ArticleScientific reports2015
Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Recent advances in mass spectrometry (MS)-based glycoproteomics in complex biological samples.Trends in analytical chemistry : TRAC · 2019Article
- Mapping human N-linked glycoproteins and glycosylation sites using mass spectrometry.Trends in analytical chemistry : TRAC · 2019Article
- Article
- Regulation of TNF-Related Apoptosis-Inducing Ligand Signaling by Glycosylation.International journal of molecular sciences · 2018Review
- Comparison of Enrichment Methods for Intact N- and O-Linked Glycopeptides Using Strong Anion Exchange and Hydrophilic Interaction Liquid Chromatography.Analytical chemistry · 2017Article
- Glycomic and glycoproteomic analysis of glycoproteins-a tutorial.Analytical and bioanalytical chemistry · 2017Article
- Recent Advances in the Analysis of Complex Glycoproteins.Analytical chemistry · 2017Review
- Chemical Glycoproteomics.Chemical reviews · 2016Review
- In-depth mapping of the mouse brain N-glycoproteome reveals widespread N-glycosylation of diverse brain proteins.Oncotarget · 2016Article
- Reliable LC-MS quantitative glycomics using iGlycoMab stable isotope labeled glycans as internal standards.Electrophoresis · 2016Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Due to the important roles of N-glycoproteins in various biological processes, the global N-glycoproteome analysis has been paid much attention. However, by current strategies for N-glycoproteome profiling, peptides with glycosylated Asn at N-terminus (PGANs), generated by protease digestion, could hardly be identified, due to the poor deglycosylation capacity by enzymes. However, theoretically, PGANs occupy 10% of N-glycopeptides in the typical tryptic digests. Therefore, in this study, we developed a novel strategy to identify PGANs by releasing N-glycans through the N-terminal site-selective succinylation assisted enzymatic deglycosylation. The obtained PGANs information is beneficial to not only achieve the deep coverage analysis of glycoproteomes, but also discover the new biological functions of such modification.
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