Evidence map›Paper›PMID 17012321›Full record

ArticleBiophysical journal2006

A voltage-sensor water pore.

J Alfredo Freites, Douglas J Tobias, Stephen H White

Abstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Does Proton Conduction in the Voltage-Gated HThe journal of physical chemistry. B · 2017
    Article
  7. The Hv1 proton channel responds to mechanical stimuli.The Journal of general physiology · 2016
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Electric fingerprint of voltage sensor domains.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Gating pore currents and the resting state of Nav1.4 voltage sensor domains.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. The influence of lipids on voltage-gated ion channels.Current opinion in structural biology · 2012
    Review
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.

J Alfredo FreitesInstitute for Genomics and Bioinformatics, University of California, Irvine, CA 92697, USA.
Douglas J Tobias
Stephen H White

Funding

Cold Neutrons For Biology And TechnologyR01RR014812 · NCRR · UNIVERSITY OF CALIFORNIA IRVINE · PI WHITE, STEPHEN H. · 2001 to 2005
$5.4M
Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
Concerted membrane diffraction and simulation studiesR01GM068002 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2003 to 2006
$989k
NCRR NIH HHS R01 RR014812NCRR NIH HHS RR-14812NIGMS NIH HHS GM-68002NIGMS NIH HHS GM-74637NIGMS NIH HHS R01 GM068002NIGMS NIH HHS R01 GM074637
6 · The paper itself

Abstract

Voltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close in response to changes in transmembrane potential. Recent experimental studies suggest that VS domains are independent structural units. This independence is revealed dramatically by a voltage-dependent proton-selective channel (Hv), which has a sequence homologous to the VS domains of voltage-gated potassium channels (Kv). Here we show by means of molecular dynamics simulations that the isolated open-state VS domain of the KvAP channel in a lipid membrane has a configuration consistent with a water channel, which we propose as a common feature underlying the conductance of protons, and perhaps other cations, through VS domains.

Indexed as

AnimalsBiophysicsCationsComputer SimulationIon Channel GatingIon ChannelsLipid BilayersModels, MolecularMolecular ConformationPhosphatidylcholinesPotassium ChannelsPotassium Channels, Voltage-GatedProtonsTime FactorsWater1-palmitoyl-2-oleoylphosphatidylcholineCationsIon ChannelsLipid BilayersPhosphatidylcholinesPotassium ChannelsPotassium Channels, Voltage-GatedProtonsWater

Identifiers

PMID17012321
PMCPMC1635690

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.