HSC70 Heat-Shock Proteins
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Subject Areas on Research
- A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins.
- Changes in protein function underlie the disease spectrum in patients with CHIP mutations.
- Human erythrocyte clathrin and clathrin-uncoating protein.
- Proteomic identification and functional characterization of MYH9, Hsc70, and DNAJA1 as novel substrates of HDAC6 deacetylase activity.
- Purinergic receptor X7 is a key modulator of metabolic oxidative stress-mediated autophagy and inflammation in experimental nonalcoholic steatohepatitis.
- Selective externalization of an ATP-binding protein structurally related to the clathrin-uncoating ATPase/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation.
- The 70-kDa heat shock cognate protein (Hsc73) gene is enhanced by ovarian hormones in the ventromedial hypothalamus.
- The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.