References analysis of the Wikipedia article "Enzyme kinetics" in the English version

arxiv.org (Global: 69^th place; English: 59^th place)

Almaas E, Kovács B, Vicsek T, Oltvai ZN, Barabási AL (February 2004). "Global organization of metabolic fluxes in the bacterium Escherichia coli". Nature. 427 (6977): 839–843. arXiv:q-bio/0403001. Bibcode:2004Natur.427..839A. doi:10.1038/nature02289. PMID 14985762. S2CID 715721.

Xue X, Liu F, Ou-Yang ZC (September 2006). "Single molecule Michaelis-Menten equation beyond quasistatic disorder". Physical Review E. 74 (3 Pt 1) 030902. arXiv:cond-mat/0604364. Bibcode:2006PhRvE..74c0902X. doi:10.1103/PhysRevE.74.030902. PMID 17025584. S2CID 41674948.

doi.org (Global: 2^nd place; English: 2^nd place)

Bothner B, Chavez R, Wei J, Strupp C, Phung Q, Schneemann A, Siuzdak G (May 2000). "Monitoring enzyme catalysis with mass spectrometry". The Journal of Biological Chemistry. 275 (18): 13455–9. doi:10.1074/jbc.275.18.13455. PMID 10788458.

Xie XS, Lu HP (June 1999). "Single-molecule enzymology". The Journal of Biological Chemistry. 274 (23): 15967–15970. doi:10.1074/jbc.274.23.15967. PMID 10347141.

Lu HP (June 2004). "Single-molecule spectroscopy studies of conformational change dynamics in enzymatic reactions". Current Pharmaceutical Biotechnology. 5 (3): 261–269. doi:10.2174/1389201043376887. PMID 15180547.

Schnell JR, Dyson HJ, Wright PE (2004). "Structure, dynamics, and catalytic function of dihydrofolate reductase". Annual Review of Biophysics and Biomolecular Structure. 33: 119–140. doi:10.1146/annurev.biophys.33.110502.133613. PMID 15139807.

Gibson QH (1969). "[6] Rapid mixing: Stopped flow". Rapid mixing: Stopped flow. Methods in Enzymology. Vol. 16. pp. 187–228. doi:10.1016/S0076-6879(69)16009-7. ISBN 978-0-12-181873-9.

Renders M, Frère JM, Toye D, Herdewijn P (September 2019). "Full Pre-Steady-State Kinetic Analysis of Single Nucleotide Incorporation by DNA Polymerases". Current Protocols in Nucleic Acid Chemistry. 78 (1) e98. doi:10.1002/cpnc.98. PMID 31529783.

Duggleby RG (1995). "[3] Analysis of enzyme progress curves by nonlinear regression". Analysis of enzyme progress curves by non-linear regression. Methods in Enzymology. Vol. 249. pp. 61–90. doi:10.1016/0076-6879(95)49031-0. ISBN 978-0-12-182150-0. PMID 7791628.

Córdova-Isaza A, Jiménez-Mármol S, Guerra Y, Salas-Sarduy E (January 2023). "Enzyme Inhibitors from Gorgonians and Soft Corals". Marine Drugs. 21 (2): 104. doi:10.3390/md21020104. PMC 9963996. PMID 36827145.

Murray JB, Dunham CM, Scott WG (January 2002). "A pH-dependent conformational change, rather than the chemical step, appears to be rate-limiting in the hammerhead ribozyme cleavage reaction". Journal of Molecular Biology. 315 (2): 121–130. doi:10.1006/jmbi.2001.5145. PMID 11779233. S2CID 18102624.

Deisseroth A, Dounce AL (July 1970). "Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role". Physiological Reviews. 50 (3): 319–75. doi:10.1152/physrev.1970.50.3.319. PMID 4912904.

Dias Gomes M, Woodley JM (October 2019). "Considerations when Measuring Biocatalyst Performance". Molecules (Basel, Switzerland). 24 (19): 3573. doi:10.3390/molecules24193573. PMC 6804192. PMID 31623317.

Stroppolo ME, Falconi M, Caccuri AM, Desideri A (September 2001). "Superefficient enzymes". Cellular and Molecular Life Sciences. 58 (10): 1451–1460. doi:10.1007/PL00000788. PMC 11337273. PMID 11693526. S2CID 24874575.

Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R (May 2011). "The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters". Biochemistry. 50 (21): 4402–4410. doi:10.1021/bi2002289. PMID 21506553.

Walsh R, Martin E, Darvesh S (January 2010). "A method to describe enzyme-catalyzed reactions by combining steady state and time course enzyme kinetic parameters". Biochimica et Biophysica Acta (BBA) - General Subjects. 1800 (1): 1–5. doi:10.1016/j.bbagen.2009.10.007. PMID 19840832.

