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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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Detalhes bibliográficos
Main Authors: 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
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2007
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Acesso em linha: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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