{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chavez JD"],"funding":["NCRR NIH HHS","National Heart, Lung, and Blood Institute","NHLBI NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["14094-14102"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7995634"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["92(20)"],"pubmed_abstract":["Chemical cross-linking with mass spectrometry (XL-MS) has emerged as a useful tool for the large-scale study of protein structures and interactions from complex biological samples including intact cells and tissues. Quantitative XL-MS (qXL-MS) provides unique information on protein conformational and interaction changes resulting from perturbations such as drug treatment and disease state. Previous qXL-MS studies relied on the incorporation of stable isotopes into the cross-linker (primarily deuterium) or metabolic labeling with SILAC. Here, we introduce isobaric quantitative protein interaction reporter (iqPIR) technology which utilizes stable isotopes selectively incorporated into the cross-linker design, allowing for isobaric cross-linked peptide pairs originating from different samples"],"journal":["Analytical chemistry"],"pubmed_title":["Isobaric Quantitative Protein Interaction Reporter Technology for Comparative Interactome Studies."],"pmcid":["PMC7995634"],"funding_grant_id":["1R35GM136255","S10 RR025107","R35 GM136255","R01 GM086688","R01 GM097112","5R01GM086688","R01 HL144778","5R01HL144778"],"pubmed_authors":["Keller A","Bruce JE","Chavez JD","Mohr JP"],"additional_accession":[]},"is_claimable":false,"name":"Isobaric Quantitative Protein Interaction Reporter Technology for Comparative Interactome Studies.","description":"Chemical cross-linking with mass spectrometry (XL-MS) has emerged as a useful tool for the large-scale study of protein structures and interactions from complex biological samples including intact cells and tissues. Quantitative XL-MS (qXL-MS) provides unique information on protein conformational and interaction changes resulting from perturbations such as drug treatment and disease state. Previous qXL-MS studies relied on the incorporation of stable isotopes into the cross-linker (primarily deuterium) or metabolic labeling with SILAC. Here, we introduce isobaric quantitative protein interaction reporter (iqPIR) technology which utilizes stable isotopes selectively incorporated into the cross-linker design, allowing for isobaric cross-linked peptide pairs originating from different samples","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-04-29T10:08:21.313Z","creation":"2025-02-19T03:53:35.36Z"},"accession":"S-EPMC7995634","cross_references":{"pubmed":["32969639"],"doi":["10.1021/acs.analchem.0c03128"]}}