Evidence map›Paper›PMID 24550255›Full record

ArticleeLife2014

Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel.

Yong Wang, Yanxin Liu, Hannah A Deberg, Takeshi Nomura, Melinda Tonks Hoffman, Paul R Rohde, Klaus Schulten, Boris Martinac, Paul R Selvin

Abstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing 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

81 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Mechanomedicine: Present state and future promise.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Asymmetric Nature of MscL Opening Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025
    Article
  11. Article
  12. Review
  13. Multifunctional Nanomaterials Mediate Cholesterol Depletion for Cancer Treatment.Angewandte Chemie (International ed. in English) · 2024
    Review
  14. Article
  15. Microbial membrane transport proteins and their biotechnological applications.World journal of microbiology & biotechnology · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Mechanosensitive aquaporins.Biophysical reviews · 2023
    Review
  20. Article

21 more citing papers are in PubMed but not listed here.

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

9 authors.

Yong WangDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, United States.
Yanxin Liu
Hannah A Deberg
Takeshi Nomura
Melinda Tonks Hoffman
Paul R Rohde
Klaus Schulten
Boris Martinac
Paul R Selvin

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI PEROZO, EDUARDO A · 2010 to 2017
$31.9M
WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
Nanometric Fluorescence Imaging of Single Motor ProteinsR01GM068625 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SELVIN, PAUL R · 2004 to 2012
$2.8M
NIGMS NIH HHS 9P41GM104601NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM06788NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01 GM068625NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

The mechanosensitive channel of large conductance, which serves as a model system for mechanosensitive channels, has previously been crystallized in the closed form, but not in the open form. Ensemble measurements and electrophysiological sieving experiments show that the open-diameter of the channel pore is >25 Å, but the exact size and whether the conformational change follows a helix-tilt or barrel-stave model are unclear. Here we report measurements of the distance changes on liposome-reconstituted MscL transmembrane α-helices, using a 'virtual sorting' single-molecule fluorescence energy transfer. We observed directly that the channel opens via the helix-tilt model and the open pore reaches 2.8 nm in diameter. In addition, based on the measurements, we developed a molecular dynamics model of the channel structure in the open state which confirms our direct observations. DOI: http://dx.doi.org/10.7554/eLife.01834.001.

Indexed as

Ion Channel GatingMechanotransduction, CellularCloning, MolecularEscherichia coli ProteinsFluorescence Resonance Energy TransferFluorescent DyesIon ChannelsKineticsLiposomesMembrane PotentialsMolecular Dynamics SimulationMutationPorosityProtein Structure, SecondaryStructure-Activity RelationshipEscherichia coli ProteinsFluorescent DyesIon ChannelsLiposomesMscL protein, E colibarrel-stave modelhelix-tilt modelMscL

Identifiers

PMID24550255
PMCPMC3925968

What OpenQuestion holds

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LicenceCC BY
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.