Evidence map›Paper›PMID 25319769›Full record

ArticleJournal of muscle research and cell motility2014

A new mechanokinetic model for muscle contraction, where force and movement are triggered by phosphate release.

David A Smith

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

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  13. 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
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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

1 author at 1 institution in 1 country.

David A SmithDepartment of Zoology, La Trobe University, Melbourne, VIC, 3083, Australia, david.smith@latrobe.edu.au.
La Trobe University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The atomic structure of myosin-S1 suggests that its working stroke, which generates tension and shortening in muscle, is triggered by the release of inorganic phosphate from the active site. This mechanism is the basis of a new mechanokinetic model for contractility, using the biochemical actomyosin ATPase cycle, strain-dependent kinetics and dimeric myosins on buckling rods. In this model, phosphate-dependent aspects of contractility arise from a rapid reversible release of phosphate from the initial bound state (A.M.ADP.Pi), which triggers the stroke. Added phosphate drives bound myosin towards this initial state, and the transient tension response to a phosphate jump reflects the rate at which it detaches from actin. Predictions for the tensile and energetic properties of striated muscle as a function of phosphate level, including the tension responses to length steps and Pi-jumps, are compared with experimental data from rabbit psoas fibres at 10 °C. The phosphate sensitivity of isometric tension is maximal when the actin affinity of M.ADP.Pi is near unity. Hence variations in actin affinity modulate the phosphate dependence of isometric tension, and may explain why phosphate sensitivity is temperature-dependent or absent in different muscles.

Indexed as

Models, BiologicalAnimalsBiomechanical PhenomenaMuscle ContractionMuscle Fibers, SkeletalMyosinsPhosphatesRabbitsMyosinsPhosphates

Identifiers

PMID25319769
OpenAlexW2327099584

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.