Evidence map›Paper›PMID 40471653›Full record

ArticleJournal of chemical information and modeling2025

Asymmetric Nature of MscL Opening Revealed by Molecular Dynamics Simulations.

Olga N Rogacheva, Wojciech Kopec

Abstract read
In one paragraph

Article in Journal of chemical information and modeling, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

2 authors.

Olga N RogachevaComputational Biomolecular Dynamics Group, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.ORCID 0000-0001-7084-4215
Wojciech KopecComputational Biomolecular Dynamics Group, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.ORCID 0000-0001-8801-9563

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bacterial mechanosensitive channel, MscL, opens in response to elevated membrane tension during osmotic shock. Some mutations, like L17A and V21A, can reduce the activation tension threshold, thus offering an approach to study the mechanism of MscL gating. We employed all-atom molecular dynamics to simulate the L17A, V21A double mutant of MscL under a tension of 30 mN/m. Under these conditions, the closed state initially adopts a funnel-like conformation. Subsequently, five chains of MscL undergo sequential transitions into asymmetric states (S1, S2, etc.). Within its "open" fragment, the S1 state is similar to the expanded state of

Indexed as

Escherichia coli ProteinsIon Channel GatingIon ChannelsMolecular Dynamics SimulationMutationProtein ConformationEscherichia coli ProteinsIon ChannelsMscL protein, E coli

Identifiers

PMID40471653
PMCPMC12199302

What OpenQuestion holds

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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.