메뉴 건너뛰기




Volumn 46, Issue 14, 2003, Pages 2834-2845

Docking and database screening reveal new classes of Plasmodium falciparum dihydrofolate reductase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

2 [1 [4 [(3,5 DICHLORO 4 PYRIDYL)OXY]PHENYL]ETHYLIDENE]HYDRAZINE 1 CARBOTHIOAMIDE; 4 (3,5 DICHLOROPHENOXY) N HYDROXY 3 NITROBENZAMIDINE; 4,6 DIAMINO 1,2 DIHYDRO 2,2 DIMETHYL 1 [3 (2,4,5 TRICHLOROPHENOXY)PROPOXY] 1,3,5 TRIAZINE; AMIDINE; ANTIMALARIAL AGENT; CYCLOGUANIL; DIHYDROFOLATE REDUCTASE INHIBITOR; HYDRAZINE; PYRIMETHAMINE; RCL 2894 1; SULFADOXINE; SULFONAMIDE; THIOUREA DERIVATIVE; UNCLASSIFIED DRUG; UREA;

EID: 0037784010     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030781p     Document Type: Article
Times cited : (92)

References (56)
  • 1
    • 0031728357 scopus 로고    scopus 로고
    • Malaria: A 21st century solution for an ancient disease
    • Wirth, D. Malaria: a 21st century solution for an ancient disease. Nat. Med. 1998, 4, 1360-1362.
    • (1998) Nat. Med. , vol.4 , pp. 1360-1362
    • Wirth, D.1
  • 2
    • 0000715174 scopus 로고    scopus 로고
    • Dihydrofolate reductase and antifolate resistance in malaria
    • Sirawaraporn, W. Dihydrofolate reductase and antifolate resistance in malaria. Drug Resist. Updates 1998, 1, 397-406.
    • (1998) Drug Resist. Updates , vol.1 , pp. 397-406
    • Sirawaraporn, W.1
  • 3
    • 0036358879 scopus 로고    scopus 로고
    • Resistance to antifolates in Plasmodium falciparum, the causative agent of tropical malaria
    • Warhurst, D. C. Resistance to antifolates in Plasmodium falciparum, the causative agent of tropical malaria. Sci. Prog. 2002, 85, 89-111.
    • (2002) Sci. Prog. , vol.85 , pp. 89-111
    • Warhurst, D.C.1
  • 5
    • 0033051342 scopus 로고    scopus 로고
    • Towards an understanding of drug resistance in malaria: Three-dimensional structure of Plasmodium falciparum dihydrofolate reductase by homology building
    • Lemcke, T.; Christensen, I. T.; Jorgensen, F. S. Towards an understanding of drug resistance in malaria: three-dimensional structure of Plasmodium falciparum dihydrofolate reductase by homology building. Bioorg. Med. Chem. 1999, 7, 1003-1011.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 1003-1011
    • Lemcke, T.1    Christensen, I.T.2    Jorgensen, F.S.3
  • 7
    • 0037008362 scopus 로고    scopus 로고
    • Molecular modeling of wild-type and antifolate resistant mutant Plasmodium falciparum DHFR
    • Delfino, R. T.; Santos-Filho, O. A.; Figueroa-Villar, J. D. Molecular modeling of wild-type and antifolate resistant mutant Plasmodium falciparum DHFR. Biophys. Chem. 2002, 98, 287-300.
    • (2002) Biophys. Chem. , vol.98 , pp. 287-300
    • Delfino, R.T.1    Santos-Filho, O.A.2    Figueroa-Villar, J.D.3
  • 8
    • 0031734331 scopus 로고    scopus 로고
    • Antimalarial drug discovery: Development of inhibitors of dihydrofolate reductase active in drug resistance
    • Warhurst, D. C. Antimalarial drug discovery: development of inhibitors of dihydrofolate reductase active in drug resistance. Drug Discovery Today 1998, 3, 538-546.
