A perturbation solution of Michaelis-Menten kinetics in a ``total framework
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Publication:714677
DOI10.1007/S10910-011-9957-6zbMATH Open1401.92089OpenAlexW1975553365MaRDI QIDQ714677FDOQ714677
Authors: Guido Dell'Acqua, Alberto Bersani 
Publication date: 11 October 2012
Published in: Journal of Mathematical Chemistry (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/s10910-011-9957-6
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Cites Work
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- The total quasi-steady-state approximation for complex enzyme reactions
- Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity
- The total quasi-steady-state approximation for fully competitive enzyme reactions
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Cited In (31)
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- A simplified perturbation solution of Michaelis-Menten kinetics equations in a ``total framework
- Extending the kinetic solution of the classic Michaelis--Menten model of enzyme action
- Stability analysis of the Michaelis-Menten approximation of a mixed mechanism of a phosphorylation system
- Analytical bounding functions for diffusion problems with Michaelis- Menten kinetics
- A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics.
- Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation?
- Heineken, Tsuchiya and Aris: ``On the mathematical status of the pseudo-steady state hypothesis. A classic from Volume 1 of \textit{Mathematical Biosciences}
- On a stochastic approach to model the double phosphorylation/dephosphorylation cycle
- An alternative approach to Michaelis-Menten kinetics that is based on the renormalization group
- The total quasi-steady-state for multiple alternative substrate reactions
- Tihonov theory and center manifolds for inhibitory mechanisms in enzyme kinetics
- Title not available (Why is that?)
- Approximation of enzyme kinetics for high enzyme concentration by a first order perturbation approach
- Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions
- Solving linear unbranched pathways with Michaelis-Menten kinetics using the Lambert \(W\)-function
- Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem
- New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
- Computation of solutions to the generalized Michaelis-Menton equation
- Asymptotic expansions in enzyme reactions with high enzyme concentrations
- On the qualitative behaviour of oscillating biochemical systems: the stochastic approach
- Singular Perturbation Techniques and Asymptotic Expansions for Some Complex Enzyme Reactions
- Leading order asymptotics in the Goldbeter-Koshland switch
- Quasi-steady-state approximations derived from the stochastic model of enzyme kinetics
- The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics
- On the appropriate use of asymptotic expansions in enzyme kinetics
- Michaelis-Menten equation for degradation of insoluble substrate
- Algorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanism
- Ramp approximations of Michaelis-Menten functions in a model of plant metabolism
- Uniform Asymptotic Expansions beyond the tQSSA for the Goldbeter--Koshland Switch
- Upper and lower bounds from the maximum principle. Intercellular diffusion with Michaelis-Menten kinetics
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