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Folding proteins in fatal ways

Author

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  • Dennis J. Selkoe

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

Abstract

Human diseases characterized by insoluble extracellular deposits of proteins have been recognized for almost two centuries. Such amyloidoses were once thought to represent arcane secondary phenomena of questionable pathogenic significance. But it is has now become clear that many different proteins can misfold and form extracellular or intracellular aggregates that initiate profound cellular dysfunction. Particularly challenging examples of such disorders occur in the post-mitotic environment of the neuron and include Alzheimer's and Parkinson's diseases. Understanding some of the principles of protein folding has helped to explain how such diseases arise, with attendant therapeutic insights.

Suggested Citation

  • Dennis J. Selkoe, 2003. "Folding proteins in fatal ways," Nature, Nature, vol. 426(6968), pages 900-904, December.
    • Handle: RePEc:nat:nature:v:426:y:2003:i:6968:d:10.1038_nature02264
    DOI: 10.1038/nature02264
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    Citations

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    Cited by:

    1. Mookyung Cheon & Iksoo Chang & Sandipan Mohanty & Leila M Luheshi & Christopher M Dobson & Michele Vendruscolo & Giorgio Favrin, 2007. "Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils," PLOS Computational Biology, Public Library of Science, vol. 3(9), pages 1-12, September.
    2. Wen-Ting Chu & Ji-Long Zhang & Qing-Chuan Zheng & Lin Chen & Hong-Xing Zhang, 2013. "Insights into the Folding and Unfolding Processes of Wild-Type and Mutated SH3 Domain by Molecular Dynamics and Replica Exchange Molecular Dynamics Simulations," PLOS ONE, Public Library of Science, vol. 8(5), pages 1-9, May.
    3. Etienne Maisonneuve & Adrien Ducret & Pierre Khoueiry & Sabrina Lignon & Sonia Longhi & Emmanuel Talla & Sam Dukan, 2009. "Rules Governing Selective Protein Carbonylation," PLOS ONE, Public Library of Science, vol. 4(10), pages 1-12, October.
    4. Noah S Bieler & Tuomas P J Knowles & Daan Frenkel & Robert Vácha, 2012. "Connecting Macroscopic Observables and Microscopic Assembly Events in Amyloid Formation Using Coarse Grained Simulations," PLOS Computational Biology, Public Library of Science, vol. 8(10), pages 1-10, October.
    5. Elodie Monsellier & Matteo Ramazzotti & Niccolò Taddei & Fabrizio Chiti, 2008. "Aggregation Propensity of the Human Proteome," PLOS Computational Biology, Public Library of Science, vol. 4(10), pages 1-9, October.
    6. Allen W Bryan Jr. & Matthew Menke & Lenore J Cowen & Susan L Lindquist & Bonnie Berger, 2009. "BETASCAN: Probable β-amyloids Identified by Pairwise Probabilistic Analysis," PLOS Computational Biology, Public Library of Science, vol. 5(3), pages 1-11, March.
    7. Carlos Família & Sarah R Dennison & Alexandre Quintas & David A Phoenix, 2015. "Prediction of Peptide and Protein Propensity for Amyloid Formation," PLOS ONE, Public Library of Science, vol. 10(8), pages 1-16, August.
    8. Stefan Auer & Filip Meersman & Christopher M Dobson & Michele Vendruscolo, 2008. "A Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric Aggregates," PLOS Computational Biology, Public Library of Science, vol. 4(11), pages 1-7, November.

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