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• W2156644003 abstract "Noting that the glutamine (Q) amino acid side-chain bears a striking resemblance to urea, the chemical denaturant, we argue on biophysical grounds that polyQ chains should possess a potent denaturant activity. Using live-cell confocal microscopy, we demonstrate that the surface of a polyQ inclusion denatures cytosolic proteins by binding and trapping them in an immobilized ring. We also show the reverse effect: that elevated local concentrations of unfolded protein in the cytosol can drive the co-localization and accumulation of short polyQ tracts that normally do not aggregate. Such a urea-like mechanism explains many past observations about polyQ-driven disruption of proteostasis and neurodegeneration." @default.
• W2156644003 created "2016-06-24" @default.
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• W2156644003 creator A5033916915 @default.
• W2156644003 date "2010-12-19" @default.
• W2156644003 modified "2023-10-10" @default.
• W2156644003 title "Polyglutamine shows a urea-like affinity for unfolded cytosolic protein" @default.
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• W2156644003 doi "https://doi.org/10.1016/j.febslet.2010.12.023" @default.
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