    • (1998) Drug Discovery Today , vol.3 , pp. 538-546
    • Warhurst, D.C.1
  • 9
    • 0034644146 scopus 로고    scopus 로고
    • Development of a lead inhibitor for the A16V+S108T mutant of dihydrofolate reductase from the cycloguanil-resistant strain (T9/94) of Plasmodium falciparum
    • Yuthavong, Y.; Vilaivan, T.; Chareonsethakul, N.; Kamchonwongpaisan, S.; Sirawaraporn, W.; Quarrell, R.; Lowe, G. Development of a lead inhibitor for the A16V+S108T mutant of dihydrofolate reductase from the cycloguanil-resistant strain (T9/94) of Plasmodium falciparum. J. Med. Chem. 2000, 43, 2738-2744.
    • (2000) J. Med. Chem. , vol.43 , pp. 2738-2744
    • Yuthavong, Y.1    Vilaivan, T.2    Chareonsethakul, N.3    Kamchonwongpaisan, S.4    Sirawaraporn, W.5    Quarrell, R.6    Lowe, G.7
  • 10
    • 0026730489 scopus 로고
    • Structure based strategies for drug design and discovery
    • Kuntz, I. D. Structure based strategies for drug design and discovery. Science 1992, 257, 1078-1082.
    • (1992) Science , vol.257 , pp. 1078-1082
    • Kuntz, I.D.1
  • 11
    • 15944378734 scopus 로고
    • A perspective of modern methods in computer-aided drug design
    • Boyd, D. B., Ed.; VCH: New York
    • Balbes, L. M.; Mascarella, S. W.; Boyd, D. B. A perspective of modern methods in computer-aided drug design. In Reviews in Computational Chemistry; Boyd, D. B., Ed.; VCH: New York, 1994; pp 337-379.
    • (1994) Reviews in Computational Chemistry , pp. 337-379
    • Balbes, L.M.1    Mascarella, S.W.2    Boyd, D.B.3
  • 12
    • 0008583952 scopus 로고
    • Challenges in structure-based drug design
    • Newton, C. G., Ed.; Academic: London
    • Kuntz, I. D.; Meng, E. C.; Shoichet, B. K. Challenges in structure-based drug design. In New Perspectives in Drug Design; Newton, C. G., Ed.; Academic: London, 1995; pp 137-153.
    • (1995) New Perspectives in Drug Design , pp. 137-153
    • Kuntz, I.D.1    Meng, E.C.2    Shoichet, B.K.3
  • 13
    • 0008613646 scopus 로고
    • Applications of computeraided drug design techniques to lead generation
    • Newton, C. G., Ed.; Academic: London
    • Mason, J. S.; McLay, I. M.; Lewis, R. A. Applications of computeraided drug design techniques to lead generation. In New Perspectives in Drug Design; Newton, C. G., Ed.; Academic: London, 1995; pp 225-253.
    • (1995) New Perspectives in Drug Design , pp. 225-253
    • Mason, J.S.1    McLay, I.M.2    Lewis, R.A.3
  • 14
    • 0027522358 scopus 로고
    • Structure-based discovery of inhibitors of thymidylate synthase
    • Shoichet, B. K.; Stroud, R. M.; Santi, D. V.; Kuntz, I. D.; Perry, K. M. Structure-based discovery of inhibitors of thymidylate synthase. Science 1993, 259, 1445-1450.
    • (1993) Science , vol.259 , pp. 1445-1450
    • Shoichet, B.K.1    Stroud, R.M.2    Santi, D.V.3    Kuntz, I.D.4    Perry, K.M.5
  • 16
    • 0030534012 scopus 로고    scopus 로고
    • Three-dimensional structure database searches
    • Boyd, D. B., Ed.; VCH: New York
    • Good, A. C.; Mason, S. J. Three-dimensional structure database searches. In Reviews in Computational Chemistry; Boyd, D. B., Ed.; VCH: New York, 1996; pp 67-110.
