Evidence map›Paper›PMID 27481712›Full record

ReviewThe Journal of general physiology2016

Insights into the structure and function of HV1 from a meta-analysis of mutation studies.

Thomas E DeCoursey, Deri Morgan, Boris Musset, Vladimir V Cherny

Abstract readReview
In one paragraph

Review in The Journal of general physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Modulators of the Human Voltage-Gated Proton Channel HPharmaceuticals (Basel, Switzerland) · 2025
    Review
  2. Article
  3. Fluctuating hydrogen-bond network of the Hv1 ion channel.Computational and structural biotechnology journal · 2025
    Article
  4. Article
  5. Article
  6. Transcendent Aspects of Proton Channels.Annual review of physiology · 2024
    Review
  7. Review
  8. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Hydrophobic gasket mutation produces gating pore currents in closed human voltage-gated proton channels.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. HThe Journal of eukaryotic microbiology · 2018
    Article
  19. Gating currents indicate complex gating of voltage-gated proton channels.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. HistidineThe Journal of general physiology · 2018
    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

4 authors.

Thomas E DeCourseyDepartment of Molecular Biophysics and Physiology, Rush University, Chicago, IL 60612 tdecours@rush.edu.ORCID 0000-0002-4263-180X
Deri MorganDepartment of Molecular Biophysics and Physiology, Rush University, Chicago, IL 60612.
Boris MussetInstitut für Physiologie, PMU Klinikum Nürnberg, 90419 Nürnberg, Germany.
Vladimir V ChernyDepartment of Molecular Biophysics and Physiology, Rush University, Chicago, IL 60612.

Funding

Selectivity and Permeation in the Human Voltage-gated Proton Channel, hHv1R01GM102336 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI DECOURSEY, THOMAS E, SMITH, SUSAN M.E. · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM102336
6 · The paper itself

Abstract

The voltage-gated proton channel (HV1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for HV1 were identified, a vast array of mutations have been generated and characterized. Accessing this potentially useful resource is hindered, however, by the sheer number of mutations and interspecies differences in amino acid numbering. This review organizes all existing information in a logical manner to allow swift identification of studies that have characterized any particular mutation. Although much can be gained from this meta-analysis, important questions about the inner workings of HV1 await future revelation.

Indexed as

Ion Channel GatingMutationAnimalsHumansIon ChannelsProtein ConformationHVCN1 protein, humanIon Channels

Identifiers

PMID27481712
PMCPMC4969798

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.