STORI Plots Enable Accurate Tracking of Individual Ion Signals
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Charge detection mass spectrometry (CDMS) of low-level signals is currently limited to the analysis of individual ions that generate a persistent signal during the entire observation period. Ions that disintegrate during the observation period produce reduced frequency domain signal amplitudes, which lead to an underestimation of the ion charge state, and thus the ion mass. The charge assignment can only be corrected through an accurate determination of the time of ion disintegration. The traditional mechanisms for temporal signal analysis have severe limitations for temporal resolution, spectral resolution, and signal-to-noise ratios. Selective Temporal Overview of Resonant Ions (STORI) plots provide a new framework to accurately analyze low-level time domain signals of individual ions. STORI plots allow for complete correction of intermittent signals, the differentiation of single and multiple ions at the same frequency, and the association of signals that spontaneously change frequency.
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CDMS measures m/z and z for individual ions in an electrostatic ion trap from frequency and amplitude of the signal, which can be converted into mass.
“CDMS analysis of intact proteins is achieved by simultaneously measuring m/z and z for individual ions contained in an electrostatic ion trap from the frequency and amplitude of the resulting signal, which can then be converted into a mass measurement [111].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [111]
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- [13]High throughput charge detection mass spectrometry, Botamanenko D, Todd AR, Jarrold MF: MP494, Proceedings of the 67th ASMS Conference on Mass Spectrometry and Allied Topics, Atlanta, Georgia, June 2–6, 2019.
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Self-citationDodge, G. J., Anderson, A. J., He, Y., Liu, W., Viner, R., & Imperiali, B. (2023) · doi:10.1101/2023.06.16.545297 · Cited by 1 · see citing works
Ctortecka, C., Jaishankar, D., Su, P., Huang, C., Plá, I., Henning, N. F. C., Hollas, M. A. R., Callegari, M., Taylor, M. E., Lee, Y. M., et al. (2026) · medRxiv · doi:10.64898/2026.02.02.26345404 · Cited by 1 · see citing works
Self-citationLyutvinskiy, Y., Nagornov, K. O., Kozhinov, A. N., Gasilova, N., Menin, L., Meng, Z., Zhang, X., Saei, A. A., Tsybin, Y. O., Makarov, A., et al. (2021) · ChemRxiv · doi:10.26434/chemrxiv-2021-f6n9j
Self-citationIn Pursuit of Rare, Subtle, and Fleeting Post-Translational Modifications
Labant, M. (2023) · Genetic Engineering & Biotechnology News · doi:10.1089/gen.43.02.13
Dodge, G. J., Anderson, A. J., He, Y., Liu, W., Viner, R., & Imperiali, B. (2023) · doi:10.7554/elife.91125.1
Kuo, S.-T. A., Xi, Z., Cong, X., Yan, X., & Russell, D. H. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.27.640645
Characterization of Virus Vectors for Gene Therapy by Charge Detection Mass Spectrometry
Nakatsuka, R. (2025) · Journal of the Mass Spectrometry Society of Japan · doi:10.5702/massspec.24-032
Cleland, T. P., & Trizna, M. G. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00328 · Cited by 1 · see citing works
Applying distinct CDMS strategies to observe non-classical virus capsid assemblyPreprint
Thiede, L., Haris, A., Damjanović, T., Kung, J. C. K., Müller-Guhl, J., Pogan, R., Rothe, J., Schultze, W., Ugelstad, S., Eatough, D., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.29.721378
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Self-citationProtein Aggregation Capture for Top-down ProteomicsPreprint
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The Rise of Top‐Down Mass Spectrometry for the Characterization of Oligonucleotide Therapeutics
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Self-citationTargeted Analysis of >1500 Plasma Proteoforms via Individual Ion Mass Spectrometry
Sánchez, A., Plá, I., Peterson, K. N., White, V., Fisher, T. D., Hollas, M. A. R., Su, T., Le, N. H. V., Harrington, C., Cravedi, P., et al. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00449
Self-citationProtein Aggregation Capture for Top-Down Proteomics
Feltenstein, I. G., & Drown, B. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00583
- Authors
- Kafader, J. O., Beu, S. C., Early, B. P., Melani, R. D., Durbin, K. R., Zabrouskov, V., Makarov, A. A., Maze, J. T., Shinholt, D. L., Yip, P. F., Kelleher, N. L., Compton, P. D., & Senko, M. W.
- Affiliations
- Northwestern University (US)
- S.C. Beu Consulting, 78729, Austin, TX, USA
- Thermo Fisher Scientific (United States) (US)
- Thermo Fisher Scientific (Germany) (DE)
- Thermo Fisher Scientific, 78728, Austin, TX, USA
- ORCID
- Venue
- Journal of the American Society for Mass Spectrometry
- Publisher
- American Chemical Society (ACS)
- Published
- 2019-09-11
- Volume
- 30
- Issue
- 11
- Pages
- 2200-2203
- ISSN
- 1044-0305 (ISSN-L)
- PMC
- PMC6852666
- OpenAlex
- W2972833804
- Cited by
- 85
- References
- 18
- Citations by year
- 2026: 18 · 2025: 15 · 2024: 16 · 2023: 14 · 2022: 8 · 2021: 7 · 2020: 5 · 2019: 2
- FWCI
- 2.19
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of the American Society for Mass Spectrometry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Thermo Fisher Scientific
- National Resource for Translational and Developmental Proteomics (Grant P41 GM108569)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Physical Sciences › Engineering › Computational Mechanics › Ion-surface interactions and analysis
- Keywords
- charge detection mass spectrometry, time-domain signal analysis, intermittent signals, signal-to-noise ratio
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