ArticleAnalytical biochemistry2016
An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates.
Article in Analytical biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed.
- Studying Exoribonuclease Activity Using Fluorescence Anisotropy Assay.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Analysis of Protein Degradation in Ferroptosis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Biology of the Extracellular Proteasome.Biomolecules · 2022Review
- Kinetic Analysis of AAA+ Translocases by Combined Fluorescence and Anisotropy Methods.Biophysical journal · 2020Article
- How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell.Biomolecules · 2019Review
- Article
- A Practical Review of Proteasome Pharmacology.Pharmacological reviews · 2019Review
- A High-Throughput Assay for Monitoring Ubiquitination in Real Time.Frontiers in chemistry · 2019Article
- Highlighting the Proteasome: Using Fluorescence to Visualize Proteasome Activity and Distribution.Frontiers in molecular biosciences · 2019Review
- Reprogramming a Deubiquitinase into a Transamidase.ACS chemical biology · 2018Article
- Measurement of the Multiple Activities of 26S Proteasomes.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Genetic and Epigenetic Strategies Potentiate Gal4 Activation to Enhance Fitness in Recently Diverged Yeast Species.Current biology : CB · 2017Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The 26S proteasome is the molecular machine at the center of the ubiquitin proteasome system and is responsible for adjusting the concentrations of many cellular proteins. It is a drug target in several human diseases, and assays for the characterization of modulators of its activity are valuable. The 26S proteasome consists of two components: a core particle, which contains the proteolytic sites, and regulatory caps, which contain substrate receptors and substrate processing enzymes, including six ATPases. Current high-throughput assays of proteasome activity use synthetic fluorogenic peptide substrates that report directly on the proteolytic activity of the proteasome, but not on the activities of the proteasome caps that are responsible for protein recognition and unfolding. Here, we describe a simple and robust assay for the activity of the entire 26S proteasome using fluorescence anisotropy to follow the degradation of fluorescently labeled protein substrates. We describe two implementations of the assay in a high-throughput format and show that it meets the expected requirement of ATP hydrolysis and the presence of a canonical degradation signal or degron in the target protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.