Mardo Kõivomägi

This study identifies a unique docking interface on cyclin D that binds Rb, a key cell cycle regulator, and shows that targeting this interface can inhibit cell proliferation.

This study identifies phosphorylation-dependent binding of APC to β-TrCP1 as a mechanism regulating β-catenin destruction in Wnt signaling.

The paper identifies CDK2 substrates in mouse ESCs, revealing HMCES phosphorylation's role in AP-site repair and ESC proliferation.

The paper screens peptide-binding pockets across cancer cell lines to identify therapeutic vulnerabilities and dependencies, finding that peptide inhibition can reveal hidden dependencies and enhance drug efficacy.

This study identifies distinct allosteric networks in CDK4 and CDK6 that explain their differential kinase activity, inhibitor binding, and roles in cell cycle regulation and drug resistance.

The paper challenges a model proposing that protein synthesis increases in pre-Start G1, finding that Whi5 concentration remains constant and Cln3 increase is not due to synthesis.