Singular Perturbation Techniques and Asymptotic Expansions for Some Complex Enzyme Reactions
From MaRDI portal
Publication:5013644
DOI10.1007/978-3-030-34713-0_5zbMath1478.92072OpenAlexW3004153323MaRDI QIDQ5013644
A. Milanesi, Pierluigi Vellucci, Giovanna Tomassetti, Alessandro Borri, Alberto Maria Bersani
Publication date: 2 December 2021
Published in: Nonlinear Dynamics of Structures, Systems and Devices (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1007/978-3-030-34713-0_5
Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Singular perturbations for ordinary differential equations (34E15)
Cites Work
- Unnamed Item
- Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution
- A perturbation solution of Michaelis-Menten kinetics in a ``total framework
- Time-dependent closed form solutions for fully competitive enzyme reactions
- The total quasi-steady-state approximation for complex enzyme reactions
- Mathematical biology. Vol. 1: An introduction.
- Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
- A kinetic analysis of coupled (or auxiliary) enzyme reactions
- Antagonism and bistability in protein interaction networks
- Extending the quasi-steady state approximation by changing variables
- The total quasi-steady-state approximation is valid for reversible enzyme kinetics
- Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant
- Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity
- Tihonov theory and center manifolds for inhibitory mechanisms in enzyme kinetics
- The total quasi-steady-state approximation for fully competitive enzyme reactions
- New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
