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Article

Mutations in beta-actin: influence on polymer formation and on interactions with myosin and profilin.

FEBS letters - 23 Aug 1993

Aspenström P, Schutt C E, Lindberg U, Karlsson R

Abstract excerpt

Two beta-actin mutants, one with proline 38 replaced with alanine (P38A) and the other with cysteine-374 replaced with serine (C374S), as well as the wild-type beta-actin, were expressed in the yeast, S. cerevisiae, purified to homogeneity, and analyzed in vitro for polymerizability and interaction with DNase I, myosin, and profilin. Both mutations interfered with the polymerization of the actin, and with its...

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Source

Identifiers

PMID: 8354391
DOI: 10.1016/0014-5793(93)80215-g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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