ArticleJournal of the American Society for Mass Spectrometry2018
Sequencing Larger Intact Proteins (30-70 kDa) with Activated Ion Electron Transfer Dissociation.
Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Implementation of Infrared-Activated Negative Electron Transfer Dissociation (IR-NETD) Using Xenon on a Quadrupole-Orbitrap-Quadrupole Linear Ion Trap Mass Spectrometer.Journal of the American Society for Mass Spectrometry · 2026Article
- Impact of Charge Reduction on Sequence Coverage of Proteins by 193 nm Ultraviolet Photodissociation.Journal of the American Society for Mass Spectrometry · 2025Article
- Capillary Zone Electrophoresis-Mass Spectrometry of Intact G Protein-Coupled Receptors Enables Proteoform Profiling.Analytical chemistry · 2025Article
- Emerging opportunities for intact and native protein analysis using chemical proteomics.Analytica chimica acta · 2025Review
- Leveraging Ion-Ion and Ion-Photon Activation to Improve the Sequencing of Proteins Carrying Multiple Disulfide Bonds: The Human Serum Albumin Case Study.Journal of the American Society for Mass Spectrometry · 2024Article
- Mobility-Assisted Pseudo-MSJournal of the American Society for Mass Spectrometry · 2024Article
- Pilot Study for Deciphering Post-Translational Modifications and Proteoforms of Tau Protein by Capillary Electrophoresis-Mass Spectrometry.Journal of proteome research · 2024Article
- Mass Spectrometry-Based Top-Down Proteomics in Nanomedicine: Proteoform-Specific Measurement of Protein Corona.ACS nano · 2024Article
- Synthesis of colicin Ia neoglycoproteins: tools towards glyco-engineering of bacterial cell surfaces.RSC advances · 2024Article
- Protein Complex Heterogeneity and Topology Revealed by Electron Capture Charge Reduction and Surface Induced Dissociation.ACS central science · 2024Article
- Mass spectrometry-intensive top-down proteomics: an update on technology advancements and biomedical applications.Analytical methods : advancing methods and applications · 2024Review
- Protein complex heterogeneity and topology revealed by electron capture charge reduction and surface induced dissociation.bioRxiv : the preprint server for biology · 2024Article
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Characterization of an Omnitrap-Orbitrap Platform Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation, and Electron Capture Dissociation for the Analysis of Peptides and Proteins.Analytical chemistry · 2023Article
- Characterizing the top-down sequencing of protein ions prior to mobility separation in a timsTOF.The Analyst · 2023Article
- Deciphering combinatorial post-translational modifications by top-down mass spectrometry.Current opinion in chemical biology · 2022Review
- Enhanced Top-Down Protein Characterization with Electron Capture Dissociation and Cyclic Ion Mobility Spectrometry.Analytical chemistry · 2022Article
- Practical Effects of Intramolecular Hydrogen Rearrangement in Electron Transfer Dissociation-Based Proteomics.Journal of the American Society for Mass Spectrometry · 2022Article
- Improved Sequence Analysis of Intact Proteins by Parallel Ion Parking during Electron Transfer Dissociation.Analytical chemistry · 2021Article
- Improved Protein and PTM Characterization with a Practical Electron-Based Fragmentation on Q-TOF Instruments.Journal of the American Society for Mass Spectrometry · 2021Article
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Authors and funding
3 authors.
Funding
Abstract
The analysis of intact proteins via mass spectrometry can offer several benefits to proteome characterization, although the majority of top-down experiments focus on proteoforms in a relatively low mass range (<30 kDa). Recent studies have focused on improving the analysis of larger intact proteins (up to ~75 kDa), but they have also highlighted several challenges to be addressed. One major hurdle is the efficient dissociation of larger protein ions, which often to do not yield extensive fragmentation via conventional tandem MS methods. Here we describe the first application of activated ion electron transfer dissociation (AI-ETD) to proteins in the 30-70 kDa range. AI-ETD leverages infrared photo-activation concurrent to ETD reactions to improve sequence-informative product ion generation. This method generates more product ions and greater sequence coverage than conventional ETD, higher-energy collisional dissociation (HCD), and ETD combined with supplemental HCD activation (EThcD). Importantly, AI-ETD provides the most thorough protein characterization for every precursor ion charge state investigated in this study, making it suitable as a universal fragmentation method in top-down experiments. Additionally, we highlight several acquisition strategies that can benefit characterization of larger proteins with AI-ETD, including combination of spectra from multiple ETD reaction times for a given precursor ion, multiple spectral acquisitions of the same precursor ion, and combination of spectra from two different dissociation methods (e.g., AI-ETD and HCD). In all, AI-ETD shows great promise as a method for dissociating larger intact protein ions as top-down proteomics continues to advance into larger mass ranges. Graphical Abstract ᅟ.
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