The human HSP 70 / HSP 40 chaperone family
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چکیده
منابع مشابه
The Effect of Resistance and Progressive Training on HSP 70 and Glucose
Skeletal muscle may develop adaptive chaperone and enhancementdefense system through daily exercisestimulation. The present study investigated resistance and exhaustion training alters the expression of chaperoneproteins. These proteins function to maintain homeostasis, facilitate repair from injury and provide protection. Exercise-induced production of HSPs in skeletal muscle and peripheral le...
متن کاملThe Effect of Resistance and Progressive Training on HSP 70 and Glucose
Skeletal muscle may develop adaptive chaperone and enhancementdefense system through daily exercisestimulation. The present study investigated resistance and exhaustion training alters the expression of chaperoneproteins. These proteins function to maintain homeostasis, facilitate repair from injury and provide protection. Exercise-induced production of HSPs in skeletal muscle and peripheral le...
متن کاملChaperone-assisted protein folding in the cell cytoplasm.
Folding of polypeptides in the cell typically requires the assistance of a set of proteins termed molecular chaperones. Chaperones are an essential group of proteins necessary for cell viability under both normal and stress conditions. There are several chaperone systems which carry out a multitude of functions all aimed towards insuring the proper folding of target proteins. Chaperones can ass...
متن کاملThe C. elegans UNC-23 protein, a member of the BCL-2-associated athanogene (BAG) family of chaperone regulators, interacts with HSP-1 to regulate cell attachment and maintain hypodermal integrity
Mutations in the unc-23 gene in the free-living nematode, Caenorhabditis elegans result in detachment and dystrophy of the anterior body wall musculature and a bent-head phenotype when grown on solid substrate. We have determined that the unc-23 gene product is the nematode ortholog of the human BAG-2 protein, a member of the Bcl-2 associated athanogene (BAG) family of molecular chaperone regul...
متن کاملBAG-1 modulates the chaperone activity of Hsp70/Hsc70.
The 70 kDa heat shock family of molecular chaperones is essential to a variety of cellular processes, yet it is unclear how these proteins are regulated in vivo. We present evidence that the protein BAG-1 is a potential modulator of the molecular chaperones, Hsp70 and Hsc70. BAG-1 binds to the ATPase domain of Hsp70 and Hsc70, without requirement for their carboxy-terminal peptide-binding domai...
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