Advances in mass spectrometry‐based glycoproteomics

Protein glycosylation, an important PTM, plays an essential role in a wide range of biological processes such as immune response, intercellular signaling, inflammation, and host–pathogen interaction. Aberrant glycosylation has been correlated with various diseases. However, studying protein glycosyl...

Full description

Saved in:
Bibliographic Details
Published inElectrophoresis Vol. 39; no. 24; pp. 3104 - 3122
Main Authors Yu, Aiying, Zhao, Jingfu, Peng, Wenjing, Banazadeh, Alireza, Williamson, Seth D., Goli, Mona, Huang, Yifan, Mechref, Yehia
Format Journal Article
LanguageEnglish
Published Germany Wiley Subscription Services, Inc 01.12.2018
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Protein glycosylation, an important PTM, plays an essential role in a wide range of biological processes such as immune response, intercellular signaling, inflammation, and host–pathogen interaction. Aberrant glycosylation has been correlated with various diseases. However, studying protein glycosylation remains challenging because of low abundance, microheterogeneities of glycosylation sites, and poor ionization efficiency of glycopeptides. Therefore, the development of sensitive and accurate approaches to characterize protein glycosylation is crucial. The identification and characterization of protein glycosylation by MS is referred to as the field of glycoproteomics. Methods such as enrichment, metabolic labeling, and derivatization of glycopeptides in conjunction with different MS techniques and bioinformatics tools, have been developed to achieve an unequivocal quantitative and qualitative characterization of glycoproteins. This review summarizes the recent developments in the field of glycoproteomics over the past 6 years (2012 to 2018).
Bibliography:See the article online to view Figs. 1–6 in color.
Color online
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
ObjectType-Review-3
content type line 23
ISSN:0173-0835
1522-2683
1522-2683
DOI:10.1002/elps.201800272