Evidence map›Paper›PMID 23352164›Full record

ArticleNeuron2013

Voltage-sensing domain of voltage-gated proton channel Hv1 shares mechanism of block with pore domains.

Liang Hong, Medha M Pathak, Iris H Kim, Dennis Ta, Francesco Tombola

Abstract read
In one paragraph

Article in Neuron, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

64 citing papers in PubMed.

  1. Article
  2. Article
  3. Modulators of the Human Voltage-Gated Proton Channel HPharmaceuticals (Basel, Switzerland) · 2025
    Review
  4. Hv1 channel in immune cells and pharmacology.Pharmacological research · 2025
    Review
  5. Article
  6. Article
  7. Deep Learning-Based Ion Channel Kinetics Analysis for Automated Patch Clamp Recording.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  8. Voltage sensors.Molecular pharmacology · 2025
    Review
  9. Article
  10. Identification of a Novel Structural Class of HJournal of chemical information and modeling · 2024
    Article
  11. Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Molecular determinants of inhibition of the human proton channel hHv1 by the designer peptide C6 and a bivalent derivative.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Liang HongDepartment of Physiology and Biophysics, University of California, Irvine, CA 92697, USA.
Medha M Pathak
Iris H Kim
Dennis Ta
Francesco Tombola

Funding

Mechanisms of Permeation and Gating of Voltage-Sensing DomainsR01GM098973 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI TOMBOLA, FRANCESCO · 2011 to 2025
$4.5M
NIGMS NIH HHS R01 GM098973NIGMS NIH HHS R01GM098973
6 · The paper itself

Abstract

Voltage-gated sodium, potassium, and calcium channels are made of a pore domain (PD) controlled by four voltage-sensing domains (VSDs). The PD contains the ion permeation pathway and the activation gate located on the intracellular side of the membrane. A large number of small molecules are known to inhibit the PD by acting as open channel blockers. The voltage-gated proton channel Hv1 is made of two VSDs and lacks the PD. The location of the activation gate in the VSD is unknown and open channel blockers for VSDs have not yet been identified. Here, we describe a class of small molecules which act as open channel blockers on the Hv1 VSD and find that a highly conserved phenylalanine in the charge transfer center of the VSD plays a key role in blocker binding. We then use one of the blockers to show that Hv1 contains two intracellular and allosterically coupled gates.

Indexed as

AnimalsConserved SequenceFemaleHumansIon Channel GatingIon ChannelsPhenylalaninePorinsProtein BindingProtein Structure, TertiaryXenopusHVCN1 protein, humanIon ChannelsPhenylalaninePorins

Identifiers

PMID23352164
PMCPMC3559007

What OpenQuestion holds

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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.