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• W2891136419 abstract "Advancement in our knowledge of deubiquitinases (DUBs) and their biological functions requires biochemical tools permitting interrogation of DUB activities under physiologically relevant conditions. Activity-based DUB probes (DUB ABPs) have been widely used in investigating the function and activity of DUBs. However, most ubiquitin (Ub)-based DUB ABPs are not cell-permeable, limiting their utility to purified proteins and cell lysates. Lysis of cells usually leads to dilution of the cytoplasm and disruption of the normal cellular organization, which may alter the activity of many DUBs and DUB complexes. Here, we report a new class of cell-permeable DUB ABPs that enable intracellular DUB profiling. We used a semisynthetic approach to generate modular ubiquitin-based DUB probes containing a reactive warhead for covalent trapping of DUBs with a catalytic cysteine. We employed cell-penetrating peptides (CPPs), particualrly cyclic polyarginine (cR10), to deliver the DUB ABPs into cells, as confirmed using live..." @default.
• W2891136419 created "2018-09-27" @default.
• W2891136419 creator A5004940895 @default.
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• W2891136419 date "2018-09-21" @default.
• W2891136419 modified "2023-10-15" @default.
• W2891136419 title "Cell-Permeable Activity-Based Ubiquitin Probes Enable Intracellular Profiling of Human Deubiquitinases" @default.
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• W2891136419 doi "https://doi.org/10.1021/jacs.8b05147" @default.
• W2891136419 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8011864" @default.
• W2891136419 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30240200" @default.
• W2891136419 hasPublicationYear "2018" @default.
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