ArticleACS chemical biology2020
Application of a Sulfoxonium Ylide Electrophile to Generate Cathepsin X-Selective Activity-Based Probes.
Article in ACS chemical biology, 2020. 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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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Cathepsin Z/X: Breaking Down the Known and Unknown.International journal of molecular sciences · 2026Review
- Loss of Cathepsin Z enhances pro-inflammatory macrophage responses and promotes tissue regeneration.Disease models & mechanisms · 2026Article
- Probing the activity of cysteine cathepsins in inflammatory bowel diseases.Scientific reports · 2025Article
- Expanding the Library of Covalent Cysteine Cathepsin Probes Featuring Sulfoxonium Ylide Electrophiles.ACS omega · 2024Article
- Cathepsin X deficiency alters the processing and localisation of cathepsin L and impairs cleavage of a nuclear cathepsin L substrate.Biological chemistry · 2024Article
- The thiol-sulfoxonium ylide photo-click reaction for bioconjugation.Chemical science · 2023Article
- Cathepsins in oral diseases: mechanisms and therapeutic implications.Frontiers in immunology · 2023Review
- Inverse Drug Discovery identifies weak electrophiles affording protein conjugates.Current opinion in chemical biology · 2022Review
- Asymmetric transformations from sulfoxonium ylides.Chemical science · 2022Review
- Near-Infrared Fluorescent Probes for the Detection of Cancer-Associated Proteases.ACS chemical biology · 2021Review
- Molecular probes for selective detection of cysteine cathepsins.Organic & biomolecular chemistry · 2021Review
- Proteomics Analysis of Tears and Saliva From Sjogren's Syndrome Patients.Frontiers in pharmacology · 2021Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 4 countries.
Funding
Abstract
Cathepsin X/Z/P is cysteine cathepsin with unique carboxypeptidase activity. Its expression is associated with cancer and neurodegenerative diseases, although its roles during normal physiology are still poorly understood. Advances in our understanding of its function have been hindered by a lack of available tools that can specifically measure the proteolytic activity of cathepsin X. We present a series of activity-based probes that incorporate a sulfoxonium ylide warhead, which exhibit improved specificity for cathepsin X compared to previously reported probes. We apply these probes to detect cathepsin X activity in cell and tissue lysates, in live cells and in vivo, and to localize active cathepsin X in mouse tissues by microscopy. Finally, we utilize an improved method to generate chloromethylketones, necessary intermediates for synthesis of acyloxymethylketones probes, by way of sulfoxonium ylide intermediates. In conclusion, the probes presented in this study will be valuable for investigating cathepsin X pathophysiology.
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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.