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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31 January 2020

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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

2

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31 January 2020

Uwe Fink

3

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31 January 2020

Muralidar Dasari

4

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31 January 2020

Marcus Fändrich

5

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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

cites work

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Spatial persistence of angular correlations in amyloid fibrils.

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Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction

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Amyloid-a state in many guises: survival of the fittest fibril fold

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Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

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Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host

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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.

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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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A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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

21 January 2018

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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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Unique identification of supramolecular structures in amyloid fibrils by solid-state NMR spectroscopy

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

21 January 2018

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Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR

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Structural complexity of a composite amyloid fibril

21 January 2018

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Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

21 January 2018

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Supramolecular interactions probed by 13C-13C solid-state NMR spectroscopy

21 January 2018

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Proton-detected solid-state NMR spectroscopy of fibrillar and membrane proteins.

21 January 2018

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Structure calculation from unambiguous long-range amide and methyl 1H-1H distance restraints for a microcrystalline protein with MAS solid-state NMR spectroscopy

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High resolution 1H-detected solid-state NMR spectroscopy of protein aliphatic resonances: access to tertiary structure information

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Polymorphism in an Amyloid‐Like Fibril‐Forming Model Peptide

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Determination of Secondary Structure Populations in Disordered States of Proteins Using Nuclear Magnetic Resonance Chemical Shifts

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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

21 January 2018

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21 January 2018

Identifiers

DOI

10.1002/ANIE.201200965

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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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