Since it has been reported that c-ABL can physically interact with ERα66 to form a complex and inhibition of ABL activity sensitizes breast cancer cells to chemotherapy drugs [55, 56], it is possible that ERα36, as its full-length ERα66, interacts with BCR-ABL, contributing to the activation of the BCR-ABL-Tyr177-mediated GRB2-RAS-MAPK pathway and that its inhibition by SNG inhibitors plus TKIs effectively disrupts the BCR-ABL-Tyr177-GRB2 complex and inhibits its downstream pathway (Figure 8B). This evidence concerns the gene ABL1 and breast carcinoma.