<unk>  is described as a "STAMP inhibitor," which means "specifically targeting the ABL myristoyl pocket." The wild-type ABL has a myristoylated N-terminus, which binds to an allosteric site, but the ABL fusion protein does not have the myristoylated domain. In the wild-type protein, when myristoylated N-terminus binds to the allosteric site, the kinase has reduced activity. Since the mutant fusion protein does not have the myristoylated N-terminus domain, it is not subject to this form of regulation, and thus the fusion protein is constitutively active.<unk>  binds to the allosteric site, resulting in an inhibition of bcr-abl activity. Unlike other bcr-abl inhibitors, such as imatinib,<unk>  does not bind to the ATP-binding site on the active site of the enzyme.<unk>  and active site bcr-abl inhibitors have non-overlapping resistance mutations. The mutations A337V and P223S overcome the inhibitory activity of<unk> , but<unk>  is not affected by the notorious T315I mutation that affects most ATP-competitive active site inhibitors, except ponatinib.
Asciminib
Deferasirox
Calcifediol
Deferoxamine
Naloxegol
Deferiprone
Fursultiamine
Morazone