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Amyloidogenesis

FlAsH illuminates Aβ aggregation

Nature Chemical Biology volume 7, pages 581–582 (2011)Cite this article

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Protein misfolding, oligomerization and aggregation are implicated in a variety of neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. New research sheds light on the process of amyloid-β aggregation in vitro, identifying nucleated conformational conversion of oligomers as the mechanism for generating amyloid fibrils.

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Figure 1: Amyloid-β aggregation through nucleated conformational conversion.

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Authors and Affiliations

  1. and the Department of Neurodegeneration and Restorative Research, Tiago F. Outeiro is in the Cell and Molecular Neuroscience Unit at the Instituto de Medicina Molecular and the Instituto de Fisiologia in the Faculdade de Medicina da Universidade de Lisboa in Lisboa, Portugal, Center for Molecular Physiology of the Brain, Universitätsmedizin Göttingen, Göttingen, Germany.,

    Tiago F Outeiro

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  1. Tiago F Outeiro
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Correspondence to Tiago F Outeiro.

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The author declares no competing financial interests.

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Outeiro, T. FlAsH illuminates Aβ aggregation. Nat Chem Biol 7, 581–582 (2011). https://doi.org/10.1038/nchembio.636

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