Abstract
The ubiquitin-proteasome system oversees cellular protein degradation in order to regulate various critical processes, such as cell cycle control and DNA repair. Ubiquitination can serve as a marker for mutation, chemical damage, transcriptional or translational errors, and heat-induced denaturation. However, aberrant ubiquitination and degradation of tumor suppressor proteins may result in the growth and metastasis of cancer. Hence, targeting the ubiquitination cascade reaction has become a potential strategy for treating malignant diseases. Meanwhile, computer-aided methods have become widely accepted as fast and efficient techniques for early stage drug discovery. This review summarizes ubiquitination regulators that have been discovered via virtual screening and their applications for cancer treatment.
Highlights
Ubiquitin is a 76-residue protein that is highly conserved in most eukaryotes (Finley and Chau, 1991; Ben-Neriah, 2002)
Virtual screening has emerged as an indispensable part of drug discovery efforts and has become widely employed in pharmaceutical research
We have highlighted the use of virtual screening strategies to identify ubiquitination regulators, including E2, E3, proteasome and deubiquitinating enzymes (DUBs) regulators
Summary
Ubiquitin is a 76-residue protein that is highly conserved in most eukaryotes (Finley and Chau, 1991; Ben-Neriah, 2002). Ubiquitination Regulators and Virtual Screening protein (Rape, 2018). Virtual screening has been employed for identifying inhibitors of cancer targets (Zhong et al, 2016; Li et al, 2020). Utomo et al (2012) used virtual screening to identify drug-like compounds that can interrupt the stability of the p53mortalin complex interaction, an anticancer target.
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