நொதி இயக்கவியல் (Tamil Wikipedia)

Analysis of information sources in references of the Wikipedia article "நொதி இயக்கவியல்" in Tamil language version.

refsWebsite

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37nih.gov

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29doi.org

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3pubmedcentral.gov

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131^st place

3archive.org

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2biochemj.org

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2sciencedirect.com

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1jbc.org

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1lemoyne.edu

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1wikimedia.org

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1annualreviews.org

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1wikipedia.org

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1asm.org

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1febsjournal.org

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annualreviews.org

arjournals.annualreviews.org

Kraut J (1977). "Serine proteases: structure and mechanism of catalysis". Annu. Rev. Biochem. 46: 331–58. doi:10.1146/annurev.bi.46.070177.001555. பப்மெட்:332063. http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.bi.46.070177.001555?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub%3dncbi.nlm.nih.gov. ^{[தொடர்பிழந்த இணைப்பு]}

archive.org

Northrop D (1981). "The expression of isotope effects on enzyme-catalyzed reactions". Annu. Rev. Biochem. 50: 103–31. doi:10.1146/annurev.bi.50.070181.000535. பப்மெட்:7023356. https://archive.org/details/sim_annual-review-of-biochemistry_1981_50_annual/page/103.
Christianson DW, Cox JD (1999). "Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes". Annu. Rev. Biochem. 68: 33–57. doi:10.1146/annurev.biochem.68.1.33. பப்மெட்:10872443. https://archive.org/details/sim_annual-review-of-biochemistry_1999_68/page/33.
Kraut D, Carroll K, Herschlag D (2003). "Challenges in enzyme mechanism and energetics". Annu. Rev. Biochem. 72: 517–71. doi:10.1146/annurev.biochem.72.121801.161617. பப்மெட்:12704087. https://archive.org/details/sim_annual-review-of-biochemistry_2003_72/page/517.

asm.org

mmbr.asm.org

Helmstaedt K, Krappmann S, Braus GH (September 2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiol. Mol. Biol. Rev. 65 (3): 404–21, table of contents. doi:10.1128/MMBR.65.3.404-421.2001. பப்மெட்:11528003. பப்மெட் சென்ட்ரல்:99034. http://mmbr.asm.org/cgi/content/full/65/3/404.

biochemj.org

Bravo IG, Busto F, De Arriaga D, et al. (September 2001). "A normalized plot as a novel and time-saving tool in complex enzyme kinetic analysis". Biochem. J. 358 (Pt 3): 573–83. பப்மெட்:11577687. பப்மெட் சென்ட்ரல்:1222113. http://www.biochemj.org/bj/358/0573/bj3580573.htm.
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". Biochem. J. 358 (Pt 3): 585–98. பப்மெட்:11577688. பப்மெட் சென்ட்ரல்:1222114. http://www.biochemj.org/bj/358/0585/bj3580585.htm.

