MOAG-4 promotes the aggregation of &#945;-synuclein by competing with self-protective electrostatic interactions.

Yoshimura, Yuichi; Holmberg, Mats A; Kukic, Predrag; Andersen, Camilla B; Mata-Cabana, Alejandro; Falsone, S Fabio; Vendruscolo, Michele; Nollen, Ellen A A; Mulder, Frans A A

MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.

Yoshimura, Yuichi; Holmberg, Mats A; Kukic, Predrag; Andersen, Camilla B; Mata-Cabana, Alejandro; Falsone, S Fabio; Vendruscolo, Michele; Nollen, Ellen A A; Mulder, Frans A A.

Afiliação

Yoshimura Y; Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark.
Holmberg MA; University of Groningen, University Medical Centre Groningen, European Research Institute for the Biology of Aging, 9700 AD Groningen, The Netherlands.
Kukic P; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Andersen CB; Interdisciplinary Nanoscience Center (iNANO) and Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark.
Mata-Cabana A; University of Groningen, University Medical Centre Groningen, European Research Institute for the Biology of Aging, 9700 AD Groningen, The Netherlands.
Falsone SF; Institute of Pharmaceutical Sciences, University of Graz, Schubertstr. 1, 8010 Graz, Austria.
Vendruscolo M; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Nollen EAA; University of Groningen, University Medical Centre Groningen, European Research Institute for the Biology of Aging, 9700 AD Groningen, The Netherlands.
Mulder FAA; Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark. Electronic address: fmulder@chem.au.dk.

J Biol Chem ; 292(20): 8269-8278, 2017 05 19.

Article em En | MEDLINE | ID: mdl-28336532

Assuntos

Proteínas de Caenorhabditis elegans/química; Caenorhabditis elegans/química; Proteínas do Tecido Nervoso/química; Agregados Proteicos; alfa-Sinucleína/química; Doença de Alzheimer; Animais; Caenorhabditis elegans/genética; Caenorhabditis elegans/metabolismo; Proteínas de Caenorhabditis elegans/genética; Proteínas de Caenorhabditis elegans/metabolismo; Humanos; Proteínas do Tecido Nervoso/genética; Proteínas do Tecido Nervoso/metabolismo; Doença de Parkinson; Eletricidade Estática; alfa-Sinucleína/genética; alfa-Sinucleína/metabolismo

Palavras-chave

neurodegenerative disease; nuclear magnetic resonance (NMR); protein aggregation; protein structure; α-synuclein (α-synuclein)

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Caenorhabditis elegans / Proteínas de Caenorhabditis elegans / Alfa-Sinucleína / Agregados Proteicos / Proteínas do Tecido Nervoso Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Dinamarca

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