<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chavez JD</submitter><funding>NCRR NIH HHS</funding><funding>National Heart, Lung, and Blood Institute</funding><funding>NHLBI NIH HHS</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>14094-14102</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7995634</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>92(20)</volume><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</pubmed_abstract><journal>Analytical chemistry</journal><pubmed_title>Isobaric Quantitative Protein Interaction Reporter Technology for Comparative Interactome Studies.</pubmed_title><pmcid>PMC7995634</pmcid><funding_grant_id>1R35GM136255</funding_grant_id><funding_grant_id>S10 RR025107</funding_grant_id><funding_grant_id>R35 GM136255</funding_grant_id><funding_grant_id>R01 GM086688</funding_grant_id><funding_grant_id>R01 GM097112</funding_grant_id><funding_grant_id>5R01GM086688</funding_grant_id><funding_grant_id>R01 HL144778</funding_grant_id><funding_grant_id>5R01HL144778</funding_grant_id><pubmed_authors>Keller A</pubmed_authors><pubmed_authors>Bruce JE</pubmed_authors><pubmed_authors>Chavez JD</pubmed_authors><pubmed_authors>Mohr JP</pubmed_authors></additional><is_claimable>false</is_claimable><name>Isobaric Quantitative Protein Interaction Reporter Technology for Comparative Interactome Studies.</name><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</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Oct</publication><modification>2026-04-29T10:08:21.313Z</modification><creation>2025-02-19T03:53:35.36Z</creation></dates><accession>S-EPMC7995634</accession><cross_references><pubmed>32969639</pubmed><doi>10.1021/acs.analchem.0c03128</doi></cross_references></HashMap>