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276 related items for PubMed ID: 30288641

  • 1. A Kinetic Analysis of Coupled (or Auxiliary) Enzyme Reactions.
    Eilertsen J, Schnell S.
    Bull Math Biol; 2018 Dec; 80(12):3154-3183. PubMed ID: 30288641
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  • 3. Phase-plane geometries in coupled enzyme assays.
    Eilertsen J, Stroberg W, Schnell S.
    Math Biosci; 2018 Dec; 306():126-135. PubMed ID: 30261179
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  • 4. On the Validity of the Stochastic Quasi-Steady-State Approximation in Open Enzyme Catalyzed Reactions: Timescale Separation or Singular Perturbation?
    Eilertsen J, Schnell S.
    Bull Math Biol; 2021 Nov 26; 84(1):7. PubMed ID: 34825985
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  • 8. The quasi-steady-state approximations revisited: Timescales, small parameters, singularities, and normal forms in enzyme kinetics.
    Eilertsen J, Schnell S.
    Math Biosci; 2020 Jul 26; 325():108339. PubMed ID: 32184091
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  • 9. The Michaelis-Menten Reaction at Low Substrate Concentrations: Pseudo-First-Order Kinetics and Conditions for Timescale Separation.
    Eilertsen J, Schnell S, Walcher S.
    Bull Math Biol; 2024 May 04; 86(6):68. PubMed ID: 38703247
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  • 13. Single molecule Michaelis-Menten equation beyond quasistatic disorder.
    Xue X, Liu F, Ou-Yang ZC.
    Phys Rev E Stat Nonlin Soft Matter Phys; 2006 Sep 04; 74(3 Pt 1):030902. PubMed ID: 17025584
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  • 14. An investigation of the relationships between rate and driving force in simple uncatalysed and enzyme-catalysed reactions with applications of the findings to chemiosmotic reactions.
    Stoner CD.
    Biochem J; 1992 Apr 15; 283 ( Pt 2)(Pt 2):541-52. PubMed ID: 1533514
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  • 15. On the estimation errors of KM and V from time-course experiments using the Michaelis-Menten equation.
    Stroberg W, Schnell S.
    Biophys Chem; 2016 Dec 15; 219():17-27. PubMed ID: 27677118
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  • 17. Practical steady-state enzyme kinetics.
    Lorsch JR.
    Methods Enzymol; 2014 Dec 15; 536():3-15. PubMed ID: 24423262
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