{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16"],"submitter":["Schedlowski M"],"pubmed_abstract":["Proteins function through complex interaction networks that govern nearly all aspects of cellular physiology. Identifying protein-protein interactions (PPIs) under native conditions remains challenging due to the transient nature of many complexes and technical limitations of conventional approaches. We present TIE-UP-SIN (Targeted Interactome Experiment for Unknown Proteins by Stable Isotope Normalization), a robust and reproducible method for <i>in vivo</i> identification of PPIs. This approach combines metabolic labeling with <sup>15</sup>N isotopes, reversible <i>in vivo</i> formaldehyde crosslinking, affinity purification, and quantitative mass spectrometry. TIE-UP-SIN is specifically designed to preserve transient or weak interactions during purification and to quantify interaction p"],"journal":["Frontiers in microbiology"],"pagination":["1657647"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12434083"],"repository":["biostudies-literature"],"pubmed_title":["TIE-UP-SIN: a novel method for enhanced identification of protein-protein interactions."],"pmcid":["PMC12434083"],"pubmed_authors":["Salazar MG","Schedlowski M","Steil L","Surmann K","Reder A","Hentschker C","Harms M","Hoffmuller T","Volker U","Michalik S"],"additional_accession":[]},"is_claimable":false,"name":"TIE-UP-SIN: a novel method for enhanced identification of protein-protein interactions.","description":"Proteins function through complex interaction networks that govern nearly all aspects of cellular physiology. Identifying protein-protein interactions (PPIs) under native conditions remains challenging due to the transient nature of many complexes and technical limitations of conventional approaches. We present TIE-UP-SIN (Targeted Interactome Experiment for Unknown Proteins by Stable Isotope Normalization), a robust and reproducible method for <i>in vivo</i> identification of PPIs. This approach combines metabolic labeling with <sup>15</sup>N isotopes, reversible <i>in vivo</i> formaldehyde crosslinking, affinity purification, and quantitative mass spectrometry. TIE-UP-SIN is specifically designed to preserve transient or weak interactions during purification and to quantify interaction p","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025","modification":"2026-06-03T02:54:15.165Z","creation":"2026-04-23T03:13:08.706Z"},"accession":"S-EPMC12434083","cross_references":{"pubmed":["40959229"],"doi":["10.3389/fmicb.2025.1657647"]}}