ArticleJournal of the American Society for Mass Spectrometry2017
A Priori Intrinsic PTM Size Parameters for Predicting the Ion Mobilities of Modified Peptides.
Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Leveraging pretrained deep protein language model to predict peptide collision cross section.Communications chemistry · 2025Article
- Peptide collision cross sections of 22 post-translational modifications.Analytical and bioanalytical chemistry · 2023Article
- Ionmob: a Python package for prediction of peptide collisional cross-section values.Bioinformatics (Oxford, England) · 2023Article
- Tandem Trapped Ion Mobility Spectrometry/Mass Spectrometry (tTIMS/MS) Reveals Sequence-Specific Determinants of Top-Down Protein Fragment Ion Cross Sections.Analytical chemistry · 2022Article
- Effect of Phosphorylation on the Collision Cross Sections of Peptide Ions in Ion Mobility Spectrometry.Mass spectrometry (Tokyo, Japan) · 2021Article
- New mass spectrometry technologies contributing towards comprehensive and high throughput omics analyses of single cells.The Analyst · 2019Review
- Fast and Effective Ion Mobility-Mass Spectrometry Separation of d-Amino-Acid-Containing Peptides.Analytical chemistry · 2017Article
- Broad Separation of Isomeric Lipids by High-Resolution Differential Ion Mobility Spectrometry with Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- A Database of Transition-Metal-Coordinated Peptide Cross-Sections: Selective Interaction with Specific Amino Acid Residues.Journal of the American Society for Mass Spectrometry · 2017Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rising profile of ion mobility spectrometry (IMS) in proteomics has driven the efforts to predict peptide cross-sections. In the simplest approach, these are derived by adding the contributions of all amino acid residues and post-translational modifications (PTMs) defined by their intrinsic size parameters (ISPs). We show that the ISPs for PTMs can be calculated from properties of constituent atoms, and introduce the "impact scores" that govern the shift of cross-sections from the central mass-dependent trend for unmodified peptides. The ISPs and scores tabulated for 100 more common PTMs enable predicting the domains for modified peptides in the IMS/MS space that would guide subproteome investigations. Graphical Abstract ᅟ.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.