메뉴 건너뛰기




Volumn 10, Issue 2, 2005, Pages 121-128

Targeting DHFR in parasitic protozoa

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DIAMINO 5 [5' [(5 CARBOXYPENTYL) 2' METHOXY]BENZYL]PYRIMIDINE; 2,4 DIAMINO 5 METHYL 6 (2',5' DIMETHOXYPHENYLTHIO)PYRROLO[2,3 D]PYRIMIDINE; 2,4 DIAMINO 6 [2' O (3 CARBOXYPROPYL)OXYDIBENZ[B,F]AZEPIN 5 YL]METHYLPTERIDINE; 4,6 DIAMINO 1,2 DIHYDRO 2,2 DIMETHYL 1 [3 (2,4,5 TRICHLOROPHENOXY)PROPOXY] 1,3,5 TRIAZINE; ATOVAQUONE; ATOVAQUONE PLUS PROGUANIL; CHLORCYCLOGUANIL; CHLORPROGUANIL; CHLORPROGUANIL PLUS DAPSONE; CLINDAMYCIN; COTRIMOXAZOLE; CYCLOGUANIL; DIHYDROFOLATE REDUCTASE; DIHYDROFOLATE REDUCTASE INHIBITOR; DIHYDROPTEROATE SYNTHASE; FANSIDAR; FOLIC ACID ANTAGONIST; FOLINIC ACID; METHOTREXATE; N [3 (2,4,5 TRICHLOROPHENOXY)PROPOXY] N' ISOPROPYLIMIDOCARBONIMIDIC DIAMIDE; PIRITREXIM; PROGUANIL; PTERIDINE DERIVATIVE; PYRIMETHAMINE; PYRIMIDINE DERIVATIVE; SULFADIAZINE; SULFADOXINE; THYMIDYLATE SYNTHASE; TRIMETHOPRIM; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 13844298790     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(04)03308-2     Document Type: Review
Times cited : (132)

References (52)
  • 1
    • 6044232985 scopus 로고    scopus 로고
    • Sneaking in through the back entrance: The biology of malaria liver stages
    • Frevert U. Sneaking in through the back entrance: the biology of malaria liver stages. Trends Parasitol. 20:2004;417-424
    • (2004) Trends Parasitol , vol.20 , pp. 417-424
    • Frevert, U.1
  • 2
    • 0033647231 scopus 로고    scopus 로고
    • Toxoplasma gondii: From animals to humans
    • Tenter A., et al. Toxoplasma gondii: from animals to humans. Int. J. Parasitol. 30:2000;1217-1258
    • (2000) Int. J. Parasitol , vol.30 , pp. 1217-1258
    • Tenter, A.1
  • 4
    • 0033658151 scopus 로고    scopus 로고
    • Epidemiology of Cryptosporidium: Transmission, detection and identification
    • Fayer R., et al. Epidemiology of Cryptosporidium: transmission, detection and identification. Int. J. Parasitol. 30:2000;1305-1322
    • (2000) Int. J. Parasitol , vol.30 , pp. 1305-1322
    • Fayer, R.1
  • 5
    • 0030623684 scopus 로고    scopus 로고
    • Cryptosporidiosis: An emerging, highly infectious threat
    • Guerrant R. Cryptosporidiosis: an emerging, highly infectious threat. Emerg. Infect. Dis. 3:1997;51-57
    • (1997) Emerg. Infect. Dis. , vol.3 , pp. 51-57
    • Guerrant, R.1
  • 6
    • 0030071699 scopus 로고    scopus 로고
    • Cryptosporidiosis: An unrecognized cause of diarrhea in elderly hospitalized patients
    • Neill M., et al. Cryptosporidiosis: an unrecognized cause of diarrhea in elderly hospitalized patients. Clin. Infect. Dis. 22:1996;168-170
    • (1996) Clin. Infect. Dis. , vol.22 , pp. 168-170
    • Neill, M.1
  • 7
    • 0028211256 scopus 로고
    • Cryptosporidiosis in child-care settings: A review of the literature and recommendations for prevention and control
    • Cordell R., et al. Cryptosporidiosis in child-care settings: a review of the literature and recommendations for prevention and control. Pediatr. Infect. Dis. J. 13:1994;310-317
    • (1994) Pediatr. Infect. Dis. J. , vol.13 , pp. 310-317
    • Cordell, R.1
  • 8
    • 0028364913 scopus 로고
    • A massive outbreak in Milwaukee of Cryptosporidium infection transmitted through the public water supply
    • MacKenzie W., et al. A massive outbreak in Milwaukee of Cryptosporidium infection transmitted through the public water supply. N. Engl. J. Med. 331:1994;161-167
    • (1994) N. Engl. J. Med. , vol.331 , pp. 161-167
    • MacKenzie, W.1
  • 9
    • 0026619403 scopus 로고
