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Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary
BACKGROUND: Cysteinyl residues in actin are glutathionylated, ie. form a mixed disulfide with glutathione, even in the absence of exogenous oxidative stress. Glutathionylation inhibits actin polymerization and reversible actin glutathionylation is a redox dependent mechanism for regulation of the cy...
| Autores principales: | , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
BioMed Central
2007
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2228301/ https://www.ncbi.nlm.nih.gov/pubmed/18070357 http://dx.doi.org/10.1186/1471-2091-8-26 |