Evidence map›Paper›PMID 29925021›Full record

ArticleBiophysical journal2018

Gating Currents in the Hv1 Proton Channel.

Victor De La Rosa, Ian Scott Ramsey

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. HInternational journal of molecular sciences · 2025
    Review
  2. Voltage sensors.Molecular pharmacology · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Cholesterol inhibits human voltage-gated proton channel hHv1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. The voltage sensor is responsible for ΔpH dependence in HProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. A family of hyperpolarization-activated channels selective for protons.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Victor De La RosaDepartment of Physiology and Biophysics, School of Medicine, Virginia Commonwealth University, Richmond, Virginia.
Ian Scott RamseyDepartment of Physiology and Biophysics, School of Medicine, Virginia Commonwealth University, Richmond, Virginia. Electronic address: isramsey@vcu.edu.

Funding

Molecular Mechanisms of Hv1 Voltage-Gated Proton Channel FunctionR01GM092908 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI RAMSEY, IAN SCOTT · 2011 to 2015
$1.4M
NIGMS NIH HHS R01 GM092908
6 · The paper itself

Abstract

The Hv1 proton channel shares striking structural homology with fourth transmembrane helical segment-type voltage-sensor (VS) domains but manifests distinctive functional properties, including a proton-selective "aqueous" conductance and allosteric control of voltage-dependent gating by changes in the transmembrane pH gradient. The mechanisms responsible for Hv1's functional properties remain poorly understood, in part because methods for measuring gating currents that directly report VS activation have not yet been described. Here, we describe an approach that allows robust and reproducible measurement of gating-associated charge movements in Hv1. Gating currents reveal that VS activation and proton-selective aqueous conductance opening are thermodynamically distinct steps in the Hv1 activation pathway and show that pH changes directly alter VS activation. The availability of an assay for gating currents in Hv1 may aid future efforts to elucidate the molecular mechanisms of gating cooperativity, pH-dependent modulation, and H

Indexed as

Ion Channel GatingCell LineHumansHydrogen-Ion ConcentrationIon ChannelsKineticsMutationProtein DomainsThermodynamicsHVCN1 protein, humanIon Channels

Identifiers

PMID29925021
PMCPMC6026397

What OpenQuestion holds

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Registered trials

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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.