{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Toroitich EK"],"funding":["Hsu Laboratory","UVA Cancer Center","NIDA NIH HHS","Melanoma Research Alliance","NCI NIH HHS","National Institutes of Health","University of Virginia Cancer Center","NCI Cancer Center Support"],"pagination":["2134-2139"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8206015"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(12)"],"pubmed_abstract":["Sulfonyl-triazoles have emerged as a new reactive group for covalent modification of tyrosine sites on proteins through sulfur-triazole exchange (SuTEx) chemistry. The extent to which this sulfur electrophile can be tuned for developing ligands with cellular activity remains largely underexplored. Here, we performed fragment-based ligand discovery in live cells to identify SuTEx compounds capable of liganding tyrosine sites on diverse protein targets. We verified our quantitative chemical proteomic findings by demonstrating concentration-dependent activity of SuTEx ligands, but not inactive counterparts, against recombinant protein targets directly in live cells. Our structure-activity relationship studies identified the SuTEx ligand HHS-0701 as a cell-active inhibitor capable of blocking "],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["Discovery of a Cell-Active SuTEx Ligand of Prostaglandin Reductase 2."],"pmcid":["PMC8206015"],"funding_grant_id":["5P30CA044579-27","R01 DA043571","DA043571","P30 CA044579"],"pubmed_authors":["Hsu KL","Libby AH","Brodowski SM","Toroitich EK","Ciancone AM","Hahm HS"],"additional_accession":[]},"is_claimable":false,"name":"Discovery of a Cell-Active SuTEx Ligand of Prostaglandin Reductase 2.","description":"Sulfonyl-triazoles have emerged as a new reactive group for covalent modification of tyrosine sites on proteins through sulfur-triazole exchange (SuTEx) chemistry. The extent to which this sulfur electrophile can be tuned for developing ligands with cellular activity remains largely underexplored. Here, we performed fragment-based ligand discovery in live cells to identify SuTEx compounds capable of liganding tyrosine sites on diverse protein targets. We verified our quantitative chemical proteomic findings by demonstrating concentration-dependent activity of SuTEx ligands, but not inactive counterparts, against recombinant protein targets directly in live cells. Our structure-activity relationship studies identified the SuTEx ligand HHS-0701 as a cell-active inhibitor capable of blocking ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2025-04-22T03:14:25.963Z","creation":"2025-02-18T23:32:16.766Z"},"accession":"S-EPMC8206015","cross_references":{"pubmed":["33861519"],"doi":["10.1002/cbic.202000879"]}}