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Structural insights into functional amyloid inhibition in Gram −ve bacteria
Amyloids are proteinaceous aggregates known for their role in debilitating degenerative diseases involving protein dysfunction. Many forms of functional amyloid are also produced in nature and often these systems require careful control of their assembly to avoid the potentially toxic effects. The b...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5135000/ https://www.ncbi.nlm.nih.gov/pubmed/27913673 http://dx.doi.org/10.1042/BST20160245 |
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author | Hawthorne, William Rouse, Sarah Sewell, Lee Matthews, Stephen J. |
author_facet | Hawthorne, William Rouse, Sarah Sewell, Lee Matthews, Stephen J. |
author_sort | Hawthorne, William |
collection | PubMed |
description | Amyloids are proteinaceous aggregates known for their role in debilitating degenerative diseases involving protein dysfunction. Many forms of functional amyloid are also produced in nature and often these systems require careful control of their assembly to avoid the potentially toxic effects. The best-characterised functional amyloid system is the bacterial curli system. Three natural inhibitors of bacterial curli amyloid have been identified and recently characterised structurally. Here, we compare common structural features of CsgC, CsgE and CsgH and discuss the potential implications for general inhibition of amyloid. |
format | Online Article Text |
id | pubmed-5135000 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-51350002016-12-16 Structural insights into functional amyloid inhibition in Gram −ve bacteria Hawthorne, William Rouse, Sarah Sewell, Lee Matthews, Stephen J. Biochem Soc Trans Structural Aspects of Infectious Disease Amyloids are proteinaceous aggregates known for their role in debilitating degenerative diseases involving protein dysfunction. Many forms of functional amyloid are also produced in nature and often these systems require careful control of their assembly to avoid the potentially toxic effects. The best-characterised functional amyloid system is the bacterial curli system. Three natural inhibitors of bacterial curli amyloid have been identified and recently characterised structurally. Here, we compare common structural features of CsgC, CsgE and CsgH and discuss the potential implications for general inhibition of amyloid. Portland Press Ltd. 2016-12-15 2016-12-02 /pmc/articles/PMC5135000/ /pubmed/27913673 http://dx.doi.org/10.1042/BST20160245 Text en © 2016 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0) . |
spellingShingle | Structural Aspects of Infectious Disease Hawthorne, William Rouse, Sarah Sewell, Lee Matthews, Stephen J. Structural insights into functional amyloid inhibition in Gram −ve bacteria |
title | Structural insights into functional amyloid inhibition in Gram −ve bacteria |
title_full | Structural insights into functional amyloid inhibition in Gram −ve bacteria |
title_fullStr | Structural insights into functional amyloid inhibition in Gram −ve bacteria |
title_full_unstemmed | Structural insights into functional amyloid inhibition in Gram −ve bacteria |
title_short | Structural insights into functional amyloid inhibition in Gram −ve bacteria |
title_sort | structural insights into functional amyloid inhibition in gram −ve bacteria |
topic | Structural Aspects of Infectious Disease |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5135000/ https://www.ncbi.nlm.nih.gov/pubmed/27913673 http://dx.doi.org/10.1042/BST20160245 |
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