Evidence map›Paper›PMID 16172377›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Effect of temperature on the working stroke of muscle myosin.

V Decostre, P Bianco, V Lombardi, G Piazzesi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 14% 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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 98 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Article
  6. Ice gliding diatoms establish record-low temperature limits for motility in a eukaryotic cell.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. The Mechanism of Modulation of Cardiac Force by Temperature.International journal of molecular sciences · 2025
    Article
  10. Review
  11. Article
  12. Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022
    Article
  13. Acute Effects of Global Postural Re-Education on Non-Specific Low Back Pain. Does Time-of-Day Play a Role?International journal of environmental research and public health · 2021
    Article
  14. Article
  15. Myosin Cross-Bridge Behaviour in Contracting Muscle-The TInternational journal of molecular sciences · 2019
    Article
  16. Review
  17. Article
  18. Article
  19. Myosin filament activation in the heart is tuned to the mechanical task.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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 at 1 institution in 2 countries.

V DecostreLaboratory of Physiology, Dipartimento di Biologia Animale e Genetica, Università degli Studi di Firenze, Via G. Sansone 1, 50019 Sesto Fiorentino, Italy.
P Bianco
V Lombardi
G Piazzesi
University of Florence · IT

Funding

The molecular mechanism of muscle contractionR01AR049033 · NIAMS · UNIVERSITY OF FLORENCE · PI LOMBARDI, VINCENZO · 2003 to 2006
$422k
NIAMS NIH HHS R01 AR049033NIAMS NIH HHS R01AR049033-01
6 · The paper itself

Abstract

Muscle contraction is due to myosin motors that transiently attach with their globular head to an actin filament and generate force. After a sudden reduction of the load below the maximum isometric force (T0), the attached myosin heads execute an axial movement (the working stroke) that drives the sliding of the actin filament toward the center of the sarcomere by an amount that is larger at lower load and is 11 nm near zero load. Here, we show that an increase in temperature from 2 to 17 degrees C, which increases the average isometric force per attached myosin head by 60%, does not affect the amount of filament sliding promoted by a reduction in force from T0 to 0.7T0, whereas it reduces the sliding under low load by 2.5 nm. These results exclude the possibility that the myosin working stroke is due to the release of the mechanical energy stored in the initial endothermic force-generating process and show that, at higher temperatures, the working stroke energy is greater because of higher force, although the stroke length is smaller at low load. We conclude the following: (i) the working stroke is made by a series of state transitions in the attached myosin head; (ii) the temperature increases the probability for the first transition, competent for isometric force generation; and (iii) the temperature-dependent rise in work at high load can be accounted for by the larger free energy drop that explains the rise in isometric force.

Indexed as

Muscle ContractionTemperatureAnimalsElasticityMuscle, SkeletalMyosinsRana esculentaThermodynamicsMyosins

Identifiers

PMID16172377
PMCPMC1236584
OpenAlexW1981676531

What OpenQuestion holds

Textmetadata
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.