Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation

The cellular abundance of the cyclin-dependent kinase (Cdk) inhibitor p27 is regulated by the ubiquitin–proteasome system. Activation of p27 degradation is seen in proliferating cells and in many types of aggressive human carcinomas. p27 can be phosphorylated on threonine 187 by Cdks, and cyclin E/C...

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Vydáno v:	Genes Dev
Hlavní autoři:	Montagnoli, Alessia, Fiore, Francesca, Eytan, Esther, Carrano, Andrea C., Draetta, Giulio F., Hershko, Avram, Pagano, Michele
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Cold Spring Harbor Laboratory Press 1999
Témata:	Research Paper
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC316946/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10323868/ https://ncbi.nlm.nih.govhttps://doi.org/10.1101/gad.13.9.1181
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