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:Binding kinetics of five drugs to beta2-adrenoceptor using peak profiling method and nonlinear chromatography
Next One:Bioactive compounds of Shuang–Huang–Lian prescription and an insight into its binding mechanism by β2‐adrenoceptor chromatography coupled with site‐directed molecular docking