{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hoenger Ramazanova RD"],"funding":["Medical Research Council","Wellcome Trust","Institute of Cancer Research"],"pagination":["5209-5220"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11537259"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(11)"],"pubmed_abstract":["Integrating cross-linking mass spectrometry (XL-MS) into structural biology workflows provides valuable information about the spatial arrangement of amino acid stretches, which can guide elucidation of protein assembly architecture. Additionally, the combination of XL-MS with peptide quantitation techniques is a powerful approach to delineate protein interface dynamics across diverse conditions. While XL-MS is increasingly effective with isolated proteins or small complexes, its application to whole-cell samples poses technical challenges related to analysis depth and throughput. The use of enrichable cross-linkers has greatly improved the detectability of protein interfaces in a proteome-wide scale, facilitating global protein-protein interaction mapping. Therefore, bringing together enri"],"journal":["Journal of proteome research"],"pubmed_title":["PhoXplex: Combining Phospho-enrichable Cross-Linking with Isobaric Labeling for Quantitative Proteome-Wide Mapping of Protein Interfaces."],"pmcid":["PMC11537259"],"funding_grant_id":["223745/Z/21/Z","MR/W006553/1","208391/Z/17/Z"],"pubmed_authors":["Wright JC","Choudhary JS","Roumeliotis TI","Hoenger Ramazanova RD"],"additional_accession":[]},"is_claimable":false,"name":"PhoXplex: Combining Phospho-enrichable Cross-Linking with Isobaric Labeling for Quantitative Proteome-Wide Mapping of Protein Interfaces.","description":"Integrating cross-linking mass spectrometry (XL-MS) into structural biology workflows provides valuable information about the spatial arrangement of amino acid stretches, which can guide elucidation of protein assembly architecture. Additionally, the combination of XL-MS with peptide quantitation techniques is a powerful approach to delineate protein interface dynamics across diverse conditions. While XL-MS is increasingly effective with isolated proteins or small complexes, its application to whole-cell samples poses technical challenges related to analysis depth and throughput. The use of enrichable cross-linkers has greatly improved the detectability of protein interfaces in a proteome-wide scale, facilitating global protein-protein interaction mapping. Therefore, bringing together enri","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2025-04-04T03:05:29.509Z","creation":"2025-04-04T03:05:29.509Z"},"accession":"S-EPMC11537259","cross_references":{"pubmed":["39422127"],"doi":["10.1021/acs.jproteome.4c00567"]}}