ArticleChembiochem : a European journal of chemical biology2017
Activity-Based Probes for HECT E3 Ubiquitin Ligases.
Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Tsg101 mimicry of canonical E2 enzymes underlies its role in ubiquitin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025Review
- Reconstitution and Structural Analysis of a HECT Ligase-Ubiquitin Complex via an Activity-Based Probe.ACS chemical biology · 2021Article
- Decoding the messaging of the ubiquitin system using chemical and protein probes.Cell chemical biology · 2021Review
- Tools for Decoding Ubiquitin Signaling in DNA Repair.Frontiers in cell and developmental biology · 2021Review
- Ubiquitomics: An Overview and Future.Biomolecules · 2020Review
- Development and application of ubiquitin-based chemical probes.Chemical science · 2020Review
- Protein Engineering in the Ubiquitin System: Tools for Discovery and Beyond.Pharmacological reviews · 2020Review
- Strategies to Target Specific Components of the Ubiquitin Conjugation/Deconjugation Machinery.Frontiers in chemistry · 2019Review
- Small molecule inhibitors reveal allosteric regulation of USP14 via steric blockade.Cell research · 2018Article
- Article
- Activity-Based Probes for HECT E3 Ubiquitin Ligases.Chembiochem : a European journal of chemical biology · 2017Article
- The deubiquitinase TRABID stabilizes the K29/K48-specific E3 ubiquitin ligase HECTD1.The Journal of biological chemistryArticle
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3 authors.
Funding
Abstract
Activity-based probes (ABPs) have been used to dissect the biochemical/structural properties and cellular functions of deubiquitinases. However, their utility in studying cysteine-based E3 ubiquitin ligases has been limited. In this study, we evaluate the use of ubiquitin-ABPs (Ub-VME and Ub-PA) and a novel set of E2-Ub-ABPs on a panel of HECT E3 ubiquitin ligases. Our in vitro data show that ubiquitin-ABPs can label HECT domains. We also provide the first evidence that, in addition to the RBR E3 ubiquitin ligase Parkin, E2-Ub-ABPs can also label the catalytic HECT domains of NEDD4, UBE3C, and HECTD1. Importantly, the endogenous proteasomal E3 ligase UBE3C was also successfully labelled by Ub-PA and His-UBE2D2-Ub-ABP in lysate of cells grown under basal conditions. Our findings provide novel insights into the use of ABPs for the study of HECT E3 ubiquitin ligases.
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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.