Phosphorylation modifies the molecular stability of β-amyloid deposits

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...

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Main Authors: Nasrollah Rezaei-Ghaleh, Mehriar Amininasab, Sathish Kumar, Jochen Walter, Markus Zweckstetter
Format: Article
Language:English
Published: Nature Publishing Group 2016-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms11359
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spelling doaj-b51e7f2b30e242a2be7281a13feadd102021-05-11T10:54:42ZengNature Publishing GroupNature Communications2041-17232016-04-01711910.1038/ncomms11359Phosphorylation modifies the molecular stability of β-amyloid depositsNasrollah Rezaei-Ghaleh0Mehriar Amininasab1Sathish Kumar2Jochen Walter3Markus Zweckstetter4German Center for Neurodegenerative Diseases (DZNE)Department of Cell and Molecular Biology, School of Biology, College of Science, University of TehranDepartment of Neurology, University of BonnDepartment of Neurology, University of BonnGerman Center for Neurodegenerative Diseases (DZNE)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.https://doi.org/10.1038/ncomms11359
collection DOAJ
language English
format Article
sources DOAJ
author Nasrollah Rezaei-Ghaleh
Mehriar Amininasab
Sathish Kumar
Jochen Walter
Markus Zweckstetter
spellingShingle Nasrollah Rezaei-Ghaleh
Mehriar Amininasab
Sathish Kumar
Jochen Walter
Markus Zweckstetter
Phosphorylation modifies the molecular stability of β-amyloid deposits
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2016-04-01
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.
url https://doi.org/10.1038/ncomms11359
work_keys_str_mv AT nasrollahrezaeighaleh phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT mehriaramininasab phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT sathishkumar phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT jochenwalter phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
AT markuszweckstetter phosphorylationmodifiesthemolecularstabilityofbamyloiddeposits
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