References
- Bohacek, R. S., Dalgamo, D. C., Hatada, M., Jacobsen, V. A., Lynch, B. A., Macek, K. J., Merry, T., Metcalf III, C. A., Narula, S. S., Sawyer, T. K., Shakespeare, W. C., Violette, S. M., and Weigele, M., X-ray structure of citrate bound to Src SH2 leads to a high-affinity, bone-targeted Src SH2 inhibitor. J. Med. Cnem., 44, 660-663 (2001) https://doi.org/10.1021/jm0002681
- Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C., and Kraut, J., Crystal structures of Escherichia coli and Lactobacillus cesei dihydrofolate reductase refined at 1.7 resolution. J. Biol. Chem., 257(22), 13650-13662 (1982)
- Bruice, P. Y., Organic Chemistry (fourth eds). Prentice Hall, New Jersey, (1995)
- Bystroff, C., Oatley, S. J., and Kraut, J., Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoen-zyme and the folate NADP+ ternary complex: Substrate binoing and a model for the transition state. Biochemistry, 29, 3263-3277 (1990) https://doi.org/10.1021/bi00465a018
- Cody, V., Luft, J. R., Ciszak, E., Kalman, T. I., and Freisham, J. H., Crystal structure determination at 2.3 of recombinant hur Jar dihydrofolate reductase ternary complex with NADPH and methotrexate--tetrazole. Anticancer Drug Design, 7, 483-491 (1992)
- Cody, V. Wojtczak, A., Kalman, T. I., Freisham, J. H., and Blakley, R. L., Conformational analysis of human dihydrofolate reductase inhibitor complexes: Crystal structure determiration of wild type and F31 mutant binary and ternary inhibitor complexes. Ayling, J. E., Nair, M. G. and Baugh, C. M. (Eds.), In Chemistry and Biology of Pteridines and Folates. Plenum Press, New York, pp. 48-486, (1993)
- Cody, V., Galitsky, N., Luft, J. R., Pangborn, W., Gangjee, A., Deyraj, R., Queener, S. F., and Blakley, R. L., Comparison of ternary complexes of Pneumocystis carinii and wild type human dihydrofolate reductase with coenzyme NADPH and arovel classical antitumor furo[2,3-d]pyrimidine antifolate. Acia Crystallographica, D53, 638 (1997)
- Cody, V., Galitsky, N., Luft, J. R., Pangborn, W., Blakley, R L., and Gangjee, A., Comparison of ternary crystal complexes of F3 i variants of human dihydrofolate reductase with NADPH and a classical antitumor furopyrimidine. Anticancer Drug Des., 13, 307-315 (1998)
- Cocco, L., Roth, B., Temple, C. Jr., Montgomery, J. A., London, R. E., and Blakley, R. L., Protonated state of methotrexate, trirethoprirn, and pyrimethamine bound to dihydrofolate reeucase. Arch. Biochem. Biophys., 226, 567-577 (1983) https://doi.org/10.1016/0003-9861(83)90326-0
- Fierke, C. A., Johnson, K. A., and Benkovic, S. J., Construction and evaluation of the kinetics scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry, 26 4085-4092 (1987) https://doi.org/10.1021/bi00387a052
-
Foye W. O., Banijamali, A. R. and Patarapanich, C., Synthesis and antimicrobial activities of
$N^{4}$ -2-acetoxyethoxymethyl) thiose nlcarbazones and$N^{3}$ -(2-acetoxyethoxymethyl) thioureas. J. Pharm. Sci., 75, 1180-1184 (1986) https://doi.org/10.1002/jps.2600751213 - Foye W. O., Dabade, S. V., Kelly, C. J., Lebrun, E., and van Rapenbusch, R., Synthesis and dihydrofolate reductase inhibitory activity of N4-2-L glutaryl-N1-heteroaryl thiosemica bazones. Med. Chem. Res., 8, 542-553 (1998)
- Gokhale, V. M., and Kulkarni, V. M., Selectivity analysis of 5-(arylttlio)-2,4-diaminoquinazolines as inhibitors of Candida albicans dihydrofolate reductase by molecular dynamics siroulations. J. Comput. Aided Mol., Des. 14, 495-500 (2000) https://doi.org/10.1023/A:1008189724803
- Graffner-Nordberg, M., Marelius, J., Ohlsson, S., Persson, A., Swecberg, G., Anderson, P., Andersson, S. E., Aqvist, J., and Hallberg, A., Computational predictions of binding affinities to dihydrofolate reductase: Synthesis and biological evaluation of methotrexate analogues. J. Med. Chem., 43, 9852-3861 (2000)
