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Multistep Conformation Selection in Amyloid Assembly
[Image: see text] Defining pathways for amyloid assembly could impact therapeutic strategies for as many as 50 disease states. Here we show that amyloid assembly is subject to different forces regulating nucleation and propagation steps and provide evidence that the more global β-sheet/β-sheet facia...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5709775/ https://www.ncbi.nlm.nih.gov/pubmed/29111722 http://dx.doi.org/10.1021/jacs.7b09362 |
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author | Hsieh, Ming-Chien Liang, Chen Mehta, Anil K. Lynn, David G. Grover, Martha A. |
author_facet | Hsieh, Ming-Chien Liang, Chen Mehta, Anil K. Lynn, David G. Grover, Martha A. |
author_sort | Hsieh, Ming-Chien |
collection | PubMed |
description | [Image: see text] Defining pathways for amyloid assembly could impact therapeutic strategies for as many as 50 disease states. Here we show that amyloid assembly is subject to different forces regulating nucleation and propagation steps and provide evidence that the more global β-sheet/β-sheet facial complementarity is a critical determinant for amyloid nucleation and structural selection. |
format | Online Article Text |
id | pubmed-5709775 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-57097752017-12-04 Multistep Conformation Selection in Amyloid Assembly Hsieh, Ming-Chien Liang, Chen Mehta, Anil K. Lynn, David G. Grover, Martha A. J Am Chem Soc [Image: see text] Defining pathways for amyloid assembly could impact therapeutic strategies for as many as 50 disease states. Here we show that amyloid assembly is subject to different forces regulating nucleation and propagation steps and provide evidence that the more global β-sheet/β-sheet facial complementarity is a critical determinant for amyloid nucleation and structural selection. American Chemical Society 2017-11-07 2017-11-29 /pmc/articles/PMC5709775/ /pubmed/29111722 http://dx.doi.org/10.1021/jacs.7b09362 Text en Copyright © 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Hsieh, Ming-Chien Liang, Chen Mehta, Anil K. Lynn, David G. Grover, Martha A. Multistep Conformation Selection in Amyloid Assembly |
title | Multistep
Conformation Selection in Amyloid Assembly |
title_full | Multistep
Conformation Selection in Amyloid Assembly |
title_fullStr | Multistep
Conformation Selection in Amyloid Assembly |
title_full_unstemmed | Multistep
Conformation Selection in Amyloid Assembly |
title_short | Multistep
Conformation Selection in Amyloid Assembly |
title_sort | multistep
conformation selection in amyloid assembly |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5709775/ https://www.ncbi.nlm.nih.gov/pubmed/29111722 http://dx.doi.org/10.1021/jacs.7b09362 |
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