Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein

Autores
Esteban Martin, Santiago; Silvestre Ryan, Jordi; Bertoncini, Carlos Walter; Salvatella, Xavier
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Structural conversion of the presynaptic, intrinsically disordered protein α-synuclein into amyloid fibrils underlies neurotoxicity in Parkinson's disease. The detailed mechanism by which this conversion occurs is largely unknown. Here, we identify a discrete pattern of transient tertiary interactions in monomeric α-synuclein involving amino acid residues that are, in the fibrillar state, part of β-strands. Importantly, this pattern of pairwise interactions does not correspond to that found in the amyloid state. A redistribution of this network of fibril-like contacts must precede aggregation into the amyloid structure.
Fil: Esteban Martin, Santiago. Barcelona Supercomputing Center. Research Programme in Computational Biology; España
Fil: Silvestre Ryan, Jordi. Institute for Research in Biomedicine. Research Programme in Computational Biology; España
Fil: Bertoncini, Carlos Walter. Institute for Research in Biomedicine. Research Programme in Computational Biology; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Salvatella, Xavier. Institute for Research in Biomedicine. Research Programme in Computational Biology; España. Institució Catalana de Recerca i Estudis Avançats; España
Materia
Proteínas Intrínsecamente Desordenadas
Biología Estructural
Resonancia Magnética Nuclear
Proteínas Amiloides
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/4833
Acceder
id CONICETDig_84f64e6f1ae7f4d9e1e02fe63a335d62
oai_identifier_str oai:ri.conicet.gov.ar:11336/4833
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Identification of fibril-like tertiary contacts in soluble monomeric α-synucleinEsteban Martin, SantiagoSilvestre Ryan, JordiBertoncini, Carlos WalterSalvatella, XavierProteínas Intrínsecamente DesordenadasBiología EstructuralResonancia Magnética NuclearProteínas Amiloideshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Structural conversion of the presynaptic, intrinsically disordered protein α-synuclein into amyloid fibrils underlies neurotoxicity in Parkinson's disease. The detailed mechanism by which this conversion occurs is largely unknown. Here, we identify a discrete pattern of transient tertiary interactions in monomeric α-synuclein involving amino acid residues that are, in the fibrillar state, part of β-strands. Importantly, this pattern of pairwise interactions does not correspond to that found in the amyloid state. A redistribution of this network of fibril-like contacts must precede aggregation into the amyloid structure.Fil: Esteban Martin, Santiago. Barcelona Supercomputing Center. Research Programme in Computational Biology; EspañaFil: Silvestre Ryan, Jordi. Institute for Research in Biomedicine. Research Programme in Computational Biology; EspañaFil: Bertoncini, Carlos Walter. Institute for Research in Biomedicine. Research Programme in Computational Biology; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Salvatella, Xavier. Institute for Research in Biomedicine. Research Programme in Computational Biology; España. Institució Catalana de Recerca i Estudis Avançats; EspañaElsevier2013-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4833Esteban Martin, Santiago; Silvestre Ryan, Jordi; Bertoncini, Carlos Walter; Salvatella, Xavier; Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein; Elsevier; Biophysical Journal; 105; 5; 9-2013; 1192-11980006-3495enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006349513008667info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2013.07.044info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/pmid/PMC3762368info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3762368/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:05:51Zoai:ri.conicet.gov.ar:11336/4833instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:05:51.934CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
title Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
spellingShingle Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
Esteban Martin, Santiago
Proteínas Intrínsecamente Desordenadas
Biología Estructural
Resonancia Magnética Nuclear
Proteínas Amiloides
title_short Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
title_full Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
title_fullStr Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
title_full_unstemmed Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
title_sort Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein
dc.creator.none.fl_str_mv Esteban Martin, Santiago
Silvestre Ryan, Jordi
Bertoncini, Carlos Walter
Salvatella, Xavier
author Esteban Martin, Santiago
author_facet Esteban Martin, Santiago
Silvestre Ryan, Jordi
Bertoncini, Carlos Walter
Salvatella, Xavier
author_role author
author2 Silvestre Ryan, Jordi
Bertoncini, Carlos Walter
Salvatella, Xavier
author2_role author
author
author
dc.subject.none.fl_str_mv Proteínas Intrínsecamente Desordenadas
Biología Estructural
Resonancia Magnética Nuclear
Proteínas Amiloides
topic Proteínas Intrínsecamente Desordenadas
Biología Estructural
Resonancia Magnética Nuclear
Proteínas Amiloides
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Structural conversion of the presynaptic, intrinsically disordered protein α-synuclein into amyloid fibrils underlies neurotoxicity in Parkinson's disease. The detailed mechanism by which this conversion occurs is largely unknown. Here, we identify a discrete pattern of transient tertiary interactions in monomeric α-synuclein involving amino acid residues that are, in the fibrillar state, part of β-strands. Importantly, this pattern of pairwise interactions does not correspond to that found in the amyloid state. A redistribution of this network of fibril-like contacts must precede aggregation into the amyloid structure.
Fil: Esteban Martin, Santiago. Barcelona Supercomputing Center. Research Programme in Computational Biology; España
Fil: Silvestre Ryan, Jordi. Institute for Research in Biomedicine. Research Programme in Computational Biology; España
Fil: Bertoncini, Carlos Walter. Institute for Research in Biomedicine. Research Programme in Computational Biology; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Salvatella, Xavier. Institute for Research in Biomedicine. Research Programme in Computational Biology; España. Institució Catalana de Recerca i Estudis Avançats; España
description Structural conversion of the presynaptic, intrinsically disordered protein α-synuclein into amyloid fibrils underlies neurotoxicity in Parkinson's disease. The detailed mechanism by which this conversion occurs is largely unknown. Here, we identify a discrete pattern of transient tertiary interactions in monomeric α-synuclein involving amino acid residues that are, in the fibrillar state, part of β-strands. Importantly, this pattern of pairwise interactions does not correspond to that found in the amyloid state. A redistribution of this network of fibril-like contacts must precede aggregation into the amyloid structure.
publishDate 2013
dc.date.none.fl_str_mv 2013-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/4833
Esteban Martin, Santiago; Silvestre Ryan, Jordi; Bertoncini, Carlos Walter; Salvatella, Xavier; Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein; Elsevier; Biophysical Journal; 105; 5; 9-2013; 1192-1198
0006-3495
url http://hdl.handle.net/11336/4833
identifier_str_mv Esteban Martin, Santiago; Silvestre Ryan, Jordi; Bertoncini, Carlos Walter; Salvatella, Xavier; Identification of fibril-like tertiary contacts in soluble monomeric α-synuclein; Elsevier; Biophysical Journal; 105; 5; 9-2013; 1192-1198
0006-3495
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006349513008667
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2013.07.044
info:eu-repo/semantics/altIdentifier/doi/
info:eu-repo/semantics/altIdentifier/pmid/PMC3762368
info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3762368/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613899830165504
score 13.070432

Publicaciones similares