Understanding glycoprotein structural heterogeneity and interactions: Insights from native mass spectrometry |
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| Institution: | 1. Department of Chemistry, University of Oxford, Oxford, UK;2. Kavli Institute for Nanoscience Discovery, University of Oxford, Oxford, UK;1. Biomolecular & Analytical Mass Spectrometry Group, Department of Chemistry, University of Antwerp, 2020 Antwerp, Belgium;2. UA-VITO Centre for Proteomics, University of Antwerp, 2020 Antwerp, Belgium;1. Department of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO Box 111, 80101 Joensuu, Finland;2. Department of Clinical Microbiology, Institute of Clinical Medicine and Biocenter Kuopio, University of Eastern Finland, PO Box 1627, 70211 Kuopio, Finland;3. Institute of Dentistry, School of Medicine, University of Eastern Finland, PO Box 1627, 70211 Kuopio, Finland;1. Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, the Netherlands;2. Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, the Netherlands;3. Faculty of Biology, Center for Medical Biotechnology, University Duisburg-Essen, 45117 Essen, Germany;4. School of Biosciences, Cardiff University, Cardiff CF10 3US, UK;3. Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands;4. 4Netherlands Proteomics Center, Padualaan 8, 3584 CH Utrecht, The Netherlands;5. 5Department of Molecular and Cellular Hemostasis, Sanquin Research, Amsterdam 1066 CX, the Netherlands;1. State Key Laboratory of Electroanalytical Chemistry, Jilin Province Key Laboratory of Chinese Medicine Chemistry and Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, 130021, China;2. School of Applied Chemistry and Engineering, University of Science and Technology of China, Hefei, 230029, China;3. Experiment Center for Science and Technology, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, China;1. Bioinformatics Program, Boston University, United States;2. Dept. of Biochemistry, Boston University, United States |
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| Abstract: | Protein glycosylation is critical since it connects complex metabolic pathways to diverse proteoforms, fine-tunes protein structures and exerts biological functions. Aberrant glycosylation on the other hand is associated with many diseases, including cancers, inflammation and metabolic disorders. By resolving monosaccharide residues on intact glycoprotein complexes, native mass spectrometry can shed light on glycan heterogeneity, glycoprotein structure and molecular recognition. Here, we focus on the two most prevalent forms of glycosylation, namely N- and O- linked, and discuss recent progress in native mass spectrometry for elucidating glycoprotein structural heterogeneity and relating specific glycan repertoires to glycoprotein interactions. |
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