Evidence map›Paper›PMID 23589829›Full record

ReviewPhysiological reviews2013

Voltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) family.

Thomas E DeCoursey

Open access · greenAbstract readReview
In one paragraph

Review in Physiological reviews, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed
12.1field-weighted citation impact, top 1% 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

145 citing papers in PubMed, 223 citations in OpenAlex.

  1. Voltage-sensing domains: structural and functional diversity.European biophysics journal : EBJ · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Voltage-gated proton channel Hv1/VSOP regulates reciprocal interactions between F-actin and endosomes in microglia.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Hv1 channel in immune cells and pharmacology.Pharmacological research · 2025
    Review
  10. CaBiomolecules · 2025
    Review
  11. Article
  12. Modular architecture of KEMBO reports · 2025
    Review
  13. Ion channel mutations and cancer.Biochemistry and biophysics reports · 2025
    Review
  14. Fluctuating hydrogen-bond network of the Hv1 ion channel.Computational and structural biotechnology journal · 2025
    Article
  15. Article
  16. Review
  17. Quantitative insights into the mechanism of proton conduction and selectivity for the human voltage-gated proton channel Hv1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Identification of a Novel Structural Class of HJournal of chemical information and modeling · 2024
    Article
  20. Review

85 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Thomas E DeCourseyDept. of Molecular Biophysics and Physiology, Rush University Medical Center HOS-036, 1750 West Harrison, Chicago, IL 60612, USA. tdecours@rush.edu
Rush University Medical Center · US

Funding

Structure-Function Releationships of Voltage-Gated Proton ChannelsR01GM087507 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI DECOURSEY, THOMAS E · 2010 to 2013
$1.2M
NIGMS NIH HHS R01 GM087507NIGMS NIH HHS R01-GM087507
6 · The paper itself

Abstract

Voltage-gated proton channels (H(V)) are unique, in part because the ion they conduct is unique. H(V) channels are perfectly selective for protons and have a very small unitary conductance, both arguably manifestations of the extremely low H(+) concentration in physiological solutions. They open with membrane depolarization, but their voltage dependence is strongly regulated by the pH gradient across the membrane (ΔpH), with the result that in most species they normally conduct only outward current. The H(V) channel protein is strikingly similar to the voltage-sensing domain (VSD, the first four membrane-spanning segments) of voltage-gated K(+) and Na(+) channels. In higher species, H(V) channels exist as dimers in which each protomer has its own conduction pathway, yet gating is cooperative. H(V) channels are phylogenetically diverse, distributed from humans to unicellular marine life, and perhaps even plants. Correspondingly, H(V) functions vary widely as well, from promoting calcification in coccolithophores and triggering bioluminescent flashes in dinoflagellates to facilitating killing bacteria, airway pH regulation, basophil histamine release, sperm maturation, and B lymphocyte responses in humans. Recent evidence that hH(V)1 may exacerbate breast cancer metastasis and cerebral damage from ischemic stroke highlights the rapidly expanding recognition of the clinical importance of hH(V)1.

Indexed as

AnimalsHomeostasisHumansIon Channel GatingIon ChannelsProtonsSignal TransductionIon ChannelsProtons

Identifiers

PMID23589829
PMCPMC3677779
OpenAlexW2167684488

What OpenQuestion holds

Textmetadata
LicenceTDM
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.