ArticleBiophysical journal1999
Water in actin polymerization.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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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.
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Who cites it
6 citing papers in PubMed, 31 citations in OpenAlex.
- Crowding alters F-actin secondary structure and hydration.Communications biology · 2023Article
- Role of Changes in State of Bound Water and Tissue Stiffness in Development of Age-Related Diseases.Polymers · 2020Review
- Cell wounding and repair in ventilator injured lungs.Respiratory physiology & neurobiology · 2008Review
- Effects of solution crowding on actin polymerization reveal the energetic basis for nucleotide-dependent filament stability.Journal of molecular biology · 2008Article
- Radial compression of microtubules and the mechanism of action of taxol and associated proteins.Biophysical journal · 2005Article
- Thymosin-beta(4) changes the conformation and dynamics of actin monomers.Biophysical journal · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have addressed the question whether water is part of the G- to F-actin polymerization reaction. Under osmotic stress, the critical concentration for G-Ca-ATP actin was reduced for six different osmolytes. These results are interpreted as showing that reducing water activity favored the polymerized state. The magnitude of the effect correlated, then saturated, with increasing MW of the osmolyte and suggested that up to 10-12 fewer water molecules were associated with actin when it polymerized. By contrast, osmotic effects were insignificant for Mg-ATP actin. The nucleotide binding site of the Mg conformation is more closed than the Ca and more closely resembles the closed actin conformation in the polymerized state. These results suggest that the water may come from the cleft of the nucleotide binding site.
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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.