Beal SL (December 1983). "Computation of the explicit solution to the Michaelis-Menten equation". Journal of Pharmacokinetics and Biopharmaceutics. 11 (6): 641–657. doi:10.1007/BF01059062. PMID 6689584. S2CID 32571415.

Schnell S, Mendoza C (1997). "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.

Goudar CT, Sonnad JR, Duggleby RG (January 1999). "Parameter estimation using a direct solution of the integrated Michaelis-Menten equation" (PDF). Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1429 (2): 377–383. doi:10.1016/s0167-4838(98)00247-7. PMID 9989222. Archived from the original (PDF) on 9 November 2015.

Goudar CT, Harris SK, McInerney MJ, Suflita JM (December 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.

Jones ME (December 1992). "Analysis of algebraic weighted least-squares estimators for enzyme parameters". The Biochemical Journal. 288 ( Pt 2) (Pt 2): 533–538. doi:10.1042/bj2880533. PMC 1132043. PMID 1463456.

Tseng SJ, Hsu JP (August 1990). "A comparison of the parameter estimating procedures for the Michaelis-Menten model". Journal of Theoretical Biology. 145 (4): 457–464. Bibcode:1990JThBi.145..457T. doi:10.1016/S0022-5193(05)80481-3. PMID 2246896.

Bravo IG, Busto F, De Arriaga D, Ferrero MA, Rodríguez-Aparicio LB, Martínez-Blanco H, Reglero A (September 2001). "A normalized plot as a novel and time-saving tool in complex enzyme kinetic analysis". The Biochemical Journal. 358 (Pt 3): 573–583. doi:10.1042/bj3580573. PMC 1222113. PMID 11577687.

Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)". Genome Biology. 4 (9) R54. doi:10.1186/gb-2003-4-9-r54. PMC 193654. PMID 12952533.

Galanakis CM, Patsioura A, Gekas V (2015). "Enzyme kinetics modeling as a tool to optimize food industry: a pragmatic approach based on amylolytic enzymes". Critical Reviews in Food Science and Nutrition. 55 (12): 1758–70. doi:10.1080/10408398.2012.725112. PMID 24758273.

Nienhaus K, Nienhaus GU (2017). "Different Mechanisms of Catalytic Complex Formation in Two L-Tryptophan Processing Dioxygenases". Frontiers in Molecular Biosciences. 4 94. doi:10.3389/fmolb.2017.00094. PMC 5758539. PMID 29354636.

Dirr H, Reinemer P, Huber R (March 1994). "X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function". European Journal of Biochemistry. 220 (3): 645–661. doi:10.1111/j.1432-1033.1994.tb18666.x. PMID 8143720.

Stone SR, Morrison JF (July 1988). "Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates". Biochemistry. 27 (15): 5493–5499. doi:10.1021/bi00415a016. PMID 3052577.

Fisher PA (1994). Enzymologic mechanism of replicative DNA polymerases in higher eukaryotes. Progress in Nucleic Acid Research and Molecular Biology. Vol. 47. pp. 371–97. doi:10.1016/S0079-6603(08)60257-3. ISBN 978-0-12-540047-3. PMID 8016325.

Pey AL, Megarity CF, Timson DJ (January 2019). "NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just enough mobility, in just the right places". Bioscience Reports. 39 (1) BSR20180459. doi:10.1042/BSR20180459. PMC 6328894. PMID 30518535.

Akerman SE, Müller S (August 2003). "2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum". Molecular and Biochemical Parasitology. 130 (2): 75–81. doi:10.1016/S0166-6851(03)00161-0. PMID 12946843.

Bravo IG, Barrallo S, Ferrero MA, Rodríguez-Aparicio LB, Martínez-Blanco H, Reglero A (September 2001). "Kinetic properties of the acylneuraminate cytidylyltransferase from Pasteurella haemolytica A2". The Biochemical Journal. 358 (Pt 3): 585–598. doi:10.1042/bj3580585. PMC 1222114. PMID 11577688.

Kraut J (1977). "Serine proteases: structure and mechanism of catalysis". Annual Review of Biochemistry. 46: 331–358. doi:10.1146/annurev.bi.46.070177.001555. PMID 332063.

Cornish-Bowden, Athel; Cárdenas, María Luz (1987). "Co-operativity in monomeric enzymes". J. Theor. Biol. 124 (1): 1–23. Bibcode:1987JThBi.124....1C. doi:10.1016/s0022-5193(87)80248-5. PMID 3309473.

