ArticleMethods in enzymology2014
Bacterial actin-like proteins: purification and characterization of self-assembly properties.
Article in Methods in enzymology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- The evolution of spherical cell shape; progress and perspective.Biochemical Society transactions · 2019Review
- Archaeal actin from a hyperthermophile forms a single-stranded filament.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Bacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular Functions.The Journal of biological chemistry · 2015Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The sequence, structure, and assembly dynamics of eukaryotic actins are conserved across phyla. In contrast, actin-like proteins (ALPs) from eubacteria share little sequence homology, form polymers with different architectures, and assemble with different kinetics. The structural and functional diversity of the bacterial ALPs appears to arise from their (i) high degree of functional specialization and (ii) small number of regulatory factors. To understand the molecular mechanism by which a given ALP carries out its biological function, we must, therefore, understand its unique architecture and assembly dynamics. In this chapter, we provide a basic toolbox for studying the self-assembly of uncharacterized ALPs, including methods for characterizing the architecture and stability of polymers, specifying the mechanism of their nucleation, and measuring their rate of growth. Determining these basic properties provides a stable base for more complex reconstitutions of biological function.
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