doi.org

dx.doi.org

Xie XS, Lu HP (June 1999). "Single-molecule enzymology". J. Biol. Chem. 274 (23): 15967–70. doi:10.1074/jbc.274.23.15967. பப்மெட்:10347141. http://www.jbc.org/cgi/content/full/274/23/15967. பார்த்த நாள்: 2010-12-28.
Lu H (2004). "Single-molecule spectroscopy studies of conformational change dynamics in enzymatic reactions". Current pharmaceutical biotechnology 5 (3): 261–9. doi:10.2174/1389201043376887. பப்மெட்:15180547.
Schnell J, Dyson H, Wright P (2004). "Structure, dynamics, and catalytic function of dihydrofolate reductase". Annual review of biophysics and biomolecular structure 33: 119–40. doi:10.1146/annurev.biophys.33.110502.133613. பப்மெட்:15139807.
Gibson QH (1969). "Rapid mixing: Stopped flow". Methods Enzymol 16: 187–228. doi:10.1016/S0076-6879(69)16009-7.
Duggleby RG (1995). "Analysis of enzyme progress curves by non-linear regression". Methods Enzymol 249: 61–90. doi:10.1016/0076-6879(95)49031-0. பப்மெட்:7791628.
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". J. Mol. Biol. 315 (2): 121–30. doi:10.1006/jmbi.2001.5145. பப்மெட்:11779233.
Stroppolo ME, Falconi M, Caccuri AM, Desideri A (2001). "Superefficient enzymes". Cell. Mol. Life Sci. 58 (10): 1451–60. doi:10.1007/PL00000788. பப்மெட்:11693526.
Tseng SJ, Hsu JP (August 1990). "A comparison of the parameter estimating procedures for the Michaelis-Menten model". J. Theor. Biol. 145 (4): 457–64. doi:10.1016/S0022-5193(05)80481-3. பப்மெட்:2246896.
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): 839–43. doi:10.1038/nature02289. பப்மெட்:14985762.
Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)". Genome Biol. 4 (9): R54. doi:10.1186/gb-2003-4-9-r54. பப்மெட்:12952533.
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". Eur. J. Biochem. 220 (3): 645–61. doi:10.1111/j.1432-1033.1994.tb18666.x. பப்மெட்: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): 5493–9. doi:10.1021/bi00415a016. பப்மெட்:3052577.
Fisher PA (1994). "Enzymologic mechanism of replicative DNA polymerases in higher eukaryotes". Prog. Nucleic Acid Res. Mol. Biol. 47: 371–97. doi:10.1016/S0079-6603(08)60257-3. பப்மெட்:8016325.
Akerman SE, Müller S (August 2003). "2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum". Mol. Biochem. Parasitol. 130 (2): 75–81. doi:10.1016/S0166-6851(03)00161-0. பப்மெட்:12946843. http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T29-49321S6-2&_coverDate=08%2F31%2F2003&_alid=466052639&_rdoc=1&_fmt=&_orig=search&_qd=1&_cdi=4913&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=965e18a4c2ad0af711ba05d1a46dc855. பார்த்த நாள்: 2010-12-28.
Kraut J (1977). "Serine proteases: structure and mechanism of catalysis". Annu. Rev. Biochem. 46: 331–58. doi:10.1146/annurev.bi.46.070177.001555. பப்மெட்:332063. http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.bi.46.070177.001555?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub%3dncbi.nlm.nih.gov. ^{[தொடர்பிழந்த இணைப்பு]}
Ricard J, Cornish-Bowden A (July 1987). "Co-operative and allosteric enzymes: 20 years on". Eur. J. Biochem. 166 (2): 255–72. doi:10.1111/j.1432-1033.1987.tb13510.x. பப்மெட்: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): 5525–30. doi:10.1021/bi00415a021. பப்மெட்:3179266.
