Heat shock protein 90 inhibitors augment endogenous wild-type p53 expression but down-regulate the adenovirally-induced expression by inhibiting a proteasome activity

Heat shock protein 90 (HSP90) inhibitors suppressed MDM4 functions which mediated p53 ubiquitination, and blocked a chaperon function which influenced expression of the client proteins. We examined cytotoxic effects of the inhibitors, 17-allylamino-17-demetheoxygeldanamycin (17-AAG) and 17-dimethyla...

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Detalles Bibliográficos
Autores principales: Chai, Kuan, Ning, Xuerao, Nguyễn, Thảo Thi Thanh, Zhong, Boya, Morinaga, Takao, Li, Zhihan, Shingyoji, Masato, Tada, Yuji, Tatsumi, Koichiro, Shimada, Hideaki, Hiroshima, Kenzo, Yamaguchi, Naoto, Tagawa, Masatoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2018
Materias:
Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5995238/
https://www.ncbi.nlm.nih.gov/pubmed/29899847
http://dx.doi.org/10.18632/oncotarget.25452

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5995238/
https://www.ncbi.nlm.nih.gov/pubmed/29899847
http://dx.doi.org/10.18632/oncotarget.25452

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