bp(GO:"ATP metabolic process")
ATP hydrolysisis essential for the chaperone activity of HSP70 and HSP90, causing conformational changes that result in substrate binding (11). PubMed:25784053
ATP hydrolysisis essential for the chaperone activity of HSP70 and HSP90, causing conformational changes that result in substrate binding (11). PubMed:25784053
Hsp90 requires ATP to perform these functions including protein degradation, protein folding, prevention of protein aggregation, and protein modification (Echeverría et al., 2011). PubMed:29311797
After hydrolysis the Hsp90 N termini separate, releasing the client protein in an active state (Figure 7b). PubMed:23746257
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.