期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 13, 期 4, 页码 421-426出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2009.07.022
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资金
- National Institute of Health [RO1GM049077]
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [R01HD061923] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM049077] Funding Source: NIH RePORTER
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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