Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein

The development of small-molecule pharmacological chaperones as therapeutics for protein misfolding diseases has proven challenging, partly because their mechanism of action remains unclear. Here we study Fe-TMPyP, a tetrapyrrole that binds to the prion protein PrP and inhibits misfolding, examining...

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Detalles Bibliográficos
Autores principales: Gupta, Amar Nath, Neupane, Krishna, Rezajooei, Negar, Cortez, Leonardo M., Sim, Valerie L., Woodside, Michael T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4931252/
https://www.ncbi.nlm.nih.gov/pubmed/27346148
http://dx.doi.org/10.1038/ncomms12058

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4931252/
https://www.ncbi.nlm.nih.gov/pubmed/27346148
http://dx.doi.org/10.1038/ncomms12058

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