Evidence map›Paper›PMID 41996489›Full record

ArticleScience advances2026

Cryo-EM structure of shutdown human nonmuscle myosin 2A.

David Casas-Mao, Glenn Carrington, Michelle Peckham

Abstract read
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026
    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

3 authors.

David Casas-MaoAstbury Centre for Structural Molecular Biology & School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.ORCID 0000-0002-5586-5859
Glenn CarringtonAstbury Centre for Structural Molecular Biology & School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.ORCID 0000-0003-4060-4725
Michelle PeckhamAstbury Centre for Structural Molecular Biology & School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.ORCID 0000-0002-3754-2028

Funding

Wellcome Trust
6 · The paper itself

Abstract

Determining the high-resolution structure of the widely expressed nonmuscle myosin 2A (NM2A), in its dephosphorylated shutdown state, is important in understanding its regulation and disease roles. In shutdown molecules, the coiled-coil tail wraps around the myosin heads, preventing them from forming filaments and binding to actin. We have solved the shutdown structure of NM2A to a global resolution of 3.0 angstroms in the head region and 6.3 angstroms for the whole molecule. This reveals specific ionic interactions that explain why the path of the coiled coil and the shutdown mechanism for NM2A differ from those of β-cardiac myosin and provides key insight into how specific mutations likely destabilize the shutdown state, leading to disease.

Indexed as

Cryoelectron MicroscopyNonmuscle Myosin Type IIAActinsHumansModels, MolecularMutationPhosphorylationProtein BindingProtein ConformationActinsNonmuscle Myosin Type IIA

Identifiers

PMID41996489
PMCPMC13089345

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.