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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/263430
Ver los metadatos del registro completo
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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 Técnicas2025-09-03T10:00:01Zoai: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:34982025-09-03 10:00:01.907CONICET 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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1842269615442362368 |
score |
13.13397 |