Mihkel Örd

The paper identifies a non-canonical helical binding motif in MAD1 that specifically interacts with Cyclin B1 to recruit CDK1 to the SAC, revealing a mechanism for B-type cyclin recognition.

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 new HCF1 binding partners and molecular determinants, revealing how HCF1 regulates transcription and O-GlcNAcylation through affinity-dependent mechanisms.

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.

The paper identifies and characterizes cyclin-CDK docking motifs through high-throughput peptide binding assays and structural analysis, revealing a broader repertoire of motif types and binding mechanisms.

The paper introduces SIMBA, a functional assay to quantify SLiM binding, showing in vivo binding strength correlates with in vitro affinity and revealing context-dependent recognition determinants.

The paper identifies a furin cleavage motif in SARS-CoV2 Spike protein that requires a specific RRxR motif for cleavage and shows that phosphorylation of adjacent serines inhibits furin activity.

The paper analyzes fungal G1 cyclin docking motifs to determine their sequence features and regulatory potency in vivo.