{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Warren J"],"funding":["NIBIB NIH HHS","NEI NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["302-319"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11775715"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5(1)"],"pubmed_abstract":["Proteins regulate biological functions through the formation of distinct protein complexes. Identification and characterization of these protein-protein interactions are critical to deciphering their mechanism of action. Different antibody-based or cross-linking-based methods have been developed to identify the protein-protein interactions. However, these methods require genetic engineering or other means to disrupt the native environments. To circumvent this limitation, we introduce here SMAP3-ID (small-molecule-assisted identification of protein-protein interactions through proximity) method to identify protein-protein interactions in native cellular environment. This method combines a selective ligand for binding to a protein of interest for photo-cross-linking, a live-cell-compatible b"],"journal":["JACS Au"],"pubmed_title":["SMAP3-ID for Identification of Endogenous Protein-Protein Interactions Reveals Regulation of Mitochondrial Activity by Lamins."],"pmcid":["PMC11775715"],"funding_grant_id":["R21 EB028425","P30 CA069533","R01 GM122820","R01 CA211866","R01 CA278058","P30 EY010572","R01 CA245964"],"pubmed_authors":["David LL","Petrie SK","Li BX","Xiao X","Warren J","Wang J","Chao B","Dhoro F","Reddy A"],"additional_accession":[]},"is_claimable":false,"name":"SMAP3-ID for Identification of Endogenous Protein-Protein Interactions Reveals Regulation of Mitochondrial Activity by Lamins.","description":"Proteins regulate biological functions through the formation of distinct protein complexes. Identification and characterization of these protein-protein interactions are critical to deciphering their mechanism of action. Different antibody-based or cross-linking-based methods have been developed to identify the protein-protein interactions. However, these methods require genetic engineering or other means to disrupt the native environments. To circumvent this limitation, we introduce here SMAP3-ID (small-molecule-assisted identification of protein-protein interactions through proximity) method to identify protein-protein interactions in native cellular environment. This method combines a selective ligand for binding to a protein of interest for photo-cross-linking, a live-cell-compatible b","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2025-04-04T23:11:11.985Z","creation":"2025-04-04T23:11:11.985Z"},"accession":"S-EPMC11775715","cross_references":{"pubmed":["39886595"],"doi":["10.1021/jacsau.4c00988"]}}