    • Antifolates: The next generation
    • Fleming G., et al. Antifolates: the next generation. Semin. Oncol. 19:1992;707-719
    • (1992) Semin. Oncol. , vol.19 , pp. 707-719
    • Fleming, G.1
  • 10
    • 0027351189 scopus 로고
    • Karnofsky Memorial Lecture: Ode to methotrexate
    • Bertino J. Karnofsky Memorial Lecture: Ode to methotrexate. J. Clin. Oncol. 11:1993;5-14
    • (1993) J. Clin. Oncol. , vol.11 , pp. 5-14
    • Bertino, J.1
  • 11
    • 0020106085 scopus 로고
    • Trimethoprim-sulfamethoxazole: An assessment of more than 12 years of use
    • Salter A. Trimethoprim-sulfamethoxazole: An assessment of more than 12 years of use. Rev. Infect. Dis. 4:1982;196-236
    • (1982) Rev. Infect. Dis. , vol.4 , pp. 196-236
    • Salter, A.1
  • 12
    • 0023123973 scopus 로고
    • 2,4-Diamino-5-benzylpyrimidines as antibacterial agents. 7. Analysis of the effect of 3,5-dialkyl substituent size and shape on binding to four different dihydrofolate reductase enzymes
    • Roth B., et al. 2,4-Diamino-5-benzylpyrimidines as antibacterial agents. 7. Analysis of the effect of 3,5-dialkyl substituent size and shape on binding to four different dihydrofolate reductase enzymes. J. Med. Chem. 30:1987;348-356
    • (1987) J. Med. Chem. , vol.30 , pp. 348-356
    • Roth, B.1
  • 13
    • 1542283603 scopus 로고    scopus 로고
    • Sustained efficacy of sulfadoxine-pyrimethamine for uncomplicated falciparum malaria in Malawi after 10 years as first-line treatment: Five-year prospective study
    • Plowe C., et al. Sustained efficacy of sulfadoxine-pyrimethamine for uncomplicated falciparum malaria in Malawi after 10 years as first-line treatment: five-year prospective study. BMJ. 328:2004;545-548
    • (2004) BMJ , vol.328 , pp. 545-548
    • Plowe, C.1
  • 14
    • 0030813699 scopus 로고    scopus 로고
    • The efficacy of antifolate antimalarial combinations in Africa: A predictive model based on pharmacodynamic and pharmacokinetic analyses
    • Watkins W., et al. The efficacy of antifolate antimalarial combinations in Africa: A predictive model based on pharmacodynamic and pharmacokinetic analyses. Parasitol. Today. 13:1997;459-464
    • (1997) Parasitol. Today , vol.13 , pp. 459-464
    • Watkins, W.1
  • 15
    • 1542267798 scopus 로고    scopus 로고
    • Gene transfer in the evolution of parasite nucleotide biosynthesis
    • Striepen B., et al. Gene transfer in the evolution of parasite nucleotide biosynthesis. Proc. Natl. Acad. Sci. U. S. A. 101:2004;3154-3159
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3154-3159
    • Striepen, B.1
  • 16
    • 11144353587 scopus 로고    scopus 로고
    • Complete genome sequence of the Apicomplexan, Cryptosporidium parvum
    • Abrahamsen M., et al. Complete genome sequence of the Apicomplexan, Cryptosporidium parvum. Science. 304:2004;441-445
    • (2004) Science , vol.304 , pp. 441-445
    • Abrahamsen, M.1
  • 17
    • 0242501573 scopus 로고    scopus 로고
    • Insights into antifolate resistance from malarial DHFR-TS structures
    • Yuvaniyama J., et al. Insights into antifolate resistance from malarial DHFR-TS structures. Nat. Struct. Biol. 10:2003;357-365
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 357-365
    • Yuvaniyama, J.1
  • 18
    • 0016234504 scopus 로고
    • Cyclization and N-dealkylation of chloro-guanide by rabbit and rat hepatic microsomes
    • Armstrong C., et al. Cyclization and N-dealkylation of chloro-guanide by rabbit and rat hepatic microsomes. Tox. App. Pharm. 29:1974;90
    • (1974) Tox. App. Pharm. , vol.29 , pp. 90
    • Armstrong, C.1
  • 19
