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Description
The variability of the C-terminal domain of GSTs enables these enzymes to use a variety of substrates to bind activated glutathione to most hydrophobic compounds containing electrophilic atoms [4]
Mortality can be reduced by as much as 40%
We further modified 1907 by N -myristoylation to identify an optimized lead peptide (2012) with improved cell permeability, drug metabolism, pharmacokinetic (DMPK) properties, and in vitro efficacy
Interplay between cAMPCRP and c-di-GMP in Vibrio cholerae biofilm formation
