Evidence map›Paper›PMID 15277576›Full record

ArticleThe Journal of general physiology2004

Gating transitions in bacterial ion channels measured at 3 microns resolution.

George Shapovalov, Henry A Lester

Abstract read
In one paragraph

Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Asymmetric Nature of MscL Opening Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025
    Article
  2. Mechanosensitive channel MscL gating transitions coupling with constriction point shift.Protein science : a publication of the Protein Society · 2024
    Article
  3. Article
  4. Article
  5. On Bottlenecks, Helmholtz and Hearing.Function (Oxford, England) · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Single-channel recordings of RyR1 at microsecond resolution in CMOS-suspended membranes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The role of lipids in mechanosensation.Nature structural & molecular biology · 2015
    Article
  17. Article
  18. Article
  19. Feeling the hidden mechanical forces in lipid bilayer is an original sense.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Review
  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

2 authors.

George ShapovalovDivision of Biology, California Institute of Technology, Pasadena, CA 91125, USA.
Henry A Lester

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-062532NIGMS NIH HHS P01 GM062532
6 · The paper itself

Abstract

Ion channels of high conductance (>200 pS) are widespread among prokaryotes and eukaryotes. Two examples, the Escherichia coli mechanosensitive ion channels Ec-MscS and Ec-MscL, pass currents of 125-300 pA. To resolve temporal details of conductance transitions, a patch-clamp setup was optimized for low-noise recordings at a time resolution of 3 microns (10-20 times faster than usual). Analyses of the high-resolution recordings confirm that Ec-MscL visits many subconductance states and show that most of the intersubstate transitions occur more slowly than the effective resolution of 3 micros. There is a clear trend toward longer transition times for the larger transitions. In Ec-MscS recordings, the majority of the observed full conductance transitions are also composite. We detected a short-lived (approximately 20 microns) Ec-MscS substate at 2/3 of full conductance; transitions between 2/3 and full conductance did not show fine structure and had a time course limited by the achieved resolution. Opening and closing transitions in MscS are symmetrical and are not preceded or followed by smaller, rapid currents ("anticipations" or "regrets"). Compared with other, lower-conductance channels, these measurements may detect unusually early states in the transitions from fully closed to fully open. Increased temporal resolution at the single-molecule level reveals that some elementary steps of structural transitions are composite and follow several alternative pathways, while others still escape resolution. High-bandwidth, low-noise single-channel measurements may provide details about state transitions in other high-conductance channels; and similar procedures may also be applied to channel- and nanopore-based single-molecule DNA measurements.

Indexed as

Bacterial ProteinsEscherichia coliEscherichia coli ProteinsIon Channel GatingIon ChannelsPatch-Clamp TechniquesSensitivity and SpecificityBacterial ProteinsEscherichia coli ProteinsIon Channels

Identifiers

PMID15277576
PMCPMC2229625

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.