{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shin S"],"funding":["Institute for Basic Science","National Research Foundation of Korea (NRF)","National Research Foundation of Korea","Institute for Basic Science (IBS)"],"pagination":["554"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11082246"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(1)"],"pubmed_abstract":["Promiscuous labeling enzymes, such as APEX2 or TurboID, are commonly used in in situ biotinylation studies of subcellular proteomes or protein-protein interactions. Although the conventional approach of enriching biotinylated proteins is widely implemented, in-depth identification of specific biotinylation sites remains challenging, and current approaches are technically demanding with low yields. A novel method to systematically identify specific biotinylation sites for LC-MS analysis followed by proximity labeling showed excellent performance compared with that of related approaches in terms of identification depth with high enrichment power. The systematic identification of biotinylation sites enabled a simpler and more efficient experimental design to identify subcellular localized pro"],"journal":["Communications biology"],"pubmed_title":["Super-resolution proximity labeling with enhanced direct identification of biotinylation sites."],"pmcid":["PMC11082246"],"funding_grant_id":["IBS-R008-D1","NRF-2022R1A2B5B03001658","NRF-2019M3E5D3073104","NRF-2021R1A6A3A01087055","NRF-2020R1C1C1013927"],"pubmed_authors":["Shin S","Jang DG","Lee SY","Kim J","Kang MG","Rhee HW","Kim JS"],"additional_accession":[]},"is_claimable":false,"name":"Super-resolution proximity labeling with enhanced direct identification of biotinylation sites.","description":"Promiscuous labeling enzymes, such as APEX2 or TurboID, are commonly used in in situ biotinylation studies of subcellular proteomes or protein-protein interactions. Although the conventional approach of enriching biotinylated proteins is widely implemented, in-depth identification of specific biotinylation sites remains challenging, and current approaches are technically demanding with low yields. A novel method to systematically identify specific biotinylation sites for LC-MS analysis followed by proximity labeling showed excellent performance compared with that of related approaches in terms of identification depth with high enrichment power. The systematic identification of biotinylation sites enabled a simpler and more efficient experimental design to identify subcellular localized pro","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-07-14T20:31:07.546Z","creation":"2025-08-12T03:05:00.653Z"},"accession":"S-EPMC11082246","cross_references":{"pubmed":["38724559"],"doi":["10.1038/s42003-024-06112-w"]}}