Eukaryotic cells organize their intracellular components into organelles that can be
membrane-bound or membraneless. A large number of membraneless organelles, including …

Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …

Misfolding, aggregation, and aberrant accumulation of proteins are central components in
the progression of neurodegenerative disease. Cellular molecular chaperone systems …

The accumulation of amyloid Tau aggregates is implicated in Alzheimer's disease (AD) and
other tauopathies. Molecular chaperones are known to maintain protein homeostasis. Here …

Protein aggregates are formed in cells with profoundly perturbed proteostasis, where the
generation of misfolded proteins exceeds the cellular refolding and degradative capacity …

Hsp104 is a hexameric AAA+ ATPase and protein disaggregase found in yeast, which
couples ATP hydrolysis to the dissolution of diverse polypeptides trapped in toxic …

Alzheimer's disease and related disorders feature neurofibrillary tangles and other
neuropathological lesions composed of detergent-insoluble tau protein. In recent structural …

Liquid–liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs) and the
action of molecular chaperones are tightly connected. An important class of molecular …

Intrinsically disordered proteins (IDPs) do not have rigid 3D structures, showing changes in
their folding depending on the environment or ligands. Intrinsically disordered proteins are …

Angelman syndrome (AS) is a neurodevelopmental disorder caused by the loss of maternal
UBE3A, a ubiquitin protein ligase E3A. Here, we study neurons derived from patients with …