Professor
Supervisor of Doctorate Candidates
Hits:
Impact Factor5.9
DOI number:10.1021/acs.analchem.5b01679.
Abstract:Protein glycosylation is one of the most important protein modifications. Glycosylation site occupancy alteration has been implicated in human diseases and cancers. However, current glycoproteomic methods focus on the identification and quantification of glycosylated peptides and glycosylation sites but not glycosylation occupancy or glycoform stoichiometry. Here we describe a method for large-scale determination of the absolute glycosylation stoichiometry using three independent relative ratios. Using this method, we determined 117 absolute N-glycosylation occupancies in OVCAR-3 cells. Finally, we investigated the possible functions and the determinants for partial glycosylation.
Indexed by:Journal paper
Discipline:Natural Science
First-Level Discipline:Biology
Document Type:J
Translation or Not:no
Date of Publication:2015-01-07
Included Journals:SCI
Pre One:21. Shisheng Sun*, Hui Zhang. Identification and Validation of Atypical N-Glycosylation Sites. Analytical chemistry. 2015. 87 (24): 11948–11951.
Next One:19. Punit Shah, Xiangchun Wang, Weiming Yang, Shadi Toghi Eshghi, Shisheng Sun, Naseruddin Hoti, Lijun Chen, Shuang Yang, Jered Pasay, Abby Rubin, Hui Zhang*. Integrated Proteomic and Glycoproteomic Analyses of Prostate Cancer Cells Reveal Glycoprotein Alteration in Protein Abundance and Glycosylation. Molecular & Cellular Proteomics. 2015, 14 (10): 2753-2763.