    • 0030801206 scopus 로고    scopus 로고
    • Resistance to antifolates in Plasmodium falciparum monitored by sequence analysis of dihydropteroate synthase and dihydrofolate reductase alleles in a large number of field samples of diverse origins
    • Wang P., et al. Resistance to antifolates in Plasmodium falciparum monitored by sequence analysis of dihydropteroate synthase and dihydrofolate reductase alleles in a large number of field samples of diverse origins. Mol. Biochem. Parasitol. 89:1997;161-177
    • (1997) Mol. Biochem. Parasitol , vol.89 , pp. 161-177
    • Wang, P.1
  • 20
    • 0027083519 scopus 로고
    • Drug resistant malaria, with special reference to Thailand
    • Looareesuwan S., et al. Drug resistant malaria, with special reference to Thailand. Southeast Asian J. Trop. Med. Public Health. 23:1992;621-634
    • (1992) Southeast Asian J. Trop. Med. Public Health , vol.23 , pp. 621-634
    • Looareesuwan, S.1
  • 21
    • 0030858470 scopus 로고    scopus 로고
    • Assessment of the pharmocodynamic properties of antimalarial drugs in vivo
    • White N. Assessment of the pharmocodynamic properties of antimalarial drugs in vivo. Antimicrob. Agents Chemother. 41:1997;1413-1422
    • (1997) Antimicrob. Agents Chemother , vol.41 , pp. 1413-1422
    • White, N.1
  • 22
    • 0035702490 scopus 로고    scopus 로고
    • Pyrimethamine-sulfadoxine resistance in Plasmodium falciparum: What next?
    • Sibley C., et al. Pyrimethamine-sulfadoxine resistance in Plasmodium falciparum: what next? Trends Parasitol. 17:2001;582-588
    • (2001) Trends Parasitol , vol.17 , pp. 582-588
    • Sibley, C.1
  • 23
    • 0031037364 scopus 로고    scopus 로고
    • Antifolate-resistant mutants of Plasmodium falciparum dihydrofolate reductase
    • Sirawaraporn W., et al. Antifolate-resistant mutants of Plasmodium falciparum dihydrofolate reductase. Proc. Natl. Acad. Sci. U. S. A. 94:1997;1124-1129
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1124-1129
    • Sirawaraporn, W.1
  • 24
    • 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., et al. 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. 43:2000;2738-2744
    • (2000) J. Med. Chem. , vol.43 , pp. 2738-2744
    • Yuthavong, Y.1
  • 25
    • 0029611218 scopus 로고
    • Mechanisms of drug resistance in malaria
    • Cowman A. Mechanisms of drug resistance in malaria. Aust. N. Z. J. Med. 25:1995;837-844
    • (1995) Aust. N. Z. J. Med. , vol.25 , pp. 837-844
    • Cowman, A.1
  • 26
    • 0028933048 scopus 로고
    • In vitro activities of novel antifolate drug combinations against Plasmodium falciparum and human granulocyte CFUs
    • Winstanley P., et al. In vitro activities of novel antifolate drug combinations against Plasmodium falciparum and human granulocyte CFUs. Antimicrob. Agents Chemother. 39:1995;948-952
    • (1995) Antimicrob. Agents Chemother , vol.39 , pp. 948-952
    • Winstanley, P.1
  • 27
    • 0031963057 scopus 로고    scopus 로고
    • Kenyan Plasmodium falciparum field isolates: Correlation between pyrimethamine and chlorcycloguanil activity in vitro and point mutations in the dihydrofolate reductase domain
    • Nzila A., et al. Kenyan Plasmodium falciparum field isolates: correlation between pyrimethamine and chlorcycloguanil activity in vitro and point mutations in the dihydrofolate reductase domain. Antimicrob. Agents Chemother. 42:1998;164-169
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 164-169
    • Nzila, A.1
  • 28
    • 2942623924 scopus 로고    scopus 로고
