interaction of haloacetonitriles with glutathione and glutathione-s-transferase

interaction of haloacetonitriles with glutathione and glutathione-s-transferase S-transferase: A versatile dynamic enzyme Glutathione Transferase Haloacetonitrile stability in cell culture

Name: interaction of haloacetonitriles with glutathione and glutathione-s-transferase S-transferase: A versatile dynamic enzyme Glutathione Transferase Haloacetonitrile stability in cell culture
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Haloacetonitrile stability in cell culture media used in vitro toxicological studies ScienceDirect Health risk assessment of haloacetonitriles in drinking water based on internal dose ScienceDirect Glutathione S transferase: A versatile and dynamic enzyme ScienceDirect Overexpression of Glutathione S Transferases in Human Diseases: Drug Targets and Therapeutic Implications PDF) Studies on the mechanism of haloacetonitriles toxicity: Inhibition of rat hepatic glutathione S transferases in vitro

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For example, wild-type TP53 is able to inhibit glycolysis by suppressing the expression of GLUT1, GLUT3, and GLUT4 (160, 161), and regulating the expression of enzymes involved in the glycolytic pathway, such as HK2 (162), phosphofructokinase 1 (PFK1) (163), phosphoglycerate mutase (PGM) (163), pyruvate dehydrogenase (PDH), parkin 2 (PARK2) (164), and pyruvate dehydrogenase kinase (PDK2) (165)

This notion receives some support from microarray analysis of GRX gene expression in mutants with pertur- bations in leaf glutathione redox state, in which specic members of class III were the only GRX that were found to respond (Mhamdi et al