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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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| Publicat a: | Nat Commun |
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| Autors principals: | , , , , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Nature Publishing Group
2016
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4931252/ https://ncbi.nlm.nih.gov/pubmed/27346148 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/ncomms12058 |
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