Helmstaedt K, Krappmann S, Braus GH (September 2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiol. Mol. Biol. Rev. 65 (3): 404–21, table of contents. doi:10.1128/MMBR.65.3.404-421.2001. பப்மெட்:11528003. பப்மெட் சென்ட்ரல்:99034. http://mmbr.asm.org/cgi/content/full/65/3/404.
Schirmer T, Evans PR (January 1990). "Structural basis of the allosteric behaviour of phosphofructokinase". Nature 343 (6254): 140–5. doi:10.1038/343140a0. பப்மெட்:2136935.
Bender ML, Begué-Cantón ML, Blakeley RL, et al. (December 1966). "The determination of the concentration of hydrolytic enzyme solutions: alpha-chymotrypsin, trypsin, papain, elastase, subtilisin, and acetylcholinesterase". J. Am. Chem. Soc. 88 (24): 5890–913. doi:10.1021/ja00976a034. பப்மெட்:5980876.
Cleland WW (January 2005). "The use of isotope effects to determine enzyme mechanisms". Arch. Biochem. Biophys. 433 (1): 2–12. doi:10.1016/j.abb.2004.08.027. பப்மெட்:15581561. http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WB5-4DD8DXJ-8&_coverDate=01%2F01%2F2005&_alid=466049795&_rdoc=1&_fmt=&_orig=search&_qd=1&_cdi=6701&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=cf322c4a1c7db6b9f89551a8469a1a2d. பார்த்த நாள்: 2010-12-28.
Northrop D (1981). "The expression of isotope effects on enzyme-catalyzed reactions". Annu. Rev. Biochem. 50: 103–31. doi:10.1146/annurev.bi.50.070181.000535. பப்மெட்:7023356. https://archive.org/details/sim_annual-review-of-biochemistry_1981_50_annual/page/103.
Cleland WW (1982). "Use of isotope effects to elucidate enzyme mechanisms". CRC Crit. Rev. Biochem. 13 (4): 385–428. doi:10.3109/10409238209108715. பப்மெட்:6759038.
Christianson DW, Cox JD (1999). "Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes". Annu. Rev. Biochem. 68: 33–57. doi:10.1146/annurev.biochem.68.1.33. பப்மெட்:10872443. https://archive.org/details/sim_annual-review-of-biochemistry_1999_68/page/33.
Kraut D, Carroll K, Herschlag D (2003). "Challenges in enzyme mechanism and energetics". Annu. Rev. Biochem. 72: 517–71. doi:10.1146/annurev.biochem.72.121801.161617. பப்மெட்:12704087. https://archive.org/details/sim_annual-review-of-biochemistry_2003_72/page/517.
Leatherbarrow RJ (December 1990). "Using linear and non-linear regression to fit biochemical data". Trends Biochem. Sci. 15 (12): 455–8. doi:10.1016/0968-0004(90)90295-M. பப்மெட்:2077683.
Koshland DE (February 1958). "Application of a Theory of Enzyme Specificity to Protein Synthesis". Proc. Natl. Acad. Sci. U.S.A. 44 (2): 98–104. doi:10.1073/pnas.44.2.98. பப்மெட்:16590179.
Hammes G (2002). "Multiple conformational changes in enzyme catalysis". Biochemistry 41 (26): 8221–8. doi:10.1021/bi0260839. பப்மெட்:12081470.
Sutcliffe M, Scrutton N (2002). "A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes". Eur. J. Biochem. 269 (13): 3096–102. doi:10.1046/j.1432-1033.2002.03020.x. பப்மெட்:12084049. http://content.febsjournal.org/cgi/content/full/269/13/3096. பார்த்த நாள்: 2010-12-28.

