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Development and evaluation of a highly reliable assay for SUMO-specific protease inhibitors.
- Source :
-
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2016 May 01; Vol. 26 (9), pp. 2124-8. Date of Electronic Publication: 2016 Mar 23. - Publication Year :
- 2016
-
Abstract
- SUMOylation, as a post-translational modification of proteins, plays essential regulatory roles in a variety of pathological conditions. In the dynamic process of SUMOylation and deSUMOylation, SENPs (SUMO-specific proteases), in charge of deconjugation of SUMO (small ubiquitin-related modifier) from substrate proteins, have recently been found to be potential therapeutic targets for cancer treatment. A reliable and practical assay is much needed to accelerate the discovery of SENPs inhibitors. We established a quantitative assay based on readily available SDS-PAGE-Coomassie system using RanGAP-SUMO as the substrate, thus avoiding the use of expensive fluorescent dyes or the error-prone fluorescent reporter. Its reproducibility and reliability were also evaluated in this report.<br /> (Copyright © 2016. Published by Elsevier Ltd.)
- Subjects :
- Benzamides analysis
Coloring Agents
Cysteine Endopeptidases chemistry
Cysteine Endopeptidases genetics
GTPase-Activating Proteins chemistry
GTPase-Activating Proteins genetics
Humans
Hydrolysis
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Rosaniline Dyes
Enzyme Assays methods
Protease Inhibitors analysis
Subjects
Details
- Language :
- English
- ISSN :
- 1464-3405
- Volume :
- 26
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Bioorganic & medicinal chemistry letters
- Publication Type :
- Academic Journal
- Accession number :
- 27032332
- Full Text :
- https://doi.org/10.1016/j.bmcl.2016.03.080