Publications by authors named "Amanda J Daniels"
HspA1A, a molecular chaperone, translocates to the plasma membrane (PM) of stressed and cancer cells. This translocation results in HspA1A's cell-surface presentation, which renders tumors radiation insensitive. To specifically inhibit the lipid-driven HspA1A's PM translocation and devise new therapeutics it is imperative to characterize the unknown HspA1A's lipid-binding regions and determine the relationship between the chaperone and lipid-binding functions.
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- This report examines how natural single nucleotide polymorphisms (SNPs) impact the function of the HSPA1A gene, which is crucial for stress response in humans.
- All mutant proteins can still hydrolyze ATP, but three mutants do so at a significantly lower rate than the wild-type, while some show increased reaction entropies.
- Mutations also influence the ability of HSPA1A to refold proteins and prevent apoptosis, with some leading to increased cell death compared to the wild-type, suggesting alterations in the protein's chaperone activities.