Modeling amyloids in bacteria

Anna Villar-Piqué; Salvador Ventura

doi:10.1186/1475-2859-11-166

Modeling amyloids in bacteria

Anna Villar-Piqué, Salvador Ventura^*

^*Autor corresponent d’aquest treball

Producció científica: Contribució a revista › Article › Recerca › Avaluat per experts

24 Cites (Scopus)

Resum

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.

Idioma original	Anglès
Número d’article	166
Nombre de pàgines	3
Revista	Microbial cell factories (Print)
Volum	11
DOIs	https://doi.org/10.1186/1475-2859-11-166
Estat de la publicació	Publicada - 28 de des. 2012

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10.1186/1475-2859-11-166

https://ddd.uab.cat/record/225172

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Link to publication in Scopus

Una visión integrada de la agregación proteica: analisis in silico, in vitro, celular, transcriptomico y proteomico (INTAG)
Ventura Zamora, S. (PI), Castillo Cano, V. (Investigador/a), Espargaro Colome, A. (Investigador/a), Sabate Lagunas, R. (Investigador/a) & Villar Pique, A. (Investigador/a)
1/01/11 → 31/03/14
Projecte: Projectes i Ajuts a la Recerca

Com citar-ho

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title = "Modeling amyloids in bacteria",

abstract = "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.",

author = "Anna Villar-Piqu{\'e} and Salvador Ventura",

note = "Funding Information: Work in our lab is supported by grants BFU2010-14901 from Ministerio de Ciencia e Innovaci{\'o}n (Spain) and 2009-SGR 760 from AGAUR (Generalitat de Catalunya). SV has been granted an ICREA ACADEMIA award (ICREA).",

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AU - Ventura, Salvador

N1 - Funding Information: Work in our lab is supported by grants BFU2010-14901 from Ministerio de Ciencia e Innovación (Spain) and 2009-SGR 760 from AGAUR (Generalitat de Catalunya). SV has been granted an ICREA ACADEMIA award (ICREA).

PY - 2012/12/28

Y1 - 2012/12/28

N2 - 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.

AB - 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.

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ER -

Modeling amyloids in bacteria

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Una visión integrada de la agregación proteica: analisis in silico, in vitro, celular, transcriptomico y proteomico (INTAG)

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