CPP reveals structural changes in the proteome in Alzheimer disease

Neurodegenerative diseases are characterized by an accumulation of misfolded proteins. Cells normally recognize misfolded proteins and attempt to refold or to pass them on for proteasomal degradation. Chaperone proteins are central to recognizing and in refolding client proteins. When chaperone proteins fail to fulfill this function, conformationally altered proteins accumulate and can cause cell death.

High-throughput methods for phosphotyrosine signaling

The need for scalable methods for functional annotation of phosphotyrosine sites has led the Olsen group, Novo Nordisk Foundation Center for Protein Research in Copenhagen, to develop a new mass spectrometry-based workflow for high-throughput analyses. In a recent study, they implemented this new workflow used to describe how cancer mutations close to tyrosine phosphorylation sites in the EGF receptor rewire signaling pathways by switching protein interactors.