Evidence map›Paper›PMID 32621864›Full record

ArticleBiophysical journal2020

In-Lipid Structure of Pressure-Sensitive Domains Hints Mechanosensitive Channel Functional Diversity.

Charalampos Kapsalis, Yue Ma, Bela E Bode, Christos Pliotas

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  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. Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. 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

4 authors at 2 institutions in 1 country.

Charalampos KapsalisBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews, United Kingdom.
Yue MaAstbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, United Kingdom; School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Bela E BodeBiomedical Sciences Research Complex, School of Chemistry, University of St Andrews, St Andrews, United Kingdom. Electronic address: beb2@st-andrews.ac.uk.
Christos PliotasBiomedical Sciences Research Complex, School of Biology, University of St Andrews, St Andrews, United Kingdom; Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, United Kingdom; School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom. Electronic address: c.pliotas@leeds.ac.uk.
University of Leeds · GBUniversity of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R013780/1Biotechnology and Biological Sciences Research Council BB/S018069/1Wellcome TrustWellcome Trust 099149/Z/12/Z
6 · The paper itself

Abstract

The mechanosensitive channel of large conductance (MscL) from Mycobacterium tuberculosis has been used as a structural model for rationalizing functional observations in multiple MscL orthologs. Although these orthologs adopt similar structural architectures, they reportedly present significant functional differences. Subtle structural discrepancies on mechanosensitive channel nanopockets are known to affect mechanical gating and may be linked to large variability in tension sensitivity among these membrane channels. Here, we modify the nanopocket regions of MscL from Escherichia coli and M. tuberculosis and employ PELDOR/DEER distance and 3pESEEM deuterium accessibility measurements to interrogate channel structure within lipids, in which both channels adopt a closed conformation. Significant in-lipid structural differences between the two constructs suggest a more compact E. coli MscL at the membrane inner-leaflet, as a consequence of a rotated TM2 helix. Observed differences within lipids could explain E. coli MscL's higher tension sensitivity and should be taken into account in extrapolated models used for MscL gating rationalization.

Indexed as

Escherichia coliEscherichia coli ProteinsElectron Spin Resonance SpectroscopyIon Channel GatingIon ChannelsEscherichia coli ProteinsIon ChannelsMscL protein, E coli

Identifiers

PMID32621864
PMCPMC7376121
OpenAlexW3036575374

What OpenQuestion holds

Textmetadata
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.