Oliver Hantschel is a tenured Full Professor of Biochemistry and Director of the Institute for Physiological Chemistry at the Faculty of Medicine of the Philipps-University Marburg Research career. After undergraduate studies in Biochemistry at the University of Regensburg and Rockefeller University, he obtained a PhD degree (summa cum laude) from European Molecular Biology Laboratory in Heidelberg in 2004 for his thesis on the structure and regulation of the non-receptor tyrosine kinase c-Abl. Dr. Hantschel obtained his postdoctoral training at the Center for Molecular Medicine in Vienna with Giulio Superti-Furga (2004-2010), where he headed an independent subgroup and studied the selectivity and resistance mechanisms of kinase inhibitors, the signaling networks of Abl kinase fusions in leukemias and continued his work on allosteric regulation of BCR::ABL1. In parallel, Dr. Hantschel was teaching at the Medical University of Vienna and obtained my venia legend (Habilitation) in Experimental Haematology in 2010. In 2011, he built up my independent group at the École Polytechnique Fédérale de Lausanne as an Assistant Professor and endowed Chair in Translational Oncology. In 2020, he moved to Marburg after having received several offers for Full Professorships in Germany and Austria. Dr. Hantschel comprehensive structural analysis of the ABL1 kinase identified the myristoyl binding pocket as a critical regulator of BCR::ABL1 kinase activity in CML (Cell 2003, Cell 2003, Mol Cell 2006), which formed the basis for the development of the allosteric BCR::ABL1 inhibitor asciminib (Scemblix, Novartis; 3rd line treatment of CML in 2021, 1st line approval in 2024). First mechanisms of primary (Leukemia 2024) and secondary (Blood 2024) asciminib resistance were shown by his lab. In addition, he structurally and functionally characterized most other domains of BCR::ABL1, e.g. F-actin binding domain (Mol Cell 2004), DHPH domains (Nat Commun 2017), and identified a novel allosteric mechanism by the SH2-kinase domain interface in ABL1 (Cell 2010), BTK (Nat Commun 2017) and FES (Cell 2007). In parallel, they mapped the signaling networks of ABL1 fusion oncoproteins by interaction- and phosphoproteomics: BCR::ABL1 (PNAS 2009) and NUP214::ABL1 (Leukemia 2008, Haematologica 2014) core protein complex, differential signaling of p210 and p190 BCR::ABL1 isoforms (Leukemia 2017) in chronic vs. acute leukemias. He contributed to the first selectivity data for inhibitors of BCR::ABL1 (Blood 2007, Leukemia 2009) and JAK2 (Leukemia 2014), which identified clinically relevant offtargets connected to side-effects. He also identified TKI resistance mechanisms by deletion mutations (Leukemia 2008) and SH3-SH2 mutations (Blood 2010). His interest in kinase signaling and targeting of proteinprotein interaction has led him to develop high-affinity Monobody (Mb) protein inhibitors to several "untargetable" oncoproteins, including the SHP2 tyrosine phosphatase (PNAS 2013), STAT transcription factors (Nat Commun 2021) and SH2 domain-pY interactions (Cell 2011, JBC 2016, JMB 2017). To explore the potential of Mbs as novel protein therapeutics, they developed methods to deliver Mbs to cells using biologically-inspired delivery using the bacterial T3SS (CCAS 2024) and chimeric toxins (ACS Chem Biol 2019), improved biological stability/immunogenicity (“mirrorimage” D-monobodies: Nat Commun 2024) and assessed PK and biodistribution (Front Pharmacol 2024) laying thefoundation for in vivo development (SMW 2017).