Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies

Autores
Cehlar, Ondrej; Njemoga, Stefana; Horvath, Marian; Cizmazia, Erik; Bednarikova, Zuzana; Barrera Guisasola, Exequiel Ernesto
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this review, we focus on the biophysical and structural aspects of the oligomeric states of physiologically intrinsically disordered proteins and peptides tau, amyloid-β and α-synuclein and partly disordered prion protein and their isolations from animal models and human brains. These protein states may be the most toxic agents in the pathogenesis of Alzheimer’s and Parkinson’s disease. It was shown that oligomers are important players in the aggregation cascade of these proteins. The structural information about these structural states has been provided by methods such as solution and solid-state NMR, cryo-EM, crosslinking mass spectrometry, AFM, TEM, etc., as well as from hybrid structural biology approaches combining experiments with computational modelling and simulations. The reliable structural models of these protein states may provide valuable information for future drug design and therapies.
Fil: Cehlar, Ondrej. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Njemoga, Stefana. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Horvath, Marian. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Cizmazia, Erik. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Bednarikova, Zuzana. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Barrera Guisasola, Exequiel Ernesto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Materia
Oligomer
Amyloid-β
α-synuclein
tau protein
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/263430
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/263430
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and PrionopathiesCehlar, OndrejNjemoga, StefanaHorvath, MarianCizmazia, ErikBednarikova, ZuzanaBarrera Guisasola, Exequiel ErnestoOligomerAmyloid-βα-synucleintau proteinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In this review, we focus on the biophysical and structural aspects of the oligomeric states of physiologically intrinsically disordered proteins and peptides tau, amyloid-β and α-synuclein and partly disordered prion protein and their isolations from animal models and human brains. These protein states may be the most toxic agents in the pathogenesis of Alzheimer’s and Parkinson’s disease. It was shown that oligomers are important players in the aggregation cascade of these proteins. The structural information about these structural states has been provided by methods such as solution and solid-state NMR, cryo-EM, crosslinking mass spectrometry, AFM, TEM, etc., as well as from hybrid structural biology approaches combining experiments with computational modelling and simulations. The reliable structural models of these protein states may provide valuable information for future drug design and therapies.Fil: Cehlar, Ondrej. Slovak Academy of Sciences. Institute of Botany; EslovaquiaFil: Njemoga, Stefana. Slovak Academy of Sciences. Institute of Botany; EslovaquiaFil: Horvath, Marian. Slovak Academy of Sciences. Institute of Botany; EslovaquiaFil: Cizmazia, Erik. Slovak Academy of Sciences. Institute of Botany; EslovaquiaFil: Bednarikova, Zuzana. Slovak Academy of Sciences. Institute of Botany; EslovaquiaFil: Barrera Guisasola, Exequiel Ernesto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaMolecular Diversity Preservation International2024-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/263430Cehlar, Ondrej; Njemoga, Stefana; Horvath, Marian; Cizmazia, Erik; Bednarikova, Zuzana; et al.; Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 25; 23; 12-2024; 1-311422-0067CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/25/23/13049info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms252313049info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:10:52Zoai:ri.conicet.gov.ar:11336/263430instacron: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 10:10:52.396CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
title Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
spellingShingle Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
Cehlar, Ondrej
Oligomer
Amyloid-β
α-synuclein
tau protein
title_short Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
title_full Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
title_fullStr Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
title_full_unstemmed Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
title_sort Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies
dc.creator.none.fl_str_mv Cehlar, Ondrej
Njemoga, Stefana
Horvath, Marian
Cizmazia, Erik
Bednarikova, Zuzana
Barrera Guisasola, Exequiel Ernesto
author Cehlar, Ondrej
author_facet Cehlar, Ondrej
Njemoga, Stefana
Horvath, Marian
Cizmazia, Erik
Bednarikova, Zuzana
Barrera Guisasola, Exequiel Ernesto
author_role author
author2 Njemoga, Stefana
Horvath, Marian
Cizmazia, Erik
Bednarikova, Zuzana
Barrera Guisasola, Exequiel Ernesto
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Oligomer
Amyloid-β
α-synuclein
tau protein
topic Oligomer
Amyloid-β
α-synuclein
tau protein
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In this review, we focus on the biophysical and structural aspects of the oligomeric states of physiologically intrinsically disordered proteins and peptides tau, amyloid-β and α-synuclein and partly disordered prion protein and their isolations from animal models and human brains. These protein states may be the most toxic agents in the pathogenesis of Alzheimer’s and Parkinson’s disease. It was shown that oligomers are important players in the aggregation cascade of these proteins. The structural information about these structural states has been provided by methods such as solution and solid-state NMR, cryo-EM, crosslinking mass spectrometry, AFM, TEM, etc., as well as from hybrid structural biology approaches combining experiments with computational modelling and simulations. The reliable structural models of these protein states may provide valuable information for future drug design and therapies.
Fil: Cehlar, Ondrej. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Njemoga, Stefana. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Horvath, Marian. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Cizmazia, Erik. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Bednarikova, Zuzana. Slovak Academy of Sciences. Institute of Botany; Eslovaquia
Fil: Barrera Guisasola, Exequiel Ernesto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
description In this review, we focus on the biophysical and structural aspects of the oligomeric states of physiologically intrinsically disordered proteins and peptides tau, amyloid-β and α-synuclein and partly disordered prion protein and their isolations from animal models and human brains. These protein states may be the most toxic agents in the pathogenesis of Alzheimer’s and Parkinson’s disease. It was shown that oligomers are important players in the aggregation cascade of these proteins. The structural information about these structural states has been provided by methods such as solution and solid-state NMR, cryo-EM, crosslinking mass spectrometry, AFM, TEM, etc., as well as from hybrid structural biology approaches combining experiments with computational modelling and simulations. The reliable structural models of these protein states may provide valuable information for future drug design and therapies.
publishDate 2024
dc.date.none.fl_str_mv 2024-12
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/11336/263430
Cehlar, Ondrej; Njemoga, Stefana; Horvath, Marian; Cizmazia, Erik; Bednarikova, Zuzana; et al.; Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 25; 23; 12-2024; 1-31
1422-0067
CONICET Digital
CONICET
url http://hdl.handle.net/11336/263430
identifier_str_mv Cehlar, Ondrej; Njemoga, Stefana; Horvath, Marian; Cizmazia, Erik; Bednarikova, Zuzana; et al.; Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies; Molecular Diversity Preservation International; International Journal of Molecular Sciences; 25; 23; 12-2024; 1-31
1422-0067
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1422-0067/25/23/13049
info:eu-repo/semantics/altIdentifier/doi/10.3390/ijms252313049
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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
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score 13.070432

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