Evidence map›Paper›PMID 41262985›Full record

ReviewFrontiers in physiology2025

Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.

Marco Caremani, Irene Pertici, Ilaria Morotti, Pasquale Bianco, Massimo Reconditi, Gabriella Piazzesi, Vincenzo Lombardi, Marco Linari

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Frontiers in physiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Marco CaremaniPhysioLab, University of Florence, Florence, Italy.
Irene PerticiPhysioLab, University of Florence, Florence, Italy.
Ilaria MorottiPhysioLab, University of Florence, Florence, Italy.
Pasquale BiancoPhysioLab, University of Florence, Florence, Italy.
Massimo ReconditiPhysioLab, University of Florence, Florence, Italy.
Gabriella PiazzesiPhysioLab, University of Florence, Florence, Italy.
Vincenzo LombardiPhysioLab, University of Florence, Florence, Italy.
Marco LinariPhysioLab, University of Florence, Florence, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the striated muscle, the molecular motor myosin II functions in two bipolar arrays in each thick filament, converting chemical energy into steady force and shortening by cyclic ATP-driven interactions with nearby actin filaments. The fundamental steps in energy transduction are the working stroke, an inter-domain tilting of the lever arm about the actin-attached catalytic domain, generating up to ∼5 pN force or ∼10 nm of filament sliding, and the release of the ATP hydrolysis product orthophosphate (Pi) from the nucleotide-binding site, which is associated with a large free energy release. The two events are not simultaneous, as first demonstrated by the force response to a stepwise change in [Pi] (the Pi transient), showing the saturation kinetics characteristic of a two-step reaction. However, while high-resolution crystal structures of the myosin motor suggest that Pi release precedes the working stroke,

Indexed as

actin–myosin cyclechemo-mechanical couplingenergy transduction by myosinmyosin working stroke kineticsorthophosphate releaseunconventional actin–myosin ATPase cycle

Identifiers

PMID41262985
PMCPMC12623182

What OpenQuestion holds

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Registered trials

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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.