Genomic alterations may make cancer cells more dependent than normal cells on
mechanisms of proteostasis, including protein folding and degradation. This proposition is …

The clinical successes of proteasome inhibitors for the treatment of cancer have highlighted
the therapeutic potential of targeting this protein degradation system. However, proteasome …

The ubiquitin–proteasome system (UPS) comprises a network of enzymes that is
responsible for maintaining cellular protein homeostasis. The therapeutic potential of this …

SUMOylation is a reversible post-translational modification that regulates protein function
through covalent attachment of small ubiquitin-like modifier (SUMO) proteins. The process of …

Growth factors and nutrients enhance protein synthesis and suppress overall protein
degradation by activating the protein kinase mammalian target of rapamycin (mTOR) …

Small ubiquitin-like modifier (SUMO) family proteins regulate target-protein functions by post-
translational modification. However, a potent and selective inhibitor targeting the SUMO …

Covering: up to 2020 The National Cancer Institute of the United States (NCI) has initiated a
Cancer Moonshot program entitled the NCI Program for Natural Product Discovery. As part …

Post-translational modifications of cellular substrates with ubiquitin and ubiquitin-like
proteins (UBLs), including ubiquitin, SUMOs, and neural precursor cell–expressed …

Aminoacyl transfer RNA (tRNA) synthetases (aaRSs) are attractive drug targets, and we
present class I and II aaRSs as previously unrecognized targets for adenosine 5 …

In the last decade, the ubiquitin–proteasome system has emerged as a valid target for the
development of novel therapeutics. E3 ubiquitin ligases are particularly attractive targets …