ArticleBiophysical journal2011
A model of threshold behavior reveals rescue mechanisms of bystander proteins in conformational diseases.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Development, growth and maintenance of β-cell mass: models are also part of the story.Molecular aspects of medicine · 2015Review
- Inferring the Effects of Honokiol on the Notch Signaling Pathway in SW480 Colon Cancer Cells.Cancer informatics · 2014Article
- Surveying the floodgates: estimating protein flux into the endoplasmic reticulum lumen in Saccharomyces cerevisiae.Frontiers in physiology · 2014Article
- Dominant protein interactions that influence the pathogenesis of conformational diseases.The Journal of clinical investigation · 2013Article
- Article
- Cellular strategies for regulating functional and nonfunctional protein aggregation.Cell reports · 2012Article
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2 authors.
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Abstract
Conformational diseases result from the failure of a specific protein to fold into its correct functional state. The misfolded proteins can lead to the toxic aggregation of proteins. Protein misfolding in conformational diseases often displays a threshold behavior characterized by a sudden shift between nontoxic to toxic levels of misfolded proteins. In some conformational diseases, evidence suggests that misfolded proteins interact with bystander proteins (unfolded and native folded proteins), eliciting a misfolded phenotype. These bystander isomers would follow their normal physiological pathways in absence of misfolded proteins. In this article, we present a general mechanism of bystander and misfolded protein interaction which we have used to investigate how the threshold behavior in protein misfolding is triggered in conformational diseases. Using a continuous flow reactor model of the endoplasmic reticulum, we found that slight changes in the bystander protein residence time in the endoplasmic reticulum or the ratio of basal misfolded to bystander protein inflow rates can trigger the threshold behavior in protein misfolding. Our analysis reveals three mechanisms to rescue bystander proteins in conformational diseases. The results of our model can now help direct experiments to understand the threshold behavior and develop therapeutic strategies targeting the modulation of conformational diseases.
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