Evidence map›Paper›PMID 16500980›Full record

ArticleBiophysical journal2006

Voltage-dependent hydration and conduction properties of the hydrophobic pore of the mechanosensitive channel of small conductance.

Steven A Spronk, Donald E Elmore, Dennis A Dougherty

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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Anomalous behavior of water inside the SecY translocon.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. On the origin of ion selectivity in the Cys-loop receptor family.Journal of molecular neuroscience : MN · 2010
    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

3 authors.

Steven A SpronkDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, USA.
Donald E Elmore
Dennis A Dougherty

Funding

STRUCTURE AND FUNCTION OF MECHANOSENSITIVE ION CHANNELSP01GM062532 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DOUGHERTY, DENNIS A · 2000 to 2004
$4.5M
NIGMS NIH HHS GM 62532NIGMS NIH HHS P01 GM062532
6 · The paper itself

Abstract

A detailed picture of water and ion properties in small pores is important for understanding the behavior of biological ion channels. Several recent modeling studies have shown that small, hydrophobic pores exclude water and ions even if they are physically large enough to accommodate them, a mechanism called hydrophobic gating. This mechanism has been implicated in the gating of several channels, including the mechanosensitive channel of small conductance (MscS). Although the pore in the crystal structure of MscS is wide and was initially hypothesized to be open, it is lined by hydrophobic residues and may represent a nonconducting state. Molecular dynamics simulations were performed on MscS to determine whether or not the structure can conduct ions. Unlike previous simulations of hydrophobic nanopores, electric fields were applied to this system to model the transmembrane potential, which proved to be important. Although simulations without a potential resulted in a dehydrated, occluded pore, the application of a potential increased the hydration of the pore and resulted in current flow through the channel. The calculated channel conductance was in good agreement with experiment. Therefore, it is likely that the MscS crystal structure is closer to a conducting than a nonconducting state.

Indexed as

Ion Channel GatingMembrane PotentialsModels, ChemicalModels, MolecularCell MembraneComputer SimulationDiffusionElectric ConductivityEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsIon ChannelsPorosityProtein ConformationWaterEscherichia coli ProteinsIon ChannelsMscS protein, E coliWater

Identifiers

PMID16500980
PMCPMC1440736

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.