Unknown

Dataset Information

0

Large-scale quantitative glycoproteomics analysis of site-specific glycosylation occupancy.


ABSTRACT: 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.

SUBMITTER: Pan S 

PROVIDER: S-EPMC3463725 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Large-scale quantitative glycoproteomics analysis of site-specific glycosylation occupancy.

Pan Sheng S   Tamura Yasuko Y   Chen Ru R   May Damon D   McIntosh Martin W MW   Brentnall Teresa A TA  

Molecular bioSystems 20120814 11


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 c  ...[more]

Similar Datasets

| S-EPMC7001331 | biostudies-literature
| S-EPMC7572468 | biostudies-literature
| S-EPMC3993895 | biostudies-other
| S-EPMC6428843 | biostudies-other
2019-04-02 | PXD011533 | Pride
| S-EPMC3658474 | biostudies-literature
| S-EPMC5057071 | biostudies-literature
| S-EPMC6683751 | biostudies-literature
| S-EPMC4263068 | biostudies-literature
| S-EPMC3448770 | biostudies-literature