Michaelis–Menten kinetics (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Michaelis–Menten kinetics" in English language version.

refsWebsite

Global rank English rank

39doi.org

2^nd place

39nih.gov

4^th place

6semanticscholar.org

11^th place

8^th place

5harvard.edu

18^th place

17^th place

2archive.org

6^th place

2acs.org

1,248^th place

1,104^th place

1whonamedit.com

2,888^th place

2,730^th place

1lemoyne.edu

6,850^th place

8,237^th place

1worldcat.org

5^th place

1jstor.org

26^th place

20^th place

1pearsonhighered.com

low place

1psu.edu

207^th place

136^th place

1zenodo.org

621^st place

380^th place

acs.org

pubs.acs.org

Michaelis, L.; Menten, M.L. (1913). "Die Kinetik der Invertinwirkung". Biochem Z. 49: 333–369. (recent translation, and an older partial translation)
Lineweaver, H.; Burk, D. (1934). "The Determination of Enzyme Dissociation Constants". Journal of the American Chemical Society. 56 (3): 658–666. doi:10.1021/ja01318a036.

archive.org

Henri, Victor (1903). Lois Générales de l'Action des Diastases. Paris: Hermann.
Lehninger, A.L.; Nelson, D.L.; Cox, M.M. (2005). Lehninger principles of biochemistry. New York: W.H. Freeman. ISBN 978-0-7167-4339-2.

