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Nature 455, 1189-1190 (30 October 2008) | doi:10.1038/4551189a; Published online 29 October 2008
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Laboratory Manager / Principal Research Assistant
- Wellcome Trust Sanger Institute
- Hinxton, Cambridge, CB10 1SA, UK
Research Psychiatrist
- Scripps Research Institute
- La Jolla, CA
Structural biology: Serpins' mystery solved
James C. Whisstock1 & Stephen P. Bottomley1
Abstract
Polymers of misfolded proteins underlie many diseases, including major neurodegenerative disorders. Structural data on how such aggregates of serpin proteins form answer several outstanding questions.
Ever since Alois Alzheimer and his colleagues first described abnormal aggregates of the amyloid protein in the brain of a patient who died of a form of dementia now known as Alzheimer's disease, biochemists have been fascinated by the molecular events associated with such protein misfolding. They hope that understanding the molecular basis of protein misfolding will aid the development of drugs against not only Alzheimer's disease, but also a range of disorders caused by misfolded proteins.
- James C. Whisstock and Stephen P. Bottomley are in the NHMRC Program on Protease Systems Biology, Department of Biochemistry and Molecular Biology, and in the ARC Centre of Excellence in Structural and Functional Microbial Genomics, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia.
Email: james.whisstock@med.monash.edu.au
Email: steve.bottomley@med.monash.edu.au
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