{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ruwolt M"],"funding":["European Research Council","Leibniz-Forschungsinstitut f?r Molekulare Pharmakologie"],"pagination":["5248-5255"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10061366"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["95(12)"],"pubmed_abstract":["Cross-linking mass spectrometry (XL-MS) is a universal tool for probing structural dynamics and protein-protein interactions <i>in vitro</i> and <i>in vivo</i>. Although cross-linked peptides are naturally less abundant than their unlinked counterparts, recent experimental advances improved cross-link identification by enriching the cross-linker-modified peptides chemically with the use of enrichable cross-linkers. However, mono-links (<i>i.e.</i>, peptides modified with a hydrolyzed cross-linker) still hinder efficient cross-link identification since a large proportion of measurement time is spent on their MS2 acquisition. Currently, cross-links and mono-links cannot be separated by sample preparation techniques or chromatography because they are chemically almost identical. Here, we foun"],"journal":["Analytical chemistry"],"pubmed_title":["Real-Time Library Search Increases Cross-Link Identification Depth across All Levels of Sample Complexity."],"pmcid":["PMC10061366"],"funding_grant_id":["949184"],"pubmed_authors":["He Y","Broichhagen J","Barshop W","Viner R","Ruwolt M","Huguet R","Borges Lima D","Liu F"],"additional_accession":[]},"is_claimable":false,"name":"Real-Time Library Search Increases Cross-Link Identification Depth across All Levels of Sample Complexity.","description":"Cross-linking mass spectrometry (XL-MS) is a universal tool for probing structural dynamics and protein-protein interactions <i>in vitro</i> and <i>in vivo</i>. Although cross-linked peptides are naturally less abundant than their unlinked counterparts, recent experimental advances improved cross-link identification by enriching the cross-linker-modified peptides chemically with the use of enrichable cross-linkers. However, mono-links (<i>i.e.</i>, peptides modified with a hydrolyzed cross-linker) still hinder efficient cross-link identification since a large proportion of measurement time is spent on their MS2 acquisition. Currently, cross-links and mono-links cannot be separated by sample preparation techniques or chromatography because they are chemically almost identical. Here, we foun","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2026-05-29T07:50:10.24Z","creation":"2024-11-21T05:10:07.978Z"},"accession":"S-EPMC10061366","cross_references":{"pubmed":["36926872"],"doi":["10.1021/acs.analchem.2c05141"]}}