Evidence map›Paper›PMID 18801839›Full record

ReviewThe Journal of physiology2008

Voltage-gated proton channels: what's next?

Thomas E DeCoursey

Abstract readReview
In one paragraph

Review in The Journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. A Bioelectronic Platform Modulates pH in Biologically Relevant Conditions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Article
  5. Voltage and pH sensing by the voltage-gated proton channel, HJournal of the Royal Society, Interface · 2018
    Review
  6. Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  7. Taking Electrons out of Bioelectronics: From Bioprotonic Transistors to Ion Channels.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2017
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. The Concise Guide to PHARMACOLOGY 2013/14: ion channels.British journal of pharmacology · 2013
    Article
  14. Review
  15. Review
  16. Article
  17. Biophysical properties of the voltage gated proton channel H(V)1.Wiley interdisciplinary reviews. Membrane transport and signaling · 2012
    Article
  18. Article
  19. Voltage-gated proton channels.Comprehensive Physiology · 2012
    Review
  20. 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

1 author.

Thomas E DeCourseyDepartment of Molecular Biophysics and Physiology, Rush University Medical Center, 1750 W. Harrison, Chicago, IL 60612, USA. tdecours@rush.edu

Funding

VOLTAGE-GATED PROTON CHANNELS IN HUMAN NEUTROPHILSR01HL061437 · NHLBI · RUSH UNIVERSITY MEDICAL CENTER · PI DECOURSEY, THOMAS E · 2000 to 2008
$2.6M
NHLBI NIH HHS HL-61437NHLBI NIH HHS R01 HL061437
6 · The paper itself

Abstract

This review is an attempt to identify and place in context some of the many questions about voltage-gated proton channels that remain unsolved. As the gene was identified only 2 years ago, the situation is very different than in fields where the gene has been known for decades. For the proton channel, most of the obvious and less obvious structure-function questions are still wide open. Remarkably, the proton channel protein strongly resembles the voltage-sensing domain of many voltage-gated ion channels, and thus offers a novel approach to study gating mechanisms. Another surprise is that the proton channel appears to function as a dimer, with two separate conduction pathways. A number of significant biological questions remain in dispute, unanswered, or in some cases, not yet asked. This latter deficit is ascribable to the intrinsic difficulty in evaluating the importance of one component in a complex system, and in addition, to the lack, until recently, of a means of performing an unambiguous lesion experiment, that is, of selectively eliminating the molecule in question. We still lack a potent, selective pharmacological inhibitor, but the identification of the gene has allowed the development of powerful new tools including proton channel antibodies, siRNA and knockout mice.

Indexed as

ProtonsAnimalsBinding SitesHumansHydrogen-Ion ConcentrationIon Channel GatingIon ChannelsKineticsMiceMice, KnockoutModels, MolecularPhosphorylationZincIon ChannelsProtonsZinc

Identifiers

PMID18801839
PMCPMC2655391

What OpenQuestion holds

Textmetadata
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.