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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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| 出版年: | Nat Commun |
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| 主要な著者: | , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Nature Publishing Group
2016
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| 主題: | |
| オンライン･アクセス: | 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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