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α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

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  • Tim Bartels

    (Center for Neurologic Diseases, Brigham and Women’s Hospital and Harvard Medical School)

  • Joanna G. Choi

    (Center for Neurologic Diseases, Brigham and Women’s Hospital and Harvard Medical School)

  • Dennis J. Selkoe

    (Center for Neurologic Diseases, Brigham and Women’s Hospital and Harvard Medical School)

Abstract

A new look at α-synuclein Pathogenic aggregation of α-synuclein (αSyn) is implicated in Parkinson's disease and related disorders. αSyn has long been regarded as a natively unfolded monomer that acquires secondary structure only when it binds to its target. This model is the basis for a number of published studies, but Bartels et al. report that endogenous αSyn isolated under entirely non-denaturing conditions from brain tissue, cell lines and living human cells occurs principally as a folded tetramer. This finding suggests that destabilization of the αSyn tetramer precedes misfolding and aggregation in synucleinopathies, and that agents that stabilize the normal tetramer may reduce αSyn pathogenicity.

Suggested Citation

  • Tim Bartels & Joanna G. Choi & Dennis J. Selkoe, 2011. "α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation," Nature, Nature, vol. 477(7362), pages 107-110, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7362:d:10.1038_nature10324
    DOI: 10.1038/nature10324
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    Cited by:

    1. Micaela Pivato & Giorgia De Franceschi & Laura Tosatto & Erica Frare & Dhruv Kumar & Daniel Aioanei & Marco Brucale & Isabella Tessari & Marco Bisaglia & Bruno Samori & Patrizia Polverino de Laureto &, 2012. "Covalent α-Synuclein Dimers: Chemico-Physical and Aggregation Properties," PLOS ONE, Public Library of Science, vol. 7(12), pages 1-14, December.
    2. Yemima R. Butler & Yuqing Liu & Ramhari Kumbhar & Peiran Zhao & Kundlik Gadhave & Ning Wang & Yanmei Li & Xiaobo Mao & Wenjing Wang, 2022. "α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Vanessa C Ducas & Elizabeth Rhoades, 2014. "Investigation of Intramolecular Dynamics and Conformations of α-, β- and γ-Synuclein," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-10, January.

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