DBeQ

DBeQ is a selective and reversible inhibitor of p97 ATPase (IC50 = 1.5 μM) which induces caspase-3 and caspase-7 rapidly.
p97 knows also as VCP ( Cdc48 in yeast) is a hexameric ATPase of the AAA family which disassembles SNARE proteins after membrane fusion.[1] It is involved in a fusion of homotypic membranes, protein degradation, and activation of membrane-bound transcription factors.[2] p97 is one of the most abundant proteins in the eukaryotic cytosol and its segregase function has been linked to a large number of biological processes including endoplasmic reticulum-associated degradation(ERAD), mitochondrial associated degradation, ubiquitin fusion degradation, homotypic membrane fusion, cell cycle regulation, autophagy and transcription factor regulation.[3]
DBeQ can block the degradation of endoplasmic reticulum-associated degradation (ERAD) reporters and also block autophagosome maturation,all of which are proven to be important in cancer therapy.[4,5] DBeQ is ATP-sensitive and selectively target D1and D2 domain with ODD-Luc IC50 56 μM, Luc-ODC IC50 45 μM,UbG76VGFP IC50 2.3 μM, much less affected by the presence of p47 than the other quinazolines.[6,7]
References:
1.  Zhang, X. et al. "Structure of the AAA ATPase p97". Molecular cell 2000, 6 (6): 1473–84.
2.  Madsen, L. et al. "New ATPase regulators--p97 goes to the PUB.". Int J Biochem Cell Biol 2009, 41 (12): 2380–8.
3.  Eli Chapman. et al. “Inhibitors of the AAA+ Chaperone p97”. Molecules 2015, 20(2), 3027-3049.
4.  Liu, Y. Et al. “VCP/p97,down-regulated by microRNA-129-5p, could regulate the progression of hepatocellular carcinoma”. PLoS One 2012, 7, e35800.
5.  Laguë, M.N. et al. “Proteomic profiling of a mouse model for ovarian granulosa cell tumor identifies VCP as a highly sensitive serum tumor marker in several human cancers.” PLoS One 2012, 7, e42470.
6.  Fang, C.J. et al. “Evaluating p97 inhibitor analogues for their domain selectivity and potency against the p97–p47 complex.” Chem. Med. Chem. 2014.
7.  Chou, T.F. et al. “Specific inhibition of p97/VCP ATPase and kinetic analysis demonstrated interaction between D1 and D2 ATPase domains.” J. Mol. Biol. 2014, 426, 2886–2899.