The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Fragment correlation mass spectrometry: Determining the structures of biopolymers in a complex mixture without isolating individual components
Open accessPublished version of a preprint
Abstract
Fragment correlation mass spectrometry correlates ion pairs generated from the same fragmentation pathway, achieved by covariance mapping of tandem mass spectra generated with an unmodified linear ion trap without preseparation. We enable the identification of different precursors at different charge states in a complex mixture from a large isolation window, empowering an analytical approach for data-independent acquisition. The method resolves and matches isobaric fragments, internal ions, and disulfide bond fragments. We suggest that this method represents a major advance for analyzing structures of biopolymers in mixtures.
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Cites
How many human proteoforms are there?
Aebersold, R., Agar, J. N., Amster, I. J., Baker, M. S., Bertozzi, C. R., Boja, E. S., Costello, C. E., Cravatt, B. F., Fenselau, C., Garcia, B. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2576 · Cited by 907
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Research works printed but not linked: 14
- 10.1126/science.1124619 · DOI
- 10.1146/annurev.biochem.70.1.437 · DOI
- 10.1038/s41592-019-0457-0 · DOI · Paper page
- 10.1007/s00249-019-01348-5 · DOI
- 10.1002/anie.202315904 · DOI
- T. Driver , Two-dimensional partial-covariance mass spectrometry of large molecules based on fragment correlations. Phys. Rev. X 10, 041004 (2020).
- 10.1021/acs.analchem.1c00332 · DOI
- 10.1021/acs.analchem.1c00895 · DOI
- 10.1038/nmeth705 · DOI
- 10.1088/0953-4075/49/15/152004 · DOI
- 10.1126/science.246.4933.1029 · DOI
- 10.1126/science.2675315 · DOI · Paper page
- 10.1007/s11095-020-02868-y · DOI
- 10.1073/pnas.2304735120 · DOI
Metadata
- Authors
- Li, Y., Cavet, G., Zare, R. N., & Driver, T.
- Affiliations
- Stanford University (US)
- Flatiron Bio, Palo Alto, CA 94301
- SLAC National Accelerator Laboratory (US)
- Corresponding author
- Zare, Richard N.
- Driver, Taran
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2024-07-29
- Volume
- 121
- Issue
- 32
- Pages
- e2409676121-e2409676121
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC11317569
- OpenAlex
- W4401071082
- Cited by
- 6
- References
- 1
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 2
- FWCI
- 0.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- ChemRxiv (acceptedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- DOD | USAF | AMC | Air Force Office of Scientific Research (AFOSR FA9550-21-1-0170)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- tandem mass spectrometry, covariance mapping, linear ion trap, data-independent acquisition, complex mixtures, precursor identification, charge states
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