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Extracellular ribonuclease from bacillus licheniformis (Balifase), a New member of the N1/T1 RNase superfamily
Sokurenko Y.
The N1/T1 RNase superfamily comprises enzymes with well-established antitumor effects
Time-course of enzyme-catalyzed competing substrate degradation for michaelian behavior and for enzymes showing activation/inhibition by excess substrate
Goličnik M., Masson P.
the effect of an “invisible” substrate (B) on the time-course of enzyme-catalyzed substrate degradation of a
Bioluminescent enzyme inhibition-based assay to predict the potential toxicity of carbon nanomaterials
Есимбекова, Е. Н., Немцева, Е. В., Безруких, А. Е., Жукова, Г. В., Лисица, А. Е., Лоншакова-Мукина, В. И., Римацкая, Н. В., Сутормин, О. С., Кратасюк, В. А.
A bioluminescent enzyme inhibition-based assay was applied to predict the potential toxicity
Slow-binding inhibition of cholinesterases, pharmacological and toxicological relevance
Masson P., Lushchekina S.
© 2016 Elsevier Inc. All rights reserved. Slow-binding inhibition (SBI) of enzymes is characterized
Inhibition of sialidase activity as a therapeutic approach
Glanz V.Y.
is inhibiting viral sialidase (neuraminidase). This enzyme cleaves the sialic acid link between the newly formed
Slow-binding inhibition of cholinesterases, pharmacological and toxicological relevance
Masson P., Lushchekina S.
© 2016 Elsevier Inc. All rights reserved. Slow-binding inhibition (SBI) of enzymes is characterized
Sensitivity and selectivity of electrochemical enzyme sensors for inhibitor determination
Evtugyn G., Budnikov H., Nikolskaya E.
The performance of electrochemical biosensors developed for the determination of inhibiting species
Mechanism of DNA cleavage by the DNA/RNA-non-specific Anabaena sp. PCC 7120 endonuclease NucA and its inhibition by NuiA
Meiss G., Gimadutdinow O., Haberland B., Pingoud A.
, is not inhibited by NuiA, suggesting that small molecules gain access to the active site of NucA in the enzyme
1,3-Disubstituted p-tert-butylcalix[4]arenes as cholinesterase inhibitors
Stoikova E., Evtugyn G., Belyakova S., Khrustalev A., Stoikov I., Antipin I., Budnikov H., Konovalov A.
. The interaction of calix[4]arene with the enzyme is described in accordance with the formal kinetics
Phytochemical, antimicrobial, antioxidant and enzyme inhibitory potential of medicinal plant Dryopteris ramosa (Hope) C. Chr.
Alam F., Khan S.H.A., Asad M.H.H.B.
glucosidase enzyme at a concentration of 0.5 mg/ml. In case of acetylcholine esterase inhibition assay

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