Cargando…
Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids
As primary p53 antagonists, Mdm2 and the closely related Mdm4 are relevant cancer therapeutic targets. We have previously described a series of cell-permeable stapled peptides that bind to Mdm2 with high affinity, resulting in activation of the p53 tumour suppressor. Within this series, highest affi...
Autores principales: | Chee, Sharon Min Qi, Wongsantichon, Jantana, Siau, Jiawei, Thean, Dawn, Ferrer, Fernando, Robinson, Robert C., Lane, David P., Brown, Christopher J., Ghadessy, Farid J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5724825/ https://www.ncbi.nlm.nih.gov/pubmed/29228061 http://dx.doi.org/10.1371/journal.pone.0189379 |
Ejemplares similares
-
Structure of a Stapled Peptide Antagonist Bound to Nutlin-Resistant Mdm2
por: Chee, Sharon Min Qi, et al.
Publicado: (2014) -
The p53–Mdm2 interaction and the E3 ligase activity of Mdm2/Mdm4 are conserved from lampreys to humans
por: Coffill, Cynthia R., et al.
Publicado: (2016) -
Assessing the Efficacy of Mdm2/Mdm4-Inhibiting Stapled Peptides Using Cellular Thermal Shift Assays
por: Xiong Tan, Ban, et al.
Publicado: (2015) -
Anatomy of Mdm2 and Mdm4 in evolution
por: Tan, Ban Xiong, et al.
Publicado: (2017) -
Stereoisomerism of stapled peptide inhibitors of the p53-Mdm2 interaction: an assessment of synthetic strategies and activity profiles
por: Yuen, Tsz Ying, et al.
Publicado: (2019)