Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures.
22.
"' Hsp33 protein "'is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation.
23.
As a molecular chaperone, this protein may affect the folding or stability of other ciliary or basal body proteins.
24.
In the case of CASA, dysfunctional, nonnative proteins are recognized by molecular chaperones and become ubiquitinated by chaperone-associated ubiquitin ligases.
25.
It assists in the folding of other proteins, acting as a kind of molecular chaperone ( thus the name ).
26.
Other pro-survival factors interacting with class III ?-tubulin enabling cellular adaptation to oxidative stress include the molecular chaperone HSP70 / GRP75.
27.
Zinc finger and BTB domain-containing protein 16 and BAG family molecular chaperone regulator function as co-chaperone proteins in processes involving HB-EGF.
28.
Normally when a protein does not fold correctly, molecular chaperones in the cell can encourage refolding back into its active form.
29.
DNAJC6 belongs to the evolutionarily conserved DNAJ / HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity.
30.
It also shows homology to prefoldins which are small molecular weight proteins that assemble into molecular chaperone complexes to affect protein folding.
