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- W2016030567 abstract "Actin binding protein from human blood platelets is shown to exist in the resting platelet as a phosphorylated protein and contains two residues of phosphate per 260,000 kd. Removal of one-half of these residues with E. coli alkaline phosphatase results in the loss of its ability to crosslink F-actin into a low speed sedimentable complex (its cytoskeleton) and to bind to an F-actin affinity column. Thus, phosphorylation-dephosphorylation of ABP may be an important regulatory mechanism by which the platelet regulates its shape via its cytoskeletal structure." @default.
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- W2016030567 date "1984-01-01" @default.
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- W2016030567 title "Role of actin binding protein phosphorylation in platelet cytoskeleton assembly" @default.
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- W2016030567 doi "https://doi.org/10.1016/0006-291x(84)91332-9" @default.
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