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Solid-state NMR sequential assignments of α-synuclein

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Abstract

Parkinson’s disease is amongst the most frequent and most devastating neurodegenerative diseases. It is tightly associated with the assembly of proteins into high-molecular weight protein species, which propagate between neurons in the central nervous system. The principal protein involved in this process is α-synuclein which is a structural component of the Lewy bodies observed in diseased brain. We here present the solid-state NMR sequential assignments of a new fibrillar form of this protein, the first one with a well-ordered and rigid N-terminal part.

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Acknowledgments

This work was supported by the Agence Nationale de la Recherche (ANR-07-PCVI-0013-03, ANR-PCV08 321323 and ANR08-PCVI-0022-02), the ETH Zurich, the Swiss National Science Foundation (Grant 200020_124611), the Era-Net Neuron (project MIPROTRAN, ANR-08-NEUR-001-01) and the Centre National de la Recherche Scientifique. We also acknowledge support from the European Commission under the Seventh Framework Programme (FP7), contract Bio-NMR 261863.

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Authors and Affiliations

  1. Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland

    Julia Gath & Beat H. Meier

  2. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France

    Birgit Habenstein & Anja Böckmann

  3. Laboratoire d’Enzymologie et Biochimie Structurales, UPR 3082 CNRS, Avenue de la Terrasse, 91198, Gif-sur-Yvette, France

    Luc Bousset & Ronald Melki

Authors
  1. Julia Gath
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  2. Birgit Habenstein
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  3. Luc Bousset
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  4. Ronald Melki
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  5. Beat H. Meier
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  6. Anja Böckmann
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Corresponding authors

Correspondence to Ronald Melki, Beat H. Meier or Anja Böckmann.

Additional information

Julia Gath, Birgit Habenstein and Luc Bousset have contributed equally to this work.

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Gath, J., Habenstein, B., Bousset, L. et al. Solid-state NMR sequential assignments of α-synuclein. Biomol NMR Assign 6, 51–55 (2012). https://doi.org/10.1007/s12104-011-9324-3

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  • DOI: https://doi.org/10.1007/s12104-011-9324-3

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