14 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
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Inhibition of estrone sulfatase (ES) by alkyl and cycloalkyl ester derivatives of 4-[(aminosulfonyl)oxy] benzoic acid.
Kingston University
The mechanism of the irreversible inhibition of estrone sulfatase (ES) through the consideration of a range of methane- and amino-sulfonate-based compounds.
Kingston University
Inhibition of estrone sulfatase (ES) by derivatives of 4-[(aminosulfonyl)oxy] benzoic acid.
Kingston University
Design, synthesis and biochemical evaluation of AC ring mimics as novel inhibitors of the enzyme estrone sulfatase (ES).
Kingston University
Acid dissociation constant, a potential physicochemical factor in the inhibition of the enzyme estrone sulfatase (ES).
Kingston University
Determination and use of a transition state for the enzyme estrone sulfatase (ES) from a proposed reaction mechanism.
Kingston University
Hydrophobicity, a physicochemical factor in the inhibition of the enzyme estrone sulfatase (ES).
Kingston University
Derivation of a possible transition-state for the reaction catalysed by the enzyme estrone Sulfatase (ES).
Kingston University
Structure activity relationship study of known inhibitors of the enzyme 5 alpha-reductase (5AR).
Kingston University
Synthesis, biochemical evaluation and rationalisation of the inhibitory activity of a range of 4-substituted phenyl alkyl imidazole-based inhibitors of the enzyme complex 17alpha-hydroxylase/17,20-lyase (P450(17alpha)).
Kingston University
Synthesis, biochemical evaluation and rationalisation of the inhibitory activity of a series of 4-hydroxyphenyl ketones as potential inhibitors of 17beta-hydroxysteroid dehydrogenase type 3 (17beta-HSD3).
Kingston University
Enzyme inhibition as a potential therapeutic strategy to treat COVID-19 infection.
Kingston University