    • (1996) Reviews in Computational Chemistry , pp. 67-110
    • Good, A.C.1    Mason, S.J.2
  • 17
    • 0003641220 scopus 로고    scopus 로고
    • Accelrys: San Diego, CA
    • Catalyst, version 4.6; Accelrys: San Diego, CA, 2000.
    • (2000) Catalyst, Version 4.6
  • 19
    • 0023931977 scopus 로고
    • Crystal structure of human dihydrofolate reductase complexed with folate
    • Oefner, C.; D'Arcy, A.; Winkler, F. K. Crystal structure of human dihydrofolate reductase complexed with folate. Eur. J. Biochem. 1988, 174, 377-385.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 377-385
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3
  • 20
    • 0025270551 scopus 로고
    • Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate NADP+ ternary complex. Substrate binding and a model for the transition state
    • Bystroff, C.; Oatley, S. J.; Kraut, J. Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry 1990, 29, 3263-3277.
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 21
    • 0025037428 scopus 로고
    • Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate
    • Davies, J. F.; Delcamp, T. J.; Prendergast, N. J.; Ashford, V. A.; Freisheim, J. H.; Kraut, J. Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. Biochemistry 1990, 29, 9467-9479.
    • (1990) Biochemistry , vol.29 , pp. 9467-9479
    • Davies, J.F.1    Delcamp, T.J.2    Prendergast, N.J.3    Ashford, V.A.4    Freisheim, J.H.5    Kraut, J.6
  • 22
    • 0026775924 scopus 로고
    • Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin
    • McTigue, M. A.; Davies, J. F., 2nd; Kaufman, B. T.; Kraut, J. Crystal structure of chicken liver dihydrofolate reductase complexed with NADP+ and biopterin. Biochemistry 1992, 31, 7264-7273.
    • (1992) Biochemistry , vol.31 , pp. 7264-7273
    • McTigue, M.A.1    Davies J.F. II2    Kaufman, B.T.3    Kraut, J.4
  • 23
    • 0027176323 scopus 로고
    • Crystal structures of chicken liver dihydrofolate reductase: Binary thioNADP+ and ternary thioNADP+.biopterin complexes
    • McTigue, M. A.; Davies, J. F.; Kaufman, B. T.; Kraut, J. Crystal structures of chicken liver dihydrofolate reductase: binary thioNADP+ and ternary thioNADP+.biopterin complexes. Biochemistry 1993, 32, 6855-6862.
    • (1993) Biochemistry , vol.32 , pp. 6855-6862
    • McTigue, M.A.1    Davies, J.F.2    Kaufman, B.T.3    Kraut, J.4
  • 24
    • 0028985318 scopus 로고
    • Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: Mechanistic implications
    • Reyes, V. M.; Sawaya, M. R.; Brown, K. A.; Kraut, J. Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications. Biochemistry 1995, 34, 2710-2723.
    • (1995) Biochemistry , vol.34 , pp. 2710-2723
    • Reyes, V.M.1    Sawaya, M.R.2    Brown, K.A.3    Kraut, J.4
  • 25
    • 0031798641 scopus 로고    scopus 로고
    • Comparison of ternary crystal complexes of F31 variants of human dihydrofolate reductase with NADPH and a classical antitumor furopyrimidine
    • Cody, V.; Galitsky, N.; Luft, J. R.; Pangborn, W.; Blakley, R. L.; Gangjee, A. Comparison of ternary crystal complexes of F31 variants of human dihydrofolate reductase with NADPH and a classical antitumor furopyrimidine. Anti-Cancer Drug Des. 1998, 13, 307-315.
    • (1998) Anti-Cancer Drug Des. , vol.13 , pp. 307-315
    • Cody, V.1    Galitsky, N.2    Luft, J.R.3    Pangborn, W.4    Blakley, R.L.5    Gangjee, A.6
  • 26
    • 0022546047 scopus 로고
    • Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis
    • Howell, E. E.; Villafranca, J. E.; Warren, M. S.; Oatley, S. J.; Kraut, J. Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis. Science 1986, 231, 1123-1128.
