{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dorig C"],"funding":["European Research Council","Promedica Stiftung","EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020)"],"pagination":["1562-1576"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12440823"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(9)"],"pubmed_abstract":["Methods to systematically monitor protein complex dynamics are needed. We introduce serial ultrafiltration combined with limited proteolysis-coupled mass spectrometry (FLiP-MS), a structural proteomics workflow that generates a library of peptide markers specific to changes in PPIs by probing differences in protease susceptibility between complex-bound and monomeric forms of proteins. The library includes markers mapping to protein-binding interfaces and markers reporting on structural changes that accompany PPI changes. Integrating the marker library with LiP-MS data allows for global profiling of protein-protein interactions (PPIs) from unfractionated lysates. We apply FLiP-MS to Saccharomyces cerevisiae and probe changes in protein complex dynamics after DNA replication stress, identify"],"journal":["Nature biotechnology"],"pubmed_title":["Global profiling of protein complex dynamics with an experimental library of protein interaction markers."],"pmcid":["PMC12440823"],"funding_grant_id":["1508/M","866004","823839"],"pubmed_authors":["Schwede T","Dorig C","Volkmar N","de Souza N","Barral Y","Studer G","Pantolini L","Paleari C","Frommelt F","Marulli C","Picotti P","Peskett T"],"additional_accession":[]},"is_claimable":false,"name":"Global profiling of protein complex dynamics with an experimental library of protein interaction markers.","description":"Methods to systematically monitor protein complex dynamics are needed. We introduce serial ultrafiltration combined with limited proteolysis-coupled mass spectrometry (FLiP-MS), a structural proteomics workflow that generates a library of peptide markers specific to changes in PPIs by probing differences in protease susceptibility between complex-bound and monomeric forms of proteins. The library includes markers mapping to protein-binding interfaces and markers reporting on structural changes that accompany PPI changes. Integrating the marker library with LiP-MS data allows for global profiling of protein-protein interactions (PPIs) from unfractionated lysates. We apply FLiP-MS to Saccharomyces cerevisiae and probe changes in protein complex dynamics after DNA replication stress, identify","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-03T07:59:58.094Z","creation":"2026-04-26T03:12:02.137Z"},"accession":"S-EPMC12440823","cross_references":{"pubmed":["39415059"],"doi":["10.1038/s41587-024-02432-8"]}}