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dc.contributor.author
Villar Piqué, Anna
dc.contributor.author
Rossetti, Giulia
dc.contributor.author
Ventura, Salvador
dc.contributor.author
Carloni, Paolo
dc.contributor.author
Fernandez, Claudio Oscar
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dc.contributor.author
Outeiro, Tiago Fleming
dc.date.available
2018-06-28T13:56:21Z
dc.date.issued
2017-01
dc.identifier.citation
Villar Piqué, Anna; Rossetti, Giulia; Ventura, Salvador; Carloni, Paolo; Fernandez, Claudio Oscar; et al.; Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics; Taylor and Francis Inc.; Communicative and Integrative Biology; 10; 1; 1-2017; 1-4
dc.identifier.issn
1942-0889
dc.identifier.uri
http://hdl.handle.net/11336/50317
dc.description.abstract
Copper is one of the metals described to bind the Parkinson disease-related protein α-synuclein (aSyn), and to promote its aggregation. Although histidine at position 50 in the aSyn sequence is one of the most studied copper-anchoring sites, its precise role in copper binding and aSyn aggregation is still unclear. Previous studies suggested that this residue does not significantly affect copper-mediated aSyn aggregation. However, our findings showed that the aggregation of the pathological H50Q aSyn mutant is enhanced by copper hints otherwise. Despite the inexistence of a model for aSyn H50Q-copper complexation, we discuss possible mechanisms by which this metal contributes to the misfolding and self-assembly of this particular aSyn mutant. Considering the genetic association of the H50Q mutation with familial forms of Parkinson disease, and the fact that copper homeostasis is deregulated in this disorder, understanding the interplay between both factors will shed light into the molecular and cellular mechanisms triggering the development and spreading of the aSyn pathology.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Taylor and Francis Inc.
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Amyloid
dc.subject
Copper
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H50q Mutation
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Parkinson Disease
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Protein Aggregation
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Α-Synuclein
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Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Copper(II) and the pathological H50Q α-synuclein mutant: Environment meets genetics
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-06-26T22:23:22Z
dc.journal.volume
10
dc.journal.number
1
dc.journal.pagination
1-4
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Austin
dc.description.fil
Fil: Villar Piqué, Anna. University Medical Centre Gottingen; Alemania
dc.description.fil
Fil: Rossetti, Giulia. Institute for Advanced Simulation; Alemania. Westfalische Technische Hochschule Aachen University; Alemania. Julich Supercomputing Centre; Alemania
dc.description.fil
Fil: Ventura, Salvador. Universitat Autònoma de Barcelona; España
dc.description.fil
Fil: Carloni, Paolo. Institute for Advanced Simulation; Alemania
dc.description.fil
Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina. Max Planck Laboratory for Structural Biology; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones Para El Descubrimiento de Farmacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones Para El Descubrimiento de Farmacos de Rosario; Argentina
dc.description.fil
Fil: Outeiro, Tiago Fleming. University Medical Centre Gottingen; Alemania. Max Planck Institute for Experimental Medicine; Alemania
dc.journal.title
Communicative and Integrative Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1080/19420889.2016.1270484
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/19420889.2016.1270484
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