    • (1986) Science , vol.231 , pp. 1123-1128
    • Howell, E.E.1    Villafranca, J.E.2    Warren, M.S.3    Oatley, S.J.4    Kraut, J.5
  • 27
    • 0026788011 scopus 로고
    • Structure and function of alternative proton-relay mutants of dihydrofolate reductase
    • David, C. L.; Howell, E. E.; Farnum, M. F.; Villafranca, J. E.; Oatley, S. J.; Kraut, J. Structure and function of alternative proton-relay mutants of dihydrofolate reductase. Biochemistry 1992, 31, 9813-9822.
    • (1992) Biochemistry , vol.31 , pp. 9813-9822
    • David, C.L.1    Howell, E.E.2    Farnum, M.F.3    Villafranca, J.E.4    Oatley, S.J.5    Kraut, J.6
  • 28
    • 0036277069 scopus 로고    scopus 로고
    • Mutational analysis of Plasmodium falciparum dihydrofolate reductase: The role of aspartate 54 and phenylalanine 223 on catalytic activity and antifolate binding
    • Sirawaraporn, W.; Sirawaraporn, R.; Yongkiettrakul, S.; Anuwatwora, A.; Rastelli, G.; Kamchonwongpaisan, S.; Yuthavong, Y. Mutational analysis of Plasmodium falciparum dihydrofolate reductase: the role of aspartate 54 and phenylalanine 223 on catalytic activity and antifolate binding. Mol. Biochem. Parasitol. 2002, 121, 185-193.
    • (2002) Mol. Biochem. Parasitol. , vol.121 , pp. 185-193
    • Sirawaraporn, W.1    Sirawaraporn, R.2    Yongkiettrakul, S.3    Anuwatwora, A.4    Rastelli, G.5    Kamchonwongpaisan, S.6    Yuthavong, Y.7
  • 29
    • 0019490836 scopus 로고
    • Carbon-13 nuclear magnetic resonance study of protonation of methotrexate and aminopterin bound to dihydrofolate reductase
    • Cocco, L.; Groff, J. P.; Temple, C., Jr.; Montgomery, J. A.; London, R. E.; Blakley, R. L. Carbon-13 nuclear magnetic resonance study of protonation of methotrexate and aminopterin bound to dihydrofolate reductase. Biochemistry 1981, 20, 3972-3978.
    • (1981) Biochemistry , vol.20 , pp. 3972-3978
    • Cocco, L.1    Groff, J.P.2    Temple C., Jr.3    Montgomery, J.A.4    London, R.E.5    Blakley, R.L.6
  • 31
    • 0009540431 scopus 로고    scopus 로고
    • Advanced Chemistry Development: Toronto, Canada
    • ACD/log D Suite, version 4.5; Advanced Chemistry Development: Toronto, Canada.
    • ACD/log D Suite, Version 4.5
  • 32
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • Lipinski, C. A. Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods 2000, 44, 235-249.
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 33
  • 34
    • 0035324932 scopus 로고    scopus 로고
    • Comparison of the NCI open database with seven large chemical structural databases
    • Voigt, J. H.; Bienfait, B.; Wang, S.; Nicklaus, M. C. Comparison of the NCI open database with seven large chemical structural databases. J. Chem. Inf. Comput. Sci. 2001, 41, 702-712.
    • (2001) J. Chem. Inf. Comput. Sci. , vol.41 , pp. 702-712
    • Voigt, J.H.1    Bienfait, B.2    Wang, S.3    Nicklaus, M.C.4
  • 35
    • 0035254959 scopus 로고    scopus 로고
    • Docking molecules by families to increase the diversity of hits in database screens: Computational strategy and experimental evaluation
    • Su, A. I.; Lorber, D. M.; Weston, G. S.; Baase, W. A.; Matthews, B. W.; Shoichet, B. K. Docking molecules by families to increase the diversity of hits in database screens: computational strategy and experimental evaluation. Proteins 2001, 42, 279-293.
