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This article, Identification of mutagenic small molecules from imulsion extract, was written by RelentlessRecusant. Please do not edit this fiction without the writer's permission.

Identification of mutagenic small molecules from imulsion extract

Davis et. al. (2532). Department of Molecular Genetics, Bastion Public Health Service. Nature (541): 173-177.

Recently, it has been reported that natural imulsion poses a substantiative health risk to the adult human [DeMarshall et. al (2531). Nature (538): 1749-1953]. Because of the extensive employment of imulsion in modernized society, we wished to characterize the modalities by which imulsion exerts its health-risking effects. Bulk hybridization of imulsion extract to high-density beads through non-specific glutathione S-transferase (GST) transfer and screening of a library of primary human cell lysates has yielded three previously-uncharacterized small-molecules from imulsion extract, which we have named IMC-1 through IMC-3 (“imulsion mutagenic compound”) that have an affinity for targets in the human proteome. We decided to further characterize IMC-1, which we named “teratomorphin”, and show that it has a high binding affinity (Ki = 0.07 nM and 0.03 nM, respectively) for human FGFR3 (fibroblast growth factor receptor 3) and ACVR1 (activin receptor-like kinase 1). X-ray crystallography studies indicate that teratomorphin binds to FGFR3 and ACVR1 through allosteric non-ATP-competitive mechanisms, and that through luciferase receptor assays in transiently-transfected fibroblasts and endothelial cells, teratomorphin is a highly potent activator of both FGFR1 and ACVR1, mimicking constitutive FGF and BMP signaling.

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