Reversible Inhibition
Reversible Inhibition - Related Videos
08:35
Inducible and Reversible Dominant-negative (DN) Protein Inhibition
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2019
Here we present a protocol to develop a dominant-negative inducible system, in which any protein can be conditionally inactivated by reversibly overexpressing a dominant-negative mutant version of it.
09:43
Using Optogenetics to Reverse Neuroplasticity and Inhibit Cocaine Seeking in Rats
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Cited by 1 •
2021
The methods described here outline a procedure used to optogenetically reverse cocaine-induced plasticity in a behaviorally-relevant circuit in rats. Sustained low-frequency optical stimulation of thalamo-amygdala synapses induces long-term depression (LTD). In vivo optogenetically-induced LTD in cocaine-experienced rats resulted in the subsequent attenuation of cue-motivated drug seeking.
10:10
Reverse Total Shoulder Arthroplasty
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Cited by 5 •
2011
Reverse total shoulder arthroplasty is indicated for the treatment of conditions that cannot be treated with conventional arthroplasty or other procedures. These primarily include degenerative and incapacitating conditions with irreparable rotator cuff and loss of the normal biomechanical coupling of the shoulder.
09:39
Creation of Reversible Cholestatic Rat Model
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2011
Cholestasis is a clinical condition commonly encountered by both surgeons and gastroenterologists. Creation of a reversible cholestatic rat model can be challenging in view of the smaller size and unique hepatopancreatobiliary anatomy in rats. This video article demonstrates the creation of a reversible cholestatic model.
03:26
Reverse Transcriptase Activity as a Marker for Virus-Like Particle Production
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2026
Source: Scarborough, R. J., et al. Evaluation of the Efficacy And Toxicity of RNAs Targeting HIV-1 Production for Use in Gene or Drug Therapy. J. Vis. Exp. (2016).This video demonstrates a reverse transcriptase (RT) assay to assess the effect of a test RNA on virus-like particle (VLP) production. Cells are co-transfected with plasmids, and RT activity is measured as a quantitative indicator of VLP output. A decrease in RT activity reflects suppression of viral gene expression by the test RNA.
FAQs
Competitive inhibition is evaluated through the relationship between inhibitor binding and substrate access: both are considered at the enzyme’s active site, so inhibitor presence matters when substrate and inhibitor compete for that location. By contrast, binding elsewhere can change enzyme shape without directly occupying the active site. This comparison helps separate different kinetic mechanisms.
Binding location matters because it determines whether the inhibitor directly interferes with substrate access or changes the enzyme’s shape from another site. Active-site binding represents competition with the substrate, whereas binding elsewhere can alter catalytic behavior without blocking that site directly. These distinct effects provide a mechanistic basis for interpreting changes in reaction kinetics.
Substrate concentration and reaction rate provide complementary evidence about inhibitor behavior. Researchers measure how rapidly the enzyme acts under different substrate concentrations, then compare those results with inhibitor-free conditions. The resulting patterns help determine whether reduced activity is associated with active-site competition or with an inhibitor that changes enzyme behavior through another binding location.
A basic workflow measures enzyme reaction rates across a range of substrate concentrations, first without an inhibitor and then with the inhibitor present. Researchers compare the two sets of measurements to identify how activity changes. This approach links the observed rate pattern to the inhibitor’s binding behavior and supports classification of the inhibition mechanism.
Researchers distinguish these forms by comparing reaction-rate measurements across substrate concentrations in the presence and absence of an inhibitor. The comparison reveals whether the inhibitor behaves like a competitor for the active site or produces a different kinetic pattern associated with binding elsewhere. This classification helps connect experimental observations with the underlying enzyme mechanism.
Reversible inhibition is useful for examining metabolic regulation and tracing how biochemical pathways respond when enzyme activity changes temporarily. It also supports drug development by providing a way to control enzyme function without permanently modifying the protein. In biology, these applications help researchers connect enzyme kinetics with pathway behavior and therapeutic control.