Yinxing Zhu

Abstract EGFR L858R is an activating mutation associated with aberrant EGFR signalling, and molecules capable of recognising this mutant remain of research interest. In this study, a virtual peptide library containing 59 319 heptapeptides was screened against the EGFR L858R crystal structure, leading to the identification of four peptides with favourable predicted binding ability.

3. Discussion Emerging of new reassortment viruses and drug resistance to conventional vaccination and antiviral therapies raises concerns about future pandemics. Since in viruses the evolution of resistance to host-targeted therapeutics is deemed to be slow, we aimed to identify potential host factors that can act as anti-viral targets. Based on the previous genome scale screens for host factors required for IAV replication, we screened and chose TNPO3 for further research.