{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Biggs GS"],"funding":["RCUK | Engineering and Physical Sciences Research Council (EPSRC)","Cancer Research UK","Medical Research Council","The Francis Crick Institute","RCUK | Engineering and Physical Sciences Research Council","Wellcome Trust","Engineering and Physical Sciences Research Council"],"pagination":["73"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11697256"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Identifying pharmacological probes for human proteins represents a key opportunity to accelerate the discovery of new therapeutics. High-content screening approaches to expand the ligandable proteome offer the potential to expedite the discovery of novel chemical probes to study protein function. Screening libraries of reactive fragments by chemoproteomics offers a compelling approach to ligand discovery, however, optimising sample throughput, proteomic depth, and data reproducibility remains a key challenge. We report a versatile, label-free quantification proteomics platform for competitive profiling of cysteine-reactive fragments against the native proteome. This high-throughput platform combines SP4 plate-based sample preparation with rapid chromatographic gradients. Data-independent a"],"journal":["Nature communications"],"pubmed_title":["Robust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics."],"pmcid":["PMC11697256"],"funding_grant_id":["CC2075","EP/V038028/1","CC2000","CC2057"],"pubmed_authors":["Cawood EE","Wilders H","Chen P","van der Zouwen AJ","Bush JT","Nightingale L","Rittinger K","Boulton SJ","Riziotis IG","House D","Vuorinen A","McCarthy WJ","Skehel JM","Powell AJ","Pettinger J","Biggs GS"],"additional_accession":[]},"is_claimable":false,"name":"Robust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics.","description":"Identifying pharmacological probes for human proteins represents a key opportunity to accelerate the discovery of new therapeutics. High-content screening approaches to expand the ligandable proteome offer the potential to expedite the discovery of novel chemical probes to study protein function. Screening libraries of reactive fragments by chemoproteomics offers a compelling approach to ligand discovery, however, optimising sample throughput, proteomic depth, and data reproducibility remains a key challenge. We report a versatile, label-free quantification proteomics platform for competitive profiling of cysteine-reactive fragments against the native proteome. This high-throughput platform combines SP4 plate-based sample preparation with rapid chromatographic gradients. Data-independent a","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-01T11:08:00.533Z","creation":"2025-04-19T05:59:33.061Z"},"accession":"S-EPMC11697256","cross_references":{"pubmed":["39746958"],"doi":["10.1038/s41467-024-55057-5"]}}