Pages that link to "Item:Q253479"
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The following pages link to Michaelis-Menten kinetics at high enzyme concentrations (Q253479):
Displaying 50 items.
- A new piecewise spectral homotopy analysisof the Michaelis-Menten enzymatic reactions model (Q398592) (← links)
- Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation? (Q431971) (← links)
- Applying structural transition theory to describe enzyme kinetics in heterogeneous systems (Q460904) (← links)
- Solution method for the transformed time-dependent Michaelis-Menten enzymatic reaction model (Q500690) (← links)
- Dynamics of a system for migration from proliferative to dormant status (Q520253) (← links)
- Modeling the action of drugs on cellular enzymes by means of optimal control techniques (Q551833) (← links)
- Quasi steady-state approximations in complex intracellular signal transduction networks - a word of caution (Q551897) (← links)
- Simplification of a complex signal transduction model using invariants and flow equivalent servers (Q652148) (← links)
- Enzyme kinetics with a twist (Q652718) (← links)
- A perturbation solution of Michaelis-Menten kinetics in a ``total'' framework (Q714677) (← links)
- Extension and justification of quasi-steady-state approximation for reversible bimolecular binding (Q887141) (← links)
- Deterministic and stochastic models of enzymatic networks-applications to pharmaceutical research (Q929149) (← links)
- The total quasi-steady-state approximation for complex enzyme reactions (Q1010015) (← links)
- Krylov and steady-state techniques for the solution of the chemical master equation for the mitogen-activated protein kinase cascade (Q1027792) (← links)
- A kinetic analysis of coupled (or auxiliary) enzyme reactions (Q1633265) (← links)
- Michaelis-Menten equation for degradation of insoluble substrate (Q1698530) (← links)
- Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions (Q1708501) (← links)
- Operating regimes of covalent modification cycles at high enzyme concentrations (Q1746117) (← links)
- Guaranteed error bounds for structured complexity reduction of biochemical networks (Q1784387) (← 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)
- Repair of irradiated cells by Michaelis-Menten enzyme catalysis: the Lambert function for integrated rate equations in description of surviving fractions (Q2014806) (← links)
- The total quasi-steady-state for multiple alternative substrate reactions (Q2143462) (← links)
- On the anti-quasi-steady-state conditions of enzyme kinetics (Q2164666) (← 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)
- Long-term behaviours of autocatalytic sets (Q2235506) (← links)
- On a stochastic approach to model the double phosphorylation/dephosphorylation cycle (Q2245650) (← links)
- Reduced models of networks of coupled enzymatic reactions (Q2263461) (← 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)
- Introducing total substrates simplifies theoretical analysis at non-negligible enzyme concentrations: pseudo first-order kinetics and the loss of zero-order ultrasensitivity (Q2340012) (← links)
- On the validity and errors of the pseudo-first-order kinetics in ligand-receptor binding (Q2407278) (← links)
- Layered decomposition for the model order reduction of timescale separated biochemical reaction networks (Q2415563) (← 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 transformed time-dependent Michaelis-Menten enzymatic reaction model and its asymptotic stability (Q2441094) (← 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)
- 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)
- Approximation of enzyme kinetics for high enzyme concentration by a first order perturbation approach (Q2636422) (← links)
- Asymptotic expansions in enzyme reactions with high enzyme concentrations (Q3095571) (← links)
- A collocation approach to solve the Riccati-type differential equation systems (Q4902839) (← links)
