scispace - formally typeset
M

Maciej Masłyk

Researcher at John Paul II Catholic University of Lublin

Publications -  58
Citations -  972

Maciej Masłyk is an academic researcher from John Paul II Catholic University of Lublin. The author has contributed to research in topics: Steroid sulfatase & Candida albicans. The author has an hindex of 15, co-authored 50 publications receiving 602 citations. Previous affiliations of Maciej Masłyk include The Catholic University of America & CEU San Pablo University.

Papers
More filters
Journal ArticleDOI

Synthesis, biological activity and structural study of new benzotriazole-based protein kinase CK2 inhibitors

TL;DR: Docking studies as well as crystallographic analysis allowed us to identify ligand–CK2 interactions that account for the molecular recognition process, and can help to further optimize this family of compounds as CK2 inhibitors.
Journal ArticleDOI

Phosphorylation of thymidylate synthase from various sources by human protein kinase CK2 and its catalytic subunits.

TL;DR: Human TS exhibits unaltered K(m) values for dUMP and N(5,10)-methylenetetrahydrofolate, but a 50% lower turnover number, pointing to a strong influence of Ser(124) phosphorylation on its catalytic efficiency.
Journal ArticleDOI

Synthesis and Biological Evaluation of Fluorinated 3-Phenylcoumarin-7-O-Sulfamate Derivatives as Steroid Sulfatase Inhibitors.

TL;DR: The initial results of this study report on a series of 3‐phenylcoumarin sulfamate‐based compounds containing C‐F bonds as novel inhibitors of steroid sulfatase, possessing more than 10 times higher inhibitory potency than coumarin‐7‐O‐sulfamate.
Journal ArticleDOI

Phosphate tricyclic coumarin analogs as steroid sulfatase inhibitors: synthesis and biological activity

TL;DR: In the course of the investigation, the largest inhibitory effects in the STS enzyme assays were observed for the three compounds 9p, 9r and 9s, with IC50 values of 36.4, 37.4 and 21.5 μM.
Journal ArticleDOI

Benzimidazole inhibitors of protein kinase CK2 potently inhibit the activity of atypical protein kinase Rio1

TL;DR: Docking studies revealed that TIBI can occupy the ATP-binding site of Rio1 in a manner similar to toyocamycin, and enhances the thermostability of the enzyme.