Biomolecular condensates, membrane-less entities arising from liquid–liquid phase
separation, hold dichotomous roles in health and disease. Alongside their physiological …

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

Maintaining a healthy proteome is fundamental for the survival of all organisms. Integral to
this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding …

Abstract Heat shock protein (HSP) 90, an important component of the molecular chaperone
network, is closely concerned with cellular signaling pathways and stress response by …

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 …

The ATP-dependent Hsp70 chaperones (DnaK in E. coli) mediate protein folding in
cooperation with J proteins and nucleotide exchange factors (E. coli DnaJ and GrpE …

HSP70 and HSP90 are two powerful chaperone machineries involved in survival and
proliferation of tumor cells. Residing in various cellular compartments, HSP70 and HSP90 …

Fluorescence resonance energy transfer (FRET) is a powerful spectroscopic method for
measuring distances in the 2–8 nm range. Often, conformational changes and molecular …

Hsp90 is a molecular chaperone that interacts with a specific set of client proteins and
assists their folding. The underlying molecular mechanisms, involving dynamic transitions …

Neurodegenerative diseases are one of the leading causes of disability and death
worldwide. Intracellular transduction pathways that end in the activation of specific …