Atomic resolution map of the soluble amyloid beta assembly toxic surfaces† †Electronic supplementary information (ESI) available: Methods, 15N-DEST profiles, and additional statistical analyses. See DOI: 10.1039/c9sc01331h

@article{Ahmed2019AtomicRM,
  title={Atomic resolution map of the soluble amyloid beta assembly toxic surfaces† †Electronic supplementary information (ESI) available: Methods, 15N-DEST profiles, and additional statistical analyses. See DOI: 10.1039/c9sc01331h},
  author={Rashik Ahmed and Michael Akcan and Adree Khondker and M. Rheinst{\"a}dter and J. C. Bozelli and R. Epand and V. Huynh and Ryan G Wylie and Stephen Boulton and Jinfeng Huang and C. Verschoor and G. Melacini},
  journal={Chemical Science},
  year={2019},
  volume={10},
  pages={6072 - 6082}
}
Atomic resolution map of the soluble amyloid beta assembly (Aβn) “toxic surfaces” that facilitate the early pathogenic events in Alzheimer's disease (AD). 
Self‐Assembly and Neurotoxicity of β‐Amyloid (21–40) Peptide Fragment: The Regulatory Role of GxxxG Motifs
TLDR
The results indicate that G33xxxG37 is the primary motif responsible for Aβ neurotoxicity, hence providing a direct structure–function correlation and Targeting this motif can be a promising strategy to prevent neuronal cell death associated with Alzheimer's and other related diseases, such as type II diabetes and Parkinson's. Expand
Enhanced self-assembly of the 7–12 sequence of amyloid-β peptide by tyrosine bromination
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TLDR
The molecular architecture of heteromerization between 4F and Aβ(M1-42) discovered in this study provides evidence towards the understanding of the role of apolipoproteins or their truncated fragments in exacerbating AD pathology. Expand
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TLDR
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TLDR
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Halogenation of the N‐Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid‐β Sequence 7–12
Abstract Here, we demonstrate that introduction of halogen atoms at the tyrosine 10 phenol ring of the DSGYEV sequence derived from the flexible amyloid‐β N‐terminus, promotes its self‐assembly inExpand
Molecular Mechanism for the Suppression of Alpha Synuclein Membrane Toxicity by an Unconventional Extracellular Chaperone.
TLDR
The findings suggest that the extracellular proteostasis network may regulate αS cell-to-cell transmission not only by reducing the populations of membrane-binding competent αS oligomers but possibly also by shielding the membrane interface from residual toxic species. Expand
Degradation of Alzheimer’s amyloid-β by a catalytically inactive insulin-degrading enzyme
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