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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...
Autores principales: | Ford, Amy E., Denicourt, Catherine, Morano, Kevin A. |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2019
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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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