Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
Avermectin transepithelial transport in MDR1- and MRP-transfected canine kidney monolayers
The data confirm that ivermectin and selamectin are substrates for P-gp in four additional cell lines, but suggest that they are not significant substrate for MRP1 or MRP2 where there is background expression of P- gp.
Selamectin is a potent substrate and inhibitor of human and canine P-glycoprotein.
- J. Griffin, N. Fletcher, R. Clemence, S. Blanchflower, D. Brayden
- Chemistry, MedicineJournal of veterinary pharmacology and…
- 1 June 2005
The data suggest that ivermectin and selamectin are potent P-gp substrates, while moxidectin is a weak one.
Re‐engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild‐type enzyme
It is revealed that the enzyme’s discrimination in favour of NAD+ and against NADP+ had been greatly underestimated and has indeed been abated by a factor of > 16 000 by the mutagenesis, creating an entirely false view of the initial coenzyme specificity and also of the effects of Mutagenesis.
An Examination by Site-Directed Mutagenesis of Putative Key Residues in the Determination of Coenzyme Specificity in Clostridial NAD+-Dependent Glutamate Dehydrogenase
Sequence and structure comparisons of various glutamate dehydrogenases (GDH) and other nicotinamide nucleotide-dependent dehydrogenases have potentially implicated certain residues in coenzyme…
Examination of coenzyme specificity in clostridial glutamate dehydrogenase by site-directed mutagenesis
The –SH Protection Method for Determining Accurate Kd Values for Enzyme-Coenzyme Complexes of NAD+-Dependent Glutamate Dehydrogenase and Engineered Mutants: Evidence for Nonproductive NADPH Complexes
Study of the effects of NAD+, NADH and NADPH at various concentrations in protecting against inactivation by 200 μM DTNB allowed determination of Kd values for binding of these coenzymes to each protein, yielding surprising results.