- Jacques, S. L., Ejim, L. J., and Wright, G. D., Homoserine dehy-drogenase from Saccharomyces cerevisiae: Kinetic mechanism and stereochemistry of hydride transfer. Biochim. Biophys. Acta, 1544, 42-54 (2001) https://doi.org/10.1016/S0167-4838(00)00202-8
-
Lebrun, E., Tu, Y. X., van Rapenbusch, R., Banijamali, A. R., and Foye, W. O., Inhibition of bovine dihydrofolate reductase and enhancement of methotrexate sensitivity by
$N^{4}$ -(2-acetoxyethoxymethyl)-2-acetylpyridine thiosemicarbazone. Biochim. Biophys. Acta., 1034, 81-85 (1990) https://doi.org/10.1016/0304-4165(90)90156-Q - McMartin, C., and Bohacek, R. S., QXP: Powerful, rapid computer algorithms for structure-based drug design. J. Comput. Aided Mol. Des., 11, 333-344 (1997) https://doi.org/10.1023/A:1007907728892
- Meiering, E. M., and Wagner, G., Detection of long-lived bound water molecules in complexes of human dihydrofolate reductase with methotrexate and NADPH. J. Mol. BioI., 247, 294-308 (1995a) https://doi.org/10.1006/jmbi.1994.0140
- Meiering, E. M., Li, H., Delcamp, T. J., Freisheim, J. H., and Wagner, G., Contributions of tryptophan 24 and glutamate 30 to binding long-lived water molecules in the ternary complex of human dihydrofolate reductase with methotrexate and NADPH studied by site-directed mutagenesis and nuclear magnetic resonance spectroscopy. J. Mol. Biol., 247, 309-325 (1995b) https://doi.org/10.1006/jmbi.1994.0141
- Metcalf III, C. A., Eyermann, C. J., Bohacek, R. S., Haraldson, C. A., Varkhedkar, V. M., Lynch, B. A., Bartlett, C., Violette, S. M., and Sawyer, T. K., Structure-based design and solidphase parallel synthesis of phosphorylated nonpeptides to explore hydrophobic binding at the src SH2 (Src SH2) domain. J. Comb. Chem., 2, 305-313 (2000) https://doi.org/10.1021/cc990074a
- Sawaya, M., and Kraut, J., Loop and subdomain movements in the mechanism of escherichia coli dihydrofolate reductase: Crystallographic evidence. Biochemistry, 36, 586-603 (1997) https://doi.org/10.1021/bi962337c
- Schweitzer, B. I., Dicker, A. P., and Bertino, J. R., Dihydrofolate reductase as a therapeutic target. FASEB J., 4, 2441-2452 (1990) https://doi.org/10.1096/fasebj.4.8.2185970
- Shakespeare, W., Yang, M., Bohacek, R., Cerasoli, F., Stebbins, K., Sundaramoorthi, R., Azimioara, M., Vu, C., Pradeepan, S., Metcalf III, C., Haraldson, C., Merry, T., Dalgamo, D., Narula, S., Hatada, M., Lu, X., van Schravendijk, M. R, Adams, S., Violette, S., Smith, J., Guan, W, Bartlett, C., Herson, J., Luliucci, J., Weigele, M., and Sawyer, T., Structure-based design of an osteoclast-selective, nonpeptide Src homology 2 inhibitor with in vivo antiresorptive activity. Proc. Natl. Acad. Sci., 97, 9373-9378 (2000) https://doi.org/10.1073/pnas.97.17.9373
- Stilz, H. U., Guba, W., Jablonka, B., Just, M., Klingler, O., Konig, W, Wehner, V., and Zoller, G., Discovery of an orally active non-peptide fibrinogen receptor antagonist based on the hydantoin scaffold. J. Med. Chem., 44, 1158-1176 (2001) https://doi.org/10.1021/jm001068s
- Vu, C. B., Corpuz, E. G., Merry, T. J., Pradeepan, S. G., Bartlett, C., Bohacek, R. S., Botfield, M. C., Eyermann, C. J., Lynch, B. A, MacNeil, I. A., Ram, M. K., van Schravendijk, M. R., Violette, S., and Sawyer, T. K., Discovery of potent and selective SH2 inhibitors of the tyrosine kinase ZAP-70. J. Med. Chem., 42, 4088-4098 (1999) https://doi.org/10.1021/jm990229t
- Weiner, S. J., Kollman, P. A., Case, D. A., Singh, U. C., Ghio, C., Algona, C., Profeta, S., and Weiner, P., A new force field for molecular mechanical simulation of nucleic acids and proteins. J. Am. Chem. Soc., 106, 765-784 (1984) https://doi.org/10.1021/ja00315a051
- Whitlow, M., Howard, A. J., Stewart, D., Hardman, K. D., Kuyper, L. F., Baccanari, D. P., Fling, M. E., and Tansik, R. L., X-ray crystallographic studies of Candida albicans dihydrofolate reductase: High resolution structures of the holoenzyme and an inhibited ternary complex. J. Biol. Chem., 48, 30289-30298 (1997)