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- W2130233701 abstract "Protein aggregation is related to many human disorders and constitutes a major bottleneck in protein production. However, little is known about the conformational properties of in vivo formed aggregates and how they relate to the specific polypeptides embedded in them. Here, we show that the kinetic and thermodynamic stability of the inclusion bodies formed by the Aβ42 Alzheimer peptide and its Asp19 alloform differ significantly and correlate with their amyloidogenic propensity and solubility inside the cell. Our results indicate that the nature of the polypeptide chain determines the specific conformational properties of intracellular aggregates. This implies that different protein inclusions impose dissimilar challenges to the cellular quality-control machinery." @default.
- W2130233701 created "2016-06-24" @default.
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- W2130233701 date "2008-10-07" @default.
- W2130233701 modified "2023-10-15" @default.
- W2130233701 title "Kinetic and thermodynamic stability of bacterial intracellular aggregates" @default.
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- W2130233701 doi "https://doi.org/10.1016/j.febslet.2008.09.049" @default.
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