Ontology highlight
ABSTRACT:
SUBMITTER: Provenzani R
PROVIDER: S-EPMC5895059 | biostudies-literature | 2018
REPOSITORIES: biostudies-literature
Provenzani Riccardo R Tarvainen Ilari I Brandoli Giulia G Lempinen Antti A Artes Sanna S Turku Ainoleena A Jäntti Maria Helena MH Talman Virpi V Yli-Kauhaluoma Jari J Tuominen Raimo K RK Boije Af Gennäs Gustav G
PloS one 20180411 4
Protein kinase C (PKC) isoforms play a pivotal role in the regulation of numerous cellular functions, making them extensively studied and highly attractive drug targets. Utilizing the crystal structure of the PKCδ C1B domain, we have developed hydrophobic isophthalic acid derivatives that modify PKC functions by binding to the C1 domain of the enzyme. In the present study, we aimed to improve the drug-like properties of the isophthalic acid derivatives by increasing their solubility and enhancin ...[more]