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

Small-molecule chaperones that can prevent protein misfolding have potential applications for treating diseases such as Alzheimer’s and ALS. Here the authors use high-resolution force spectroscopy to gain insight into the mechanism of action of an iron-tetrapyrrole with anti-prion properties.

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Autores principales:	Amar Nath Gupta, Krishna Neupane, Negar Rezajooei, Leonardo M. Cortez, Valerie L. Sim, Michael T. Woodside
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/abfdd6108de1499990d9c141d9020588
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spelling	oai:doaj.org-article:abfdd6108de1499990d9c141d90205882021-12-02T15:35:18ZPharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein10.1038/ncomms120582041-1723https://doaj.org/article/abfdd6108de1499990d9c141d90205882016-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms12058https://doaj.org/toc/2041-1723Small-molecule chaperones that can prevent protein misfolding have potential applications for treating diseases such as Alzheimer’s and ALS. Here the authors use high-resolution force spectroscopy to gain insight into the mechanism of action of an iron-tetrapyrrole with anti-prion properties.Amar Nath GuptaKrishna NeupaneNegar RezajooeiLeonardo M. CortezValerie L. SimMichael T. WoodsideNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Amar Nath Gupta Krishna Neupane Negar Rezajooei Leonardo M. Cortez Valerie L. Sim Michael T. Woodside Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein
description	Small-molecule chaperones that can prevent protein misfolding have potential applications for treating diseases such as Alzheimer’s and ALS. Here the authors use high-resolution force spectroscopy to gain insight into the mechanism of action of an iron-tetrapyrrole with anti-prion properties.
format	article
author	Amar Nath Gupta Krishna Neupane Negar Rezajooei Leonardo M. Cortez Valerie L. Sim Michael T. Woodside
author_facet	Amar Nath Gupta Krishna Neupane Negar Rezajooei Leonardo M. Cortez Valerie L. Sim Michael T. Woodside
author_sort	Amar Nath Gupta
title	Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein
title_short	Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein
title_full	Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein
title_fullStr	Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein
title_full_unstemmed	Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein
title_sort	pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/abfdd6108de1499990d9c141d9020588
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Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein

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