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 …

HSP90 is a molecular chaperone that associates with numerous substrate proteins called
clients. It plays many important roles in human biology and medicine, but determinants of …

Heat shock protein 90 (Hsp90), one of the most abundant and conserved molecular
chaperones, is essential in eukaryotic cells.[1, 2] Different from other well‑known mo‑lecular …

Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of
numerous client proteins many of which are involved in essential cellular processes like …

Crosstalk between different types of posttranslational modification is an emerging theme in
eukaryotic biology. Particularly prominent are the multiple connections between …

Hsp90 is a major molecular chaperone that is expressed abundantly and plays a pivotal role
in assisting correct folding and functionality of its client proteins in cells. The Hsp90 client …

The heat shock protein (Hsp) 90 chaperone machinery regulates the activity of hundreds of
client proteins in the eukaryotic cytosol. It undergoes large conformational changes between …

The ErbB receptor tyrosine kinases evolved as key regulatory entities enabling the
extracellular milieu to communicate with the intracellular machinery to bring forth the …

The molecular chaperone Hsp90 (90 kDa heat-shock protein) is a remarkably versatile
protein involved in the stress response and in normal homoeostatic control mechanisms. It …