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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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| I publikationen: | Glycobiology |
|---|---|
| Huvudupphovsmän: | , , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Oxford University Press
2019
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| Ämnen: | |
| Länkar: | 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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