Evidence map›Paper›PMID 23352165›Full record

ArticleNeuron2013

Subunit interactions during cooperative opening of voltage-gated proton channels.

Feng Qiu, Santiago Rebolledo, Carlos Gonzalez, H Peter Larsson

Open access · bronzeAbstract 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 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
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

45 citing papers in PubMed, 68 citations in OpenAlex.

  1. Modulators of the Human Voltage-Gated Proton Channel HPharmaceuticals (Basel, Switzerland) · 2025
    Review
  2. Article
  3. Article
  4. Trapping Charge Mechanism in Hv1 Channels (International journal of molecular sciences · 2023
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022
    Review
  10. Review
  11. Article
  12. Discovery of KMedicinal research reviews · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Dimer interaction in the Hv1 proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Article
  19. Assessing Structural Determinants of ZnBiophysical journal · 2020
    Article
  20. 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
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Feng QiuDepartment of Physiology and Biophysics, University of Miami, 1600 NW 10th Avenue, RMSB 5123, Miami, FL 33136, USA.
Santiago Rebolledo
Carlos Gonzalez
H Peter Larsson
University of Miami · USUniversity of Valparaíso · CL

Funding

Molecular mechanisms of voltage-gated proton channelsR01HL095920 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LARSSON, HANS PETER · 2010 to 2013
$1.5M
NHLBI NIH HHS R01 HL095920NHLBI NIH HHS R01-HL095920
6 · The paper itself

Abstract

Voltage-gated proton (Hv1) channels are dimers, where each subunit has a separate permeation pathway. However, opening of the two pathways is highly cooperative. It is unclear how Hv1 channels open their permeation pathways, because Hv1 channels lack a classic pore domain. Using voltage-clamp fluorometry, we here detect two conformational changes reported by a fluorophore attached to the voltage sensor S4 in Hv1 channels. The first is voltage dependent and precedes channel opening, with properties consistent with reporting on independent S4 charge movements in the two subunits. The second is less voltage dependent and closely correlates with channel opening. Mutations that reduce dimerization or alter the intersubunit interface affect both the second conformational change and channel opening. These observations suggest that, following an initial S4 charge movement in the two subunits, there is a second, cooperative conformational change, involving interactions between subunits, that opens both pathways in Hv1 channels.

Indexed as

Amino Acid SequenceAnimalsChloride ChannelsFemaleHumansIon Channel GatingIon ChannelsMolecular Sequence DataPotassium Channels, Voltage-GatedProtein BindingProtein ConformationProtein SubunitsSodium ChannelsXenopus laevisChloride ChannelsHVCN1 protein, humanIon ChannelsPotassium Channels, Voltage-GatedProtein SubunitsSodium Channels

Identifiers

PMID23352165
PMCPMC3558936
OpenAlexW2015957314

What OpenQuestion holds

Textmetadata
LicenceTDM
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.