Cresyl diphenyl phosphate (a novel organophosphate ester) induces hepatic steatosis by directly binding to liver X receptor α: From molecule action to risk assessment.

Cresyl diphenyl phosphate (CDP), a novel organophosphate ester (OPE), has been increasingly detected in various environmental and human samples. However, its toxicity, mechanisms, and health risks remain largely unknown. In this work, we investigated CDP-induced hepatic steatosis through Liver X Receptor α (LXRα) pathway across the molecular interactions, signaling pathways, cell functions, animal effects, and population risks, and compared them to triphenyl phosphate (TPHP) and tricresyl phosphate (TCRP).

Fine particulate matter disrupts bile acid homeostasis in hepatocytes via binding to and activating farnesoid X receptor.

Fine particulate matter (PM)-induced metabolic disorders have attracted increasing attention, however, the underlying molecular mechanism of PM2.5-induced hepatic bile acid disorder remains unclear. In this study, we investigated the effects of PM components on the disruption of bile acid in hepatocytes through farnesoid X receptor (FXR) pathway.

Toxicity and risk priority ranking of polybrominated diphenyl ethers (PBDEs): A relative receptor-bound concentration approach.

Toxicity and risk priority ranking of chemicals are crucial to management and decision-making. In this work, we develop a new mechanistic ranking approach of toxicity and risk priority ranking for polybrominated diphenyl ethers (PBDEs) based on receptor-bound concentration (RBC). Based on the binding affinity constant predicted using molecular docking, internal concentration converted from human biomonitoring data via PBPK model, and the receptor concentration derived from the national center for biotechnology information (NCBI) database, the RBC of 49 PBDEs binding to 24 nuclear receptors were calculated.

Efficient production of α-ketoglutarate in the gdh deleted Corynebacterium glutamicum by novel double-phase pH and biotin control strategy.

Production of L-glutamate using a biotin-deficient strain of Corynebacterium glutamicum has a long history. The process is achieved by controlling biotin at suboptimal dose in the initial fermentation medium, meanwhile feeding NH4OH to adjust pH so that α-ketoglutarate (α-KG) can be converted to L-glutamate. In this study, we deleted glutamate dehydrogenase (gdh1 and gdh2) of C.