Evidence map›Paper›PMID 34889960›Full record

ReviewThe Journal of general physiology2022

Structural basis of the super- and hyper-relaxed states of myosin II.

Roger Craig, Raúl Padrón

Abstract readReview
In one paragraph

Review in The Journal of general physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 1 pooled it
–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

63 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  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
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Consecutive SSCs increase the SSC effect in skinned rat muscle fibres.Pflugers Archiv : European journal of physiology · 2025
    Article
  20. Article

3 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

2 authors.

Roger CraigDivision of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Chan Medical School, Worcester, MA.ORCID 0000-0002-9707-5409
Raúl PadrónDivision of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Chan Medical School, Worcester, MA.ORCID 0000-0002-1412-2450

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
Mechanism of regulation of cardiac contraction by phosphorylation of myosin binding protein CR01HL139883 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI CRAIG, ROGER W, RALPHE, JOHN CARTER · 2018 to 2021
$2.7M
Skeletal Myosin-Binding Protein C (MyBP-C): Molecular Structure and FunctionR01AR067279 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W, WARSHAW, DAVID M · 2015 to 2019
$2.3M
Structure of The Interacting-Heads Motif in Myosin Filaments and MoleculesR01AR072036 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CRAIG, ROGER W · 2017 to 2021
$2.1M
Murine 3D Engineered Tissue Model of Human MYBPC3 MutationsR01HL107367 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI RALPHE, JOHN CARTER · 2011 to 2015
$1.8M
NCRR NIH HHS P41 RR001081NHLBI NIH HHS R01 HL107367NHLBI NIH HHS R01 HL139883NIAMS NIH HHS R01 AR067279NIAMS NIH HHS R01 AR072036NIH HHS AR072036
6 · The paper itself

Abstract

Super-relaxation is a state of muscle thick filaments in which ATP turnover by myosin is much slower than that of myosin II in solution. This inhibited state, in equilibrium with a faster (relaxed) state, is ubiquitous and thought to be fundamental to muscle function, acting as a mechanism for switching off energy-consuming myosin motors when they are not being used. The structural basis of super-relaxation is usually taken to be a motif formed by myosin in which the two heads interact with each other and with the proximal tail forming an interacting-heads motif, which switches the heads off. However, recent studies show that even isolated myosin heads can exhibit this slow rate. Here, we review the role of head interactions in creating the super-relaxed state and show how increased numbers of interactions in thick filaments underlie the high levels of super-relaxation found in intact muscle. We suggest how a third, even more inhibited, state of myosin (a hyper-relaxed state) seen in certain species results from additional interactions involving the heads. We speculate on the relationship between animal lifestyle and level of super-relaxation in different species and on the mechanism of formation of the super-relaxed state. We also review how super-relaxed thick filaments are activated and how the super-relaxed state is modulated in healthy and diseased muscles.

Indexed as

MyosinsMyosin Type IIAnimalsMusclesMyosinsMyosin Type II

Identifiers

PMID34889960
PMCPMC8669498

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.