ArticleCommunications biology2026
Crosslinked F-actin networks regulate load-dependent energy conversion.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
Who cites it
1 citing paper in PubMed.
- State-dependent energy conversion produces degenerate dissipation in active actomyosin networks.bioRxiv : the preprint server for biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellular energy conversion from chemical energy to mechanical work underlies essential processes ranging from single-cell division to embryonic development. This energy is primarily derived from the hydrolysis of adenosine triphosphate (ATP), which powers motor proteins to generate forces on the filamentous cytoskeleton. While the load-dependent behaviors of individual motor proteins and ordered muscle fibers are well studied, how motor proteins collectively respond to mechanical load within cellular disordered cytoskeletal networks remains poorly understood. Here, we investigate this by reconstituting purified actomyosin networks crosslinked with various actin crosslinking proteins to mimic cellular environments. We find that structural and mechanical properties of the crosslinked networks, including inter-filament spacing, filament polarity, and network stiffness, modulate load-dependent myosin ATP consumption and inferred mechanical power generation. These findings reveal the intricate role of actin crosslinkers in regulating the mechano-chemical behavior of myosin, offering insight into how cells control energy conversion and force generation through cytoskeletal architecture.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.