Ylva Ivarsson

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.

The paper maps over 20,000 human protein-protein interactions mediated by short linear motifs using a peptide library screening approach.

The paper systematically identifies SLiM-binding interactions of USP family auxiliary domains using proteomic and biochemical methods, revealing functional redundancy and motif specificity.

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 uses AlphaFold to predict structures of host-pathogen PPIs, revealing molecular mimicry modes and convergent evolution of interaction interfaces.

This study uses phage-based deep mutational scanning to identify binding determinants of short linear motifs between human and SARS-CoV-2 proteins, refining motifs and identifying affinity-enhancing mutations.

The paper characterizes how disease mutations in intrinsically disordered regions modulate protein interactions mediated by short linear motifs, identifying both loss and gain of interactions.

This study benchmarks five motif discovery tools and seven sequence alignment tools on their ability to find short linear motifs in peptides, identifying DEME, SLiMFinder, and Opal as top performers.

The paper identifies SARS-CoV-2 protein domains that interact with human peptides and discovers antiviral peptides targeting Nsp9 and Nsp16.