ArticleJournal of the American Society for Mass Spectrometry2018
Application of Tandem Two-Dimensional Mass Spectrometry for Top-Down Deep Sequencing of Calmodulin.
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 7 papers.
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Who cites it
7 citing papers in PubMed.
- Hyphenation of Trapped Ion Mobility to Two-Dimensional Mass Spectrometry for Protein Analysis in Complex Biomixtures.Journal of the American Society for Mass Spectrometry · 2025Article
- A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Fellgett Revisited: On the Nature of Noise in Two-Dimensional Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2020Review
- Phase relationships in two-dimensional mass spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Top or Middle? Up or Down? Toward a Standard Lexicon for Protein Top-Down and Allied Mass Spectrometry Approaches.Journal of the American Society for Mass Spectrometry · 2019Article
- Two-dimensional mass spectrometry: new perspectives for tandem mass spectrometry.European biophysics journal : EBJ · 2019Review
Corrections and comments
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Authors and funding
6 authors.
Funding
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Abstract
Two-dimensional mass spectrometry (2DMS) involves simultaneous acquisition of the fragmentation patterns of all the analytes in a mixture by correlating their precursor and fragment ions by modulating precursor ions systematically through a fragmentation zone. Tandem two-dimensional mass spectrometry (MS/2DMS) unites the ultra-high accuracy of Fourier transform ion cyclotron resonance (FT-ICR) MS/MS and the simultaneous data-independent fragmentation of 2DMS to achieve extensive inter-residue fragmentation of entire proteins. 2DMS was recently developed for top-down proteomics (TDP), and applied to the analysis of calmodulin (CaM), reporting a cleavage coverage of about ~23% using infrared multiphoton dissociation (IRMPD) as fragmentation technique. The goal of this work is to expand the utility of top-down protein analysis using MS/2DMS in order to extend the cleavage coverage in top-down proteomics further into the interior regions of the protein. In this case, using MS/2DMS, the cleavage coverage of CaM increased from ~23% to ~42%. Graphical Abstract Two-dimensional mass spectrometry, when applied to primary fragment ions from the source, allows deep-sequencing of the protein calmodulin.
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Registered trials
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