febsjournal.org

content.febsjournal.org

Sutcliffe M, Scrutton N (2002). "A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes". Eur. J. Biochem. 269 (13): 3096–102. doi:10.1046/j.1432-1033.2002.03020.x. பப்மெட்:12084049. http://content.febsjournal.org/cgi/content/full/269/13/3096. பார்த்த நாள்: 2010-12-28.

jbc.org

Xie XS, Lu HP (June 1999). "Single-molecule enzymology". J. Biol. Chem. 274 (23): 15967–70. doi:10.1074/jbc.274.23.15967. பப்மெட்:10347141. http://www.jbc.org/cgi/content/full/274/23/15967. பார்த்த நாள்: 2010-12-28.

lemoyne.edu

web.lemoyne.edu

மிக்கேலிசு எல். மற்றும் மென்டென் எம்.எல் Kinetik der Invertinwirkung பையோகெம். Z. 1913; 49:333–369 ஆங்கில மொழிபெயர்ப்பு ஏப்ரல் 6, 2007 அன்று அணுக்கம் செய்யப்பட்டது

nih.gov

ncbi.nlm.nih.gov

Xie XS, Lu HP (June 1999). "Single-molecule enzymology". J. Biol. Chem. 274 (23): 15967–70. doi:10.1074/jbc.274.23.15967. பப்மெட்:10347141. http://www.jbc.org/cgi/content/full/274/23/15967. பார்த்த நாள்: 2010-12-28.
Lu H (2004). "Single-molecule spectroscopy studies of conformational change dynamics in enzymatic reactions". Current pharmaceutical biotechnology 5 (3): 261–9. doi:10.2174/1389201043376887. பப்மெட்:15180547.
Schnell J, Dyson H, Wright P (2004). "Structure, dynamics, and catalytic function of dihydrofolate reductase". Annual review of biophysics and biomolecular structure 33: 119–40. doi:10.1146/annurev.biophys.33.110502.133613. பப்மெட்:15139807.
Duggleby RG (1995). "Analysis of enzyme progress curves by non-linear regression". Methods Enzymol 249: 61–90. doi:10.1016/0076-6879(95)49031-0. பப்மெட்:7791628.
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". J. Mol. Biol. 315 (2): 121–30. doi:10.1006/jmbi.2001.5145. பப்மெட்:11779233.
Stroppolo ME, Falconi M, Caccuri AM, Desideri A (2001). "Superefficient enzymes". Cell. Mol. Life Sci. 58 (10): 1451–60. doi:10.1007/PL00000788. பப்மெட்:11693526.
Jones ME (1 January 1992). "Analysis of algebraic weighted least-squares estimators for enzyme parameters". Biochem. J. 288 (Pt 2): 533–8. பப்மெட்:1463456.
Tseng SJ, Hsu JP (August 1990). "A comparison of the parameter estimating procedures for the Michaelis-Menten model". J. Theor. Biol. 145 (4): 457–64. doi:10.1016/S0022-5193(05)80481-3. பப்மெட்:2246896.
Bravo IG, Busto F, De Arriaga D, et al. (September 2001). "A normalized plot as a novel and time-saving tool in complex enzyme kinetic analysis". Biochem. J. 358 (Pt 3): 573–83. பப்மெட்:11577687. பப்மெட் சென்ட்ரல்:1222113. http://www.biochemj.org/bj/358/0573/bj3580573.htm.
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): 839–43. doi:10.1038/nature02289. பப்மெட்:14985762.
Reed JL, Vo TD, Schilling CH, Palsson BO (2003). "An expanded genome-scale model of Escherichia coli K-12 (iJR904 GSM/GPR)". Genome Biol. 4 (9): R54. doi:10.1186/gb-2003-4-9-r54. பப்மெட்:12952533.
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". Eur. J. Biochem. 220 (3): 645–61. doi:10.1111/j.1432-1033.1994.tb18666.x. பப்மெட்: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): 5493–9. doi:10.1021/bi00415a016. பப்மெட்:3052577.
Fisher PA (1994). "Enzymologic mechanism of replicative DNA polymerases in higher eukaryotes". Prog. Nucleic Acid Res. Mol. Biol. 47: 371–97. doi:10.1016/S0079-6603(08)60257-3. பப்மெட்:8016325.
Akerman SE, Müller S (August 2003). "2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum". Mol. Biochem. Parasitol. 130 (2): 75–81. doi:10.1016/S0166-6851(03)00161-0. பப்மெட்:12946843. http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T29-49321S6-2&_coverDate=08%2F31%2F2003&_alid=466052639&_rdoc=1&_fmt=&_orig=search&_qd=1&_cdi=4913&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=965e18a4c2ad0af711ba05d1a46dc855. பார்த்த நாள்: 2010-12-28.
