Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …

In-cell structural biology aims at extracting structural information about proteins or nucleic
acids in their native, cellular environment. This emerging field holds great promise and is …

The deposition of highly ordered fibrillar-type aggregates into inclusion bodies is a hallmark
of neurodegenerative diseases such as Parkinson's disease. The high stability of such …

The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular
chaperones, which perform numerous cellular functions that affect almost all aspects of the …

Biomolecules are in constant motion. To understand how they function, and why
malfunctions can cause disease, it is necessary to describe their three-dimensional …

The 70-kDa heat shock proteins (HSP70s) are abundantly present in cancer, providing
malignant cells selective advantage by suppressing multiple apoptotic pathways, regulating …

Proteins undergoing liquid–liquid phase separation are being discovered at an increasing
rate. Since at the high concentrations present in the cell most proteins would be expected to …

Cellular redox homeostasis is precisely balanced by generation and elimination of reactive
oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and …

Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …

Stresses such as heat shock trigger the formation of protein aggregates and the induction of
a disaggregation system composed of molecular chaperones. Recent work reveals that …