembrane ProteinsMiceMutationVertebratesAcidsMembrane Proteinsotopetrin 1 protein, mouseProtonsZincacidligand gatingmolecular biophysicsnoneotopetrinproton channelsour tastestructural biologyzinc

Identifiers

PMID37053086
PMCPMC10101688
OpenAlexW4364350983

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.