{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liu X"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e2000218"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8106443"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(1)"],"pubmed_abstract":["A vast number of human cell lines are available for cell culture model-based studies, and as such the potential exists for discrepancies in findings due to cell line selection. To investigate this concept, the authors determine the relative protein abundance profiles of a panel of eight diverse, but commonly studied human cell lines. This panel includes HAP1, HEK293T, HeLa, HepG2, Jurkat, Panc1, SH-SY5Y, and SVGp12. A mass spectrometry-based proteomics workflow designed to enhance quantitative accuracy while maintaining analytical depth is used. To this end, this strategy leverages TMTpro16-based sample multiplexing, high-field asymmetric ion mobility spectrometry, and real-time database searching. The data show that the differences in the relative protein abundance profiles reflect cell l"],"journal":["Proteomics"],"pubmed_title":["Isobaric Tag-Based Protein Profiling across Eight Human Cell Lines Using High-Field Asymmetric Ion Mobility Spectrometry and Real-Time Database Searching."],"pmcid":["PMC8106443"],"funding_grant_id":["R01 GM132129","GM67945","GM","67945","132129","R01 GM067945"],"pubmed_authors":["Liu X","Paulo JA","Gygi SP"],"additional_accession":[]},"is_claimable":false,"name":"Isobaric Tag-Based Protein Profiling across Eight Human Cell Lines Using High-Field Asymmetric Ion Mobility Spectrometry and Real-Time Database Searching.","description":"A vast number of human cell lines are available for cell culture model-based studies, and as such the potential exists for discrepancies in findings due to cell line selection. To investigate this concept, the authors determine the relative protein abundance profiles of a panel of eight diverse, but commonly studied human cell lines. This panel includes HAP1, HEK293T, HeLa, HepG2, Jurkat, Panc1, SH-SY5Y, and SVGp12. A mass spectrometry-based proteomics workflow designed to enhance quantitative accuracy while maintaining analytical depth is used. To this end, this strategy leverages TMTpro16-based sample multiplexing, high-field asymmetric ion mobility spectrometry, and real-time database searching. The data show that the differences in the relative protein abundance profiles reflect cell l","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jan","modification":"2026-05-08T00:53:44.091Z","creation":"2022-02-11T14:21:51.461Z"},"accession":"S-EPMC8106443","cross_references":{"pubmed":["33015980"],"doi":["10.1002/pmic.202000218"]}}