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BI Ming, TIAN Zhi-xin. Research Progress in Structure-specific N-glycoproteomics[J]. Journal of Chinese Mass Spectrometry Society, 2021, 42(5): 897-913. DOI: 10.7538/zpxb.2021.0122
Citation: BI Ming, TIAN Zhi-xin. Research Progress in Structure-specific N-glycoproteomics[J]. Journal of Chinese Mass Spectrometry Society, 2021, 42(5): 897-913. DOI: 10.7538/zpxb.2021.0122
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Research Progress in Structure-specific N-glycoproteomics

  • School of Chemical Science & Engineering, Tongji University, Shanghai 200092, China

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    • Abstract
  • N-linked glycosylation, as one of the most common post-translation modification in proteins, is modified on asparagine residue among the N-X-T/S/C(X≠P) motif. N-glycans share a common core structure consisting of two N-acetylglusosamines and three mannoses, and which have three common types of high-mannose, hybrid and complex. N-glycosylation sites have both macro- and micro- heterogeneities and the function of each N-glycoylation is both site- and structure-specific. The precise site- and structure-specific identification and quantification of N-glycosylation is the main road of discovering disease diagnostic and prognostic biomarkers as well as drug targets. With the advancements in high-efficient enrichment materials, liquid chromatography separation technology, cascade mass spectrometry dissociation and detection technologies and bioinformatics database search methods, N-glycoproteomics enables high-throughput site- and structure-specific identification and quantification of N-glycosylation in complex systems. This paper mainly reviewed the basic procedures in the N-glycoproteomics pipeline including sample preparation, high-performance LC-MS/MS analysis and bioinformatics data processing as well as representative applications.
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