Protein–protein interactions (PPIs) have pivotal roles in life processes. The studies showed
that aberrant PPIs are associated with various diseases, including cancer, infectious …

HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein,
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …

Drought stress is one of the most adverse abiotic stresses that hinder plants' growth and
productivity, threatening sustainable crop production. It impairs normal growth, disturbs …

New drug discovery has been acknowledged as a complicated, expensive, time-consuming,
and challenging project. It has been estimated that around 12 years and 2.7 billion USD, on …

Heat shock proteins (HSPs) constitute a large family of proteins involved in protein folding
and maturation whose expression is induced by heat shock or other stressors. The major …

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 …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and
their aggregates by protein quality control (PQC), of which molecular chaperones are an …

Chaperones are central to the proteostasis network (PN) and safeguard the proteome from
misfolding, aggregation, and proteotoxicity. We categorized the human chaperome of 332 …

Protein aggregation occurs as a consequence of perturbations in protein homeostasis that
can be triggered by environmental and cellular stresses. The accumulation of protein …