Evidence map›Paper›PMID 18498736›Full record

ArticleNeuron2008

The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor.

Francesco Tombola, Maximilian H Ulbrich, Ehud Y Isacoff

Abstract read
In one paragraph

Article in Neuron, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 papers.

0numbers the graph read from it
0cells of the map it votes in
163citing 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

163 citing papers in PubMed.

  1. Article
  2. A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026
    Review
  3. Modulators of the Human Voltage-Gated Proton Channel HPharmaceuticals (Basel, Switzerland) · 2025
    Review
  4. Fluctuating hydrogen-bond network of the Hv1 ion channel.Computational and structural biotechnology journal · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Identification of a Novel Structural Class of HJournal of chemical information and modeling · 2024
    Article
  10. Review
  11. Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024
    Review
  12. Inhibition of the HFrontiers in immunology · 2024
    Article
  13. Article
  14. Trapping Charge Mechanism in Hv1 Channels (International journal of molecular sciences · 2023
    Article
  15. Article
  16. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  17. Mechanosensitive aquaporins.Biophysical reviews · 2023
    Review
  18. Review
  19. Review
  20. Article

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

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

3 authors.

Francesco TombolaDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Maximilian H Ulbrich
Ehud Y Isacoff

Funding

STRUCTURAL REARRANGEMENTS IN CHANNEL GATINGR01NS035549 · NINDS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 1996 to 2013
$4.1M
NINDS NIH HHS R01 NS035549NINDS NIH HHS R01NS035549
6 · The paper itself

Abstract

In voltage-gated channels, ions flow through a single pore located at the interface between membrane-spanning pore domains from each of four subunits, and the gates of the pore are controlled by four peripheral voltage-sensing domains. In a striking exception, the newly discovered voltage-gated Hv1 proton channels lack a homologous pore domain, leaving the location of the pore unknown. Also unknown are the number of subunits and the mechanism of gating. We find that Hv1 is a dimer and that each subunit contains its own pore and gate, which is controlled by its own voltage sensor. Our experiments show that the cytosolic domain of the channel is necessary and sufficient for dimerization and that the transmembrane part of the channel is functional also when monomerized. The results suggest a mechanism of gating whereby the voltage sensor and gate are one and the same.

Indexed as

Amino Acid SequenceAnimalsCell MembraneCloning, MolecularCysteineDose-Response Relationship, DrugElectric StimulationGreen Fluorescent ProteinsGuanidineHumansIon Channel GatingIon ChannelsMembrane PotentialsModels, MolecularMolecular ConformationOocytesCysteineGreen Fluorescent ProteinsGuanidineHVCN1 protein, humanIon Channels

Identifiers

PMID18498736
PMCPMC2430592

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.