| DOI | Resolve DOI: https://doi.org/10.1073/pnas.1615141114 |
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| Author | Search for: Noach, Ilit; Search for: Ficko-Blean, Elizabeth; Search for: Pluvinage, Benjamin; Search for: Stuart, Christopher; Search for: Jenkins, Meredith L.1; Search for: Brochu, Denis2; Search for: Buenbrazo, Nakita; Search for: Wakarchuk, Warren2; Search for: Burke, John E.; Search for: Gilbert, Michel2; Search for: Boraston, Alisdair B. |
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| Affiliation | - National Research Council of Canada. Aquatic and Crop Resource Development
- National Research Council of Canada. Human Health Therapeutics
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| Format | Text, Article |
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| Abstract | Protein glycosylation is one of the most abundant and important posttranslational modifications where the protein-linked glycans can impart specific physiochemical properties to the glycoprotein and/or the glycans themselves can mediate particular biological functions. The degradation of glycosylated proteins in normal or pathogenic processes, therefore, is an important biological process. This study reveals the molecular basis of how peptidases can use the O-glycans present on glycoproteins as a critical determinant of peptidase activity and, in doing so, provides unique insight into how peptidases may directly use posttranslational modifications present on their substrates to influence recognition and peptide bond cleavage. |
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| Publication date | 2017-01-17 |
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| Publisher | National Academy of Sciences |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 23003298 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 40c91d91-ca23-453f-bee9-e6b4d5faaeb6 |
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| Record created | 2018-05-11 |
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| Record modified | 2020-03-16 |
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