Abstract Heat shock protein 90 (HSP90) is a chaperone with vital roles in regulating
proteostasis, long recognized for its function in protein folding and maturation. A view is …

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

The use of iPSC derived brain organoid models to study neurodegenerative disease has
been hampered by a lack of systems that accurately and expeditiously recapitulate …

Abstract Systems-level assessments of protein-protein interaction (PPI) network dysfunctions
are currently out-of-reach because approaches enabling proteome-wide identification …

Hsp70s are among the most highly conserved proteins in all of biology. Through an iterative
binding and release of exposed hydrophobic residues on client proteins, Hsp70s can …

The intricate network of protein-chaperone interactions is crucial for maintaining cellular
function. Recent discoveries have unveiled the existence of specialized chaperone …

The predominantly pre-synaptic intrinsically disordered protein α-synuclein is prone to
misfolding and aggregation in synucleinopathies, such as Parkinson's disease (PD) and …

Our review seeks to elucidate the current state-of-the-art in studies of 70-kilodalton-weighed
heat shock proteins (Hsp70) in neurodegenerative diseases (NDs). The family has already …

Diseases are manifestations of complex changes in protein–protein interaction (PPI)
networks whereby stressors, genetic, environmental, and combinations thereof, alter …

Protein-protein interactions (PPIs) play a crucial role in cellular function and disease
manifestation, with dysfunctions in PPI networks providing a direct link between stressors …