ArticleJournal of muscle research and cell motility1983
The effect of cytochalasin and glutaraldehyde on F-actin filaments containing muscle and non-muscle tropomyosin.
Article in Journal of muscle research and cell motility, 1983. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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
2 citing papers in PubMed, 8 citations in OpenAlex.
- Cytochalasans and Their Impact on Actin Filament Remodeling.Biomolecules · 2023Review
- Antibodies covalently immobilized on actin filaments for fast myosin driven analyte transport.PloS one · 2012Article
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
F-actin filaments are disrupted by the action of cytochalasin and glutaraldehyde. Muscle tropomyosin which is able to polymerize can protect F-actin against fragmentation caused by these two agents. This protective effect does not occur with nonpolymerizable, brain or carboxy-peptidase A-treated skeletal muscle tropomyosins. The protection of F-actin against the action of cytochalasin and glutaraldehyde takes place under conditions where the F-actin filaments are saturated with tropomyosin, that is, at a molar ratio of tropomyosin to actin of 1:7. It is suggested that nonpolymerizable tropomyosin lacks the protective ability because its binding to F-actin is considerably weaker than the polymerizable tropomyosin and does not saturate all of the binding sites on F-actin.
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.