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Journal Abstract Search

140 related items for PubMed ID: 31211951

  • 1. Time-course of enzyme-catalyzed competing substrate degradation for michaelian behavior and for enzymes showing activation/inhibition by excess substrate.
    Goličnik M, Masson P.
    Chem Biol Interact; 2019 Aug 25; 309():108704. PubMed ID: 31211951
    [Abstract] [Full Text] [Related]

  • 2. Time-course of human cholinesterases-catalyzed competing substrate kinetics.
    Mukhametgalieva AR, Aglyamova AR, Lushchekina SV, Goličnik M, Masson P.
    Chem Biol Interact; 2019 Sep 01; 310():108702. PubMed ID: 31247192
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  • 4. Michaelis-Menten equation for degradation of insoluble substrate.
    Andersen M, Kari J, Borch K, Westh P.
    Math Biosci; 2018 Feb 01; 296():93-97. PubMed ID: 29197509
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  • 5. Sigmoidal substrate saturation curves in Michaelis-Menten mechanism as an artefact.
    Fischer E, Keleti T.
    Acta Biochim Biophys Acad Sci Hung; 1975 Feb 01; 10(3):221-7. PubMed ID: 1211106
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  • 6. Multiple alternative substrate kinetics.
    Anderson VE.
    Biochim Biophys Acta; 2015 Nov 01; 1854(11):1729-36. PubMed ID: 26051088
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  • 7. Enzyme specificity: its meaning in the general case.
    Cornish-Bowden A.
    J Theor Biol; 1984 Jun 07; 108(3):451-7. PubMed ID: 6748701
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  • 8. Kinetic analysis of enzyme systems with suicide substrate in the presence of a reversible, uncompetitive inhibitor.
    Moruno-Dávila MA, Solo CG, García-Moreno M, García-Cánovas F, Varón R.
    Biosystems; 2001 Jun 07; 61(1):5-14. PubMed ID: 11448521
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  • 10. 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 07; 219():17-27. PubMed ID: 27677118
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  • 11. Analysis of enzyme specificity by multiple substrate kinetics.
    Schellenberger V, Siegel RA, Rutter WJ.
    Biochemistry; 1993 Apr 27; 32(16):4344-8. PubMed ID: 8476864
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  • 12. Progress curves of reactions catalyzed by unstable enzymes. A theoretical approach.
    Duggleby RG.
    J Theor Biol; 1986 Nov 07; 123(1):67-80. PubMed ID: 3626585
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  • 13. Analysis of progress curves for a highly concentrated Michaelian enzyme in the presence or absence of product inhibition.
    Kellershohn N, Laurent M.
    Biochem J; 1985 Oct 01; 231(1):65-74. PubMed ID: 4062893
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  • 14. Thermodynamic Activity-Based Progress Curve Analysis in Enzyme Kinetics.
    Pleiss J.
    Trends Biotechnol; 2018 Mar 01; 36(3):234-238. PubMed ID: 29107319
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