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The Amino-Terminal PrP Domain Is Crucial to Modulate Prion Misfolding and Aggregation
The main hypothesis for prion diseases is that the cellular protein (PrP(C)) can be altered into a misfolded, β-sheet-rich isoform (PrP(Sc)), which undergoes aggregation and triggers the onset of transmissible spongiform encephalopathies. Here, we investigate the effects of amino-terminal deletion m...
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| Main Authors: | , , , , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Biophysical Society
2005
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1366767/ https://ncbi.nlm.nih.gov/pubmed/16040743 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.105.067603 |
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