Journal ArticleDOI
Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
TLDR
The molecular mechanism of prion conversion has a striking resemblance to the process of amyloid formation, suggesting that misfolded aggregates have an inherent ability to be transmissible.About:
This article is published in Trends in Biochemical Sciences.The article was published on 2006-03-01. It has received 259 citations till now. The article focuses on the topics: Protein aggregation & Amyloid.read more
Citations
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Journal ArticleDOI
Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
Claudio Soto,Sandra Pritzkow +1 more
TL;DR: A critical discussion of the role of protein misfolding and aggregation in NDs is provided, in addition to evidence supporting the hypothesis that misfolded aggregates can be transmissible by the prion principle.
Journal ArticleDOI
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders.
Mathias Jucker,Lary C. Walker +1 more
TL;DR: The theory that many chronic neurodegenerative diseases can originate and progress via the seeded corruption of misfolded proteins has the potential to unify experimental and translational approaches to these increasingly prevalent disorders.
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Adaptation: from single cells to BOLD signals
TL;DR: It is found that f MRIa provides novel insight into neural representations in the human brain, however, network responses in general and adaptation in particular are more complex than is often assumed, and an unequivocal interpretation of fMRIa results can be achieved only with great care.
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Prions: Protein Aggregation and Infectious Diseases
TL;DR: The evolution of the prion concept and how prion-like mechanisms may apply to other protein aggregation diseases are discussed and potential antiprion therapies and current developments in the realm of prion diagnostics are discussed.
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The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease.
TL;DR: Evidence is presented that links Aβ oligomers to pathogenesis in animal models and humans, with reference to seminal discoveries from cell biology and new ideas concerning pathogenic mechanisms, including relationships to diabetes and Fragile X.
References
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Journal ArticleDOI
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.
Monica Bucciantini,Elisa Giannoni,Fabrizio Chiti,Fabrizio Chiti,Fabiana Baroni,Lucia Formigli,Jesús Zurdo,Niccolò Taddei,Giampietro Ramponi,Christopher M. Dobson,Massimo Stefani +10 more
TL;DR: This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases.
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Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
TL;DR: It is proposed that this step is mechanistically relevant to amyloid formation in human prion disease and in AD; it is the formation of an ordered nucleus, which is the defining characteristic of a nucleation-dependent polymerization.
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Mice devoid of PrP are resistant to scrapie
Hansruedi Büeler,Adriano Aguzzi,Andreas W. Sailer,R.-A. Greiner,P. Autenried,Michel Aguet,Charles Weissmann +6 more
TL;DR: These experiments show that PrPC, possibly at close to normal levels, is required for the usual susceptibility to scrapie and that lack of homology between incoming prions and the host's PrP genes retards disease.
Journal ArticleDOI
Protein misfolding, evolution and disease
TL;DR: This paper is a contribution from the Oxford Centre for Molecular Sciences, which is funded by the BBSRC, EPSRC and MRC.