Evidence map›Paper›PMID 34215727›Full record

ArticleNature communications2021

Molecular-scale visualization of sarcomere contraction within native cardiomyocytes.

Laura Burbaum, Jonathan Schneider, Sarah Scholze, Ralph T Böttcher, Wolfgang Baumeister, Petra Schwille, Jürgen M Plitzko, Marion Jasnin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

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  13. Hypertrophic cardiomyopathy: insights into pathophysiology and novel therapeutic strategies from clinical studies.The Egyptian heart journal : (EHJ) : official bulletin of the Egyptian Society of Cardiology · 2025
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  14. Tapered fiber probe-based optical cardiac pacemaker.Frontiers in bioengineering and biotechnology · 2025
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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

8 authors at 1 institution in 1 country.

Laura Burbaum *Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Jonathan Schneider *Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.
Sarah ScholzeDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany.
Ralph T BöttcherDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0003-3050-7163
Wolfgang BaumeisterDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.
Petra SchwilleDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-6106-4847
Jürgen M PlitzkoDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-6402-8315
Marion JasninDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany. jasnin@biochem.mpg.de.ORCID http://orcid.org/0000-0003-1726-4566
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sarcomeres, the basic contractile units of striated muscle, produce the forces driving muscular contraction through cross-bridge interactions between actin-containing thin filaments and myosin II-based thick filaments. Until now, direct visualization of the molecular architecture underlying sarcomere contractility has remained elusive. Here, we use in situ cryo-electron tomography to unveil sarcomere contraction in frozen-hydrated neonatal rat cardiomyocytes. We show that the hexagonal lattice of the thick filaments is already established at the neonatal stage, with an excess of thin filaments outside the trigonal positions. Structural assessment of actin polarity by subtomogram averaging reveals that thin filaments in the fully activated state form overlapping arrays of opposite polarity in the center of the sarcomere. Our approach provides direct evidence for thin filament sliding during muscle contraction and may serve as a basis for structural understanding of thin filament activation and actomyosin interactions inside unperturbed cellular environments.

Indexed as

Actin CytoskeletonActinsAnimalsMaleMiceMice, Inbred C57BLMuscle ContractionMuscle, SkeletalMuscle, StriatedMyocytes, CardiacMyofibrilsRatsRats, WistarSarcomeresActins

Identifiers

PMID34215727
PMCPMC8253822
OpenAlexW3173393387

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.