ArticleJournal of muscle research and cell motility1986
Myosin specific phosphatases isolated from Dictyostelium discoideum.
Article in Journal of muscle research and cell motility, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Myosin II dynamics and cortical flow during contractile ring formation in Dictyostelium cells.The Journal of cell biology · 2001Article
- Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells.The Journal of cell biology · 1997Article
- Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells.The Journal of cell biology · 1994Article
- Release of myosin II from the membrane-cytoskeleton of Dictyostelium discoideum mediated by heavy-chain phosphorylation at the foci within the cortical actin network.The Journal of cell biology · 1992Article
- Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the essential light chain.Molecular and cellular biology · 1988Article
- Effect of heavy chain phosphorylation on the polymerization and structure of Dictyostelium myosin filaments.The Journal of cell biology · 1987Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Using native myosin phosphorylated on either the heavy chain or the light chain, we have isolated myosin phosphatases from extracts of vegetative Dictyostelium amoeba. Two phosphatases were resolved by DEAE-cellulose chromatography. One of these phosphatases removed phosphate from heavy chain or light chain at approximately the same rate. The other phosphatase appeared to be much more specific for phosphorylated myosin heavy chain. Although these enzymes removed phosphate from other phosphoprotein substrates such as histone or casein, they did so at a much lower rate. Both enzymes required magnesium for activity, but appeared to be independent of calcium.
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Registered trials
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