    • (2001) Proteins , vol.42 , pp. 279-293
    • Su, A.I.1    Lorber, D.M.2    Weston, G.S.3    Baase, W.A.4    Matthews, B.W.5    Shoichet, B.K.6
  • 36
    • 0030120054 scopus 로고    scopus 로고
    • Orientational sampling and rigid-body minimization in molecular docking revisited: On-the-fly optimization and degeneracy removal
    • Gschwend, D. A.; Kuntz, I. D. Orientational sampling and rigid-body minimization in molecular docking revisited: on-the-fly optimization and degeneracy removal. J. Comput.-Aided Mol. Des. 1996, 10, 123-132.
    • (1996) J. Comput.-Aided Mol. Des. , vol.10 , pp. 123-132
    • Gschwend, D.A.1    Kuntz, I.D.2
  • 37
    • 0032112137 scopus 로고    scopus 로고
    • Prediction of binding constants of protein ligands: A fast method for the prioritization of hits obtained from de novo design or 3D database search programs
    • Bohm, H. J. Prediction of binding constants of protein ligands: a fast method for the prioritization of hits obtained from de novo design or 3D database search programs. J. Comput.-Aided Mol. Des. 1998, 12, 309-323.
    • (1998) J. Comput.-Aided Mol. Des. , vol.12 , pp. 309-323
    • Bohm, H.J.1
  • 38
    • 0033545622 scopus 로고    scopus 로고
    • A general and fast scoring function for protein-ligand interactions: A simplified potential approach
    • Muegge, I.; Martin, Y. C. A general and fast scoring function for protein-ligand interactions: a simplified potential approach. J. Med. Chem. 1999, 42, 791-804.
    • (1999) J. Med. Chem. , vol.42 , pp. 791-804
    • Muegge, I.1    Martin, Y.C.2
  • 39
    • 0032993815 scopus 로고    scopus 로고
    • Scoring functions: A view from the bench
    • Tame, J. R. Scoring functions: a view from the bench. J. Comput.-Aided Mol. Des. 1999, 13, 99-108.
    • (1999) J. Comput.-Aided Mol. Des. , vol.13 , pp. 99-108
    • Tame, J.R.1
  • 41
    • 0036191826 scopus 로고    scopus 로고
    • Discovery of new inhibitors of aldose reductase from molecular docking and database screening
    • Rastelli, G.; Ferrari, A. M.; Costantino, L.; Gamberini, M. C. Discovery of new inhibitors of aldose reductase from molecular docking and database screening. Bioorg. Med. Chem. 2002, 10, 1437-1450.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 1437-1450
    • Rastelli, G.1    Ferrari, A.M.2    Costantino, L.3    Gamberini, M.C.4
  • 42
    • 0031587932 scopus 로고    scopus 로고
    • Lead discovery of inhibitors of the dihydrofolate reductase domain of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase
    • Toyoda, T.; Brobey, R. K.; Sano, G.; Horii, T.; Tomioka, N.; Itai, A. Lead discovery of inhibitors of the dihydrofolate reductase domain of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase. Biochem. Biophys. Res. Commun. 1997, 235, 515-519.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 515-519
    • Toyoda, T.1    Brobey, R.K.2    Sano, G.3    Horii, T.4    Tomioka, N.5    Itai, A.6
  • 43
    • 0028336046 scopus 로고
    • Computation and management of chemical properties in CACTVS: An extensible networked approach toward modularity and compatibility
    • Ihlenfeldt, W. D.; Takahashi, Y.; Abe, S.; Sasaki, S. Computation and management of chemical properties in CACTVS: an extensible networked approach toward modularity and compatibility. J. Chem. Inf. Comput. Sci. 1994, 34, 109-116.
