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 …

The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-
dependent molecular chaperones that fold and remodel proteins. Both are important …

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 …

Manipulation of individual molecules with optical tweezers provides a powerful means of
interrogating the structure and folding of proteins. Mechanical force is not only a relevant …

Cells have a remarkable ability to synthesize large amounts of protein in a very short period
of time. Under these conditions, many hydrophobic surfaces on proteins may be transiently …

The heat shock protein 90 (Hsp90) family consists of four highly conserved isoforms: the
mitochondrial TRAP-1, the endoplasmic reticulum-localised Grp94, and the cytoplasmic …

We present an approach that enables us to simultaneously access structure and dynamics
of a multidomain protein in solution. Dynamic domain arrangements are experimentally …

Heat shock protein 90 alpha (Hsp90α) is an abundantly expressed and evolutionarily
conserved molecular chaperone. Hsp90α is the inducible Hsp90 isoform, and its expression …

HSP90AB1 (heat shock protein 90 kDA alpha, class B, member 1), also known as
HSP90beta, is a member of the large family of HSPs which function as molecular …