The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
Open accessAbstract
Summary of Recent Advances Glycosylation is one of the most common post-translational modifications (PTMs) of proteins. At least 50% of human proteins are glycosylated with some estimates being as high as 70%. Glycoprotein analysis requires determining both the sites of glycosylation as well as the glycan structures associated with each site. Recent advances have led to the development of new analytical methods that employ mass spectrometry extensively making it possible to obtain the glycosylation site and the site microheterogeneity. These tools will be important for the eventual development of glycoproteomics.
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Cites
Zhang, H., Li, X.-J., Martin, D. B., & Aebersold, R. (2003) · Nature Biotechnology · doi:10.1038/nbt827 · Cited by 1,389
GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
Cooper, C. A., Gasteiger, E., & Packer, N. H. (2001) · PROTEOMICS · doi:10.1002/1615-9861(200102)1:2<340::aid-prot340>3.0.co;2-b · Cited by 471
Hägglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N., & Roepstorff, P. (2004) · Journal of Proteome Research · doi:10.1021/pr034112b · Cited by 460
Glycoproteomics based on tandem mass spectrometry of glycopeptides
Wuhrer, M., Catalina, M. I., Deelder, A. M., & Hokke, C. H. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.09.041 · Cited by 415
Protein glycosylation in development and disease
Dennis, J. W., Granovsky, M., & Warren, C. E. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199905)21:5<412::aid-bies8>3.0.co;2-5 · Cited by 396
Huddleston, M. J., Bean, M. F., & Carr, S. A. (1993) · Analytical Chemistry · doi:10.1021/ac00055a009 · Cited by 395
Håkansson, K., Cooper, H. J., Emmett, M. R., Costello, C. E., Marshall, A. G., & Nilsson, C. L. (2001) · Analytical Chemistry · doi:10.1021/ac0103470 · Cited by 359
Strategies for analysis of glycoprotein glycosylation
Geyer, H., & Geyer, R. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.10.007 · Cited by 299
Håkansson, K., Chalmers, M. J., Quinn, J. P., McFarland, M. A., Hendrickson, C. L., & Marshall, A. G. (2003) · Analytical Chemistry · doi:10.1021/ac030015q · Cited by 245
Determination of N-Glycosylation Sites and Site Heterogeneity in Glycoproteins
An, H. J., Peavy, T. R., Hedrick, J. L., & Lebrilla, C. B. (2003) · Analytical Chemistry · doi:10.1021/ac034414x · Cited by 242
Self-citation
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Hart, G. W., & Copeland, R. J. (2010) · Cell · doi:10.1016/j.cell.2010.11.008 · Cited by 643
Breast milk oligosaccharides: structure-function relationships in the neonate
Smilowitz, J. T., Lebrilla, C. B., Mills, D. A., German, J. B., & Freeman, S. L. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071813-105721 · Cited by 410
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From Omics to Multi-Omics: A Review of Advantages and Tradeoffs
Hayes, C. N., Nakahara, H., Ono, A., Tsuge, M., & Oka, S. (2024) · Genes · doi:10.3390/genes15121551 · Cited by 119
Stolfa, G., Smonskey, M. T., Boniface, R., Hachmann, A., Gulde, P., Joshi, A. D., Pierce, A. P., Jacobia, S. J., & Campbell, A. (2018) · Biotechnology Journal · doi:10.1002/biot.201700227 · Cited by 97
Metadata
- Authors
- An, H. J., Froehlich, J. W., & Lebrilla, C. B.
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 13
- Issue
- 4
- Pages
- 421-426
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W1980770700
- Cited by
- 280
- References
- 39
- FWCI
- 0.59
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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