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• W2892849801 abstract "Vitamin D receptor (VDR) ligands, such as 1α,25-dihydroxyvitamin D3 [1α,25(OH)2D3] and its analogs, have been investigated for their potential clinical use in the treatment of various diseases such as type I rickets, osteoporosis, psoriasis, leukemia, and cancer. Previously, we reported a split-luciferase-based biosensor that can detect VDR ligands and assess their affinity for the ligand binding domain (LBD) of the VDR in a short time. However, a further increase in its sensitivity was required to detect plasma levels of 1α,25(OH)2D3 and its analogs. In this study, a novel type of biosensor called LXXLL + LBD was successfully developed. Here, the split luciferase forms a functional complex based on the intermolecular interaction between the LXXLL motif and the ligand-bound form of the LBD. This biosensor has an approximately 10-fold increase in the light intensity compared to the previous versions. Additionally, the binding affinity of the vitamin D analogs for the wild-type and the rickets-associated mutant R274L of VDR was evaluated." @default.
• W2892849801 created "2018-10-05" @default.
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• W2892849801 date "2018-10-01" @default.
• W2892849801 modified "2023-10-12" @default.
• W2892849801 title "Novel biosensor using split-luciferase for detecting vitamin D receptor ligands based on the interaction between vitamin D receptor and coactivator" @default.
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• W2892849801 doi "https://doi.org/10.1016/j.bbrc.2018.09.122" @default.
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