Evidence map›Paper›PMID 29941816›Full record

ReviewInternational journal of molecular sciences2018

Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?

Alf Månsson, Marko Ušaj, Luisa Moretto, Dilson E Rassier

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. A reverse stroke characterizes the force generation of cardiac myofilaments, leading to an understanding of heart function.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Frontiers in physiology · 2020
    Review
  15. Review
  16. Review
  17. Myosin Cross-Bridge Behaviour in Contracting Muscle-The TInternational journal of molecular sciences · 2019
    Article
  18. Article
  19. Article
  20. Article
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

4 authors.

Alf MånssonDepartment Chemistry Biomedical Sciences, Linnaeus University, SE-39182 Kalmar, Sweden. alf.mansson@lnu.se.ORCID 0000-0002-5889-7792
Marko UšajDepartment Chemistry Biomedical Sciences, Linnaeus University, SE-39182 Kalmar, Sweden. marko.usaj@lnu.se.
Luisa MorettoDepartment Chemistry Biomedical Sciences, Linnaeus University, SE-39182 Kalmar, Sweden. luisa.moretto@lnu.se.
Dilson E RassierDepartment Kinesiology and Physical Education, McGill University, Montreal, QC H3A 2T5, Canada. dilson.rassier@mcgill.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In muscle, but not in single-molecule mechanics studies, actin, myosin and accessory proteins are incorporated into a highly ordered myofilament lattice. In view of this difference we compare results from single-molecule studies and muscle mechanics and analyze to what degree data from the two types of studies agree with each other. There is reasonable correspondence in estimates of the cross-bridge power-stroke distance (7⁻13 nm), cross-bridge stiffness (~2 pN/nm) and average isometric force per cross-bridge (6⁻9 pN). Furthermore, models defined on the basis of single-molecule mechanics and solution biochemistry give good fits to experimental data from muscle. This suggests that the ordered myofilament lattice, accessory proteins and emergent effects of the sarcomere organization have only minor modulatory roles. However, such factors may be of greater importance under e.g., disease conditions. We also identify areas where single-molecule and muscle data are conflicting: (1) whether force generation is an Eyring or Kramers process with just one major power-stroke or several sub-strokes; (2) whether the myofilaments and the cross-bridges have Hookean or non-linear elasticity; (3) if individual myosin heads slip between actin sites under certain conditions, e.g., in lengthening; or (4) if the two heads of myosin cooperate.

Indexed as

Actin CytoskeletonActinsActomyosinAnimalsIsometric ContractionMuscle ContractionMuscle Fibers, SkeletalMyofibrilsMyosinsActinsActomyosinMyosinsactincross-bridgemechanochemical modelmuscle fibermyofibrilmyosinoptical trapsoptical tweezers

Identifiers

PMID29941816
PMCPMC6073448

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.