Monthly Archives: February 2015

Sequence composition of disordered regions fine-tunes protein half-life

The proteasome controls the concentrations of most proteins in eukaryotic cells. It recognizes its protein substrates through ubiquitin tags and initiates degradation at disordered regions within the substrate. Here we show that the proteasome has pronounced preferences for the amino … Continue reading

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Proteome response at the edge of protein aggregation

Proteins adopt defined structures and are crucial to most cellular functions. Their misfolding and aggregation is associated with numerous degenerative human disorders such as type II diabetes, Huntington’s or Alzheimer’s diseases. Here, we aim to understand why cells promote the … Continue reading

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