International audienceThe classical way of defining enzyme inhibition has obscured the distinction between inhibitory effect and the inhibitor binding constant. This article examines the relationship between the simple binding curve used to define biomolecular interactions and the standard inhibitory term (1 + ([I]∕K i )). By understanding how this term relates to binding curves which are ubiquitously used to describe biological processes, a modifier equation which distinguishes between inhibitor binding and the inhibitory effect, is examined. This modifier equation which can describe both activation and inhibition is compared to standard inhibitory equations with the development of global data fitting templates in Excel and via the global ...
The hyperbolic parabola is commonly used to summarize kinetics for enzyme reactions and receptor bin...
A novel rate equation is derived to characterize the dose-response behavior of a moderately potent (...
Enzyme inhibition by its substrate in excess, substrate inhibition, is one of the common deviations ...
The classical way of defining enzyme inhibition has obscured the distinction between inhibitory effe...
Reproducibility of biological data is a significant problem in research today. One potential contrib...
Most general biochemistry textbooks present enzyme inhibition by showing how the basic Michaelis-Men...
Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interaction...
International audienceThe determination of inhibition mode is extremely important in the understandi...
A new graphical method is described for analyzing the results of multiple inhibition experiments. It...
<p>The Enzyme Kinetics Module from SigmaPlot 10 was used to evaluate the inhibition type and K<sub>i...
The potential of enzyme inhibition of a drug is frequently quantified in terms of IC50 values. While...
One of the central questions in the characterization of enzyme inhibitors is determining the mode of...
simple graphical method for the determination of reversible inhibition type,inhibitio constant(Ki) ...
<p>The K<sub><b>i</b></sub> values represent the mean of two independent experiments; standard devia...
<div><p>A difficulty associated with high throughput screening for enzyme inhibitors is to establish...
The hyperbolic parabola is commonly used to summarize kinetics for enzyme reactions and receptor bin...
A novel rate equation is derived to characterize the dose-response behavior of a moderately potent (...
Enzyme inhibition by its substrate in excess, substrate inhibition, is one of the common deviations ...
The classical way of defining enzyme inhibition has obscured the distinction between inhibitory effe...
Reproducibility of biological data is a significant problem in research today. One potential contrib...
Most general biochemistry textbooks present enzyme inhibition by showing how the basic Michaelis-Men...
Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interaction...
International audienceThe determination of inhibition mode is extremely important in the understandi...
A new graphical method is described for analyzing the results of multiple inhibition experiments. It...
<p>The Enzyme Kinetics Module from SigmaPlot 10 was used to evaluate the inhibition type and K<sub>i...
The potential of enzyme inhibition of a drug is frequently quantified in terms of IC50 values. While...
One of the central questions in the characterization of enzyme inhibitors is determining the mode of...
simple graphical method for the determination of reversible inhibition type,inhibitio constant(Ki) ...
<p>The K<sub><b>i</b></sub> values represent the mean of two independent experiments; standard devia...
<div><p>A difficulty associated with high throughput screening for enzyme inhibitors is to establish...
The hyperbolic parabola is commonly used to summarize kinetics for enzyme reactions and receptor bin...
A novel rate equation is derived to characterize the dose-response behavior of a moderately potent (...
Enzyme inhibition by its substrate in excess, substrate inhibition, is one of the common deviations ...