Widespread Aggregation and Neurodegenerative Diseases Are Associated with Supersaturated Proteins
Prajwal Ciryam,Gian Gaetano Tartaglia,Richard I. Morimoto,Christopher M. Dobson,Michele Vendruscolo +4 more
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TLDR
This work identifies the proteins most vulnerable to aggregation as those whose cellular concentrations are high relative to their solubilities and finds that these supersaturated proteins represent a metastable subproteome involved in pathological aggregation during stress and aging and are overrepresented in biochemical processes associated with neurodegenerative disorders.About:
This article is published in Cell Reports.The article was published on 2013-11-14 and is currently open access. It has received 240 citations till now. The article focuses on the topics: Cellular homeostasis & Protein aggregation.read more
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The amyloid state and its association with protein misfolding diseases
TL;DR: The ability to form the amyloid state is more general than previously imagined, and its study can provide unique insights into the nature of the functional forms of peptides and proteins, as well as understanding the means by which protein homeostasis can be maintained and protein metastasis avoided.
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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
TL;DR: This review describes this field of science with particular reference to the advances that have been made over the last decade in understanding of its fundamental nature and consequences and shows evidence that a complex proteostasis network actively combats protein aggregation.
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In vivo aspects of protein folding and quality control
TL;DR: A new view of protein folding is emerging, whereby the energy landscapes that proteins navigate during folding in vivo may differ substantially from those observed during refolding in vitro.
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Erratum: The amyloid state and its association with protein misfolding diseases
TL;DR: The spacing between polypeptide chains along the fibril axis is constant to a good approximation even for very different polypeptic sequences, a generic property arising from the common inter-side chain hydrogen bonding constraints.
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The proteostasis network and its decline in ageing.
TL;DR: The possibilities of pharmacological augmentation of the capacity of proteostasis networks hold great promise for delaying the onset of age-related pathologies associated with proteome deterioration and for extending healthspan.
References
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TL;DR: The relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate is discussed and some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior is described.