Results (
Vietnamese) 1:
[Copy]Copied!
Control of theexpression level of Hsp104 may provide a therapyagainst prion disease. In addition, Hsp104, along withHsp70, has been shown to be responsible for solubilizingprion-like aggregates in Saccharomyces cerevisiae[116,117]. Many other positive responses have beenreported on cellular chaperone-mediated disaggregationin vivo. A classic experiment was performedby Goloubinoff et al., who proved the phenomena ofin vitro reactivation and disaggregation of stable aggregatesof malate dehydrogenase by ClpB together withDnaK, DnaJ and GrpE (KJE), and further explainedthe mechanism of the whole disaggregation process(Fig. 5) [118].Mogk, Tomoyasu and colleagues [110,119] showedthat, in E. coli, stable protein aggregates rapidly disappearfrom the insoluble fraction following chaperoneaction during a short recovery period. Under normalconditions, chaperones repair the conformationaldefects of some mutated proteins, thus reducing theirphenotypic effects and dampening genome cleansing(elimination of damaged genes from the gene pool of a
Being translated, please wait..