The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Protein Identification by Mass Spectrometry
Open accessAbstract
During the past two decades, mass spectrometry has become established as the primary method for protein identification from complex mixtures of biological origin. This is largely attributable to the fortunate coincidence of instrumental advances that allow routine analysis of minute amounts (typically femtomoles) of involatile, polar compounds such as peptides in complex mixtures, with the rapid growth in genomic databases that are amenable to searching with mass spectrometry (MS)1 data. Like many other developing fields in science, the creation of techniques and software tools and the initial generation and interpretation of data have been the domain of experts, people who are cognizant not only of the benefits of the methods but also of their actual and potential weaknesses.
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Cites
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., & Aebersold, R. (1999) · Nature Biotechnology · doi:10.1038/13690 · Cited by 4,683 · cited 1×
“permit measurement of relative abundance (59).”
Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., & Gygi, S. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0832254100 · Cited by 1,733
Barr, J. R., Maggio, V. L., Patterson, D. G., Cooper, G. R., Henderson, L. O., Turner, W. E., Smith, S. J., Hannon, W. H., Needham, L. L., & Sampson, E. J. (1996) · Clinical Chemistry · doi:10.1093/clinchem/42.10.1676 · Cited by 347
Cited by
Protein biomarker discovery and validation: the long and uncertain path to clinical utility
Rifai, N., Gillette, M. A., & Carr, S. A. (2006) · Nature Biotechnology · doi:10.1038/nbt1235 · Cited by 1,867
Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues
Olsen, J. V., Ong, S.-E., & Mann, M. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t400003-mcp200 · Cited by 1,254
Interpretation of Shotgun Proteomic Data
Nesvizhskii, A. I., & Aebersold, R. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r500012-mcp200 · Cited by 1,025
Cheng, D., Hoogenraad, C. C., Rush, J., Ramm, E., Schlager, M. A., Duong, D. M., Xu, P., Wijayawardana, S. R., Hanfelt, J., Nakagawa, T., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.d500009-mcp200 · Cited by 510
Qian, W.-J., Liu, T., Monroe, M. E., Strittmatter, E. F., Jacobs, J. M., Kangas, L. J., Petritis, K., Camp, D. G., & Smith, R. D. (2005) · Journal of Proteome Research · doi:10.1021/pr0498638 · Cited by 317
Metadata
- Authors
- Baldwin, M. A.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 3
- Issue
- 1
- Pages
- 1-9
- ISSN
- 1535-9476 (ISSN-L)
- OpenAlex
- W2043285998
- Cited by
- 229
- References
- 4
- FWCI
- 6.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.