doi.org

"Symbolism and terminology in enzyme kinetics. Recommendations 1981". Eur. J. Biochem. 128 (2–3): 281–291. 1982. doi:10.1111/j.1432-1033.1982.tb06963.x.
"Symbolism and terminology in enzyme kinetics. Recommendations 1981". Arch. Biochem. Biophys. 234 (2): 732–740. 1983. doi:10.1016/0003-9861(83)90262-X.
"Symbolism and terminology in enzyme kinetics. Recommendations 1981". Biochem. J. 213 (3): 561–571. 1982. doi:10.1042/bj2130561. PMC 1152169. PMID 6615450.
Cornish-Bowden, A. (2014). "Current IUBMB recommendations on enzyme nomenclature and kinetics". Perspectives in Science. 1 (1–6): 74–87. Bibcode:2014PerSc...1...74C. doi:10.1016/j.pisc.2014.02.006.
Busch, T.; Petersen, M. (2021). "Identification and biochemical characterisation of tyrosine aminotransferase from Anthoceros agrestis unveils the conceivable entry point into rosmarinic acid biosynthesis in hornworts". Planta. 253 (5): 98. doi:10.1007/s00425-021-03623-2. PMC 8041713. PMID 33844079. S2CID 233212717.
M. A. Chrisman; M. J. Goldcamp; A. N. Rhodes; J. Riffle (2023). "Exploring Michaelis–Menten kinetics and the inhibition of catalysis in a synthetic mimic of catechol oxidase: an experiment for the inorganic chemistry or biochemistry laboratory". J. Chem. Educ. 100 (2): 893–899. Bibcode:2023JChEd.100..893C. doi:10.1021/acs.jchemed.9b01146. S2CID 255736240.
Huang, Y. Y.; Condict, L.; Richardson, S. J.; Brennan, C. S.; Kasapis, S. (2023). "Exploring the inhibitory mechanism of p-coumaric acid on α-amylase via multi-spectroscopic analysis, enzymatic inhibition assay and molecular docking". Food Hydrocolloids. 139: 19)08524. doi:10.1016/j.foodhyd.2023.108524. S2CID 256355620.
Cárdenas, M. L.; Cornish-Bowden, A.; Ureta, T. (1998). "Evolution and regulatory role of the hexokinases". Biochim. Biophys. Acta. 1401 (3): 242–264. doi:10.1016/S0167-4889(97)00150-X. PMID 9540816.
Chen, W.W.; Neipel, M.; Sorger, P.K. (2010). "Classic and contemporary approaches to modeling biochemical reactions". Genes Dev. 24 (17): 1861–1875. doi:10.1101/gad.1945410. PMC 2932968. PMID 20810646.
Yu, R.C.; Rappaport, S.M. (1997). "A lung retention model based on Michaelis–Menten-like kinetics". Environ Health Perspect. 105 (5): 496–503. doi:10.1289/ehp.97105496. PMC 1469867. PMID 9222134.
Keating, K.A.; Quinn, J.F. (1998). "Estimating species richness: the Michaelis–Menten model revisited". Oikos. 81 (2): 411–416. doi:10.2307/3547060. JSTOR 3547060.
Jones, A.W. (2010). "Evidence-based survey of the elimination rates of ethanol from blood with applications in forensic casework". Forensic Sci Int. 200 (1–3): 1–20. doi:10.1016/j.forsciint.2010.02.021. PMID 20304569.
Abedon, S.T. (2009). "Kinetics of phage-mediated biocontrol of bacteria". Foodborne Pathog Dis. 6 (7): 807–15. doi:10.1089/fpd.2008.0242. PMID 19459758.
Ding, Shinghua; Sachs, Frederick (1999). "Single Channel Properties of P2X2 Purinoceptors". The Journal of General Physiology. 113 (5): 695–720. doi:10.1085/jgp.113.5.695. PMC 2222910. PMID 10228183.
Dugdale, RCJ (1967). "Nutrient limitation in the sea: Dynamics, identification, and significance". Limnology and Oceanography. 12 (4): 685–695. Bibcode:1967LimOc..12..685D. doi:10.4319/lo.1967.12.4.0685.
Stroppolo, M.E.; Falconi, M.; Caccuri, A.M.; Desideri, A. (Sep 2001). "Superefficient enzymes". Cell Mol Life Sci. 58 (10): 1451–60. doi:10.1007/PL00000788. PMID 11693526. S2CID 24874575.
Deichmann, U.; Schuster, S.; Mazat, J.-P.; Cornish-Bowden, A. (2013). "Commemorating the 1913 Michaelis–Menten paper Die Kinetik der Invertinwirkung: three perspectives". FEBS J. 281 (2): 435–463. doi:10.1111/febs.12598. PMID 24180270. S2CID 5183178.
Van Slyke, D. D.; Cullen, G. E. (1914). "The mode of action of urease and of enzymes in general". J. Biol. Chem. 19 (2): 141–180. doi:10.1016/S0021-9258(18)88300-4.
Briggs, G.E.; Haldane, J.B.S. (1925). "A note on the kinetics of enzyme action". Biochem J. 19 (2): 338–339. doi:10.1042/bj0190338. PMC 1259181. PMID 16743508.
