Ion Activation Methods for Peptides and Proteins
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTIon Activation Methods for Peptides and ProteinsLuis A. MaciasLuis A. MaciasDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United StatesMore by Luis A. MaciasView Biography, Inês C. SantosInês C. SantosDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United StatesMore by Inês C. SantosView Biography, and Jennifer S. Brodbelt*Jennifer S. BrodbeltDepartment of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States*Phone: 512-471-0029. E-mail: [email protected]More by Jennifer S. BrodbeltView Biographyhttp://orcid.org/0000-0003-3207-0217Cite this: Anal. Chem. 2020, 92, 1, 227–251Publication Date (Web):October 30, 2019Publication History Published online30 October 2019Published inissue 7 January 2020https://pubs.acs.org/doi/10.1021/acs.analchem.9b04859https://doi.org/10.1021/acs.analchem.9b04859review-articleACS PublicationsCopyright © 2019 American Chemical SocietyRequest reuse permissionsArticle Views3495Altmetric-Citations71LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Dissociation,Fragmentation,Ions,Mass spectrometry,Peptides and proteins Get e-Alerts
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Effective ion activation for MS/MS analysis is essential for characterizing proteoforms.
“Effective ion activation for MS/MS analysis is essential for characterizing proteoforms [112].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [112]
CAD and HCD may cleave labile PTMs and cause unwanted neutral loss of water and ammonium.
“However, because CAD and HCD often break the most labile bonds, it may cleave labile PTMs (e.g., phosphorylation) and cause unwanted neutral loss of water and ammonium [112].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [112]
Slower reaction kinetics, protein-to-protein variability, and charge state dependence limit ECD and ETD for global proteomic analysis.
“However, the slower reaction kinetics, protein-to-protein variability, and charge state dependence of these techniques limit their application for global proteomic analysis[112].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [112]
ECD and ETD breakages along the protein backbone occur more randomly, enabling higher sequence coverage while preserving labile PTMs.
“Breakages along the protein backbone occur more randomly enabling higher sequence coverage while preserving labile PTMs.”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [112]
The increasing availability of different fragmentation tools has enabled high protein sequence coverage, improved global proteoform characterization, and characterization of higher-order protein structure.
“Overall, the growing number of different fragmentation tools available has enabled high protein sequence coverage, improved global proteoform characterization, and characterization of higher-order protein structure [112].”
From Top-down proteomics: challenges, innovations, and applications in basic and clinical research (2020) · cites this paper as [112]
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van de Waterbeemd, M., Snijder, J., Tsvetkova, I. B., Dragnea, B. G., Cornelissen, J. J. L. M., & Heck, A. J. R. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1348-6 · Cited by 47 · see citing works
Theisen, A., Yan, B. L., Brown, J. M., et al. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b01705 · Cited by 47 · see citing works
UV Photodissociation Mass Spectrometry Accurately Localize Sites of Backbone Deuteration in Peptides
Mistarz, U. H., Bellina, B., Jensen, P. F., et al. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04683 · Cited by 47 · see citing works
Donor, M. T., Mroz, A. M., & Prell, J. S. (2019) · Chemical Science · doi:10.1039/c9sc00644c · Cited by 47 · see citing works
Expanding the mass range for UVPD-based native top-down mass spectrometry
Greisch, J.-F., Tamara, S., Scheltema, R. A., Maxwell, H. W. R., Fagerlund, R. D., Fineran, P. C., Tetter, S., Hilvert, D., & Heck, A. J. R. (2019) · Chemical Science · doi:10.1039/c9sc01857c · Cited by 47 · see citing works
Shedding Light on the Frontier of Photodissociation
Brodbelt, J. S. (2011) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-010-0023-6 · Cited by 46 · see citing works
Self-citationSidoli, S., Lu, C., Coradin, M., Wang, X., Karch, K. R., Ruminowicz, C., & Garcia, B. A. (2017) · Epigenetics & Chromatin · doi:10.1186/s13072-017-0139-z · Cited by 46 · see citing works
Flagged first, then by citations
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Cited by
Sorted by citations
High-Resolution Native Mass Spectrometry
Tamara, S., den Boer, M. A., & Heck, A. J. R. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00212 · Cited by 511 · see citing works
Top-down proteomics: challenges, innovations, and applications in basic and clinical research
Brown, K. A., Melby, J. A., Roberts, D. S., & Ge, Y. (2020) · Expert Review of Proteomics · doi:10.1080/14789450.2020.1855982 · Cited by 152 · see citing works
Native Mass Spectrometry of Membrane Proteins
Keener, J. E., Zhang, G., & Marty, M. T. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04342 · Cited by 126 · see citing works
- Authors
- Macias, L. A., Santos, I. C., & Brodbelt, J. S.
- Affiliations
- The University of Texas at Austin (US)
- Corresponding author
- Brodbelt, Jennifer S.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2019-10-30
- Volume
- 92
- Issue
- 1
- Pages
- 227-251
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- PMC
- PMC6949381
- OpenAlex
- W4211007003
- Cited by
- 107
- References
- 302
- Citations by year
- 2026: 14 · 2025: 9 · 2024: 16 · 2023: 17 · 2022: 16 · 2021: 20 · 2020: 15
- FWCI
- 1.32
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- Locations
- Analytical Chemistry (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- Funders
- Welch Foundation (F-1155)
- National Institutes of Health (R01-GM103655, R01-GM121714)
- National Science Foundation (CHE1402753)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Atomic and Molecular Physics
- Keywords
- ion activation, peptide fragmentation, protein fragmentation, mass spectrometry, tandem mass spectrometry, collision-induced dissociation, post-translational modification, peptide identification, proteomics, protein sequencing
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