Professor
Supervisor of Doctorate Candidates
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Impact Factor6.35
DOI number:10.1021/acs.analchem.8b01051.
Abstract:Most serum proteins are N-linked glycosylated, and therefore the glycoproteomic profiling of serum is essential for characterization of serum proteins. In this study, we profiled serum N-glycoproteome by our recently developed N-glycoproteomic method using solid-phase extraction of N-linked glycans and glycosite-containing peptides (NGAG) coupled with LC-MS/MS and site-specific glycosylation analysis using GPQuest software. Our data indicated that half of identified N-glycosites were modified by at least two glycans, with a majority of them being sialylated. Specifically, 3/4 of glycosites were modified by biantennary N-glycans and 1/3 of glycosites were modified by triantennary sialylated N-glycans. In addition, two novel atypical glycosites (with N-X-V motif) were identified and validated from albumin and α-1B-glycoprotein. The widespread presence of these two glycosites among individuals was further confirmed by individual serum analyses.
Indexed by:Journal paper
Discipline:Natural Science
First-Level Discipline:Biology
Document Type:J
Translation or Not:no
Date of Publication:2018-05-15
Included Journals:SCI
Pre One:40. Liuyi Dang, Li Jia, Yuan Zhi, Pengfei Li, Ting Zhao, Bojing Zhu, Rongxia Lan, Yingwei Hu, Hui Zhang, Shisheng Sun*. Mapping human N-linked glycoproteins and glycosylation sites using mass spectrometry. Trends in Analytical Chemistry. 2019. 114: 143-150.
Next One:38. Jian Shu, Liuyi Dang, Dandan Zhang, Punit Shah, Lijun Chen, Hui Zhang, Shisheng Sun*. Dynamic analysis of proteomic alterations in response to N‐linked glycosylation inhibition in a drug‐resistant ovarian carcinoma cell line. The FEBS journal. 286, 8: 1594-1605.
