ArticleMethods in molecular biology (Clifton, N.J.)2023
Monitoring HECT Ubiquitination Activity In Vitro.
Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
1 citing paper in PubMed.
- Structure-based design of potent and selective inhibitors of the HECT ligase NEDD4.Communications chemistry · 2025Article
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Authors and funding
3 authors.
Funding
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Abstract
In vitro ubiquitination tools have been employed to mechanistically study the ubiquitin enzymatic cascade. Here, we describe an assay capable to monitor ubiquitin conjugation in real time using the Time-Resolved Fluorescence Resonance Energy Transfer (TR-FRET) system. The assay requires purified E1 and E2 enzymes, the HECT E3 ligase of choice and two fluorophore-labeled ubiquitins. This single step technique represents an excellent tool to study the enzymatic activity during chain elongation, to compare ligase activity in the presence or absence of the substrate, and to set-up high-throughput screenings for enzymatic activity modulators (i.e., activators or inhibitors).
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Registered trials
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