Phosphorylation modifies the molecular stability of β-amyloid deposits

Protein aggregation plays a crucial role in several neurodegenerative diseases. Here the authors demonstrate that phosphorylation of β-amyloid aggregates—the pathological hallmark of Alzheimer's disease—can change the molecular properties of aggregates, suggesting how phosphorylation contribute...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Nasrollah Rezaei-Ghaleh, Mehriar Amininasab, Sathish Kumar, Jochen Walter, Markus Zweckstetter
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
Materias:
Q
Acceso en línea:https://doaj.org/article/b51e7f2b30e242a2be7281a13feadd10
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:b51e7f2b30e242a2be7281a13feadd10
record_format dspace
spelling oai:doaj.org-article:b51e7f2b30e242a2be7281a13feadd102021-12-02T17:32:06ZPhosphorylation modifies the molecular stability of β-amyloid deposits10.1038/ncomms113592041-1723https://doaj.org/article/b51e7f2b30e242a2be7281a13feadd102016-04-01T00:00:00Zhttps://doi.org/10.1038/ncomms11359https://doaj.org/toc/2041-1723Protein aggregation plays a crucial role in several neurodegenerative diseases. Here the authors demonstrate that phosphorylation of β-amyloid aggregates—the pathological hallmark of Alzheimer's disease—can change the molecular properties of aggregates, suggesting how phosphorylation contributes to disease progression.Nasrollah Rezaei-GhalehMehriar AmininasabSathish KumarJochen WalterMarkus ZweckstetterNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Nasrollah Rezaei-Ghaleh
Mehriar Amininasab
Sathish Kumar
Jochen Walter
Markus Zweckstetter
Phosphorylation modifies the molecular stability of β-amyloid deposits
description Protein aggregation plays a crucial role in several neurodegenerative diseases. Here the authors demonstrate that phosphorylation of β-amyloid aggregates—the pathological hallmark of Alzheimer's disease—can change the molecular properties of aggregates, suggesting how phosphorylation contributes to disease progression.
format article
author Nasrollah Rezaei-Ghaleh
Mehriar Amininasab
Sathish Kumar
Jochen Walter
Markus Zweckstetter
author_facet Nasrollah Rezaei-Ghaleh
Mehriar Amininasab
Sathish Kumar
Jochen Walter
Markus Zweckstetter
author_sort Nasrollah Rezaei-Ghaleh
title Phosphorylation modifies the molecular stability of β-amyloid deposits
title_short Phosphorylation modifies the molecular stability of β-amyloid deposits
title_full Phosphorylation modifies the molecular stability of β-amyloid deposits
title_fullStr Phosphorylation modifies the molecular stability of β-amyloid deposits
title_full_unstemmed Phosphorylation modifies the molecular stability of β-amyloid deposits
title_sort phosphorylation modifies the molecular stability of β-amyloid deposits
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/b51e7f2b30e242a2be7281a13feadd10
work_keys_str_mv AT nasrollahrezaeighaleh phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT mehriaramininasab phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT sathishkumar phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT jochenwalter phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT markuszweckstetter phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
_version_ 1718380391401783296