Structural Basis of β-Amyloid-Dependent Synaptic Dysfunctions

Authors

  • Dr. Christian Haupt,

    1. Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)
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    • These authors contributed equally to this work.

  • Dr. Jörg Leppert,

    1. Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)
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    • These authors contributed equally to this work.

  • Dr. Raik Rönicke,

    1. DZNE-Standort Magdeburg c/o Leibniz-Institute for Neurobiology, Brenneckestrasse 6, 39118 Magdeburg (Germany)
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    • These authors contributed equally to this work.

  • Dr. Jessica Meinhardt,

    1. Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)
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  • Dr. Jay K. Yadav,

    1. Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)
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  • Dr. Ramadurai Ramachandran,

    1. Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)
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  • Dr. Oliver Ohlenschläger,

    1. Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)
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  • Prof. Dr. Klaus G. Reymann,

    1. DZNE-Standort Magdeburg c/o Leibniz-Institute for Neurobiology, Brenneckestrasse 6, 39118 Magdeburg (Germany)
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  • Dr. Matthias Görlach,

    Corresponding author
    1. Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)
    • Leibniz Institute for Age Research, Fritz Lipmann Institute, Beutenbergstraße 11, 07745 Jena (Germany)
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  • Priv.-Doz. Dr. Marcus Fändrich

    Corresponding author
    1. Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)
    • Max Planck Research Unit for Enzymology of Protein Folding & MLU, Weinbergweg 22, 06120 Halle (Saale) (Germany)
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  • The authors thank K. Böhm for technical assistance. The Leibniz Institute for Age Research is financially supported by the State of Thuringia and the Federal Government of Germany. K.G.R. and M.F. are supported by the country Sachsen-Anhalt (Exzellenznetzwerk Biowissenschaften). M.F. was additionally supported by grants from the DFG (SFB 610) and the BMBF (BioFuture).

Abstract

original image

Learn about Alzheimer: The molecular conformation of a toxic β-amyloid oligomer structure was determined by NMR spectroscopy (see picture). The measurements show a N-terminal β strand that controls the partitioning between oligomer and protofibril formation. Targeting the N-terminus of the peptide neutralizes Aβ-dependent neuronal dysfunctions. The data have important implications for understanding the structural basis of Alzheimer's disease.

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