Protein folding, nucleation phenomena and delayed neurodegeneration in Alzheimer's disease

Fox, Nick, Harvey, Richard J and Rossor, Martin N 1996, Protein folding, nucleation phenomena and delayed neurodegeneration in Alzheimer's disease, Reviews in the neurosciences, vol. 7, no. 1, pp. 21-28, doi: 10.1515/REVNEURO.1996.7.1.21.


Title Protein folding, nucleation phenomena and delayed neurodegeneration in Alzheimer's disease
Author(s) Fox, Nick
Harvey, Richard JORCID iD for Harvey, Richard J orcid.org/0000-0001-7796-0059
Rossor, Martin N
Journal name Reviews in the neurosciences
Volume number 7
Issue number 1
Start page 21
End page 28
Total pages 8
Publisher Walter de Gruyter
Place of publication Berlin, Germany
Publication date 1996
ISSN 0334-1763
Keyword(s) Alzheimer's disease
Amyloid
Plaques
APP
Protein folding
Prion
Summary This hypothesis attempts to explain how Alzheimer's disease can be both sporadic and autosomal dominant with catastrophic neurodegeneration occurring after decades of normal function. The production of Aβ peptide, the subunit of amyloid plaques, from the ubiquitous amyloid precursor protein is discussed. Conformational changes are argued to be crucial to the formation of these amyloid plaques and to their neurotoxicity. Parallels are drawn with prion disease where similarly a normal cellular protein becomes pathogenic once a conformational change is induced. Post-mitotic neurons in the brain are susceptible to this destructive process which is initiated by nucleation phenomena and is then self propagating. An understanding of the conformational changes involved in plaque formation may open new therapeutic avenues in Alzheimer's disease.
Language eng
DOI 10.1515/REVNEURO.1996.7.1.21
Indigenous content off
Field of Research 1109 Neurosciences
1702 Cognitive Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2011, Walter de Gruyter GmbH & Co
Persistent URL http://hdl.handle.net/10536/DRO/DU:30128011

Document type: Journal Article
Collections: Faculty of Health
School of Medicine
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