Zhou, H.X.; Rivas, G.; Minton, A.P. (2008). "Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences". Annu Rev Biophys. 37 (1): 375–97. doi:10.1146/annurev.biophys.37.032807.125817. PMC 2826134. PMID 18573087.
Mastro, A. M.; Babich, M. A.; Taylor, W. D.; Keith, A. D. (1984). "Diffusion of a small molecule in the cytoplasm of mammalian cells". Proc. Natl. Acad. Sci. USA. 81 (11): 3414–3418. Bibcode:1984PNAS...81.3414M. doi:10.1073/pnas.81.11.3414. PMC 345518. PMID 6328515.
Schnell, S.; Turner, T.E. (2004). "Reaction kinetics in intracellular environments with macromolecular crowding: simulations and rate laws". Prog Biophys Mol Biol. 85 (2–3): 235–60. CiteSeerX 10.1.1.117.1997. doi:10.1016/j.pbiomolbio.2004.01.012. PMID 15142746.
Segel, L.A.; Slemrod, M. (1989). "The quasi-steady-state assumption: A case study in perturbation". SIAM Review. 31 (3): 446–477. doi:10.1137/1031091.
Eadie, G. S. (1942). "The inhibition of cholinesterase by physostigmine and prostigmine". J. Biol. Chem. 146 (1): 85–93. doi:10.1016/S0021-9258(18)72452-6.
Hofstee, B. H. J. (1953). "Specificity of esterases". J. Biol. Chem. 199 (1): 357–364. doi:10.1016/S0021-9258(18)44843-0.
Hanes, C.S. (1932). "Studies on plant amylases. I. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley". Biochem. J. 26 (2): 1406–1421. doi:10.1042/bj0261406. PMC 1261052. PMID 16744959.
Lineweaver, H.; Burk, D. (1934). "The Determination of Enzyme Dissociation Constants". Journal of the American Chemical Society. 56 (3): 658–666. doi:10.1021/ja01318a036.
Lineweaver H, Burk D, Deming WE (1934). "The dissociation constant of nitrogen-nitrogenase in Azobacter". J. Amer. Chem. Soc. 56: 225–230. doi:10.1021/ja01316a071.
Eisenthal, R.; Cornish-Bowden, A. (1974). "The direct linear plot: a new graphical procedure for estimating enzyme kinetic parameters". Biochem. J. 139 (3): 715–720. doi:10.1042/bj1390715. PMC 1166335. PMID 4854723.
Greco, W.R.; Hakala, M.T. (1979). "Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors". J Biol Chem. 254 (23): 12104–12109. doi:10.1016/S0021-9258(19)86435-9. PMID 500698.
Storer, A. C.; Darlison, M. G.; Cornish-Bowden, A. (1975). "The nature of experimental error in enzyme kinetic measurements". Biochem. J. 151 (2): 361–367. doi:10.1042/bj1510361. PMC 1172366. PMID 1218083.
Askelöf, P; Korsfeldt, M; Mannervik, B (1975). "Error structure of enzyme kinetic experiments: Implications for weighting in regression-analysis of experimental-data". Eur. J. Biochem. 69 (1): 61–67. doi:10.1111/j.1432-1033.1976.tb10858.x. PMID 991863.
Mannervik, B.; Jakobson, I.; Warholm, M. (1986). "Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments". Biochem. J. 235 (3): 797–804. doi:10.1042/bj2350797. PMC 1146758. PMID 3753447.
Cornish-Bowden, A; Endrenyi, L. (1986). "Robust regression of enzyme kinetic data". Biochem. J. 234 (1): 21–29. doi:10.1042/bj2340021. PMC 1146522. PMID 3707541.
Schnell, S.; Mendoza, C. (1997). "A closed form solution for time-dependent enzyme kinetics". Journal of Theoretical Biology. 187 (2): 207–212. Bibcode:1997JThBi.187..207S. doi:10.1006/jtbi.1997.0425.
Olp, M.D.; Kalous, K.S.; Smith, B.C. (2020). "ICEKAT: an interactive online tool for calculating initial rates from continuous enzyme kinetic traces". BMC Bioinformatics. 21 (1): 186. doi:10.1186/s12859-020-3513-y. PMC 7222511. PMID 32410570. S2CID 218624836.
Goudar, C. T.; Sonnad, J. R.; Duggleby, R. G. (1999). "Parameter estimation using a direct solution of the integrated Michaelis–Menten equation". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1429 (2): 377–383. doi:10.1016/s0167-4838(98)00247-7. PMID 9989222.
Goudar, C. T.; Harris, S. K.; McInerney, M. J.; Suflita, J. M. (2004). "Progress curve analysis for enzyme and microbial kinetic reactions using explicit solutions based on the Lambert W function". Journal of Microbiological Methods. 59 (3): 317–326. doi:10.1016/j.mimet.2004.06.013. PMID 15488275.
Cleland, W. W. (1963). "The kinetics of enzyme-catalyzed reactions with two or more substrates or products: II. Inhibition: Nomenclature and theory". Biochim. Biophys. Acta. 67 (2): 173–187. doi:10.1016/0926-6569(63)90226-8. PMID 14021668.

