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Skp1 isoforms are differentially modified by a dual function prolyl 4-hydroxylase/N-acety lglucosaminyltransferase in a plant pathogen
Skp1 is hydroxylated by an O(2)-dependent prolyl hydroxylase (PhyA) that contributes to O(2)-sensing in the social amoeba Dictyostelium and the mammalian pathogen Toxoplasma gondii. HO-Skp1 is subject to glycosylation and the resulting pentasaccharide affects Skp1 conformation in a way that influenc...
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| Vydáno v: | Glycobiology |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Oxford University Press
2019
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6774341/ https://ncbi.nlm.nih.gov/pubmed/31281925 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/glycob/cwz049 |
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