Pages that link to "Item:Q886790"

The following pages link to Enzyme kinetics at high enzyme concentration (Q886790):

Displaying 50 items.

• Susceptibilities of an irreversible Michaelis-Menten enzyme (Q263689) (← links)
• A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model (Q398592) (← links)
• An improved method to measure all rate constants in the simplest enzyme kinetics model (Q427459) (← links)
• Computing quasi-steady state reductions (Q454281) (← links)
• Applying structural transition theory to describe enzyme kinetics in heterogeneous systems (Q460904) (← links)
• From enzyme kinetics to epidemiological models with Michaelis-Menten contact rate: design of nonstandard finite difference schemes (Q692237) (← links)
• Theoretical and computational studies of some bioreactor models (Q692268) (← links)
• A perturbation solution of Michaelis-Menten kinetics in a ``total'' framework (Q714677) (← links)
• Effects of periodic input on the quasi-steady state assumptions for enzyme-catalysed reactions (Q814942) (← links)
• Extension and justification of quasi-steady-state approximation for reversible bimolecular binding (Q887141) (← links)
• Analysis of the dynamical behavior for enzyme-catalyzed reactions with impulsive input (Q937595) (← links)
• Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations (Q1609384) (← links)
• Trend to equilibrium for a reaction-diffusion system modelling reversible enzyme reaction (Q1706280) (← links)
• Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions (Q1708501) (← links)
• All the trinomial roots, their powers and logarithms from the Lambert series, Bell polynomials and Fox-Wright function: illustration for genome multiplicity in survival of irradiated cells (Q1714102) (← links)
• Perturbation theory in the catalytic rate constant of the Henri-Michaelis-Menten enzymatic reaction (Q1936696) (← links)
• Substrate and enzyme concentration dependence of the Henri-Michaelis-Menten model probed by numerical simulation (Q1936971) (← links)
• On approximate analytical solutions of differential equations in enzyme kinetics using homotopy perturbation method (Q1945518) (← links)
• Repair of irradiated cells by Michaelis-Menten enzyme catalysis: the Lambert function for integrated rate equations in description of surviving fractions (Q2014806) (← links)
• Mathematical modeling for the prevention of methanol poisoning through ethanol by impulsive way (Q2020162) (← links)
• The total quasi-steady-state for multiple alternative substrate reactions (Q2143462) (← links)
• Stochastic enzyme kinetics and the quasi-steady-state reductions: application of the slow scale linear noise approximation à la Fenichel (Q2153739) (← links)
• Heineken, Tsuchiya and Aris: ``On the mathematical status of the pseudo-steady state hypothesis''. A classic from Volume 1 of \textit{Mathematical Biosciences} (Q2173880) (← links)
• The total quasi-steady-state approximation is valid for reversible enzyme kinetics (Q2187480) (← links)
• Analysis of compartmental models of ligand-induced endocytosis (Q2189264) (← links)
• The quasi-steady-state approximations revisited: timescales, small parameters, singularities, and normal forms in enzyme kinetics (Q2197737) (← links)
• Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant (Q2210002) (← links)
• Competitive effects in bacterial mRNA decay (Q2217734) (← links)
• Metabolic rate constants: some computational aspects (Q2228988) (← links)
• Reduced models of networks of coupled enzymatic reactions (Q2263461) (← links)
• Irreversible linear pathways in enzymatic reactions: analytical solution using the homotopy perturbation method (Q2299057) (← links)
• Efficacy of quasi-steady-state approximation in Michaelis-Menten kinetics: a stochastic signature (Q2322238) (← links)
• Maini's many contributions to mathematical enzyme kinetics: a review (Q2328226) (← links)
• Characteristic, completion or matching timescales? An analysis of temporary boundaries in enzyme kinetics (Q2328227) (← links)
• General mathematical formula for near equilibrium relaxation kinetics of basic enzyme reactions and its applications to find conformational selection steps (Q2328428) (← links)
• A new Michaelis-Menten equation valid everywhere multi-scale dynamics prevails (Q2328450) (← links)
• On the validity and errors of the pseudo-first-order kinetics in ligand-receptor binding (Q2407278) (← links)
• Approaches for the estimation of timescales in nonlinear dynamical systems: timescale separation in enzyme kinetics as a case study (Q2407293) (← links)
• Quasi-steady-state approximations derived from the stochastic model of enzyme kinetics (Q2417511) (← links)
• The total quasi-steady-state approximation for fully competitive enzyme reactions (Q2426260) (← links)
• Partial equilibrium approximations in apoptosis. I: The intracellular-signaling subsystem (Q2439162) (← links)
• A simplified perturbation solution of Michaelis-Menten kinetics equations in a ``total'' framework (Q2443858) (← links)
• Quasi-steady state in the Michaelis-Menten system (Q2470131) (← links)
• Stochastic approaches for modelling in vivo reactions (Q2490589) (← links)
• Why substrate depletion has apparent first-order kinetics in enzymatic digestion (Q2500381) (← links)
• Single-substrate enzyme kinetics: the quasi-steady-state approximation and beyond (Q2517609) (← links)
• New trends and perspectives in nonlinear intracellular dynamics: one century from Michaelis-Menten paper (Q2629039) (← links)
• Asymptotic expansions in enzyme reactions with high enzyme concentrations (Q3095571) (← links)
• Sufficient Conditions for Coordination of Coupled Nonlinear Biochemical Systems: Analysis of a Simple, Representative Example (Q4736676) (← links)
• Nonstandard finite difference schemes for Michaelis–Menten type reaction‐diffusion equations (Q4903223) (← links)