Words similar to chaperone
Example sentences for: chaperone
How can you use “chaperone” in a sentence? Here are some example sentences to help you improve your vocabulary:
Hsp90 is a highly conserved molecular chaperone necessary for viability and for proper folding, processing, and function of proteins involved in several signal transduction pathways [ 31 32 ] . Interestingly, mammalian hsp90 has been shown to specifically interact with PP5, and this interaction may have important consequences in PP5 structure and function [ 33 34 ] . An hsp90 ortholog has been described in Pf [ 35 ] , but its function is currently unknown.
Export of many, but not all, secretory proteins is dependent on interaction with SecB, a cytoplasmic chaperone that maintains the preprotein in a loosely folded conformation competent for translocation.
It has been known for over 30 years that vitamin D status influences the level of calbindin D, a cytosolic calcium-binding protein [ 6 ] believed to be the rate-limiting step in calcium absorption [ 7 ] by acting as an intracellular calcium ferry or chaperone.
Nucleoplasmin is the most abundant protein in the Xenopus oocyte nucleus and is the protein for which the term molecular chaperone was coined due to its multiple roles in the assembly of nucleosomes during early frog development [ 1 ] . Nucleoplasmin forms a pentamer and its stretches of acidic residues bind to histone H2A and H2B.
Protein phosphatase 5 has been implicated in the control of cell proliferation, in hormonal signal transduction, and in hsp90 chaperone function [ 3 11 12 13 14 15 16 17 ] . However little is known about the regulation of PP5 or its specific role in these pathways, and only one physiological substrate for PP5 has been identified to date, the apoptosis signaling kinase ASK 1 [ 13 ] . PP5 can be activated by lipid in vitro , and removal of the TPR domain or the C terminus generates an active, lipid insensitive form of the enzyme [ 18 19 20 21 ] . PP5 phosphatase activity is also altered by hCRY2 and a fragment of hsp90 in vitro [ 21 22 ] . These findings suggest that PP5 may be autoinhibited and that the binding of protein partners or lipids to the TPR domain could potentially control PP5 activity in cells, however no reports have yet documented how PP5 is regulated in vivo . The activity of PP5 homologs from cauliflower, T. brucei and P. falciparum is stimulated by polyunsaturated fatty acids in vitro [ 7 8 9 10 ] and removal of the TPR domain from P. falciparum PP5 increases activity to the same extent as lipid treatment [ 8 9 ] . This suggests that the TPR domain plays a similar inhibitory role for all PP5 homologs.
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