Project PXD005553

PRIDE Assigned Tags:
Biological Dataset

Summary

Title

Mouse glycoproteome

Description

Precise and large-scale characterization of glycoproteome is critical for understanding the biological functions of glycoproteins. Due to the complexity of glycosylation, the overall throughput, data quality and accessibility of site-specific glycosylation analysis are overwhelmingly lower than those of routine proteomic studies. Here, we introduce a workflow that robustly identifies intact glycopeptides at a proteome scale using stepped-energy mass-spectrometry (MS) and pGlyco 2.0, a dedicated search engine for large-scale glycopeptide analysis with comprehensive quality control (false discovery rate evaluation on the glycan, peptide and glycopeptide matches).

Sample Processing Protocol

Precise and large-scale characterization of glycoproteome is critical for understanding the biological functions of glycoproteins. Due to the complexity of glycosylation, the overall throughput, data quality and accessibility of site-specific glycosylation analysis are overwhelmingly lower than those of routine proteomic studies. Here, we introduce a workflow that robustly identifies intact glycopeptides at a proteome scale using stepped-energy mass-spectrometry (MS) and pGlyco 2.0, a dedicated search engine for large-scale glycopeptide analysis with comprehensive quality control (false discovery rate evaluation on the glycan, peptide and glycopeptide matches).

Data Processing Protocol

Precise and large-scale characterization of glycoproteome is critical for understanding the biological functions of glycoproteins. Due to the complexity of glycosylation, the overall throughput, data quality and accessibility of site-specific glycosylation analysis are overwhelmingly lower than those of routine proteomic studies. Here, we introduce a workflow that robustly identifies intact glycopeptides at a proteome scale using stepped-energy mass-spectrometry (MS) and pGlyco 2.0, a dedicated search engine for large-scale glycopeptide analysis with comprehensive quality control (false discovery rate evaluation on the glycan, peptide and glycopeptide matches).

Contact

pGlyco pFind, Institute of Computing Technology, CAS, Beijing, China
Mingqi Liu, Institutes of Biomedical Sciences and department of Chemistry, Fudan University, Shanghai, China ( lab head )

Submission Date

13/12/2016

Publication Date

11/10/2017

Tissue

liver

Instrument

LTQ Orbitrap

Software

Not available

Quantification

Not available

Experiment Type

Shotgun proteomics

Publication

    Liu MQ, Zeng WF, Fang P, Cao WQ, Liu C, Yan GQ, Zhang Y, Peng C, Wu JQ, Zhang XJ, Tu HJ, Chi H, Sun RX, Cao Y, Dong MQ, Jiang BY, Huang JM, Shen HL, Wong CCL, He SM, Yang PY. pGlyco 2.0 enables precision N-glycoproteomics with comprehensive quality control and one-step mass spectrometry for intact glycopeptide identification. Nat Commun. 2017 8(1):438 PubMed: 28874712