The DOI matches its Crossref record; 305 of the 305 references it cites were found in a registry or an index.
Actin and Actin-Binding Proteins
Open accessAbstract
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.
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Cited by
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The actin cytoskeleton and actin-based motility
Svitkina, T. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018267 · Cited by 761
Nonlinear dynamics of multi-omics profiles during human aging
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Vitamin D Binding Protein: A Historic Overview
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Metadata
- Authors
- Pollard, T. D.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2016-03-17
- Volume
- 8
- Issue
- 8
- Pages
- a018226
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W51164494
- Cited by
- 912
- References
- 305
- Type
- posted content
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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