Predicting mucin-type O-Glycosylation using enhancement value products from derived protein features.
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ABSTRACT:
SUBMITTER: Mohl JE
PROVIDER: S-EPMC7671581 | biostudies-literature | 2020 May
REPOSITORIES: biostudies-literature
Publications
Predicting mucin-type O-Glycosylation using enhancement value products from derived protein features.
Mohl Jonathon E JE Gerken Thomas T Leung Ming-Ying MY
Journal of theoretical & computational chemistry 20200501 3
Mucin-type O-glycosylation is one of the most common post-translational modifications of proteins. This glycosylation is initiated in the Golgi by the addition of the sugar N-acetylgalactosamine (GalNAc) onto protein Ser and Thr residues by a family of polypeptide GalNAc transferases. In humans there are 20 isoforms that are differentially expressed across tissues that serve multiple important biological roles. Using random peptide substrates, isoform specific amino acid preferences have been ob ...[more]
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