ArticleJournal of proteome research2018
Exploring ECD on a Benchtop Q Exactive Orbitrap Mass Spectrometer.
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 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed.
- Integration of alternative fragmentation techniques into standard LC-MS workflows using a single deep learning model enhances proteome coverage.Nature methods · 2026Article
- How to Use Quantum Chemistry for Analyzing Mass Spectrometry Data.Mass spectrometry (Tokyo, Japan) · 2026Review
- Electron Capture Dissociation for Discovery Top-Down Proteomics of Peptides and Small Proteins on Chromatographic Time Scales.Journal of the American Society for Mass Spectrometry · 2025Article
- Native Top-Down Analysis of Membrane Protein Complexes Directly From In Vitro and Native Membranes.Molecular & cellular proteomics : MCP · 2025Article
- External Data Systems Enable Enhanced (and Sustainable) Fourier Transform Mass Spectrometry Imaging for Legacy Hybrid Linear Ion Trap-Orbitrap Platforms.Journal of the American Society for Mass Spectrometry · 2024Article
- Online, Bottom-up Characterization of Histone H4 4-17 Isomers.Analytical chemistry · 2024Article
- To 200,000ACS central science · 2024Article
- Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry.ACS measurement science au · 2024Review
- EndoGenius: Optimized Neuropeptide Identification from Mass Spectrometry Datasets.Journal of proteome research · 2024Article
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Direct and Detailed Site-Specific Glycopeptide Characterization by Higher-Energy Electron-Activated Dissociation Tandem Mass Spectrometry.Analytical chemistry · 2024Article
- Top/Middle-Down Characterization of α-Synuclein Glycoforms.Analytical chemistry · 2023Article
- Article
- 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
- Article
- Top-"Double-Down" Mass Spectrometry of Histone H4 Proteoforms: Tandem Ultraviolet-Photon and Mobility/Mass-Selected Electron Capture Dissociations.Analytical chemistry · 2022Article
- The Omnitrap Platform: A Versatile Segmented Linear Ion Trap for Multidimensional Multiple-Stage Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Deciphering combinatorial post-translational modifications by top-down mass spectrometry.Current opinion in chemical biology · 2022Review
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
As the application of mass spectrometry intensifies in scope and diversity, the need for advanced instrumentation addressing a wide variety of analytical needs also increases. To this end, many modern, top-end mass spectrometers are designed or modified to include a wider range of fragmentation technologies, for example, ECD, ETD, EThcD, and UVPD. Still, the majority of instrument platforms are limited to more conventional methods, such as CID and HCD. While these latter methods have performed well, the less conventional fragmentation methods have been shown to lead to increased information in many applications including middle-down proteomics, top-down proteomics, glycoproteomics, and disulfide bond mapping. We describe the modification of the popular Q Exactive Orbitrap mass spectrometer to extend its fragmentation capabilities to include ECD. We show that this modification allows ≥85% matched ion intensity to originate from ECD fragment ion types as well as provides high sequence coverage (≥60%) of intact proteins and high fragment identification rates with ∼70% of ion signals matched. Finally, the ECD implementation promotes selective disulfide bond dissociation, facilitating the identification of disulfide-linked peptide conjugates. Collectively, this modification extends the capabilities of the Q Exactive Orbitrap mass spectrometer to a range of new applications.
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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.