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Glycosylation: A Phenomenon Shared by All Domains of Life

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Managing Complexity, Reducing Perplexity

Part of the book series: Springer Proceedings in Mathematics & Statistics ((PROMS,volume 67))

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Abstract

This chapter provides insights into why proteins are glycosylated and how their glycosylation can be characterized by mass spectrometry. The covalent attachment of carbohydrates to proteins during their biosynthesis is a phenomenon shared by all domains of life. Indeed the majority of proteins in living systems are glycosylated. Their carbohydrates play critical roles in a myriad of biological processes especially those involving recognition. They do this via engagement with carbohydrate binding proteins called lectins. For example mammalian sperm-egg engagement in the first step of fertilization involves carbohydrate-lectin recognition, and the human egg is coated with a carbohydrate sequence called sialyl Lewisx which also plays important recognition roles in the immune system.

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Authors and Affiliations

  1. Division of Molecular Biosciences, Faculty of Natural Sciences, Centre for Integrative Systems Biology, Imperial College London, London, SW7 2AZ, UK

    Anne Dell & Federico Sastre

Authors
  1. Anne Dell
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  2. Federico Sastre
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Correspondence to Anne Dell .

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Editors and Affiliations

  1. Department of Mathematical Sciences, Politecnico di Torino, Torino, Italy

    Marcello Delitala

  2. OECD, Paris, France

    Giulia Ajmone Marsan

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Dell, A., Sastre, F. (2014). Glycosylation: A Phenomenon Shared by All Domains of Life. In: Delitala, M., Ajmone Marsan, G. (eds) Managing Complexity, Reducing Perplexity. Springer Proceedings in Mathematics & Statistics, vol 67. Springer, Cham. https://doi.org/10.1007/978-3-319-03759-2_7

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