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153 related items for PubMed ID: 39024204

  • 1. Theory on the rate equations of Michaelis-Menten type enzyme kinetics with competitive inhibition.
    Murugan R.
    PLoS One; 2024; 19(7):e0302679. PubMed ID: 39024204
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  • 2. A steady-state approach for inhibition of heterogeneous enzyme reactions.
    Kari J, Schiano-di-Cola C, Hansen SF, Badino SF, Sørensen TH, Cavaleiro AM, Borch K, Westh P.
    Biochem J; 2020 May 29; 477(10):1971-1982. PubMed ID: 32391552
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  • 3. Validity of the Michaelis-Menten equation--steady-state or reactant stationary assumption: that is the question.
    Schnell S.
    FEBS J; 2014 Jan 29; 281(2):464-72. PubMed ID: 24245583
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  • 5. Calculation of inhibitor Ki and inhibitor type from the concentration of inhibitor for 50% inhibition for Michaelis-Menten enzymes.
    Brandt RB, Laux JE, Yates SW.
    Biochem Med Metab Biol; 1987 Jun 29; 37(3):344-9. PubMed ID: 3606895
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  • 6. Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant.
    Rami Tzafriri A, Edelman ER.
    J Theor Biol; 2007 Apr 21; 245(4):737-48. PubMed ID: 17234216
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  • 8. The unreasonable effectiveness of the total quasi-steady state approximation, and its limitations.
    Eilertsen J, Schnell S, Walcher S.
    J Theor Biol; 2024 Apr 21; 583():111770. PubMed ID: 38423205
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  • 9. The total quasi-steady-state approximation for fully competitive enzyme reactions.
    Pedersena MG, Bersani AM, Bersani E.
    Bull Math Biol; 2007 Jan 21; 69(1):433-57. PubMed ID: 16850351
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  • 11. Steady-state analysis of enzymes with non-Michaelis-Menten kinetics: The transport mechanism of Na+/K+-ATPase.
    Monti JLE, Montes MR, Rossi RC.
    J Biol Chem; 2018 Jan 26; 293(4):1373-1385. PubMed ID: 29191836
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  • 12. The kinetic effect of product instability in a Michaelis-Menten mechanism with competitive inhibition.
    Garrido-del Solo C, Moruno MA, Havsteen BH, Castellanos RV.
    Biosystems; 2000 Jan 26; 56(2-3):75-82. PubMed ID: 10880856
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  • 14. Quasi-Steady-State Approximations Derived from the Stochastic Model of Enzyme Kinetics.
    Kang HW, KhudaBukhsh WR, Koeppl H, Rempała GA.
    Bull Math Biol; 2019 May 26; 81(5):1303-1336. PubMed ID: 30756234
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  • 17. Michaelis-Menten equation for degradation of insoluble substrate.
    Andersen M, Kari J, Borch K, Westh P.
    Math Biosci; 2018 Feb 26; 296():93-97. PubMed ID: 29197509
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  • 19. 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
    [Abstract] [Full Text] [Related]

  • 20. Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible competitive inhibitor, tested by simulated progress curves.
    Moruno-Dávila MA, Garrido-del Solo C, García-Moreno M, Havsteen BH, Garcia-Sevilla F, Garcia-Cánovas F, Varón R.
    Int J Biochem Cell Biol; 2001 Feb 26; 33(2):181-91. PubMed ID: 11240375
    [Abstract] [Full Text] [Related]

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