Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/67176
Title: Discovery of inhibitors of deubiquitinase USP21
Authors: Chua, Joanna Hui Xin
Keywords: DRNTU::Science
DRNTU::Science::Biological sciences
Issue Date: 2016
Abstract: Ubiquitination plays critical roles in several cellular processes, and are hence potential therapeutic targets against several debilitating human diseases, including cancers. Among various components of the ubiquitin-proteasome system, the deubiquitinases, the enzymes that remove ubiquitin modifications from proteins, are considered as best targets for drug development. USP21 is a deubiquitinase that regulates multiple aspects of cell physiology, including negative regulation of antiviral innate immunity. Therefore, identification of USP21 inhibitors may help to boost antiviral immunity, among other functions. This project characterized 37 newly identified small-molecule inhibitors of USP21. The study was completed using a fluorescence-intensity based enzymatic assay for USP21 activity. To ensure the biochemical robustness of the compounds identified, the enzymatic assay for the screening of USP21 inhibitors was optimized and the kinetic properties of USP21 were characterized. Detailed analysis led to the identification of 12 potential drug candidates that displayed low micromolar inhibitory doses.
URI: http://hdl.handle.net/10356/67176
Rights: Nanyang Technological University
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)

Files in This Item:
File Description SizeFormat 
FYP Thesis (final).pdf
  Restricted Access
1.14 MBAdobe PDFView/Open

Page view(s) 50

325
Updated on Jun 23, 2021

Download(s)

11
Updated on Jun 23, 2021

Google ScholarTM

Check

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.