DnaJB7 Inhibitors

DnaJB7 Inhibitors typically function by inhibiting the heat shock proteins (HSPs) that DnaJB7 associates with. DnaJB7 is a co-chaperone that functions in complexes with HSP70 and HSP90, aiding in protein folding and maturation. Therefore, inhibitors of these HSPs can lead to a decrease in the functional activity of DnaJB7. Geldanamycin, 17-AAG, and Radicicol are all HSP90 inhibitors that, through their inhibition of HSP90, disrupt the HSP70-HSP90 complexes and thus reduce DnaJB7's functional activity. In a similar vein, VER-155008, MKT-077, Apoptozole, and JG-98 are HSP70 inhibitors that, by inhibiting HSP70, decrease the functional activity of DnaJB7. These inhibitors disrupt the chaperone complex, affecting the protein folding and maturation process that DnaJB7 is involved in. Other DnaJB7 inhibitors operate by influencing broader cellular processes. For instance, Cycloheximide, an inhibitor of protein synthesis, indirectly affects DnaJB7 by impeding the overall protein folding process that DnaJB7 is part of. Tunicamycin inhibits N-linked glycosylation, a post-translational modification. This action can indirectly impact DnaJB7's activity, as the protein assists in protein folding and maturation. MG132 and Bortezomib, both proteasome inhibitors, can indirectly affect the functionality of DnaJB7 by altering the protein degradation pathways that DnaJB7 may be involved in. Finally, 2-Deoxyglucose, a glycolysis inhibitor, can indirectly affect DnaJB7's activity. Given DnaJB7's role in protein homeostasis, which requires energy, inhibiting energy production can indirectly reduce its functional activity.