ArticleBiophysical journal1994
Orientation of actin filaments during motion in in vitro motility assay.
Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Fluorescence polarization/anisotropy in diagnostics and imaging.Chemical reviews · 2010Review
- Changes in actin and myosin structural dynamics due to their weak and strong interactions.Results and problems in cell differentiation · 2002Review
- Actin protofilament orientation at the erythrocyte membrane.Biophysical journal · 1999Article
- Orientation of cross-bridges in skeletal muscle measured with a hydrophobic probe.Biophysical journal · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Rhodamine-phalloidin was added to F-actin, and the orientation of transition dipoles of the dye was measured in single actin filaments by polarization of fluorescence. Rhodamine-phalloidin was well immobilized on the surface of actin, indicating that changes in orientation of the dye reported changes in orientation of actin monomers. In stationary filaments the dipoles were inclined at 49.3 degrees with respect to the filament axis. The disorganization of dipoles in stationary filaments was insignificant. When the filaments were made to translate, the average orientation of the dye did not change, but disorganization slightly increased. Disorganization increased significantly when filaments were free in solution. We concluded that, within the accuracy of our measurements (approximately 18%), actin monomers did not undergo major reorientations during motion, but that binding of myosin heads deformed the structure of filaments.
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Registered trials
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