Matthews DA, Alden RA, Bolin JT, Freer ST, Hamlin R, Xuong N, Kraut J, Poe M, Williams M, Hoogsteen K (July 1977). "Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate". Science. 197 (4302): 452–5. Bibcode:1977Sci...197..452M. doi:10.1126/science.17920. PMID17920.
Osborne MJ, Schnell J, Benkovic SJ, Dyson HJ, Wright PE (August 2001). "Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism". Biochemistry. 40 (33): 9846–59. doi:10.1021/bi010621k. PMID11502178.
Rod TH, Brooks CL (July 2003). "How dihydrofolate reductase facilitates protonation of dihydrofolate". Journal of the American Chemical Society. 125 (29): 8718–9. doi:10.1021/ja035272r. PMID12862454.
Fierke CA, Johnson KA, Benkovic SJ (June 1987). "Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli". Biochemistry. 26 (13): 4085–92. doi:10.1021/bi00387a052. PMID3307916.
Reyes VM, Sawaya MR, Brown KA, Kraut J (February 1995). "Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications". Biochemistry. 34 (8): 2710–23. doi:10.1021/bi00008a039. PMID7873554.
Sawaya MR, Kraut J (January 1997). "Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence". Biochemistry. 36 (3): 586–603. doi:10.1021/bi962337c. PMID9012674.
Chen YQ, Kraut J, Blakley RL, Callender R (June 1994). "Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications". Biochemistry. 33 (23): 7021–6. doi:10.1021/bi00189a001. PMID8003467.
Narayana N, Matthews DA, Howell EE, Nguyen-huu X (November 1995). "A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site". Nature Structural Biology. 2 (11): 1018–25. doi:10.1038/nsb1195-1018. PMID7583655. S2CID11914241.
Bradrick TD, Beechem JM, Howell EE (September 1996). "Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein". Biochemistry. 35 (35): 11414–24. doi:10.1021/bi960205d. PMID8784197.
Li R, Sirawaraporn R, Chitnumsub P, Sirawaraporn W, Wooden J, Athappilly F, Turley S, Hol WG (January 2000). "Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs". Journal of Molecular Biology. 295 (2): 307–23. doi:10.1006/jmbi.1999.3328. PMID10623528. S2CID24527344.
Hawser S, Lociuro S, Islam K (March 2006). "Dihydrofolate reductase inhibitors as antibacterial agents". Biochemical Pharmacology. 71 (7): 941–8. doi:10.1016/j.bcp.2005.10.052. PMID16359642.
Narayana N, Matthews DA, Howell EE, Nguyen-huu X (November 1995). "A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site". Nature Structural Biology. 2 (11): 1018–25. doi:10.1038/nsb1195-1018. PMID7583655. S2CID11914241.
Ng SK (2012). "Generation of High-Expressing Cells by Methotrexate Amplification of Destabilized Dihydrofolate Reductase Selection Marker". Protein Expression in Mammalian Cells. Methods in Molecular Biology. Vol. 801. pp. 161–172. doi:10.1007/978-1-61779-352-3_11. ISBN978-1-61779-351-6. PMID21987253.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (February 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID8559246. S2CID4310511.
Matthews DA, Alden RA, Bolin JT, Freer ST, Hamlin R, Xuong N, Kraut J, Poe M, Williams M, Hoogsteen K (July 1977). "Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate". Science. 197 (4302): 452–5. Bibcode:1977Sci...197..452M. doi:10.1126/science.17920. PMID17920.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (February 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID8559246. S2CID4310511.
Matthews DA, Alden RA, Bolin JT, Freer ST, Hamlin R, Xuong N, Kraut J, Poe M, Williams M, Hoogsteen K (July 1977). "Dihydrofolate reductase: x-ray structure of the binary complex with methotrexate". Science. 197 (4302): 452–5. Bibcode:1977Sci...197..452M. doi:10.1126/science.17920. PMID17920.
Osborne MJ, Schnell J, Benkovic SJ, Dyson HJ, Wright PE (August 2001). "Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism". Biochemistry. 40 (33): 9846–59. doi:10.1021/bi010621k. PMID11502178.
Rod TH, Brooks CL (July 2003). "How dihydrofolate reductase facilitates protonation of dihydrofolate". Journal of the American Chemical Society. 125 (29): 8718–9. doi:10.1021/ja035272r. PMID12862454.
Fierke CA, Johnson KA, Benkovic SJ (June 1987). "Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli". Biochemistry. 26 (13): 4085–92. doi:10.1021/bi00387a052. PMID3307916.
Reyes VM, Sawaya MR, Brown KA, Kraut J (February 1995). "Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications". Biochemistry. 34 (8): 2710–23. doi:10.1021/bi00008a039. PMID7873554.
Sawaya MR, Kraut J (January 1997). "Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence". Biochemistry. 36 (3): 586–603. doi:10.1021/bi962337c. PMID9012674.
Chen YQ, Kraut J, Blakley RL, Callender R (June 1994). "Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications". Biochemistry. 33 (23): 7021–6. doi:10.1021/bi00189a001. PMID8003467.
Narayana N, Matthews DA, Howell EE, Nguyen-huu X (November 1995). "A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site". Nature Structural Biology. 2 (11): 1018–25. doi:10.1038/nsb1195-1018. PMID7583655. S2CID11914241.
Bradrick TD, Beechem JM, Howell EE (September 1996). "Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein". Biochemistry. 35 (35): 11414–24. doi:10.1021/bi960205d. PMID8784197.
Li R, Sirawaraporn R, Chitnumsub P, Sirawaraporn W, Wooden J, Athappilly F, Turley S, Hol WG (January 2000). "Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs". Journal of Molecular Biology. 295 (2): 307–23. doi:10.1006/jmbi.1999.3328. PMID10623528. S2CID24527344.
Hawser S, Lociuro S, Islam K (March 2006). "Dihydrofolate reductase inhibitors as antibacterial agents". Biochemical Pharmacology. 71 (7): 941–8. doi:10.1016/j.bcp.2005.10.052. PMID16359642.
Narayana N, Matthews DA, Howell EE, Nguyen-huu X (November 1995). "A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site". Nature Structural Biology. 2 (11): 1018–25. doi:10.1038/nsb1195-1018. PMID7583655. S2CID11914241.
Ng SK (2012). "Generation of High-Expressing Cells by Methotrexate Amplification of Destabilized Dihydrofolate Reductase Selection Marker". Protein Expression in Mammalian Cells. Methods in Molecular Biology. Vol. 801. pp. 161–172. doi:10.1007/978-1-61779-352-3_11. ISBN978-1-61779-351-6. PMID21987253.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (February 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID8559246. S2CID4310511.
Narayana N, Matthews DA, Howell EE, Nguyen-huu X (November 1995). "A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site". Nature Structural Biology. 2 (11): 1018–25. doi:10.1038/nsb1195-1018. PMID7583655. S2CID11914241.
Li R, Sirawaraporn R, Chitnumsub P, Sirawaraporn W, Wooden J, Athappilly F, Turley S, Hol WG (January 2000). "Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs". Journal of Molecular Biology. 295 (2): 307–23. doi:10.1006/jmbi.1999.3328. PMID10623528. S2CID24527344.
Narayana N, Matthews DA, Howell EE, Nguyen-huu X (November 1995). "A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site". Nature Structural Biology. 2 (11): 1018–25. doi:10.1038/nsb1195-1018. PMID7583655. S2CID11914241.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (February 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID8559246. S2CID4310511.