{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Salovska B"],"funding":["National Institutes of Health","NIGMS NIH HHS"],"pagination":["3103-3111"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8959401"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["93(6)"],"pubmed_abstract":["The data-independent acquisition (DIA) performed in the latest high-resolution, high-speed mass spectrometers offers a powerful analytical tool for biological investigations. The DIA mass spectrometry (DIA-MS) combined with the isotopic labeling approach holds a particular promise for increasing the multiplexity of DIA-MS analysis, which could assist the relative protein quantification and the proteome-wide turnover profiling. However, the wide MS1 isolation windows employed in conventional DIA methods lead to a limited efficiency in identifying and quantifying isotope-labeled peptide pairs through peptide fragment ions. Here, we optimized a high-selectivity DIA-MS named BoxCarmax that supports the analysis of complex samples, such as those generated from Stable isotope labeling by amino a"],"journal":["Analytical chemistry"],"pubmed_title":["BoxCarmax: A High-Selectivity Data-Independent Acquisition Mass Spectrometry Method for the Analysis of Protein Turnover and Complex Samples."],"pmcid":["PMC8959401"],"funding_grant_id":["R01 GM137031","R01GM137031"],"pubmed_authors":["Li W","Liu Y","Salovska B","Di Y"],"additional_accession":[]},"is_claimable":false,"name":"BoxCarmax: A High-Selectivity Data-Independent Acquisition Mass Spectrometry Method for the Analysis of Protein Turnover and Complex Samples.","description":"The data-independent acquisition (DIA) performed in the latest high-resolution, high-speed mass spectrometers offers a powerful analytical tool for biological investigations. The DIA mass spectrometry (DIA-MS) combined with the isotopic labeling approach holds a particular promise for increasing the multiplexity of DIA-MS analysis, which could assist the relative protein quantification and the proteome-wide turnover profiling. However, the wide MS1 isolation windows employed in conventional DIA methods lead to a limited efficiency in identifying and quantifying isotope-labeled peptide pairs through peptide fragment ions. Here, we optimized a high-selectivity DIA-MS named BoxCarmax that supports the analysis of complex samples, such as those generated from Stable isotope labeling by amino a","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Feb","modification":"2026-05-31T13:01:07.634Z","creation":"2025-04-06T21:53:52.72Z"},"accession":"S-EPMC8959401","cross_references":{"pubmed":["33533601"],"doi":["10.1021/acs.analchem.0c04293"]}}