The DOI matches its Crossref record; 101 of the 101 references it cites were found in a registry or an index.
Proteomics by FTICR mass spectrometry: Top down and bottom up
Open accessAbstract
This review provides a broad overview of recent Fourier transform ion cyclotron resonance (FTICR) applications and technological developments relevant to the field of proteomics. Both the “bottom up” (peptide level) and “top down” (intact protein level) approaches are discussed and illustrated with examples. “Bottom up” topics include peptide fragmentation, the accurate mass and time (AMT) tag approach and dynamic range extension technology, aspects of quantitative proteomics measurements, post‐translational modifications, and developments in FTICR operation software focused on peptide and protein identification. Topics related to the “top down” approach include various aspects of high mass measurements, protein tandem mass spectrometry, methods for the study of protein conformations, and protein complexes as well as advanced technologies that may become of practical utility in the coming years. Finally, early examples of the integration of both FTICR approaches to biomedical proteomics applications are presented, along with an outlook for future directions. © 2004 Wiley Periodicals, Inc., Mass Spec Rev 24:168–200, 2005
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Cited by
Decoding protein modifications using top-down mass spectrometry
Siuti, N., & Kelleher, N. L. (2007) · Nature Methods · doi:10.1038/nmeth1097 · Cited by 503
Mass spectrometry approaches to glycomic and glycoproteomic analyses
Ruhaak, L. R., Xu, G., Li, Q., Goonatilleke, E., & Lebrilla, C. B. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00732 · Cited by 395
The diverse and expanding role of mass spectrometry in structural and molecular biology
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Proteins in Art, Archaeology, and Paleontology: From Detection to Identification
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Self-citation
Metadata
- Authors
- Bogdanov, B., & Smith, R. D.
- Venue
- Mass Spectrometry Reviews
- Publisher
- Wiley
- Published
- 2004-03-30
- Volume
- 24
- Issue
- 2
- Pages
- 168-200
- ISSN
- 0277-7037 (ISSN-L)
- 1098-2787
- OpenAlex
- W1984596349
- Cited by
- 447
- References
- 101
- FWCI
- 14.83
- Type
- journal article
- Language
- en
- Open access
- bronze
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