harvard.edu

ui.adsabs.harvard.edu

Cornish-Bowden, A. (2014). "Current IUBMB recommendations on enzyme nomenclature and kinetics". Perspectives in Science. 1 (1–6): 74–87. Bibcode:2014PerSc...1...74C. doi:10.1016/j.pisc.2014.02.006.
M. A. Chrisman; M. J. Goldcamp; A. N. Rhodes; J. Riffle (2023). "Exploring Michaelis–Menten kinetics and the inhibition of catalysis in a synthetic mimic of catechol oxidase: an experiment for the inorganic chemistry or biochemistry laboratory". J. Chem. Educ. 100 (2): 893–899. Bibcode:2023JChEd.100..893C. doi:10.1021/acs.jchemed.9b01146. S2CID 255736240.
Dugdale, RCJ (1967). "Nutrient limitation in the sea: Dynamics, identification, and significance". Limnology and Oceanography. 12 (4): 685–695. Bibcode:1967LimOc..12..685D. doi:10.4319/lo.1967.12.4.0685.
Mastro, A. M.; Babich, M. A.; Taylor, W. D.; Keith, A. D. (1984). "Diffusion of a small molecule in the cytoplasm of mammalian cells". Proc. Natl. Acad. Sci. USA. 81 (11): 3414–3418. Bibcode:1984PNAS...81.3414M. doi:10.1073/pnas.81.11.3414. PMC 345518. PMID 6328515.
Schnell, S.; Mendoza, C. (1997). "A closed form solution for time-dependent enzyme kinetics". Journal of Theoretical Biology. 187 (2): 207–212. Bibcode:1997JThBi.187..207S. doi:10.1006/jtbi.1997.0425.

jstor.org

Keating, K.A.; Quinn, J.F. (1998). "Estimating species richness: the Michaelis–Menten model revisited". Oikos. 81 (2): 411–416. doi:10.2307/3547060. JSTOR 3547060.

lemoyne.edu

web.lemoyne.edu

Michaelis, L.; Menten, M.L. (1913). "Die Kinetik der Invertinwirkung". Biochem Z. 49: 333–369. (recent translation, and an older partial translation)

