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...

Full description

Saved in:

Bibliographic Details
Main Authors:	Nasrollah Rezaei-Ghaleh, Mehriar Amininasab, Sathish Kumar, Jochen Walter, Markus Zweckstetter
Format:	article
Language:	EN
Published:	Nature Portfolio 2016
Subjects:	Science Q
Online Access:	https://doaj.org/article/b51e7f2b30e242a2be7281a13feadd10
Tags:	Add Tag No Tags, Be the first to tag this record!

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

Phosphorylation modifies the molecular stability of β-amyloid deposits

Similar Items