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Methods to Discover and Evaluate Proteasome Small Molecule Stimulators

Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 610 Purdue Mall, West Lafayette, IN 47907, USA
Author to whom correspondence should be addressed.
Molecules 2019, 24(12), 2341;
Received: 31 May 2019 / Revised: 18 June 2019 / Accepted: 22 June 2019 / Published: 25 June 2019
(This article belongs to the Special Issue Proteasome Regulators: Activators and Inhibitors)
Protein accumulation has been identified as a characteristic of many degenerative conditions, such as neurodegenerative diseases and aging. In most cases, these conditions also present with diminished protein degradation. The ubiquitin-proteasome system (UPS) is responsible for the degradation of the majority of proteins in cells; however, the activity of the proteasome is reduced in these disease states, contributing to the accumulation of toxic protein. It has been hypothesized that proteasome activity, both ubiquitin-dependent and -independent, can be chemically stimulated to reduce the load of protein in diseased cells. Several methods exist to identify and characterize stimulators of proteasome activity. In this review, we detail the ways in which protease activity can be enhanced and analyze the biochemical and cellular methods of identifying stimulators of both the ubiquitin-dependent and -independent proteasome activities. View Full-Text
Keywords: proteasome; stimulation; fluorescent probes; 20S CP proteasome; stimulation; fluorescent probes; 20S CP
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MDPI and ACS Style

Coleman, R.A.; Trader, D.J. Methods to Discover and Evaluate Proteasome Small Molecule Stimulators. Molecules 2019, 24, 2341.

AMA Style

Coleman RA, Trader DJ. Methods to Discover and Evaluate Proteasome Small Molecule Stimulators. Molecules. 2019; 24(12):2341.

Chicago/Turabian Style

Coleman, Rachel A.; Trader, Darci J. 2019. "Methods to Discover and Evaluate Proteasome Small Molecule Stimulators" Molecules 24, no. 12: 2341.

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