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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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Autors principals: Cordeiro, Yraima, Kraineva, Julia, Gomes, Mariana P. B., Lopes, Marilene H., Martins, Vilma R., Lima, Luís M. T. R., Foguel, Débora, Winter, Roland, Silva, Jerson L.
Format: Artigo
Idioma:Inglês
Publicat: Biophysical Society 2005
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Accés en línia: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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