Highly read on http://www.cell.com in January 2011

Neurodegenerative disorders such as Parkinson's disease are marked by the presence of toxic protein aggregates in brain cells. These aggregates seem to ensnare a range of proteins that share certain biochemical features and are involved in important cellular processes.

Martin Vabulas at the Max Planck Institute of Biochemistry in Martinsried, Germany, and his colleagues designed artificial β-sheet proteins that form clumps similar to the amyloid fibrils seen in several neurodegenerative diseases. They expressed the proteins in human cells and analysed the native proteins that bound to the aggregates. The researchers found that various proteins involved in RNA processing, protein production and other key functions were caught up in the aggregates: in a few cases, the entangled proportion was as high as 45%. These proteins tended to be larger in size and have more unstructured regions than their non-sequestered counterparts. Moreover, the proteins interact with hundreds of other essential proteins.

Cell 144, 67–78 (2011)