Evidence map›Paper›PMID 20118934›Full record

ArticleNature structural & molecular biology2010

Molecular determinants of coupling between the domain III voltage sensor and pore of a sodium channel.

Yukiko Muroi, Manoel Arcisio-Miranda, Sandipan Chowdhury, Baron Chanda

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 52 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Structural mapping of NaNature communications · 2023
    Article
  6. Voltage sensor movements of CaProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. S4-S5 linker movement during activation and inactivation in voltage-gated KProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Mechanisms of noncovalent β subunit regulation of NaThe Journal of general physiology · 2017
    Article
  14. Structures of closed and open states of a voltage-gated sodium channel.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Regulation of NaThe Journal of general physiology · 2017
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Yukiko MuroiDepartment of Physiology, School of Medicine and Public Health, University of Wisconsin, Madison, Wisconsin, USA.
Manoel Arcisio-Miranda
Sandipan Chowdhury
Baron Chanda
University of Wisconsin–Madison · US

Funding

Structural basis of modulation of Na+ channels by local anestheticsR01GM084140 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CHANDA, BARON · 2008 to 2016
$3.3M
NIGMS NIH HHS R01 GM084140
6 · The paper itself

Abstract

In a voltage-dependent sodium channel, the activation of voltage sensors upon depolarization leads to the opening of the pore gates. To elucidate the principles underlying this conformational coupling, we investigated a putative gating interface in domain III of the sodium channel using voltage-clamp fluorimetry and tryptophan-scanning mutagenesis. Most mutations have similar energetic effects on voltage-sensor activation and pore opening. However, several mutations stabilized the activated voltage sensor while concurrently destabilizing the open pore. When mapped onto a homology model of the sodium channel, most localized to hinge regions of the gating interface. Our analysis shows that these residues are involved in energetic coupling of the voltage sensor to the pore when both are in resting and when both are in activated conformations, supporting the notion that electromechanical coupling in a voltage-dependent ion channel involves the movement of rigid segments connected by elastic hinges.

Indexed as

Allosteric RegulationAmino Acid SequenceAmino Acid SubstitutionFluorometryModels, BiologicalModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesProtein Structure, TertiarySodium ChannelsSodium Channels

Identifiers

PMID20118934
PMCPMC2879147
OpenAlexW2042147650

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.