ArticleThe Journal of biological chemistry2018
Steady-state analysis of enzymes with non-Michaelis-Menten kinetics: The transport mechanism of Na
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- A scoping review of computational models on human glucose cerebral metabolism.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2026Review
- Non-hyperbolic enzyme kinetics: the case of P-type ATPases.Biophysical reviews · 2025Review
- Molecular Basis of Na, K-ATPase Regulation of Diseases: Hormone and FXYD2 Interactions.International journal of molecular sciences · 2024Review
- Procyanidin C1 from Viola odorata L. inhibits NaScientific reports · 2022Article
- Application of modified Michaelis - Menten equations for determination of enzyme inducing and inhibiting drugs.BMC pharmacology & toxicology · 2021Article
- Tumour blood flow for prediction of human prostate cancer aggressiveness: a study with Rubidium-82 PET, MRI and NaEuropean journal of nuclear medicine and molecular imaging · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
Procedures to define kinetic mechanisms from catalytic activity measurements that obey the Michaelis-Menten equation are well established. In contrast, analytical tools for enzymes displaying non-Michaelis-Menten kinetics are underdeveloped, and transient-state measurements, when feasible, are therefore preferred in kinetic studies. Of note, transient-state determinations evaluate only partial reactions, and these might not participate in the reaction cycle. Here, we provide a general procedure to characterize kinetic mechanisms from steady-state determinations. We described non-Michaelis-Menten kinetics with equations containing parameters equivalent to
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