Cargando…
An Irreversible Inhibitor of HSP72 that Unexpectedly Targets Lysine‐56
The stress‐inducible molecular chaperone, HSP72, is an important therapeutic target in oncology, but inhibiting this protein with small molecules has proven particularly challenging. Validating HSP72 inhibitors in cells is difficult owing to competition with the high affinity and abundance of its en...
Autores principales: | Pettinger, Jonathan, Le Bihan, Yann‐Vaï, Widya, Marcella, van Montfort, Rob L. M., Jones, Keith, Cheeseman, Matthew D. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5412842/ https://www.ncbi.nlm.nih.gov/pubmed/28225177 http://dx.doi.org/10.1002/anie.201611907 |
Ejemplares similares
-
Kinetic Optimization
of Lysine-Targeting Covalent
Inhibitors of HSP72
por: Pettinger, Jonathan, et al.
Publicado: (2019) -
Coupling of HSP72 α-Helix Subdomains by the Unexpected Irreversible Targeting of Lysine-56 over Cysteine-17; Coevolution of Covalent Bonding
por: Aljoundi, Aimen, et al.
Publicado: (2020) -
Discovery and Characterization of a Cryptic Secondary Binding Site in the Molecular Chaperone HSP70
por: O’Connor, Suzanne, et al.
Publicado: (2022) -
Exploiting Protein
Conformational Change to Optimize
Adenosine-Derived Inhibitors of HSP70
por: Cheeseman, Matthew D., et al.
Publicado: (2016) -
HSP72 Up-regulation with heat acclimation
por: Schneider, Suzanne M., et al.
Publicado: (2016)