nih.gov

pubmed.ncbi.nlm.nih.gov

"Symbolism and terminology in enzyme kinetics. Recommendations 1981". Biochem. J. 213 (3): 561–571. 1982. doi:10.1042/bj2130561. PMC 1152169. PMID 6615450.
Busch, T.; Petersen, M. (2021). "Identification and biochemical characterisation of tyrosine aminotransferase from Anthoceros agrestis unveils the conceivable entry point into rosmarinic acid biosynthesis in hornworts". Planta. 253 (5): 98. doi:10.1007/s00425-021-03623-2. PMC 8041713. PMID 33844079. S2CID 233212717.
Cárdenas, M. L.; Cornish-Bowden, A.; Ureta, T. (1998). "Evolution and regulatory role of the hexokinases". Biochim. Biophys. Acta. 1401 (3): 242–264. doi:10.1016/S0167-4889(97)00150-X. PMID 9540816.
Chen, W.W.; Neipel, M.; Sorger, P.K. (2010). "Classic and contemporary approaches to modeling biochemical reactions". Genes Dev. 24 (17): 1861–1875. doi:10.1101/gad.1945410. PMC 2932968. PMID 20810646.
Yu, R.C.; Rappaport, S.M. (1997). "A lung retention model based on Michaelis–Menten-like kinetics". Environ Health Perspect. 105 (5): 496–503. doi:10.1289/ehp.97105496. PMC 1469867. PMID 9222134.
Jones, A.W. (2010). "Evidence-based survey of the elimination rates of ethanol from blood with applications in forensic casework". Forensic Sci Int. 200 (1–3): 1–20. doi:10.1016/j.forsciint.2010.02.021. PMID 20304569.
Abedon, S.T. (2009). "Kinetics of phage-mediated biocontrol of bacteria". Foodborne Pathog Dis. 6 (7): 807–15. doi:10.1089/fpd.2008.0242. PMID 19459758.
Ding, Shinghua; Sachs, Frederick (1999). "Single Channel Properties of P2X2 Purinoceptors". The Journal of General Physiology. 113 (5): 695–720. doi:10.1085/jgp.113.5.695. PMC 2222910. PMID 10228183.
Stroppolo, M.E.; Falconi, M.; Caccuri, A.M.; Desideri, A. (Sep 2001). "Superefficient enzymes". Cell Mol Life Sci. 58 (10): 1451–60. doi:10.1007/PL00000788. PMID 11693526. S2CID 24874575.
Deichmann, U.; Schuster, S.; Mazat, J.-P.; Cornish-Bowden, A. (2013). "Commemorating the 1913 Michaelis–Menten paper Die Kinetik der Invertinwirkung: three perspectives". FEBS J. 281 (2): 435–463. doi:10.1111/febs.12598. PMID 24180270. S2CID 5183178.
Briggs, G.E.; Haldane, J.B.S. (1925). "A note on the kinetics of enzyme action". Biochem J. 19 (2): 338–339. doi:10.1042/bj0190338. PMC 1259181. PMID 16743508.
Zhou, H.X.; Rivas, G.; Minton, A.P. (2008). "Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences". Annu Rev Biophys. 37 (1): 375–97. doi:10.1146/annurev.biophys.37.032807.125817. PMC 2826134. PMID 18573087.
Mastro, A. M.; Babich, M. A.; Taylor, W. D.; Keith, A. D. (1984). "Diffusion of a small molecule in the cytoplasm of mammalian cells". Proc. Natl. Acad. Sci. USA. 81 (11): 3414–3418. Bibcode:1984PNAS...81.3414M. doi:10.1073/pnas.81.11.3414. PMC 345518. PMID 6328515.
Schnell, S.; Turner, T.E. (2004). "Reaction kinetics in intracellular environments with macromolecular crowding: simulations and rate laws". Prog Biophys Mol Biol. 85 (2–3): 235–60. CiteSeerX 10.1.1.117.1997. doi:10.1016/j.pbiomolbio.2004.01.012. PMID 15142746.
Hanes, C.S. (1932). "Studies on plant amylases. I. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley". Biochem. J. 26 (2): 1406–1421. doi:10.1042/bj0261406. PMC 1261052. PMID 16744959.
Eisenthal, R.; Cornish-Bowden, A. (1974). "The direct linear plot: a new graphical procedure for estimating enzyme kinetic parameters". Biochem. J. 139 (3): 715–720. doi:10.1042/bj1390715. PMC 1166335. PMID 4854723.
Greco, W.R.; Hakala, M.T. (1979). "Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors". J Biol Chem. 254 (23): 12104–12109. doi:10.1016/S0021-9258(19)86435-9. PMID 500698.
Storer, A. C.; Darlison, M. G.; Cornish-Bowden, A. (1975). "The nature of experimental error in enzyme kinetic measurements". Biochem. J. 151 (2): 361–367. doi:10.1042/bj1510361. PMC 1172366. PMID 1218083.
Askelöf, P; Korsfeldt, M; Mannervik, B (1975). "Error structure of enzyme kinetic experiments: Implications for weighting in regression-analysis of experimental-data". Eur. J. Biochem. 69 (1): 61–67. doi:10.1111/j.1432-1033.1976.tb10858.x. PMID 991863.
Mannervik, B.; Jakobson, I.; Warholm, M. (1986). "Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments". Biochem. J. 235 (3): 797–804. doi:10.1042/bj2350797. PMC 1146758. PMID 3753447.
Cornish-Bowden, A; Endrenyi, L. (1986). "Robust regression of enzyme kinetic data". Biochem. J. 234 (1): 21–29. doi:10.1042/bj2340021. PMC 1146522. PMID 3707541.
Olp, M.D.; Kalous, K.S.; Smith, B.C. (2020). "ICEKAT: an interactive online tool for calculating initial rates from continuous enzyme kinetic traces". BMC Bioinformatics. 21 (1): 186. doi:10.1186/s12859-020-3513-y. PMC 7222511. PMID 32410570. S2CID 218624836.
Goudar, C. T.; Sonnad, J. R.; Duggleby, R. G. (1999). "Parameter estimation using a direct solution of the integrated Michaelis–Menten equation". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1429 (2): 377–383. doi:10.1016/s0167-4838(98)00247-7. PMID 9989222.
Goudar, C. T.; Harris, S. K.; McInerney, M. J.; Suflita, J. M. (2004). "Progress curve analysis for enzyme and microbial kinetic reactions using explicit solutions based on the Lambert W function". Journal of Microbiological Methods. 59 (3): 317–326. doi:10.1016/j.mimet.2004.06.013. PMID 15488275.
Cleland, W. W. (1963). "The kinetics of enzyme-catalyzed reactions with two or more substrates or products: II. Inhibition: Nomenclature and theory". Biochim. Biophys. Acta. 67 (2): 173–187. doi:10.1016/0926-6569(63)90226-8. PMID 14021668.

