ArticleAnalytical chemistry2018
Linear and Differential Ion Mobility Separations of Middle-Down Proteoforms.
Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed.
- Direct histone proteoform profiling of the unannotated, endangered coral Acropora cervicornis.Nucleic acids research · 2025Article
- Online, Bottom-up Characterization of Histone H4 4-17 Isomers.Analytical chemistry · 2024Article
- Proteome Expression Signatures: Differences between Orbital and Subcutaneous Abdominal Adipose Tissues.Life (Basel, Switzerland) · 2024Article
- Bottom-up Histone Post-translational Modification Analysis using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Tandem Mass Spectrometry.Journal of proteome research · 2024Article
- High-resolution ion mobility spectrometry-mass spectrometry for isomeric separation of prostanoids after Girard's reagent T derivatization.Rapid communications in mass spectrometry : RCM · 2023Article
- Trapped Ion Mobility Spectrometry, Ultraviolet Photodissociation, and Time-of-Flight Mass Spectrometry for Gas-Phase Peptide Isobars/Isomers/Conformers Discrimination.Journal of the American Society for Mass Spectrometry · 2022Article
- Tandem-trapped ion mobility spectrometry/mass spectrometry (The Analyst · 2022Review
- Chemical biology approaches to study histone interactors.Biochemical Society transactions · 2021Review
- Proteoform Differentiation using Tandem Trapped Ion Mobility, Electron Capture Dissociation, and ToF Mass Spectrometry.Analytical chemistry · 2021Article
- Integrating ion mobility and imaging mass spectrometry for comprehensive analysis of biological tissues: A brief review and perspective.Journal of mass spectrometry : JMS · 2020Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- 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
- Evidence of Cis/Trans-Isomerization at Pro7/Pro16 in the Lasso Peptide Microcin J25.Journal of the American Society for Mass Spectrometry · 2019Article
- Article
- Middle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry.RSC advances · 2018Review
- A Novel Differential Ion Mobility Device Expands the Depth of Proteome Coverage and the Sensitivity of Multiplex Proteomic Measurements.Molecular & cellular proteomics : MCP · 2018Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Comprehensive characterization of proteomes comprising the same proteins with distinct post-translational modifications (PTMs) is a staggering challenge. Many such proteoforms are isomers (localization variants) that require separation followed by top-down or middle-down mass spectrometric analyses, but condensed-phase separations are ineffective in those size ranges. The variants for "middle-down" peptides were resolved by differential ion mobility spectrometry (FAIMS), relying on the mobility increment at high electric fields, but not previously by linear IMS on the basis of absolute mobility. We now use complete histone tails with diverse PTMs on alternative sites to demonstrate that high-resolution linear IMS, here trapped IMS (TIMS), broadly resolves the variants of ∼50 residues in full or into binary mixtures quantifiable by tandem MS, largely thanks to orthogonal separations across charge states. Separations using traveling-wave (TWIMS) and/or involving various time scales and electrospray ionization source conditions are similar (with lower resolution for TWIMS), showing the transferability of results across linear IMS instruments. The linear IMS and FAIMS dimensions are substantially orthogonal, suggesting FAIMS/IMS/MS as a powerful platform for proteoform analyses.
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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.