The DOI matches its Crossref record; 83 of the 83 references it cites were found in a registry or an index.
Ultra-fast proteomics with Scanning SWATH
Open accessAbstract
Accurate quantification of the proteome remains challenging for large sample series and longitudinal experiments. We report a data-independent acquisition method, Scanning SWATH, that accelerates mass spectrometric (MS) duty cycles, yielding quantitative proteomes in combination with short gradients and high-flow (800 µl min–1) chromatography. Exploiting a continuous movement of the precursor isolation window to assign precursor masses to tandem mass spectrometry (MS/MS) fragment traces, Scanning SWATH increases precursor identifications by ~70% compared to conventional data-independent acquisition (DIA) methods on 0.5–5-min chromatographic gradients. We demonstrate the application of ultra-fast proteomics in drug mode-of-action screening and plasma proteomics. Scanning SWATH proteomes capture the mode of action of fungistatic azoles and statins. Moreover, we confirm 43 and identify 11 new plasma proteome biomarkers of COVID-19 severity, advancing patient classification and biomarker discovery. Thus, our results demonstrate a substantial acceleration and increased depth in fast proteomic experiments that facilitate proteomic drug screens and clinical studies. Scanning SWATH increases the speed and selectivity of proteomics.
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UniProt: a worldwide hub of protein knowledge
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Self-citationA comprehensive map of molecular drug targets
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Natural proteome diversity links aneuploidy tolerance to protein turnover
Muenzner, J., Trébulle, P., Agostini, F., Zauber, H., Messner, C. B., Steger, M., Kilian, C., Lau, K., Barthel, N., Lehmann, A., et al. (2024) · Nature · doi:10.1038/s41586-024-07442-9 · Cited by 81
Self-citationSkowronek, P., Wallmann, G., Wahle, M., Willems, S., & Mann, M. (2025) · Nature Protocols · doi:10.1038/s41596-024-01104-w · Cited by 43
Teyssonnière, E. M., Trébulle, P., Muenzner, J., Loegler, V., Ludwig, D., Amari, F., Mülleder, M., Friedrich, A., Hou, J., Ralser, M., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2319211121 · Cited by 40
Self-citationAmino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost
(2024) · doi:10.1002/pro.5239 · Cited by 12
Metadata
- Authors
- Messner, C. B., Demichev, V., Bloomfield, N., Yu, J. S. L., White, M., Kreidl, M., Egger, A.-S., Freiwald, A., Ivosev, G., Wasim, F., Zelezniak, A., Jürgens, L., Suttorp, N., Sander, L. E., Kurth, F., Lilley, K. S., Mülleder, M., Tate, S., & Ralser, M.
- Venue
- Nature Biotechnology
- Published
- 2021-03-25
- Volume
- 39
- Issue
- 7
- Pages
- 846-854
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W3138817412
- Cited by
- 308
- References
- 83
- FWCI
- 17.18
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Messner, C. B., Demichev, V., Bloomfield, N., Yu, J. S. L., White, M., Kreidl, M., Egger, A.-S., Freiwald, A., Ivosev, G., Wasim, F., Zelezniak, A., Jürgens, L., Suttorp, N., Sander, L. E., Kurth, F., Lilley, K. S., Mülleder, M., Tate, S., & Ralser, M. (2021). Ultra-fast proteomics with Scanning SWATH. Nature Biotechnology. https://doi.org/10.1038/s41587-021-00860-4
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