ArticleJournal of the American Chemical Society2025
Ubiquitin Azapeptide Esters as Next-Generation Activity-Based Probes for Cysteine Enzymes in the Ubiquitin Signal Pathway.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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
4 citing papers in PubMed.
- Synthetic Strategies for Activity-Based Probes to Decode Ubiquitin-Like Modifiers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- NAE1/UBA3-UBE2M are E1 and E2 enzymes for the URM1 modification.Nature communications · 2026Article
- From Covalent Traps to Fluorescent Beacons: The Expanding Arsenal of Chemical Probes for Studying Ubiquitin and Ubiquitin-Like Proteins.Angewandte Chemie (International ed. in English) · 2026Review
- A Simple, Quick, and Scalable Route to Fluorogenic Ubiquitin and Ubiquitin-Like Protein Substrates for Assessing Activities of Deubiquitinases and Ubiquitin-Like Protein-Specific Proteases.ACS chemical biology · 2025Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Ubiquitination is a pivotal cellular process that controls protein homeostasis and regulates numerous biological functions. Its pathway operates through a cascade of enzyme reactions involving ubiquitin-activating (E1), ubiquitin-conjugating (E2), and ubiquitin-ligating (E3) enzymes and deubiquitinases (DUBs), many of which are cysteine enzymes. Activity-based ubiquitin probes were previously developed for profiling these enzymes. However, most conventional probes do not mimic natural enzyme-substrate interactions and involve chemical mechanisms different from enzyme catalysis. Their uses potentially affect the comprehensiveness of enzyme profiling results. The current study introduces a novel class of activity-based ubiquitin probes, ubiquitin azapeptide esters, designed to overcome these limitations. These probes incorporate an azaglycine ester at the ubiquitin
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Registered trials
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