Thiostrepton interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates

Here, we report a novel mechanism of proteasome inhibition mediated by Thiostrepton (Thsp), which interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates. We identified Thsp in a cell-based high-throughput screen using a fluorescent reporter sensitive to degradation by...

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Detalles Bibliográficos
Autores principales: Sandu, Cristinel, Chandramouli, Nagaranjan, Glickman, Joseph Fraser, Molina, Henrik, Kuo, Chueh-Ling, Kukushkin, Nikolay, Goldberg, Alfred L, Steller, Hermann
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Ltd 2015
Materias:
Original Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4568923/
https://www.ncbi.nlm.nih.gov/pubmed/26033448
http://dx.doi.org/10.1111/jcmm.12602

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4568923/
https://www.ncbi.nlm.nih.gov/pubmed/26033448
http://dx.doi.org/10.1111/jcmm.12602

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