ArticleAnalytical chemistry2019
Degronomics: Mapping the Interacting Peptidome of a Ubiquitin Ligase Using an Integrative Mass Spectrometry Strategy.
Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- COMMD9-regulated endothelial cell abnormality-induced hypercoagulability is associated with Budd-Chiari syndrome.International journal of surgery (London, England) · 2026Article
- High-Throughput Discovery of Substrate Peptide Sequences for E3 Ubiquitin Ligases Using a cDNA Display Method.Chembiochem : a European journal of chemical biology · 2024Article
- An artificial intelligence accelerated virtual screening platform for drug discovery.Nature communications · 2024Article
- Co-opting the E3 ligase KLHDC2 for targeted protein degradation by small molecules.Nature structural & molecular biology · 2024Article
- Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023Review
- E3 ligase autoinhibition by C-degron mimicry maintains C-degron substrate fidelity.Molecular cell · 2023Article
- PROTACs: Current Trends in Protein Degradation by Proteolysis-Targeting Chimeras.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2022Review
- Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry.Chemical science · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Human cells make use of hundreds of unique ubiquitin E3 ligases to ensure proteome fidelity and control cellular functions by promoting protein degradation. These processes require exquisite selectivity, but the individual roles of most E3s remain poorly characterized in part due to the challenges associated with identifying, quantifying, and validating substrates for each E3. We report an integrative mass spectrometry (MS) strategy for characterizing protein fragments that interact with KLHDC2, a human E3 that recognizes the extreme C-terminus of substrates. Using a combination of native MS, native top-down MS, MS of destabilized samples, and liquid chromatography MS, we identified and quantified a near complete fraction of the KLHDC2-binding peptidome in
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Registered trials
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