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Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans

Mutation in the prion gene PRNP accounts for 10–15% of human prion diseases. However, little is known about the mechanisms by which mutant prion proteins (PrPs) cause disease. Here we investigated the effects of 10 different pathogenic mutations on the conformation and ligand-binding activity of rec...

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Bibliografiset tiedot
Päätekijät: Yin, Shaoman, Pham, Nancy, Yu, Shuiliang, Li, Chaoyang, Wong, Poki, Chang, Binggong, Kang, Shin-Chung, Biasini, Emiliano, Tien, Po, Harris, David A., Sy, Man-Sun
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 2007
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC1863438/
https://ncbi.nlm.nih.gov/pubmed/17456603
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0610827104
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