Journal
NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 13, Issue 7, Pages 448-462Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3383
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Funding
- US National Institutes of Health (NIH) from the National Center for Research Resources [P41RR005351, P41RR018502]
- National Institute of General Medical Sciences [P41GM103390, P41GM103490]
- NIH [R01GM047533, R01DK075322, P01GM085354, R01GM072839]
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Protein glycosylation is a ubiquitous post-translational modification found in all domains of life. Despite their significant complexity in animal systems, glycan structures have crucial biological and physiological roles, from contributions in protein folding and quality control to involvement in a large number of biological recognition events. As a result, they impart an additional level of 'information content' to underlying polypeptide structures. Improvements in analytical methodologies for dissecting glycan structural diversity, along with recent developments in biochemical and genetic approaches for studying glycan biosynthesis and catabolism, have provided a greater understanding of the biological contributions of these complex structures in vertebrates.
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