ncbi.nlm.nih.gov

"Symbolism and terminology in enzyme kinetics. Recommendations 1981". Biochem. J. 213 (3): 561–571. 1982. doi:10.1042/bj2130561. PMC 1152169. PMID 6615450.
Busch, T.; Petersen, M. (2021). "Identification and biochemical characterisation of tyrosine aminotransferase from Anthoceros agrestis unveils the conceivable entry point into rosmarinic acid biosynthesis in hornworts". Planta. 253 (5): 98. doi:10.1007/s00425-021-03623-2. PMC 8041713. PMID 33844079. S2CID 233212717.
Chen, W.W.; Neipel, M.; Sorger, P.K. (2010). "Classic and contemporary approaches to modeling biochemical reactions". Genes Dev. 24 (17): 1861–1875. doi:10.1101/gad.1945410. PMC 2932968. PMID 20810646.
Yu, R.C.; Rappaport, S.M. (1997). "A lung retention model based on Michaelis–Menten-like kinetics". Environ Health Perspect. 105 (5): 496–503. doi:10.1289/ehp.97105496. PMC 1469867. PMID 9222134.
Ding, Shinghua; Sachs, Frederick (1999). "Single Channel Properties of P2X2 Purinoceptors". The Journal of General Physiology. 113 (5): 695–720. doi:10.1085/jgp.113.5.695. PMC 2222910. PMID 10228183.
Briggs, G.E.; Haldane, J.B.S. (1925). "A note on the kinetics of enzyme action". Biochem J. 19 (2): 338–339. doi:10.1042/bj0190338. PMC 1259181. PMID 16743508.
Zhou, H.X.; Rivas, G.; Minton, A.P. (2008). "Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences". Annu Rev Biophys. 37 (1): 375–97. doi:10.1146/annurev.biophys.37.032807.125817. PMC 2826134. PMID 18573087.
Mastro, A. M.; Babich, M. A.; Taylor, W. D.; Keith, A. D. (1984). "Diffusion of a small molecule in the cytoplasm of mammalian cells". Proc. Natl. Acad. Sci. USA. 81 (11): 3414–3418. Bibcode:1984PNAS...81.3414M. doi:10.1073/pnas.81.11.3414. PMC 345518. PMID 6328515.
Hanes, C.S. (1932). "Studies on plant amylases. I. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley". Biochem. J. 26 (2): 1406–1421. doi:10.1042/bj0261406. PMC 1261052. PMID 16744959.
Eisenthal, R.; Cornish-Bowden, A. (1974). "The direct linear plot: a new graphical procedure for estimating enzyme kinetic parameters". Biochem. J. 139 (3): 715–720. doi:10.1042/bj1390715. PMC 1166335. PMID 4854723.
Storer, A. C.; Darlison, M. G.; Cornish-Bowden, A. (1975). "The nature of experimental error in enzyme kinetic measurements". Biochem. J. 151 (2): 361–367. doi:10.1042/bj1510361. PMC 1172366. PMID 1218083.
Mannervik, B.; Jakobson, I.; Warholm, M. (1986). "Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments". Biochem. J. 235 (3): 797–804. doi:10.1042/bj2350797. PMC 1146758. PMID 3753447.
Cornish-Bowden, A; Endrenyi, L. (1986). "Robust regression of enzyme kinetic data". Biochem. J. 234 (1): 21–29. doi:10.1042/bj2340021. PMC 1146522. PMID 3707541.
Olp, M.D.; Kalous, K.S.; Smith, B.C. (2020). "ICEKAT: an interactive online tool for calculating initial rates from continuous enzyme kinetic traces". BMC Bioinformatics. 21 (1): 186. doi:10.1186/s12859-020-3513-y. PMC 7222511. PMID 32410570. S2CID 218624836.