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". Biochem. J. 358 (Pt 3): 585–98. பப்மெட்:11577688. பப்மெட் சென்ட்ரல்:1222114. http://www.biochemj.org/bj/358/0585/bj3580585.htm.
Kraut J (1977). "Serine proteases: structure and mechanism of catalysis". Annu. Rev. Biochem. 46: 331–58. doi:10.1146/annurev.bi.46.070177.001555. பப்மெட்:332063. http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.bi.46.070177.001555?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub%3dncbi.nlm.nih.gov. ^{[தொடர்பிழந்த இணைப்பு]}
Ricard J, Cornish-Bowden A (July 1987). "Co-operative and allosteric enzymes: 20 years on". Eur. J. Biochem. 166 (2): 255–72. doi:10.1111/j.1432-1033.1987.tb13510.x. பப்மெட்: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): 5525–30. doi:10.1021/bi00415a021. பப்மெட்:3179266.
Helmstaedt K, Krappmann S, Braus GH (September 2001). "Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase". Microbiol. Mol. Biol. Rev. 65 (3): 404–21, table of contents. doi:10.1128/MMBR.65.3.404-421.2001. பப்மெட்:11528003. பப்மெட் சென்ட்ரல்:99034. http://mmbr.asm.org/cgi/content/full/65/3/404.
Schirmer T, Evans PR (January 1990). "Structural basis of the allosteric behaviour of phosphofructokinase". Nature 343 (6254): 140–5. doi:10.1038/343140a0. பப்மெட்:2136935.
Hartley BS, Kilby BA (February 1954). "The reaction of p-nitrophenyl esters with chymotrypsin and insulin". Biochem. J. 56 (2): 288–97. பப்மெட்:13140189.
Bender ML, Begué-Cantón ML, Blakeley RL, et al. (December 1966). "The determination of the concentration of hydrolytic enzyme solutions: alpha-chymotrypsin, trypsin, papain, elastase, subtilisin, and acetylcholinesterase". J. Am. Chem. Soc. 88 (24): 5890–913. doi:10.1021/ja00976a034. பப்மெட்:5980876.
Cleland WW (January 2005). "The use of isotope effects to determine enzyme mechanisms". Arch. Biochem. Biophys. 433 (1): 2–12. doi:10.1016/j.abb.2004.08.027. பப்மெட்:15581561. http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WB5-4DD8DXJ-8&_coverDate=01%2F01%2F2005&_alid=466049795&_rdoc=1&_fmt=&_orig=search&_qd=1&_cdi=6701&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=cf322c4a1c7db6b9f89551a8469a1a2d. பார்த்த நாள்: 2010-12-28.
Northrop D (1981). "The expression of isotope effects on enzyme-catalyzed reactions". Annu. Rev. Biochem. 50: 103–31. doi:10.1146/annurev.bi.50.070181.000535. பப்மெட்:7023356. https://archive.org/details/sim_annual-review-of-biochemistry_1981_50_annual/page/103.
Baillie T, Rettenmeier A (1986). "Drug biotransformation: mechanistic studies with stable isotopes". Journal of clinical pharmacology 26 (6): 448–51. பப்மெட்:3734135.
Cleland WW (1982). "Use of isotope effects to elucidate enzyme mechanisms". CRC Crit. Rev. Biochem. 13 (4): 385–428. doi:10.3109/10409238209108715. பப்மெட்:6759038.
Christianson DW, Cox JD (1999). "Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes". Annu. Rev. Biochem. 68: 33–57. doi:10.1146/annurev.biochem.68.1.33. பப்மெட்:10872443. https://archive.org/details/sim_annual-review-of-biochemistry_1999_68/page/33.
Kraut D, Carroll K, Herschlag D (2003). "Challenges in enzyme mechanism and energetics". Annu. Rev. Biochem. 72: 517–71. doi:10.1146/annurev.biochem.72.121801.161617. பப்மெட்:12704087. https://archive.org/details/sim_annual-review-of-biochemistry_2003_72/page/517.
Leatherbarrow RJ (December 1990). "Using linear and non-linear regression to fit biochemical data". Trends Biochem. Sci. 15 (12): 455–8. doi:10.1016/0968-0004(90)90295-M. பப்மெட்:2077683.
Koshland DE (February 1958). "Application of a Theory of Enzyme Specificity to Protein Synthesis". Proc. Natl. Acad. Sci. U.S.A. 44 (2): 98–104. doi:10.1073/pnas.44.2.98. பப்மெட்:16590179.
Hammes G (2002). "Multiple conformational changes in enzyme catalysis". Biochemistry 41 (26): 8221–8. doi:10.1021/bi0260839. பப்மெட்:12081470.
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