Evidence map›Paper›PMID 33765442›Full record

ArticleCell2021

The molecular basis for sarcomere organization in vertebrate skeletal muscle.

Zhexin Wang, Michael Grange, Thorsten Wagner, Ay Lin Kho, Mathias Gautel, Stefan Raunser

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
19.9field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 159 citations in OpenAlex.

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  7. Subsarcomeric regulation of thin and thick filaments in skeletal muscle myofibrils.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  15. Developmental remodelling ofOpen biology · 2025
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  18. Does the Type of Semen Affect the Phosphoproteome of Turkey (International journal of molecular sciences · 2025
    Article
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  20. Article

28 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

6 authors at 2 institutions in 2 countries.

Zhexin WangDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Michael GrangeDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Thorsten WagnerDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Ay Lin KhoThe Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, Kings College London BHF Excellence Centre, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Mathias GautelThe Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences, Kings College London BHF Excellence Centre, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Stefan RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany. Electronic address: stefan.raunser@mpi-dortmund.mpg.de.
Max Planck Institute of Molecular Physiology · DEKing's College London · GB

Funding

British Heart Foundation CH/08/001/25300British Heart Foundation RG/15/8/31480Medical Research Council MR/R003106/1Wellcome TrustWellcome Trust 201543/Z/16/Z
6 · The paper itself

Abstract

Sarcomeres are force-generating and load-bearing devices of muscles. A precise molecular picture of how sarcomeres are built underpins understanding their role in health and disease. Here, we determine the molecular architecture of native vertebrate skeletal sarcomeres by electron cryo-tomography. Our reconstruction reveals molecular details of the three-dimensional organization and interaction of actin and myosin in the A-band, I-band, and Z-disc and demonstrates that α-actinin cross-links antiparallel actin filaments by forming doublets with 6-nm spacing. Structures of myosin, tropomyosin, and actin at ~10 Å further reveal two conformations of the "double-head" myosin, where the flexible orientation of the lever arm and light chains enable myosin not only to interact with the same actin filament, but also to split between two actin filaments. Our results provide unexpected insights into the fundamental organization of vertebrate skeletal muscle and serve as a strong foundation for future investigations of muscle diseases.

Indexed as

Actin CytoskeletonActininActomyosinAnimalsCryoelectron MicroscopyFemaleMiceMice, Inbred BALB CModels, MolecularMuscle, SkeletalProtein BindingSarcomeresTropomyosinActininActomyosinTropomyosinactinelectron tomographymusclemyosinsarcomerestructuretropomyosinZ-disc

Identifiers

PMID33765442
PMCPMC8054911
OpenAlexW3138595690

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.