Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface

In patients with sporadic Alzheimer’s disease part of the Asp23 residues are isomerized to L-isoaspartate (L-isoAsp23). Here the authors present the MicroED structures of wild-type and L-isoAsp23 Aβ 20–34 amyloid fibrils that both form tightly packed cores and self-associate through two distinct int...

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Autores principales:	Rebeccah A. Warmack, David R. Boyer, Chih-Te Zee, Logan S. Richards, Michael R. Sawaya, Duilio Cascio, Tamir Gonen, David S. Eisenberg, Steven G. Clarke
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/13816496598043ba832e0e479cc32bd3
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spelling	oai:doaj.org-article:13816496598043ba832e0e479cc32bd32021-12-02T14:38:46ZStructure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface10.1038/s41467-019-11183-z2041-1723https://doaj.org/article/13816496598043ba832e0e479cc32bd32019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11183-zhttps://doaj.org/toc/2041-1723In patients with sporadic Alzheimer’s disease part of the Asp23 residues are isomerized to L-isoaspartate (L-isoAsp23). Here the authors present the MicroED structures of wild-type and L-isoAsp23 Aβ 20–34 amyloid fibrils that both form tightly packed cores and self-associate through two distinct interfaces with one of these interfaces being strengthened by the isoaspartyl modification.Rebeccah A. WarmackDavid R. BoyerChih-Te ZeeLogan S. RichardsMichael R. SawayaDuilio CascioTamir GonenDavid S. EisenbergSteven G. ClarkeNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Rebeccah A. Warmack David R. Boyer Chih-Te Zee Logan S. Richards Michael R. Sawaya Duilio Cascio Tamir Gonen David S. Eisenberg Steven G. Clarke Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
description	In patients with sporadic Alzheimer’s disease part of the Asp23 residues are isomerized to L-isoaspartate (L-isoAsp23). Here the authors present the MicroED structures of wild-type and L-isoAsp23 Aβ 20–34 amyloid fibrils that both form tightly packed cores and self-associate through two distinct interfaces with one of these interfaces being strengthened by the isoaspartyl modification.
format	article
author	Rebeccah A. Warmack David R. Boyer Chih-Te Zee Logan S. Richards Michael R. Sawaya Duilio Cascio Tamir Gonen David S. Eisenberg Steven G. Clarke
author_facet	Rebeccah A. Warmack David R. Boyer Chih-Te Zee Logan S. Richards Michael R. Sawaya Duilio Cascio Tamir Gonen David S. Eisenberg Steven G. Clarke
author_sort	Rebeccah A. Warmack
title	Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
title_short	Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
title_full	Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
title_fullStr	Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
title_full_unstemmed	Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface
title_sort	structure of amyloid-β (20-34) with alzheimer’s-associated isomerization at asp23 reveals a distinct protofilament interface
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/13816496598043ba832e0e479cc32bd3
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Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface

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