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...

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Detalles Bibliográficos
Autores principales: Johansson, Magnus, Lundberg, Mathias
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Research Article
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

Internet

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

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