The total quasi-steady-state approximation is valid for reversible enzyme kinetics
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Publication:2187480
DOI10.1016/j.jtbi.2003.09.006zbMath1439.92105OpenAlexW2030955594WikidataQ79329388 ScholiaQ79329388MaRDI QIDQ2187480
Publication date: 3 June 2020
Published in: Journal of Theoretical Biology (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1016/j.jtbi.2003.09.006
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Cites Work
- Unnamed Item
- Unnamed Item
- Michaelis-Menten kinetics at high enzyme concentrations
- Enzyme kinetics at high enzyme concentration
- On the validity of the steady state assumption of enzyme kinetics
- On the Lambert \(w\) function
- Extending the quasi-steady state approximation by changing variables
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
- Simplification and Scaling
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