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 …

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 …

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 …

Members of the Hsp90 molecular chaperone family are found in the cytosol, ER,
mitochondria and chloroplasts of eukaryotic cells, as well as in bacteria. These diverse …

Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential
role in many cellular processes including cell cycle control, cell survival, hormone and other …

The ability of photosynthetic organisms to adapt to increases in environmental temperatures
is becoming more important with climate change. Heat stress is known to induce heat-shock …

Heat shock protein 90 (Hsp90) is a molecular chaperone that folds and remodels proteins,
thereby regulating the activity of numerous substrate proteins. Hsp90 is widely conserved …

Ocean warming (OW) caused by anthropogenic activities threatens ocean ecosystems.
Moreover, microplastic (MP) pollution in the global ocean is also increasing. However, the …