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Phosphorylation of Prion Protein at Serine 43 Induces Prion Protein Conformational Change
The cause of the conformational change of normal cellular prion protein (PrP) into its disease-associated form is unknown. Posttranslational modifications, such as glycosylation, acetylation, S-nitrosylation, and phosphorylation, are known to induce protein conformational changes. Here, we investiga...
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| Main Authors: | , , , , , |
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| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
Society for Neuroscience
2009
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2745063/ https://ncbi.nlm.nih.gov/pubmed/19587281 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1523/JNEUROSCI.2294-09.2009 |
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