Pages that link to "Item:Q253479"

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)
• The Michaelis-Menten-Stueckelberg theorem (Q400860) (← links)
• Is there anything left to say on enzyme kinetic constants and quasi-steady state approximation? (Q431971) (← links)
• A note on the kinetics of suicide substrates (Q454298) (← 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)
• On the validity of the quasi-steady state approximation of bimolecular reactions in solution (Q781235) (← links)
• Enzyme kinetics at high enzyme concentration (Q886790) (← 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)
• Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations (Q1609384) (← links)
• A kinetic analysis of coupled (or auxiliary) enzyme reactions (Q1633265) (← links)
• An alternative approach to Michaelis-Menten kinetics that is based on the renormalization group (Q1642113) (← 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)
• Determination of hammerhead ribozyme kinetic constants at high molar ratio ribozyme-substrate (Q1871631) (← 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)
• On the quasi-steady-state approximation in an open Michaelis-Menten reaction mechanism (Q2130743) (← 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)
• Efficacy of quasi-steady-state approximation in Michaelis-Menten kinetics: a stochastic signature (Q2322238) (← 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)