4.5 Review

Mass spectrometry in the analysis of N-linked and O-linked glycans

Journal

CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 19, Issue 5, Pages 498-506

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2009.05.005

Keywords

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Funding

  1. Biotechnology and Biological Sciences Research Council (BBSRC) [BBF0083091, B19088, BBC5196701]
  2. Analytical Glycotechnology Core of the Consortium for Functional Glycomics [GN162116]
  3. sixth European Union Research Framework Programme [011952]
  4. Wellcome Trust
  5. Biotechnology and Biological Sciences Research Council [B19088] Funding Source: researchfish
  6. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U54GM062116] Funding Source: NIH RePORTER

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Mass spectrometry (MS) continues to play a vital role in defining the structures of N-glycans and O-glycans in glycoproteins via glycomic and glycoproteomic methodologies. The former seeks to define the total N-glycan and/or O-glycan repertoire in a biological sample whilst the latter is concerned with the analysis of glycopeptides. Recent technical developments have included improvements in tandem mass spectrometry (MS/MS and MSn) sequencing methodologies, more sensitive methods for analysing sulfated and polysialylated glycans and better procedures for defining the sites of O-glycosylation. New tools have been introduced to assist data handling and publicly accessible databases are being populated with glycomics data. Progress is exemplified by recent research in the fields of glycoimmunology, reproductive glycobiology, stem cells, bacterial glycosylation and non-mucin O-glycosylation.

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