Evidence map›Paper›PMID 20876362›Full record

ArticleThe Journal of general physiology2010

An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation.

Ben Corry, Annette C Hurst, Prithwish Pal, Takeshi Nomura, Paul Rigby, Boris Martinac

Abstract read
In one paragraph

Article in The Journal of general physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
  2. Article
  3. Asymmetric Nature of MscL Opening Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Cyclodextrins increase membrane tension and are universal activators of mechanosensitive channels.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. Building a synthetic mechanosensitive signaling pathway in compartmentalized artificial cells.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors.

Ben CorrySchool of Biomedical, Biomolecular and Chemical Sciences, The University of Western Australia, Crawley WA, Australia.
Annette C Hurst
Prithwish Pal
Takeshi Nomura
Paul Rigby
Boris Martinac

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mechanosensitive channels act as molecular transducers of mechanical force exerted on the membrane of living cells by opening in response to membrane bilayer deformations occurring in physiological processes such as touch, hearing, blood pressure regulation, and osmoregulation. Here, we determine the likely structure of the open state of the mechanosensitive channel of large conductance using a combination of patch clamp, fluorescence resonance energy transfer (FRET) spectroscopy, data from previous electron paramagnetic resonance experiments, and molecular and Brownian dynamics simulations. We show that structural rearrangements of the protein can be measured in similar conditions as patch clamp recordings while controlling the state of the pore in its natural lipid environment by modifying the lateral pressure distribution via the lipid bilayer. Transition to the open state is less dramatic than previously proposed, while the N terminus remains anchored at the surface of the membrane where it can either guide the tilt of or directly translate membrane tension to the conformation of the pore-lining helix. Combining FRET data obtained in physiological conditions with simulations is likely to be of great value for studying conformational changes in a range of multimeric membrane proteins.

Indexed as

Computer SimulationEscherichia coli ProteinsFluorescence Resonance Energy TransferIon Channel GatingIon ChannelsLipid BilayersMechanotransduction, CellularMicroscopy, ConfocalModels, MolecularProtein Structure, SecondaryEscherichia coli ProteinsIon ChannelsLipid BilayersMscL protein, E coli

Identifiers

PMID20876362
PMCPMC2947060

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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.