Dima A. Sabbah

TL;DR: This review explores EGFR structure and its mutations, signaling pathway, ligand binding and EGFR dimerization, EGF/EGFR interaction, and the progress in the development of EGFR inhibitors.

TL;DR: The data suggest that conformational differences in Gln859, Ser854, Tyr836, and Ser774 may be used to design ligands that are active against both the wt and H1047R mutant isoforms, and structural and size differences in the activation and hydrophobic domains could be exploited to direct the design of isoform- and/or mutant-specific PI3K inhibitors.

TL;DR: The drug design and clinical development of dual inhibitors of PI3K and mTOR as well as the mTOR-selective inhibitors, classified based on the mechanism of action and the chemical structures are discussed.

TL;DR: In this article, an informatics approach was introduced to study post-vaccine adverse events on the systems biology level to aid the prioritization of effective preventive measures and mechanism-based pharmacotherapy by integrating the analysis of adverse event reports from the Vaccine Adverse Event Reporting System (VAERS) with systems biology methods.

TL;DR: The pharmacophore searching identified three structurally novel inhibitors of PI3Kα and its H1047R mutant, and QPLD-based docking showed that residues Asp933, Glu849, Val851, and Gln859 appeared to be key binding residues for active inhibitors.