Intrinsically disordered proteins (IDPs) are widespread in eukaryotes and participate in a
variety of important cellular processes. Numerous studies using state-of-the-art experimental …

Abstract The Heat Shock Protein 90 (Hsp90) molecular chaperone is a key driver of protein
homeostasis (proteostasis) under physiologically normal and stress conditions. In …

Protein homeostasis relies on the accurate translation and folding of newly synthesized
proteins. Eukaryotic elongation factor 2 (eEF2) promotes GTP-dependent translocation of …

Cells maintain homeostasis via dynamic regulation of stress response pathways. Stress
pathways transiently induce response regulons via negative feedback loops, but the extent …

Molecular chaperone heat shock protein 90 (Hsp90) is a ubiquitous regulator that fine-tunes
and remodels diverse client proteins, exerting profound effects on normal biology and …

The molecular chaperone Hsp90 (Heat shock protein, 90 kDa) is an abundant and essential
cytosolic protein required for the stability and/or folding of hundreds of client proteins …

SUMMARY Heat shock protein 90 (Hsp90) participates in proteostasis by facilitating protein
folding, activation, disaggregation, prevention of aggregation, degradation, and protection …

The budding yeast Kluyveromyces lactis has emerged as a promising microbial chassis in
industrial biotechnology. However, a lack of efficient molecular genetic manipulation tools …

In conventional crosslinking mass spectrometry, proteins are crosslinked using a highly
selective, bifunctional chemical reagent, which limits crosslinks to residues that are …

Hsp90α, a pivotal canonical chaperone, is renowned for its broad interaction with numerous
protein clients to maintain protein homeostasis, chromatin remodeling, and cell growth …