Matches in SemOpenAlex for { <https://semopenalex.org/work/W51164494> ?p ?o ?g. }
- W51164494 endingPage "a018226" @default.
- W51164494 startingPage "a018226" @default.
- W51164494 abstract "Organisms from all domains of life depend on filaments of the protein actin to provide structure and to support internal movements. Many eukaryotic cells use forces produced by actin polymerization for their motility, and myosin motor proteins use ATP hydrolysis to produce force on actin filaments. Actin polymerizes spontaneously, followed by hydrolysis of a bound adenosine triphosphate (ATP). Dissociation of the γ-phosphate prepares the polymer for disassembly. This review provides an overview of the properties of actin and shows how dozens of proteins control both the assembly and disassembly of actin filaments. These players catalyze nucleotide exchange on actin monomers, initiate polymerization, promote phosphate dissociation, cap the ends of polymers, cross-link filaments to each other and other cellular components, and sever filaments." @default.
- W51164494 created "2016-06-24" @default.
- W51164494 creator A5043478405 @default.
- W51164494 date "2016-03-17" @default.
- W51164494 modified "2023-10-14" @default.
- W51164494 title "Actin and Actin-Binding Proteins" @default.
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