Jarabak, Rebecca; Westley, John (1974). "Enzymic memory. Consequence of conformational mobility". Biochemistry. 13 (16): 3237–3239. doi:10.1021/bi00713a007. PMID 4842741.

Noor E, Flamholz A, Liebermeister W, Bar-Even A, Milo R (September 2013). "A note on the kinetics of enzyme action: a decomposition that highlights thermodynamic effects". FEBS Letters. 587 (17): 2772–7. Bibcode:2013FEBSL.587.2772N. doi:10.1016/j.febslet.2013.07.028. PMID 23892083.

Ricard J, Cornish-Bowden A (July 1987). "Co-operative and allosteric enzymes: 20 years on". European Journal of Biochemistry. 166 (2): 255–272. doi:10.1111/j.1432-1033.1987.tb13510.x. PMID 3301336.

Ward WH, Fersht AR (July 1988). "Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activity". Biochemistry. 27 (15): 5525–5530. doi:10.1021/bi00415a021. PMID 3179266.

Helmstaedt K, Krappmann S, Braus GH (September 2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiology and Molecular Biology Reviews. 65 (3): 404–21, table of contents. doi:10.1128/MMBR.65.3.404-421.2001. PMC 99034. PMID 11528003.

Schirmer T, Evans PR (January 1990). "Structural basis of the allosteric behaviour of phosphofructokinase". Nature. 343 (6254): 140–145. Bibcode:1990Natur.343..140S. doi:10.1038/343140a0. PMID 2136935. S2CID 4272821.

Hartley BS, Kilby BA (February 1954). "The reaction of p-nitrophenyl esters with chymotrypsin and insulin". The Biochemical Journal. 56 (2): 288–297. doi:10.1042/bj0560288. PMC 1269615. PMID 13140189.

Bender ML, Begué-Cantón ML, Blakeley RL, Brubacher LJ, Feder J, Gunter CR, et al. (December 1966). "The determination of the concentration of hydrolytic enzyme solutions: alpha-chymotrypsin, trypsin, papain, elastase, subtilisin, and acetylcholinesterase". Journal of the American Chemical Society. 88 (24): 5890–5913. Bibcode:1966JAChS..88.5890B. doi:10.1021/ja00976a034. PMID 5980876.

Cleland WW (January 2005). "The use of isotope effects to determine enzyme mechanisms". Archives of Biochemistry and Biophysics. 433 (1): 2–12. doi:10.1016/j.abb.2004.08.027. PMID 15581561.

Northrop DB (1981). "The expression of isotope effects on enzyme-catalyzed reactions". Annual Review of Biochemistry. 50: 103–131. doi:10.1146/annurev.bi.50.070181.000535. PMID 7023356.

Baillie TA, Rettenmeier AW (1986). "Drug biotransformation: mechanistic studies with stable isotopes". Journal of Clinical Pharmacology. 26 (6): 448–451. doi:10.1002/j.1552-4604.1986.tb03556.x. PMID 3734135. S2CID 39193680.

Cleland WW (1982). "Use of isotope effects to elucidate enzyme mechanisms". CRC Critical Reviews in Biochemistry. 13 (4): 385–428. doi:10.3109/10409238209108715. PMID 6759038.

Christianson DW, Cox JD (1999). "Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes". Annual Review of Biochemistry. 68: 33–57. doi:10.1146/annurev.biochem.68.1.33. PMID 10872443.

Kraut DA, Carroll KS, Herschlag D (2003). "Challenges in enzyme mechanism and energetics". Annual Review of Biochemistry. 72: 517–571. doi:10.1146/annurev.biochem.72.121801.161617. PMID 12704087.

Walsh R, Martin E, Darvesh S (December 2011). "Limitations of conventional inhibitor classifications". Integrative Biology. 3 (12): 1197–1201. doi:10.1039/c1ib00053e. PMID 22038120.

Cleland WW (February 1963). "The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection". Biochimica et Biophysica Acta. 67: 188–196. doi:10.1016/0006-3002(63)91816-x. PMID 14021669.

Walsh R, Martin E, Darvesh S (May 2007). "A versatile equation to describe reversible enzyme inhibition and activation kinetics: modeling beta-galactosidase and butyrylcholinesterase". Biochimica et Biophysica Acta (BBA) - General Subjects. 1770 (5): 733–746. doi:10.1016/j.bbagen.2007.01.001. PMID 17307293.

Hu C, Dong X (2019). "Cysteine-targeted Irreversible Inhibitors of Tyrosine Kinases and Key Interactions". Current Medicinal Chemistry. 26 (31): 5811–5824. doi:10.2174/0929867325666180713124223. PMID 30009703.

