Pharmacological chaperone for the structured domain of human prion protein

In prion diseases, the misfolded protein aggregates are derived from cellular prion protein (PrP(C)). Numerous ligands have been reported to bind to human PrP(C) (huPrP), but none to the structured region with the affinity required for a pharmacological chaperone. Using equilibrium dialysis, we scre...

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Main Authors: Nicoll, Andrew J., Trevitt, Clare R., Tattum, M. Howard, Risse, Emmanuel, Quarterman, Emma, Ibarra, Amaurys Avila, Wright, Connor, Jackson, Graham S., Sessions, Richard B., Farrow, Mark, Waltho, Jonathan P., Clarke, Anthony R., Collinge, John
Formáid: Artigo
Teanga:Inglês
Foilsithe: National Academy of Sciences 2010
Ábhair:
Biological Sciences
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC2955083/
https://ncbi.nlm.nih.gov/pubmed/20876144
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1009062107
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