articleGlycobiologySep 22, 2004Closed access

Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites

Technical University of Denmark

PubMed
Indexed incrossrefpubmed

Abstract

O-GalNAc-glycosylation is one of the main types of glycosylation in mammalian cells. No consensus recognition sequence for the O-glycosyltransferases is known, making prediction methods necessary to bridge the gap between the large number of known protein sequences and the small number of proteins experimentally investigated with regard to glycosylation status. From O-GLYCBASE a total of 86 mammalian proteins experimentally investigated for in vivo O-GalNAc sites were extracted. Mammalian protein homolog comparisons showed that a glycosylated serine or threonine is less likely to be precisely conserved than a nonglycosylated one. The Protein Data Bank was analyzed for structural information, and 12…

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886
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18.81
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100%
References
67
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Authors

4

Topics & keywords

Keywords
  • Glycosylation
  • Threonine
  • Mucin
  • Serine
  • Computational biology
  • Chemistry
  • Consensus sequence
  • Biochemistry
UN Sustainable Development Goals
  • Life in Land
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