ArticleJournal of proteome research2018
Estimating the Distribution of Protein Post-Translational Modification States by Mass Spectrometry.
Article in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Metabolic and post-translational modifications in sepsis-associated immune dysfunction: a conceptual framework.Frontiers in immunology · 2026Review
- MSModDetector: a tool for detecting mass shifts and post-translational modifications in individual ion mass spectrometry data.Bioinformatics (Oxford, England) · 2024Article
- Identification of Cofragmented Combinatorial Peptide Isomers by Two-Dimensional Partial Covariance Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Advanced Strategies for Proton-Transfer Reactions Coupled with Parallel Ion Parking on a 21 T FT-ICR MS for Intact Protein Analysis.Analytical chemistry · 2021Article
- Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry.Antioxidants (Basel, Switzerland) · 2021Article
- Decoding the protein composition of whole nucleosomes with Nuc-MS.Nature methods · 2021Article
- [Size exclusion-reverse liquid column chromatography-mass spectrometry and its application in the identification of post-translationally modified proteins in rat kidney].Se pu = Chinese journal of chromatography · 2021Article
- Article
- Thorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics.Molecular & cellular proteomics : MCP · 2020Article
- Proton Transfer Charge Reduction Enables High-Throughput Top-Down Analysis of Large Proteoforms.Analytical chemistry · 2019Article
- Proteome-Wide Identification of Lysine Propionylation in the Conidial and Mycelial Stages ofFrontiers in microbiology · 2019Article
- Unraveling Posttranslational Modification Complexity: Advances in Quantitative Histone Proteoform Mass Spectrometry.Mass spectrometry reviewsReview
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Authors and funding
3 authors.
Funding
Abstract
Post-translational modifications (PTMs) of proteins play a central role in cellular information encoding, but the complexity of PTM state has been challenging to unravel. A single molecule can exhibit a "modform" or combinatorial pattern of co-occurring PTMs across multiple sites, and a molecular population can exhibit a distribution of amounts of different modforms. How can this "modform distribution" be estimated by mass spectrometry (MS)? Bottom-up MS, based on cleavage into peptides, destroys correlations between PTMs on different peptides, but it is conceivable that multiple proteases with appropriate patterns of cleavage could reconstruct the modform distribution. We introduce a mathematical language for describing MS measurements and show, on the contrary, that no matter how many distinct proteases are available, the shortfall in information required for reconstruction worsens exponentially with increasing numbers of sites. Whereas top-down MS on intact proteins can do better, current technology cannot prevent the exponential worsening. However, our analysis also shows that all forms of MS yield linear equations for modform amounts. This permits different MS protocols to be integrated and the modform distribution to be constrained within a high-dimensional "modform region", which may offer a feasible proxy for analyzing information encoding.
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