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BOLD — A biological O ‐linked glycan database
Author(s) -
Cooper Catherine A.,
Wilkins Marc R.,
Williams Keith L.,
Packer Nicolle H.
Publication year - 1999
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(19991201)20:18<3589::aid-elps3589>3.0.co;2-m
Subject(s) - glycan , monosaccharide , fucose , chemistry , biochemistry , glycobiology , serine , threonine , phosphodiester bond , galactose , database , glycoprotein , phosphorylation , rna , computer science , gene
Glycans can be O ‐linked to proteins via the hydroxyl group of serine, threonine, tyrosine, hydroxylysine or hydroxyproline. Sometimes the glycan is O ‐linked to the hydroxyl group via a phosphodiester bond. The core monosaccharide residue may be N ‐acetylgalactosamine, N ‐acetylglucosamine, galactose, glucose, fucose, mannose, xylose or arabinose. These O ‐linked glycans can remain as a monosaccharide, but often a complex structure is built up by stepwise addition of monosaccharides. Monosaccharides known to be added include galactose, N ‐acetylglucosamine, fucose, N ‐acetylneuraminic acid, N ‐glycolylneuraminic acid and 2‐keto‐3‐deoxynonulosonic acid. O ‐linked glycans can also contain sulfate and phosphate residues. This leads to the possibility of the existence of numerous O ‐glycan structures. The biological O ‐linked database (BOLD) is a relational database that contains information on O ‐linked glycan structures, their biological sources (with a link to the SWISS‐PROT protein database), the references in which the glycan was described (with a link to MEDLINE), and the methods used to determine the glycan structure. The database provides a valuable resource for glycobiology researchers interested in O ‐linked oligosaccharide structures that have been previously described on proteins from different species and tissues.