ArticleProteomics2016
Multiplexed data independent acquisition (MSX-DIA) applied by high resolution mass spectrometry improves quantification quality for the analysis of histone peptides.
Article in Proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
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- Application of omics technologies in studies on antitumor effects of Traditional Chinese Medicine.Chinese medicine · 2024Review
- An Optimized and High-Throughput Method for Histone Propionylation and Data-Independent Acquisition Analysis for the Identification and Quantification of Histone Post-translational Modifications.Journal of the American Society for Mass Spectrometry · 2023Article
- Advantages of Multiplexing Ability of the Orbitrap Mass Analyzer in the Multi-Mycotoxin Analysis.Toxins · 2023Article
- Multi-omics in Crohn's disease: New insights from inside.Computational and structural biotechnology journal · 2023Review
- The Role of Data-Independent Acquisition for Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Parallel Notched Gas-Phase Enrichment for Improved Proteome Identification and Quantification with Fast Spectral Acquisition Rates.Journal of proteome research · 2020Article
- Quantitation of Single and Combinatorial Histone Modifications by Integrated Chromatography of Bottom-up Peptides and Middle-down Polypeptide Tails.Journal of the American Society for Mass Spectrometry · 2019Article
- One minute analysis of 200 histone posttranslational modifications by direct injection mass spectrometry.Genome research · 2019Article
- Comparison of data-acquisition methods for the identification and quantification of histone post-translational modifications on a Q Exactive HF hybrid quadrupole Orbitrap mass spectrometer.Rapid communications in mass spectrometry : RCM · 2019Article
- Integrated Analysis of Acetyl-CoA and Histone Modification via Mass Spectrometry to Investigate Metabolically Driven Acetylation.Methods in molecular biology (Clifton, N.J.) · 2019Article
- EpiProfile 2.0: A Computational Platform for Processing Epi-Proteomics Mass Spectrometry Data.Journal of proteome research · 2018Article
- Assessment of Quantification Precision of Histone Post-Translational Modifications by Using an Ion Trap and down To 50 000 Cells as Starting Material.Journal of proteome research · 2018Article
- Multicellular Tumor Spheroids Combined with Mass Spectrometric Histone Analysis To Evaluate Epigenetic Drugs.Analytical chemistry · 2017Article
- Recent Achievements in Characterizing the Histone Code and Approaches to Integrating Epigenomics and Systems Biology.Methods in enzymology · 2017Review
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3 authors at 1 institution in 1 country.
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Abstract
We present the MS-based application of the innovative, although scarcely exploited, multiplexed data-independent acquisition (MSX-DIA) for the analysis of histone PTMs. Histones are golden standard for complexity in MS based proteomics, due to their large number of combinatorial modifications, leading to isobaric peptides after proteolytic digestion. DIA has, thus, gained popularity for the purpose as it allows for MS/MS-based quantification without upfront assay development. In this work, we evaluated the performance of traditional DIA versus MSX-DIA in terms of MS/MS spectra quality, instrument scan rate and quantification precision using histones from HeLa cells. We used an MS/MS isolation window of 10 and 6 m/z for DIA and MSX-DIA, respectively. Four MS/MS scans were multiplexed for MSX-DIA. Despite MSX-DIA was programmed to perform two-fold more MS/MS events than traditional DIA, it acquired on average ∼5% more full MS scans, indicating even faster scan rate. Results highlighted an overall decrease of background ion signals using MSX-DIA, and we illustrated specific examples where peptides of different precursor masses were co-fragmented by DIA but not MSX-DIA. Taken together, MSX-DIA proved thus to be a more favorable method for histone analysis in data independent mode.
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