Bioconjugation chemistry has been used to prepare modified biomolecules with functions
beyond what nature intended. Central to these techniques is the development of highly …

The glutathione transferases (GSTs; also known as glutathione S-transferases) are major
phase II detoxification enzymes found mainly in the cytosol. In addition to their role in …

Drug candidates are generally discovered using biochemical screens employing an isolated
target protein or by utilizing cell-based phenotypic assays. Both noncovalent and covalent …

Increases in the intracellular levels of reactive oxygen species (ROS), frequently referred to
as oxidative stress, respresents a potentially toxic insult which if not counteracted will lead to …

The glutathione transferases (GSTs) are one of the most important families of detoxifying
enzymes in nature. The classic activity of the GSTs is conjugation of compounds with …

Glutathione transferases (GSTs) are enzymes that catalyze the conjugation of glutathione
(GSH) to a variety of electrophilic substances. Their best known role is as cell housekeepers …

Glutathione transferases (GSTs) are important detoxifying enzymes that catalyze the
conjugation of electrophilic substrates to glutathione. In recent years, GSTs have been of …

Selective covalent modification of a targeted protein is a powerful tool in chemical biology
and drug discovery, with applications ranging from identification and characterization of …

Growing evidence supports the view that enzymatic activity results from a subtle interplay
between chemical kinetics and molecular motions. A systematic analysis is performed here …

Mercury, cadmium, arsenic and lead are among priority metals for toxicological studies due
to the frequent human exposure and to the significant burden of disease following acute and …