Antonia A Högnäsbacka, Alex J Poot, Christophe Plisson, Jonas Bergare, David R Bonsall, Stuart P McCluskey, Lisa A Wells, Esther Kooijman, Robert C Schuit, Mariska Verlaan, Wissam Beaino, Guus A M S van Dongen, Danielle J Vugts, Charles S Elmore, Jan Passchier, Albert D Windhorst
BACKGROUND: Mutations in the epidermal growth factor receptor (EGFR) kinase domain are common in non-small cell lung cancer. Conventional tyrosine kinase inhibitors target the mutation site in the ATP binding pocket, thereby inhibiting the receptor's function. However, subsequent treatment resistance mutations in the ATP binding site are common. The EGFR allosteric inhibitor, EAI045, is proposed to have an alternative mechanism of action, disrupting receptor signaling independent of the ATP-binding site...
February 16, 2024: EJNMMI Research