The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are
involved in myriad cellular processes. Their distribution in various cellular compartments …

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 protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …

Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

Molecular chaperones govern proteome health to support cell homeostasis. An essential
eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology …

The expanding number of members in the various human heat shock protein (HSP) families
and the inconsistencies in their nomenclature have often led to confusion. Here, we propose …

Glucose-regulated protein 94 is the HSP90-like protein in the lumen of the endoplasmic
reticulum and therefore it chaperones secreted and membrane proteins. It has essential …

Leishmaniasis is a neglected infectious disease caused by several different species of
protozoan parasites of the genus Leishmania. Current strategies to control this disease are …