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A century-old debate on protein aggregation and neurodegeneration enters the clinic

Nature volume 443, pages 774779 (19 October 2006) | Download Citation

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Abstract

The correlation between neurodegenerative disease and protein aggregation in the brain has long been recognized, but a causal relationship has not been unequivocally established, in part because a discrete pathogenic aggregate has not been identified. The complexity of these diseases and the dynamic nature of protein aggregation mean that, despite progress towards understanding aggregation, its relationship to disease is difficult to determine in the laboratory. Nevertheless, drug candidates that inhibit aggregation are now being tested in the clinic. These have the potential to slow the progression of Alzheimer's disease, Parkinson's disease and related disorders and could, if administered presymptomatically, drastically reduce the incidence of these diseases. The clinical trials could also settle the century-old debate about causality.

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Acknowledgements

P.T.L. thanks the National Institutes of Health for supporting his work in this area. H.A.L. thanks R. Luthi-Carter, P. Fraering and N. Zawia for reviewing the manuscript, and the Swiss National Science Foundation for supporting research in his laboratory.

Author information

Author notes

    • Peter T. Lansbury

    Department of Neurology, Harvard Medical School and Brigham and Women's Hospital, 65 Landsdowne Street, Cambridge, Massachusetts 02139, USA. Present address: Link Medicine, 790 Memorial Drive, Cambridge, Massachusetts 02139, USA.

Affiliations

  1. Laboratory of Molecular Neurobiology and Neuroproteomics, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland.

    • Hilal A. Lashuel

Authors

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  2. Search for Hilal A. Lashuel in:

Competing interests

P.L. is currently chief scientific officer of Link Medicine, and is also an equity holder. Link Medicine is developing therapeutic strategies for several neurodegenerative diseases that are aimed at the reduction of protein aggregation.

Corresponding author

Correspondence to Peter T. Lansbury.

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