Evidence map›Paper›PMID 25730777›Full record

ArticleNature structural & molecular biology2015

A specialized molecular motion opens the Hv1 voltage-gated proton channel.

Laetitia Mony, Thomas K Berger, Ehud Y Isacoff

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 57 citations in OpenAlex.

  1. Pooled it
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  14. The voltage sensor is responsible for ΔpH dependence in HProceedings of the National Academy of Sciences of the United States of America · 2021
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  17. Dimer interaction in the Hv1 proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Laetitia Mony *Department of Molecular and Cell Biology, University of California, Berkeley, CA (USA).
Thomas K Berger *Department of Molecular and Cell Biology, University of California, Berkeley, CA (USA).
Ehud Y IsacoffDepartment of Molecular and Cell Biology, University of California, Berkeley, CA (USA).
University of California, Berkeley · US

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 R01 NS35549
6 · The paper itself

Abstract

The Hv1 proton channel is unique among voltage-gated channels for containing the pore and gate within its voltage-sensing domain. Pore opening has been proposed to include assembly of the selectivity filter between an arginine (R3) of segment S4 and an aspartate (D1) of segment S1. We determined whether gating involves motion of S1, using Ciona intestinalis Hv1. We found that channel opening is concomitant with solution access to the pore-lining face of S1, from the cytoplasm to deep inside the pore. Voltage- and patch-clamp fluorometry showed that this involves a motion of S1 relative to its surroundings. S1 motion and the S4 motion that precedes it are each influenced by residues on the other helix, thus suggesting a dynamic interaction between S1 and S4. Our findings suggest that the S1 of Hv1 has specialized to function as part of the channel's gate.

Indexed as

Ciona intestinalisIon Channel GatingModels, MolecularAmino Acid SequenceAnimalsIon ChannelsMolecular Sequence DataProtein Structure, TertiaryProtonsSequence AlignmentIon ChannelsProtons

Identifiers

PMID25730777
PMCPMC4385474
OpenAlexW2013383439

What OpenQuestion holds

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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.