Professor
Supervisor of Doctorate Candidates
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Impact Factor5.9
DOI number:10.1021/acs.analchem.5b03886.
Abstract:It is well-known that N-linked glycans usually attach to asparagine residues in the N-X-S/T motifs of proteins. However, accumulating evidence indicates that N-glycosylation could also possibly occur at other atypical motifs. In this study, we tried to identify atypical N-glycosylation sites using our recently developed solid-phase extraction of the N-linked Glycans And Glycosite-containing peptides (NGAG) method. Peptides with deamidation sites at asparagine residues but lacking a typical asparagine-X-serine/threonine sequons (N-X-S/T, X is any amino acid except proline) motif were identified from deglycosylated peptide data as potentially atypical glycosite-containing peptides. These atypical glycosites were verified by the presence of glycans on their intact glycopeptides and further confirmed by specific inhibition of cells with an N-linked glycosylation inhibitor, tunicamycin. From this study, two atypical N-linked glycosylation sites with N-X-C and N-X-V motifs were identified and validated from an ovarian cancer cell line (OVCAR-3).
Indexed by:Journal paper
Discipline:Natural Science
First-Level Discipline:Biology
Document Type:J
Translation or Not:no
Date of Publication:2015-12-15
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.
