ArticleJournal of mass spectrometry : JMS2019
Top-down mass spectrometry of intact phosphorylated β-casein: Correlation between the precursor charge state and internal fragments.
Article in Journal of mass spectrometry : JMS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Mass spectrometry structural analysis of intrinsically disordered phosphoproteins.International journal of mass spectrometry · 2025Article
- Deep Learning in Phosphoproteomics: Methods and Application in Cancer Drug Discovery.Proteomes · 2023Review
- Top-down mass spectrometry and assigning internal fragments for determining disulfide bond positions in proteins.The Analyst · 2022Article
- Deciphering combinatorial post-translational modifications by top-down mass spectrometry.Current opinion in chemical biology · 2022Review
- Transthyretin proteoforms of intraocular origin in human subretinal fluid.Experimental eye research · 2022Article
- 2-Pyridine Carboxaldehyde for Semi-Automated Soft Spot Identification in Cyclic Peptides.International journal of molecular sciences · 2022Article
- Towards understanding the formation of internal fragments generated by collisionally activated dissociation for top-down mass spectrometry.Analytica chimica acta · 2022Article
- Internal Fragments Generated by Electron Ionization Dissociation Enhance Protein Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Phosphorylated proteins play essential roles in many cellular processes, and identification and characterization of the relevant phosphoproteins can help to understand underlying mechanisms. Herein, we report a collision-induced dissociation top-down approach for characterizing phosphoproteins on a quadrupole time-of-flight mass spectrometer. β-casein, a protein with two major isoforms and five phosphorylatable serine residues, was used as a model. Peaks corresponding to intact β-casein ions with charged states up to 36
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