Professor
Supervisor of Doctorate Candidates
Hits:
Impact Factor41.667
DOI number:10.1038/nbt.3403.
Abstract:Comprehensive characterization of protein glycosylation is critical for understanding the structure and function of glycoproteins. However, due to the complexity and heterogeneity of glycoprotein conformations, current glycoprotein analyses focus mainly on either the de-glycosylated glycosylation site (glycosite)-containing peptides or the released glycans. Here, we describe a chemoenzymatic method called solid phase extraction of N-linked glycans and glycosite-containing peptides (NGAG) for the comprehensive characterization of glycoproteins that is able to determine glycan heterogeneity for individual glycosites in addition to providing information about the total N-linked glycan, glycosite-containing peptide and glycoprotein content of complex samples. The NGAG method can also be applied to quantitatively detect glycoprotein alterations in total and site-specific glycan occupancies.
Indexed by:Journal paper
Discipline:Natural Science
First-Level Discipline:Biology
Document Type:J
Translation or Not:no
Date of Publication:2016-01-01
Included Journals:SCI
Pre One:28. Punit Shah, Weiming Yang, Shisheng Sun, Jered Pasay, Nauder Faraday, Hui Zhang*. Platelet glycoproteins associated with aspirin‐treatment upon platelet activation. Proteomics. 2017, 17(6): 1600199.
Next One:26. Hui Zhang, Tao Liu, Zhen Zhang, Samuel H Payne, Bai Zhang, Jason E McDermott, Jian-Ying Zhou, Vladislav A Petyuk, Li Chen, Debjit Ray, Shisheng Sun, et al. Integrated proteogenomic characterization of human high grade serous ovarian cancer. Cell. 2016, 166 (3): 755-765.
