{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hu H"],"funding":["National Natural Science Foundation of China","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["1465"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10874396"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Protein-modifying enzymes regulate the dynamics of myriad post-translational modification (PTM) substrates. Precise characterization of enzyme-substrate associations is essential for the molecular basis of cellular function and phenotype. Methods for direct capturing global substrates of protein-modifying enzymes in living cells are with many challenges, and yet largely unexplored. Here, we report a strategy to directly capture substrates of lysine-modifying enzymes via PTM-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner. By integrating enzymatic PTM-mechanisms, and genetically encoding residue-selective photo-crosslinker into PTM-enzymes, our strategy expands the substrate profile"],"journal":["Nature communications"],"pubmed_title":["Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells."],"pmcid":["PMC10874396"],"funding_grant_id":["92053106","22177120"],"pubmed_authors":["Ma S","Tan M","Hu W","Zhou BS","Nie HJ","Guo AD","Liu T","Yao X","Liu X","Hu H","Zhai L","Jia X","Chen XH"],"additional_accession":[]},"is_claimable":false,"name":"Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells.","description":"Protein-modifying enzymes regulate the dynamics of myriad post-translational modification (PTM) substrates. Precise characterization of enzyme-substrate associations is essential for the molecular basis of cellular function and phenotype. Methods for direct capturing global substrates of protein-modifying enzymes in living cells are with many challenges, and yet largely unexplored. Here, we report a strategy to directly capture substrates of lysine-modifying enzymes via PTM-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner. By integrating enzymatic PTM-mechanisms, and genetically encoding residue-selective photo-crosslinker into PTM-enzymes, our strategy expands the substrate profile","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2026-05-29T11:40:43.93Z","creation":"2025-04-19T07:34:59.738Z"},"accession":"S-EPMC10874396","cross_references":{"pubmed":["38368419"],"doi":["10.1038/s41467-024-45765-3"]}}