Amyloids or prions? That is the question.

Despite major efforts devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the amino acid sequence. In recent years, experimental data on yeast prion domains allow to start at least partially decrypting the sequence requirem...

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Detalles Bibliográficos
Autores: Sabate R, Rousseau F, Schymkowitz J, Batlle C, Ventura S
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:España
Institución:Fundació Sant Joan de Déu
Repositorio:r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
OAI Identifier:oai:fsjd.fundanetsuite.com:p18905
Acceso en línea:https://fsjd.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=18905
Access Level:acceso abierto
Palabra clave:AD, Alzheimer's disease
CJD, Creutzfeldt-Jakob disease
PD, Parkinson's disease
PFD, prion forming domain
Q/N-rich domains
TSE, transmissible spongiform encephalopathy
amyloids
fALS, familial amyotrophic lateral sclerosis
neurodegenerative diseases
prions
protein intrinsic disorder
yeast
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network_acronym_str ES
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repository_id_str
spelling Amyloids or prions? That is the question.Sabate RRousseau FSchymkowitz JBatlle CVentura SAD, Alzheimer's diseaseCJD, Creutzfeldt-Jakob diseasePD, Parkinson's diseasePFD, prion forming domainQ/N-rich domainsTSE, transmissible spongiform encephalopathyamyloidsfALS, familial amyotrophic lateral sclerosisneurodegenerative diseasesprionsprotein intrinsic disorderyeastDespite major efforts devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the amino acid sequence. In recent years, experimental data on yeast prion domains allow to start at least partially decrypting the sequence requirements of prion formation. These experiments illustrate the need for intrinsically disordered sequence regions enriched with a particularly high proportion of glutamine and asparagine. Bioinformatic analysis suggests that these regions strike a balance between sufficient amyloid nucleation propensity on the one hand and disorder on the other, which ensures availability of the amyloid prone regions but entropically prevents unwanted nucleation and facilitates brittleness required for propagation.TAYLOR & FRANCIS INC2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://fsjd.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=18905PrionISSN: 19336896ISSNe: 1933690Xreponame:r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déuinstname:Fundació Sant Joan de DéuInglésinfo:eu-repo/semantics/openAccessoai:fsjd.fundanetsuite.com:p189052026-05-27T12:37:41Z
dc.title.none.fl_str_mv Amyloids or prions? That is the question.
title Amyloids or prions? That is the question.
spellingShingle Amyloids or prions? That is the question.
Sabate R
AD, Alzheimer's disease
CJD, Creutzfeldt-Jakob disease
PD, Parkinson's disease
PFD, prion forming domain
Q/N-rich domains
TSE, transmissible spongiform encephalopathy
amyloids
fALS, familial amyotrophic lateral sclerosis
neurodegenerative diseases
prions
protein intrinsic disorder
yeast
title_short Amyloids or prions? That is the question.
title_full Amyloids or prions? That is the question.
title_fullStr Amyloids or prions? That is the question.
title_full_unstemmed Amyloids or prions? That is the question.
title_sort Amyloids or prions? That is the question.
dc.creator.none.fl_str_mv Sabate R
Rousseau F
Schymkowitz J
Batlle C
Ventura S
author Sabate R
author_facet Sabate R
Rousseau F
Schymkowitz J
Batlle C
Ventura S
author_role author
author2 Rousseau F
Schymkowitz J
Batlle C
Ventura S
author2_role author
author
author
author
dc.subject.none.fl_str_mv AD, Alzheimer's disease
CJD, Creutzfeldt-Jakob disease
PD, Parkinson's disease
PFD, prion forming domain
Q/N-rich domains
TSE, transmissible spongiform encephalopathy
amyloids
fALS, familial amyotrophic lateral sclerosis
neurodegenerative diseases
prions
protein intrinsic disorder
yeast
topic AD, Alzheimer's disease
CJD, Creutzfeldt-Jakob disease
PD, Parkinson's disease
PFD, prion forming domain
Q/N-rich domains
TSE, transmissible spongiform encephalopathy
amyloids
fALS, familial amyotrophic lateral sclerosis
neurodegenerative diseases
prions
protein intrinsic disorder
yeast
description Despite major efforts devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the amino acid sequence. In recent years, experimental data on yeast prion domains allow to start at least partially decrypting the sequence requirements of prion formation. These experiments illustrate the need for intrinsically disordered sequence regions enriched with a particularly high proportion of glutamine and asparagine. Bioinformatic analysis suggests that these regions strike a balance between sufficient amyloid nucleation propensity on the one hand and disorder on the other, which ensures availability of the amyloid prone regions but entropically prevents unwanted nucleation and facilitates brittleness required for propagation.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://fsjd.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=18905
url https://fsjd.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=18905
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv TAYLOR & FRANCIS INC
publisher.none.fl_str_mv TAYLOR & FRANCIS INC
dc.source.none.fl_str_mv Prion
ISSN: 19336896
ISSNe: 1933690X
reponame:r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
instname:Fundació Sant Joan de Déu
instname_str Fundació Sant Joan de Déu
reponame_str r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
collection r-FSJD. Repositorio Institucional de Producción Científica de la Fundació Sant Joan de Déu
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,81155

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