Koshland DE (February 1958). "Application of a Theory of Enzyme Specificity to Protein Synthesis". Proceedings of the National Academy of Sciences of the United States of America. 44 (2): 98–104. Bibcode:1958PNAS...44...98K. doi:10.1073/pnas.44.2.98. PMC 335371. PMID 16590179.

Hammes GG (July 2002). "Multiple conformational changes in enzyme catalysis". Biochemistry. 41 (26): 8221–8228. doi:10.1021/bi0260839. PMID 12081470.

Sutcliffe MJ, Scrutton NS (July 2002). "A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes". European Journal of Biochemistry. 269 (13): 3096–3102. doi:10.1046/j.1432-1033.2002.03020.x. PMID 12084049.

Ainsley J, Lodola A, Mulholland AJ, Christov CZ, Karabencheva-Christova TG (2018). "Combined Quantum Mechanics and Molecular Mechanics Studies of Enzymatic Reaction Mechanisms". Advances in Protein Chemistry and Structural Biology. 113: 1–32. doi:10.1016/bs.apcsb.2018.07.001. ISBN 978-0-12-813916-5. PMID 30149903.

Northrop DB, Simpson FB (April 1997). "Beyond enzyme kinetics: direct determination of mechanisms by stopped-flow mass spectrometry". Bioorganic & Medicinal Chemistry. 5 (4): 641–4. doi:10.1016/s0968-0896(97)00020-5. PMID 9158861.

Michaelis L, Menten M (1913). "Die Kinetik der Invertinwirkung" [The Kinetics of Invertase Action]. Biochem. Z. (in German). 49: 333–369.; Michaelis L, Menten ML, Johnson KA, Goody RS (October 2011). "The original Michaelis constant: translation of the 1913 Michaelis-Menten paper". Biochemistry. 50 (39): 8264–8269. doi:10.1021/bi201284u. PMC 3381512. PMID 21888353.

Briggs GE, Haldane JB (1925). "A Note on the Kinetics of Enzyme Action". The Biochemical Journal. 19 (2): 338–339. doi:10.1042/bj0190338. PMC 1259181. PMID 16743508.

Cornish-Bowden A (September 2013). "The origins of enzyme kinetics". FEBS Letters. 587 (17): 2725–30. Bibcode:2013FEBSL.587.2725C. doi:10.1016/j.febslet.2013.06.009. PMID 23791665.

Flomenbom O, Velonia K, Loos D, Masuo S, Cotlet M, Engelborghs Y, et al. (February 2005). "Stretched exponential decay and correlations in the catalytic activity of fluctuating single lipase molecules". Proceedings of the National Academy of Sciences of the United States of America. 102 (7): 2368–2372. Bibcode:2005PNAS..102.2368F. doi:10.1073/pnas.0409039102. PMC 548972. PMID 15695587.

English BP, Min W, van Oijen AM, Lee KT, Luo G, Sun H, et al. (February 2006). "Ever-fluctuating single enzyme molecules: Michaelis-Menten equation revisited". Nature Chemical Biology. 2 (2): 87–94. doi:10.1038/nchembio759. PMID 16415859. S2CID 2201882.

Lu HP, Xun L, Xie XS (December 1998). "Single-molecule enzymatic dynamics". Science. 282 (5395): 1877–1882. Bibcode:1998Sci...282.1877P. doi:10.1126/science.282.5395.1877. PMID 9836635.

Bevc S, Konc J, Stojan J, Hodošček M, Penca M, Praprotnik M, Janežič D (2011). "ENZO: a web tool for derivation and evaluation of kinetic models of enzyme catalyzed reactions". PLOS ONE. 6 (7): e22265. Bibcode:2011PLoSO...622265B. doi:10.1371/journal.pone.0022265. PMC 3139599. PMID 21818304.{{cite journal}}: CS1 maint: article number as page number (link) ENZO server

drivehq.com (Global: low place; English: low place)

rdbiotech.drivehq.com

harvard.edu (Global: 18^th place; English: 17^th place)

ui.adsabs.harvard.edu

Cornish-Bowden A (September 2013). "The origins of enzyme kinetics". FEBS Letters. 587 (17): 2725–30. Bibcode:2013FEBSL.587.2725C. doi:10.1016/j.febslet.2013.06.009. PMID 23791665.

Lu HP, Xun L, Xie XS (December 1998). "Single-molecule enzymatic dynamics". Science. 282 (5395): 1877–1882. Bibcode:1998Sci...282.1877P. doi:10.1126/science.282.5395.1877. PMID 9836635.

nih.gov (Global: 4^th place; English: 4^th place)

pubmed.ncbi.nlm.nih.gov