Ylva Ivarsson’s main research interest is in the molecular interactions that underlie cellular signal transduction. In particular, her group focuses on mapping interactions between modular domains and motifs found in the intrinsically disordered regions of the human proteome. A considerable part of the human proteome is intrinsically disordered and the disordered regions are enriched in short motifs serving as docking sites for peptide binding domains. Domain-motif interactions are crucial for the wiring of signaling pathways but hese interactions are typically transient and difficult to capture through most conventional high-throughput methods. Therefore, her group has developed a novel approach for large-scale profiling of domain-motifs interactions, called Proteomic Peptide Phage Display (ProP-PD). This approach combines bioinformatics, oligonucleotide arrays, peptide phage display and next-generation sequencing. It allows the interrogation of domain-motif interactions on a proteome-wide scale and facilitates de novo motif discovery.