Journal
MOLECULAR BIOSYSTEMS
Volume 8, Issue 11, Pages 2850-2856Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2mb25268f
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Funding
- National Cancer Institute/NIH [K25CA137222, R21CA149772, R01CA107209, K07CA116296, R21CA161575]
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Disease-associated aberrant glycosylation may be protein specific and glycosylation site specific. Quantitative assessment of glycosylation changes at a site-specific molecular level may represent one of the initial steps for systematically revealing the glycosylation abnormalities associated with a disease or biological state. Comparative quantitative profiling of glycoproteome to provide accurate quantification of site-specific glycosylation occupancy has been a challenging task, requiring a concerted approach drawing from a variety of techniques. In this report, we present a quantitative glycoproteomics method that allows global scale identification and comparative quantification of glycosylation site occupancy using mass spectrometry. We further demonstrated this approach by quantitatively characterizing the N-glycoproteome of human pancreas.
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