Glycosylation and Glycoproteins

Dear Colleagues,

Sugars, which represent one of the four fundamental building blocks of life, are the most abundant biological molecules on our planet. Sugars can be combined in a myriad number of ways to form complex carbohydrate structures (glycans). The glycan repertoire (glycome) of a given cell or organism is thus many orders of magnitude more complex than the genome or the proteome. However, only over the past two decades have we begun to truly appreciate the extent to which glycan function permeates biological systems, including human health and disease.
Glycosylation is the process by which a sugar is enzymatically attached to proteins, lipids, or other organic molecules. In particular, glycosylation increases protein diversity and structure, and as such significantly impacts on the function of the resulting glycoprotein.
As the roles of glycosylation in physiological and pathological processes are increasingly being recognized, the field of glycobiology is eliciting an unprecedented interest. However, the extreme complexity and structural diversity of glycans, combined with their “non-template”-driven synthesis, pose a significant technical challenge that has stimulated advances in the field.
This Special Issue will welcome contributions in all areas of glycobiology, including studies on the function of glycans in basic biological processes and human diseases, and the regulation of glycosylation reactions in vivo, as well as technical advances to analyze the complexities of the glycoproteome.

Prof. Dr. Patricia Berninsone
Dr. Joe Tiralongo
Guest Editors

Submission

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