Evidence map›Paper›PMID 33357376›Full record

ArticleeLife2020

Graded titin cleavage progressively reduces tension and uncovers the source of A-band stability in contracting muscle.

Yong Li, Anthony L Hessel, Andreas Unger, David Ing, Jannik Recker, Franziska Koser, Johanna K Freundt, Wolfgang A Linke

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 49 citations in OpenAlex.

  1. Mechanisms, regulation and clinical relevance of necroptosis.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Popping the hood of muscle motors using time-resolved, small-angle X-ray diffraction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. The distinctive mechanical and structural signatures of residual force enhancement in myofibers.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Structure of mavacamten-free human cardiac thick filaments within the sarcomere by cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Eccentric muscle contractions: from single muscle fibre to whole muscle mechanics.Pflugers Archiv : European journal of physiology · 2023
    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

8 authors.

Yong Li *Institute of Physiology II, University of Muenster, Muenster, Germany.ORCID 0000-0001-8184-5977
Anthony L Hessel *Institute of Physiology II, University of Muenster, Muenster, Germany.
Andreas Unger *Institute of Physiology II, University of Muenster, Muenster, Germany.
David IngInstitute of Physiology II, University of Muenster, Muenster, Germany.
Jannik ReckerInstitute of Physiology II, University of Muenster, Muenster, Germany.
Franziska KoserInstitute of Physiology II, University of Muenster, Muenster, Germany.
Johanna K FreundtInstitute of Physiology II, University of Muenster, Muenster, Germany.
Wolfgang A LinkeInstitute of Physiology II, University of Muenster, Muenster, Germany.ORCID 0000-0003-0801-3773

Funding

European Research Area Network on Cardiovascular Disease consortium MINOTAURGerman Research Foundation SFB1002-A08German Research Foundation SFB1002,TPA08IZKF Muenster Li1/029/20
6 · The paper itself

Abstract

The giant muscle protein titin is a major contributor to passive force; however, its role in active force generation is unresolved. Here, we use a novel titin-cleavage (TC) mouse model that allows specific and rapid cutting of elastic titin to quantify how titin-based forces define myocyte ultrastructure and mechanics. We show that under mechanical strain, as TC doubles from heterozygous to homozygous TC muscles, Z-disks become increasingly out of register while passive and active forces are reduced. Interactions of elastic titin with sarcomeric actin filaments are revealed. Strikingly, when titin-cleaved muscles contract, myosin-containing A-bands become split and adjacent myosin filaments move in opposite directions while also shedding myosins. This establishes intact titin filaments as critical force-transmission networks, buffering the forces observed by myosin filaments during contraction. To perform this function, elastic titin must change stiffness or extensible length, unveiling its fundamental role as an activation-dependent spring in contracting muscle.

Indexed as

Muscle ContractionAnimalsFemaleMaleMiceMuscle ProteinsMuscle, SkeletalProtein KinasesTensile StrengthMuscle ProteinsProtein Kinasestitin protein, mousecell biologycontractionelasticityimmunocytochemistrymechanicsmousephysics of living systemsskeletal muscle fibersultrastructure

Identifiers

PMID33357376
PMCPMC7781594
OpenAlexW3113503656

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.