Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
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Cites work
- scientific article; zbMATH DE number 4079233 (Why is no real title available?)
- Enzyme kinetics at high enzyme concentration
- Extending the quasi-steady state approximation by changing variables
- On the validity of the steady state assumption of enzyme kinetics
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Cited in
(60)- The unreasonable effectiveness of the total quasi-steady state approximation, and its limitations
- Rigorous estimates for the quasi-steady state approximation of the Michaelis-Menten reaction mechanism at low enzyme concentrations
- On the validity of the steady state assumption of enzyme kinetics
- Maini's many contributions to mathematical enzyme kinetics: a review
- Enzyme kinetics: a critique of the quasi-steady-state approximation
- On the anti-quasi-steady-state conditions of enzyme kinetics
- Enzyme kinetics for a two-step enzymic reaction with comparable initial enzyme-substrate ratios
- Singular perturbation techniques and asymptotic expansions for some complex enzyme reactions
- Mechanism equivalence in enzyme-substrate reactions: Distributed differential delay in enzyme kinetics
- Enzyme kinetics of multiple alternative substrates
- Enzyme kinetics at high enzyme concentration
- Using singular perturbation theory to determine kinetic parameters in a non-standard coupled enzyme assay
- A study case for the analysis of asymptotic expansions beyond the tQSSA for inhibitory mechanisms in enzyme kinetics.
- Time-dependent closed form solutions for fully competitive enzyme reactions
- Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond
- Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation?
- How to derive flux control coefficients from the rate equations of classical enzyme kinetics
- An approximate solution for the transient kinetic behavior of enzyme- catalyzed reactions: The irreversible Michaelis-Menten kinetics
- Stochastic enzyme kinetics and the quasi-steady-state reductions: application of the slow scale linear noise approximation à la Fenichel
- Uniform asymptotic expansions beyond the tQSSA for the Goldbeter-Koshland switch
- A general solution for the steady-state kinetics of immobilized enzyme systems
- The total quasi-steady-state approximation is valid for reversible enzyme kinetics
- A note on the kinetics of suicide substrates
- Determination of kinetic parameters of enzyme-catalyzed reactions with a minimum number of velocity measurements
- The total quasi-steady-state approximation for complex enzyme reactions
- A comparative analysis of strict kinetic equations for the enzyme systems and equations obtained by the rapid equilibrium approach
- scientific article; zbMATH DE number 2233481 (Why is no real title available?)
- On the relationship between the Hill coefficients for steady-state and transient kinetic data: a criterion for concerted transitions in allosteric proteins
- Extension and justification of quasi-steady-state approximation for reversible bimolecular binding
- scientific article; zbMATH DE number 4053412 (Why is no real title available?)
- Single enzyme pathways and substrate fluctuations
- The effectiveness of synergistic enzymatic reaction with limited mediator stability
- Trend to equilibrium for a reaction-diffusion system modelling reversible enzyme reaction
- A probabilistic approach to compact steady-state kinetic equations for enzymic reactions
- A reconstruction of object properties with significant uncertainties
- Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics
- General mathematical formula for near equilibrium relaxation kinetics of basic enzyme reactions and its applications to find conformational selection steps
- Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions
- Approximation of enzyme kinetics for high enzyme concentration by a first order perturbation approach
- Stochastic approaches for modelling in vivo reactions
- Why substrate depletion has apparent first-order kinetics in enzymatic digestion
- Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem
- New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper
- Chemical chaos in enzyme kinetics
- A perturbation solution of Michaelis-Menten kinetics in a ``total framework
- Estimation of the error implicit in modelling multisubstrate biochemical reactions as lumped‐substrate systems
- Stochastic aspects of asymmetric autocatalysis and absolute asymmetric synthesis
- scientific article; zbMATH DE number 7705697 (Why is no real title available?)
- Monte Carlo simulations of enzymatic reactions in crowded media. Effect of the enzyme-obstacle relative size
- Reduction of intrinsic kinetic and thermodynamic barriers for enzyme-catalysed proton transfers from carbon acid substrates
- scientific article; zbMATH DE number 2134553 (Why is no real title available?)
- 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
- Enzyme kinetics with a twist
- Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation
- Michaelis-Menten equation for degradation of insoluble substrate
- A new Michaelis-Menten equation valid everywhere multi-scale dynamics prevails
- Algorithmic criteria for the validity of quasi-steady state and partial equilibrium models: the Michaelis-Menten reaction mechanism
- Two new regulatory properties arising from the transient phase kinetics of monocyclic enzyme cascades
- Hunting \(\varepsilon\): the origin and validity of quasi-steady-state reductions in enzyme kinetics
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