作者: Dipankar Ray , Kyle C. Cuneo , Alnawaz Rehemtulla , Theodore S. Lawrence , Mukesh K. Nyati
DOI: 10.1016/J.NEO.2015.08.008
关键词: Phosphorylation 、 Ubiquitin 、 Acetylation 、 Drug 、 Cancer 、 Pharmacology 、 Cancer research 、 Biology 、 Small molecule 、 Kinase 、 Oncogene Proteins
摘要: Over the past decade, inhibition of kinase activities oncogenic proteins using small molecules and antibodies has been a mainstay our anticancer drug development effort, resulting in several Food Drug Administration–approved cancer therapies. The clinical effectiveness kinase-targeted agents inconsistent, mostly because resistance. expression function oncoproteins tumor suppressors are regulated by numerous posttranslational protein modifications including phosphorylation, ubiquitination, acetylation; hence, targeting specific provides for an attractive strategy development. present review discusses hypothesis that targeted degradation oncoprotein may overcome many shortcomings seen with inhibitors approach would enable previously thought to be undruggable.