The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …

The Hsp40, Hsp70, and Hsp90 chaperone families are ancient, highly conserved, and
critical to cellular protein homeostasis. Hsp40 chaperones can transfer their protein clients to …

Molecular chaperones are essential cellular components that aid in protein folding and
preventing the abnormal aggregation of disease-associated proteins. Mutations in one such …

Hsp90s are ATP-dependent chaperones that collaborate with co-chaperones and Hsp70s to
remodel client proteins. Grp94 is the ER Hsp90 homolog essential for folding multiple …

The Hsp90 co-chaperones FKBP51 and FKBP52 play key roles in steroid-hormone-receptor
regulation, stress-related disorders, and sexual embryonic development. As a prominent …

J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much
of how they function within the network of other chaperones and protein quality control …

Hsp90 and Hsp70 are highly conserved molecular chaperones that help maintain
proteostasis by participating in protein folding, unfolding, remodeling and activation of …

Chaperone proteins are essential in all living cells to ensure protein homeostasis. Hsp90 is
a major adenosine triphosphate (ATP)-dependent chaperone highly conserved from …

Inborn errors of T cell development present a pediatric emergency in which timely curative
therapy is informed by molecular diagnosis. In 11 affected patients across four …

Hsp90 is a molecular chaperone of central importance for protein homeostasis in the cytosol
of eukaryotic cells, with key functional and structural traits conserved from yeast to man …