Proteomics

Dataset Information

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Differentially expressed N-glycopeptides in HepG2 related to LO2 cell line

ABSTRACT: With isotopically dimethyl labeling, ZIC-HILIC enrichment, C18 pre-fractionation, differentially expressed N-glycosylation in HCC HepG2 cells (relative to normal liver LO2 cells) were analyzed using penta-HILIC-MS/MS.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Kaijie Xiao  

LAB HEAD: Zhixin Tian

PROVIDER: PXD012424 | Pride | 2019-05-31

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
LO2_GP_C18_tr1_f1_pentaHILIC_75um_150min_20181116.raw Raw
LO2_GP_C18_tr1_f2_pentaHILIC_75um_150min_20181116.raw Raw
LO2_GP_C18_tr1_f3_pentaHILIC_75um_150min_20181116.raw Raw
LO2_GP_C18_tr1_f4_pentaHILIC_75um_150min_20181116.raw Raw
LO2_GP_C18_tr1_f5_pentaHILIC_75um_150min_20181116.raw Raw
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Publications

GPSeeker Enables Quantitative Structural N-Glycoproteomics for Site- and Structure-Specific Characterization of Differentially Expressed N-Glycosylation in Hepatocellular Carcinoma.

Xiao Kaijie K   Tian Zhixin Z  

Journal of proteome research 20190603 7

N-Glycosylation, being one of the most common and complex protein post-translational modifications (PTMs), is known to have microheterogeneity with the presence of different N-glycan structures at a single specific glycosite. These different structures may have exactly the same monosaccharide composition but totally different differential expressions and pathological relevance. Mass spectrometry-based N-glycoproteomics has so far been successful in large-scale characterization of these N-glycans  ...[more]

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