Alexander J. Muller

TL;DR: Analysis of tyrosine kinase activity and quantitative measurement of transformation potency in a single-step assay indicate that variation in bcr exon contribution results in a functional difference between p210bCr-abl and p185bcr-abl proteins.

TL;DR: It is shown that IDO is under genetic control of Bin1, which is attenuated in many human malignancies, and that small-molecule inhibitors of IDO cooperate with cytotoxic agents to elicit regression of established tumors refractory to single-agent therapy.

TL;DR: Evidence is provided that the D and L stereoisomers exhibit important cell type-specific variations in activity that support the suitability of D-1-methyl-tryptophan for human trials aiming to assess the utility of IDO inhibition to block host-mediated immunosuppression and enhance antitumor immunity in the setting of combined chemo-immunotherapy regimens.

TL;DR: The discovery of a novel IDO-related tryptophan catabolic enzyme termed IDO2 that is preferentially inhibited by D-1MT is reported, which has implications for understanding the evolution of tumoral immune tolerance and for interpreting preclinical and clinical responses to IDO inhibitors being developed to treat cancer, chronic infection, and other diseases.

TL;DR: BCR first-exon sequences specifically potentiate transformation and tyrosine kinase activation when they are fused to the second exon of otherwise intact c-ABL, which suggests that BCR-encoded sequences specifically interfere with negative regulation of the ABL-encoding tyrosINE kinase, which would represent a novel mechanism for the activation of nonreceptor tyrosines.