Allosteric Activation of Protein Phosphatase 5 with Small Molecules.
Journal
Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531
Informations de publication
Date de publication:
15 Aug 2024
15 Aug 2024
Historique:
medline:
15
8
2024
pubmed:
15
8
2024
entrez:
15
8
2024
Statut:
aheadofprint
Résumé
The activation of PP5 is essential for a variety of cellular processes, as it participates in a variety of biological pathways by dephosphorylating substrates. However, activation of PP5 by small molecules has been a challenge due to its native "self-inhibition" mechanism, which is controlled by the N-terminal TPR domain and the C-terminal αJ helix. Here, we reported the discovery of
Identifiants
pubmed: 39145509
doi: 10.1021/acs.jmedchem.4c00722
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM