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Thiol stress–dependent aggregation of the glycolytic enzyme triose phosphate isomerase in yeast and human cells

The eukaryotic cytosolic proteome is vulnerable to changes in proteostatic and redox balance caused by temperature, pH, oxidants, and xenobiotics. Cysteine-containing proteins are especially at risk, as the thiol side chain is subject to oxidation, adduction, and chelation by thiol-reactive compound...

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Detalles Bibliográficos
Autores principales: Ford, Amy E., Denicourt, Catherine, Morano, Kevin A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6589699/
https://www.ncbi.nlm.nih.gov/pubmed/30601716
http://dx.doi.org/10.1091/mbc.E18-10-0616

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