An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils. (Q53328520)

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31 January 2020

title

An asymmetric dimer as the basic subunit in Alzheimer's disease amyloid β fibrils (English)

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6

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Juan Miguel López del Amo

31 January 2020

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author name string

Matthias Schmidt

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31 January 2020

Uwe Fink

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31 January 2020

Muralidar Dasari

4

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Marcus Fändrich

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language of work or name

English

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publication date

8 May 2012

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Angewandte Chemie International Edition

31 January 2020

published in

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volume

51

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issue

25

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page(s)

6136-6139

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The search for an amyloid solution

31 January 2020

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Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth

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3D structure of Alzheimer's amyloid-beta(1-42) fibrils

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Paired beta-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy

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Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures

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Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils.

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Structural polymorphism of Alzheimer Abeta and other amyloid fibrils

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Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide

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Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states

21 January 2018

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The recombinant amyloid-beta peptide Abeta1-42 aggregates faster and is more neurotoxic than synthetic Abeta1-42.

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Abeta(1-28) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution

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Assignment of PolyProline II conformation and analysis of sequence--structure relationship

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Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p.

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Is polyproline II helix the killer conformation? a raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme 1 1Edited by A. R. Fersht

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21 January 2018

Identifiers

DOI

10.1002/ANIE.201200965

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22565601%20AND%20SRC:MED&resulttype=core&format=json

31 January 2020

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