Evidence map›Paper›PMID 23050239›Full record

ArticleWiley interdisciplinary reviews. Membrane transport and signaling2012

Biophysical properties of the voltage gated proton channel H(V)1.

Boris Musset, Thomas Decoursey

Abstract read
In one paragraph

Article in Wiley interdisciplinary reviews. Membrane transport and signaling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Modulators of the Human Voltage-Gated Proton Channel HPharmaceuticals (Basel, Switzerland) · 2025
    Review
  5. Review
  6. The Voltage-Gated Hv1 HInternational journal of molecular sciences · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. On the control of the proton current in the voltage-gated proton channel Hv1.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Molecular Basis of Human Sperm Capacitation.Frontiers in cell and developmental biology · 2018
    Review
  17. The inhibition of voltage-gated HPflugers Archiv : European journal of physiology · 2017
    Article
  18. Review
  19. Review
  20. Consequences of dimerization of the voltage-gated proton channel.Progress in molecular biology and translational science · 2013
    Review
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

2 authors at 1 institution in 1 country.

Boris MussetRush Medical Center, molec. biophysics and physiology, DeCoursey, Thomas; Rush Medical Center.
Thomas Decoursey
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 GM087507
6 · The paper itself

Abstract

The biophysical properties of the voltage gated proton channel (H(V)1) are the key elements of its physiological function. The voltage gated proton channel is a unique molecule that in contrast to all other ion channels is exclusively selective for protons. Alone among proton channels, it has voltage and time dependent gating like other "classical" ion channels. H(V)1 is furthermore a sensor for the pH in the cell and the surrounding media. Its voltage dependence is strictly coupled to the pH gradient across the membrane. This regulation restricts opening of the channel to specific voltages at any given pH gradient, therefore allowing H(V)1 to perform its physiological task in the tissue it is expressed in. For H(V)1 there is no known blocker. The most potent channel inhibitor is zinc (Zn(2+)) which prevents channel opening. An additional characteristic of H(V)1 is its strong temperature dependence of both gating and conductance. In contrast to single-file water filled pores like the gramicidin channel, H(V)1 exhibits pronounced deuterium effects and temperature effects on conduction, consistent with a different conduction mechanism than other ion channels. These properties may be explained by the recent identification of an aspartate in the pore of H(V)1 that is essential to its proton selectivity.

Identifiers

PMID23050239
PMCPMC3462886
OpenAlexW2083944260

What OpenQuestion holds

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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.