pearsonhighered.com

Mathews, C.K.; van Holde, K.E.; Ahern, K.G. (10 Dec 1999). Biochemistry (3 ed.). Prentice Hall. ISBN 978-0-8053-3066-3.

psu.edu

citeseerx.ist.psu.edu

Schnell, S.; Turner, T.E. (2004). "Reaction kinetics in intracellular environments with macromolecular crowding: simulations and rate laws". Prog Biophys Mol Biol. 85 (2–3): 235–60. CiteSeerX 10.1.1.117.1997. doi:10.1016/j.pbiomolbio.2004.01.012. PMID 15142746.

semanticscholar.org

api.semanticscholar.org

Busch, T.; Petersen, M. (2021). "Identification and biochemical characterisation of tyrosine aminotransferase from Anthoceros agrestis unveils the conceivable entry point into rosmarinic acid biosynthesis in hornworts". Planta. 253 (5): 98. doi:10.1007/s00425-021-03623-2. PMC 8041713. PMID 33844079. S2CID 233212717.
M. A. Chrisman; M. J. Goldcamp; A. N. Rhodes; J. Riffle (2023). "Exploring Michaelis–Menten kinetics and the inhibition of catalysis in a synthetic mimic of catechol oxidase: an experiment for the inorganic chemistry or biochemistry laboratory". J. Chem. Educ. 100 (2): 893–899. Bibcode:2023JChEd.100..893C. doi:10.1021/acs.jchemed.9b01146. S2CID 255736240.
Huang, Y. Y.; Condict, L.; Richardson, S. J.; Brennan, C. S.; Kasapis, S. (2023). "Exploring the inhibitory mechanism of p-coumaric acid on α-amylase via multi-spectroscopic analysis, enzymatic inhibition assay and molecular docking". Food Hydrocolloids. 139: 19)08524. doi:10.1016/j.foodhyd.2023.108524. S2CID 256355620.
Stroppolo, M.E.; Falconi, M.; Caccuri, A.M.; Desideri, A. (Sep 2001). "Superefficient enzymes". Cell Mol Life Sci. 58 (10): 1451–60. doi:10.1007/PL00000788. PMID 11693526. S2CID 24874575.
Deichmann, U.; Schuster, S.; Mazat, J.-P.; Cornish-Bowden, A. (2013). "Commemorating the 1913 Michaelis–Menten paper Die Kinetik der Invertinwirkung: three perspectives". FEBS J. 281 (2): 435–463. doi:10.1111/febs.12598. PMID 24180270. S2CID 5183178.
Olp, M.D.; Kalous, K.S.; Smith, B.C. (2020). "ICEKAT: an interactive online tool for calculating initial rates from continuous enzyme kinetic traces". BMC Bioinformatics. 21 (1): 186. doi:10.1186/s12859-020-3513-y. PMC 7222511. PMID 32410570. S2CID 218624836.

whonamedit.com

"Victor Henri". Whonamedit?. Retrieved 24 May 2011.

worldcat.org

Ninfa, Alexander; Ballou, David P. (1998). Fundamental laboratory approaches for biochemistry and biotechnology. Bethesda, Md.: Fitzgerald Science Press. ISBN 978-1-891786-00-6. OCLC 38325074.

zenodo.org

Segel, L.A.; Slemrod, M. (1989). "The quasi-steady-state assumption: A case study in perturbation". SIAM Review. 31 (3): 446–477. doi:10.1137/1031091.