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Modeling amyloids in bacteria
An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms. Bacterial cell factories have raised as privileged model systems to understand the mechani...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3539947/ https://www.ncbi.nlm.nih.gov/pubmed/23272903 http://dx.doi.org/10.1186/1475-2859-11-166 |
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author | Villar-Piqué, Anna Ventura, Salvador |
author_facet | Villar-Piqué, Anna Ventura, Salvador |
author_sort | Villar-Piqué, Anna |
collection | PubMed |
description | An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms. Bacterial cell factories have raised as privileged model systems to understand the mechanisms behind amyloid assembly and the cellular fitness cost associated to the formation of these aggregates. In the near future, these bacterial systems will allow implementing high-throughput screening approaches to identify effective modulators of amyloid aggregation. |
format | Online Article Text |
id | pubmed-3539947 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-35399472013-01-10 Modeling amyloids in bacteria Villar-Piqué, Anna Ventura, Salvador Microb Cell Fact Commentary An increasing number of proteins are being shown to assemble into amyloid structures, self-seeding fibrillar aggregates that may lead to pathological states or play essential biological functions in organisms. Bacterial cell factories have raised as privileged model systems to understand the mechanisms behind amyloid assembly and the cellular fitness cost associated to the formation of these aggregates. In the near future, these bacterial systems will allow implementing high-throughput screening approaches to identify effective modulators of amyloid aggregation. BioMed Central 2012-12-28 /pmc/articles/PMC3539947/ /pubmed/23272903 http://dx.doi.org/10.1186/1475-2859-11-166 Text en Copyright ©2012 Villar-Pique and Ventura; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Commentary Villar-Piqué, Anna Ventura, Salvador Modeling amyloids in bacteria |
title | Modeling amyloids in bacteria |
title_full | Modeling amyloids in bacteria |
title_fullStr | Modeling amyloids in bacteria |
title_full_unstemmed | Modeling amyloids in bacteria |
title_short | Modeling amyloids in bacteria |
title_sort | modeling amyloids in bacteria |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3539947/ https://www.ncbi.nlm.nih.gov/pubmed/23272903 http://dx.doi.org/10.1186/1475-2859-11-166 |
work_keys_str_mv | AT villarpiqueanna modelingamyloidsinbacteria AT venturasalvador modelingamyloidsinbacteria |