    • (1994) J. Chem. Inf. Comput. Sci. , vol.34 , pp. 109-116
    • Ihlenfeldt, W.D.1    Takahashi, Y.2    Abe, S.3    Sasaki, S.4
  • 44
    • 0038613208 scopus 로고    scopus 로고
    • SUBSET is available at http://cactus.nci.nih.gov/SUBSET/.
  • 46
    • 84986432941 scopus 로고
    • Automated docking with grid based energy evaluation
    • Meng, E. C.; Shoichet, B. K.; Kuntz, I. D. Automated docking with grid based energy evaluation. J. Comput. Chem. 1992, 13, 505-524.
    • (1992) J. Comput. Chem. , vol.13 , pp. 505-524
    • Meng, E.C.1    Shoichet, B.K.2    Kuntz, I.D.3
  • 50
    • 3042524904 scopus 로고
    • A well behaved electrostatic potential based method using charge restraint for deriving atomic charges: The RESP model
    • Bayly, C. I.; Cieplak, P.; Cornell, W. D.; Kollman, P. A. A well behaved electrostatic potential based method using charge restraint for deriving atomic charges: the RESP model. J. Phys. Chem. 1993, 97, 10269-10283.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10283
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 51
    • 84986516411 scopus 로고
    • Application of the multimolecule and multiconformational RESP methodology to biopolymers charge derivation for DNA, RNA and proteins
    • Cieplak, P.; Bayly, C. I.; Cornell, W. D.; Kollman, P. A. Application of the multimolecule and multiconformational RESP methodology to biopolymers charge derivation for DNA, RNA and proteins. J. Comput. Chem. 1995, 16, 1357-1377.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1357-1377
    • Cieplak, P.1    Bayly, C.I.2    Cornell, W.D.3    Kollman, P.A.4
  • 53
    • 84946450438 scopus 로고
    • Algorithms for macromolecular dynamics and constraint dynamics
    • Van Gusteren, W. F.; Berendsen, H. J. C. Algorithms for macromolecular dynamics and constraint dynamics. Mol. Phys. 1977, 34, 1311-1327.
    • (1977) Mol. Phys. , vol.34 , pp. 1311-1327
    • Van Gusteren, W.F.1    Berendsen, H.J.C.2
  • 54
    • 0021912893 scopus 로고
    • Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate resistant Leishmania tropica
    • Meek, T. D.; Garvey, E. P.; Santi, D. V. Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate resistant Leishmania tropica. Biochemistry 1985, 24, 678-686.
    • (1985) Biochemistry , vol.24 , pp. 678-686
    • Meek, T.D.1    Garvey, E.P.2    Santi, D.V.3
  • 55
    • 0027445257 scopus 로고
    • The dihydrofolate reductase domain of Plasmodium falciparum thymidylate synthase-dihydrofolate reductase: Gene synthesis, expression, and anti-folate resistant mutants
    • Sirawaraporn, W.; Prapunwattana, P.; Sirawaraporn, R.; Yuthavong, Y.; Santi, D. V. The dihydrofolate reductase domain of Plasmodium falciparum thymidylate synthase-dihydrofolate reductase: gene synthesis, expression, and anti-folate resistant mutants. J. Biol. Chem. 1993, 268, 21637-21644.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21637-21644
    • Sirawaraporn, W.1    Prapunwattana, P.2    Sirawaraporn, R.3    Yuthavong, Y.4    Santi, D.V.5
  • 56
    • 0001131495 scopus 로고
    • Behavior and analysis of steady-state and rapid equilibrium enzyme systems
    • Segal, I. H., Ed.; Wiley-Interscience: New York
    • Segal, I. H. Behavior and analysis of steady-state and rapid equilibrium enzyme systems. In Enzyme Kinetics; Segal, I. H., Ed.; Wiley-Interscience: New York, 1975; pp 100-160.
    • (1975) Enzyme Kinetics , pp. 100-160
    • Segal, I.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.