ArticleJournal of the American Society for Mass Spectrometry2008
Electron capture dissociation implementation progress in Fourier transform ion cyclotron resonance mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
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- Absorption Mode Broadband 2D MS for Proteomics and Metabolomics.Journal of the American Society for Mass Spectrometry · 2026Article
- Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026Review
- Top-Down Proteoform Analysis by 2D MS with Quadrupolar Detection.Analytical chemistry · 2023Article
- Ultra-Accurate Correlation between Precursor and Fragment Ions in Two-Dimensional Mass Spectrometry: Acetylated vs Trimethylated Histone Peptides.Journal of the American Society for Mass Spectrometry · 2023Article
- Improved ion optics for introduction of ions into a 9.4-T Fourier transform ion cyclotron resonance mass spectrometer.Journal of mass spectrometry : JMS · 2015Article
- Relative stability of peptide sequence ions generated by tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Use of top-down and bottom-up Fourier transform ion cyclotron resonance mass spectrometry for mapping calmodulin sites modified by platinum anticancer drugs.Analytical chemistry · 2011Article
- Electron capture dissociation product ion abundances at the X amino acid in RAAAA-X-AAAAK peptides correlate with amino acid polarity and radical stability.Journal of the American Society for Mass Spectrometry · 2009Article
- Simultaneous collision induced dissociation of the charge reduced parent ion during electron capture dissociation.Analytical chemistry · 2009Article
- Periodic sequence distribution of product ion abundances in electron capture dissociation of amphipathic peptides and proteins.Journal of the American Society for Mass Spectrometry · 2009Article
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Successful electron capture dissociation (ECD) Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) applications to peptide and protein structural analysis have been enabled by constant progress in implementation of improved electron injection techniques. The rate of ECD product ion formation has been increased to match the liquid chromatography and capillary electrophoresis timescales, and ECD has been combined with infrared multiphoton dissociation in a single experimental configuration to provide simultaneous irradiation, fast switching between the two techniques, and good spatial overlap between ion, photon, and electron beams. Here we begin by describing advantages and disadvantages of the various existing electron injection techniques for ECD in FT-ICR MS. We next compare multiple-pass and single-pass ECD to provide better understanding of ECD efficiency at low and high negative cathode potentials. We introduce compressed hollow electron beam injection to optimize the overlap of ion, photon, and electron beams in the ICR ion trap. Finally, to overcome significant outgassing during operation of a powerful thermal cathode, we introduce nonthermal electron emitter-based electron injection. We describe the first results obtained with cold cathode ECD, and demonstrate a general way to obtain low-energy electrons in FT-ICR MS by use of multiple-pass ECD.
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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.