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 …

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

BACKGROUND Human pregnancy requires robust hemostasis to prevent hemorrhage
during extravillous trophoblast (EVT) invasion of the decidualized endometrium, modification …

The Picornaviridae represent a large family of small plus-strand RNA viruses that cause a
bewildering array of important human and animal diseases. Morphogenesis is the least …

Heat stress transcription factors (Hsfs) regulate gene expression in response to
environmental stress. The Hsf network in plants is controlled at the transcriptional level by …

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 molecular chaperones are required for the stability and activity of a diverse range of
client proteins that have critical roles in signal transduction, cellular trafficking, chromatin …

Sti1/Hop is a modular protein required for the transfer of client proteins from the Hsp70 to the
Hsp90 chaperone system in eukaryotes. It binds Hsp70 and Hsp90 simultaneously via TPR …

Viruses are intracellular pathogens responsible for a vast number of human diseases. Due
to their small genome size, viruses rely primarily on the biosynthetic apparatus of the host for …