    • Comparison of chlorproguanil-dapsone with sulfadoxine-pyrimethamine for the treatment of uncomplicated falciparum malaria in young African children: Double-blind randomised controlled trial
    • Alloueche A., et al. Comparison of chlorproguanil-dapsone with sulfadoxine-pyrimethamine for the treatment of uncomplicated falciparum malaria in young African children: double-blind randomised controlled trial. Lancet. 363:2004;1843-1848
    • (2004) Lancet , vol.363 , pp. 1843-1848
    • Alloueche, A.1
  • 29
    • 0031282343 scopus 로고    scopus 로고
    • Plasmodium falciparum: Kinetic interactions of WR99210 with pyrimethamine-sensitive and pyrimethamine-resistant dihydrofolate reductase
    • Hekmat-Nejad M., et al. Plasmodium falciparum: Kinetic interactions of WR99210 with pyrimethamine-sensitive and pyrimethamine-resistant dihydrofolate reductase. Exp. Parasitol. 87:1997;222-228
    • (1997) Exp. Parasitol , vol.87 , pp. 222-228
    • Hekmat-Nejad, M.1
  • 30
    • 0034844550 scopus 로고    scopus 로고
    • Novel alleles of the Plasmodium falciparum dhfr highly resistant to pyrimethamine and chlorcycloguanil, but not WR99210
    • Hankins E., et al. Novel alleles of the Plasmodium falciparum dhfr highly resistant to pyrimethamine and chlorcycloguanil, but not WR99210. Mol. Biochem. Paras. 117:2001;91-102
    • (2001) Mol. Biochem. Paras. , vol.117 , pp. 91-102
    • Hankins, E.1
  • 31
    • 0027180074 scopus 로고
    • PS-15: A potent, orally active antimalarial from a new class of folic acid antagonists
    • Canfield C., et al. PS-15: a potent, orally active antimalarial from a new class of folic acid antagonists. Am. J. Trop. Med. Hyg. 49:1993;121-126
    • (1993) Am. J. Trop. Med. Hyg. , vol.49 , pp. 121-126
    • Canfield, C.1
  • 32
    • 0029858680 scopus 로고    scopus 로고
    • Activity of PS-15 and its metabolite, WR99210, against Plasmodium falciparum in an in vivo-in vitro model
    • Rieckmann K., et al. Activity of PS-15 and its metabolite, WR99210, against Plasmodium falciparum in an in vivo-in vitro model. Trans. R. Soc. Trop. Med. Hyg. 90:1996;568-571
    • (1996) Trans. R. Soc. Trop. Med. Hyg. , vol.90 , pp. 568-571
    • Rieckmann, K.1
  • 33
    • 0027177889 scopus 로고
    • Identification of highly potent and selective inhibitors of Toxoplasma gondii dihydrofolate reductase
    • Chio L-C., et al. Identification of highly potent and selective inhibitors of Toxoplasma gondii dihydrofolate reductase. Antimicrob. Agents Chemother. 37:1993;1914-1923
    • (1993) Antimicrob. Agents Chemother , vol.37 , pp. 1914-1923
    • Chio, L.-C.1
  • 34
    • 0031037171 scopus 로고    scopus 로고
    • Drug treatment of HIV-related opportunistic infections
    • Klepser M., et al. Drug treatment of HIV-related opportunistic infections. Drugs. 53:1997;40-73
    • (1997) Drugs , vol.53 , pp. 40-73
    • Klepser, M.1
  • 35
    • 0036605892 scopus 로고    scopus 로고
    • The molecular basis of sulfonamide resistance in Toxoplasma gondii and implications for the clinical management of toxoplasmosis
    • Aspinall T., et al. The molecular basis of sulfonamide resistance in Toxoplasma gondii and implications for the clinical management of toxoplasmosis. J. Infect. Dis. 185:2002;1637-1643
    • (2002) J. Infect. Dis. , vol.185 , pp. 1637-1643
    • Aspinall, T.1
  • 36
    • 0027136119 scopus 로고
    • Stable molecular transformation of Toxoplasma gondii: A selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria
    • Donald R., et al. Stable molecular transformation of Toxoplasma gondii: A selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria. Proc. Natl. Acad. Sci. U. S. A. 90:1993;11703-11707
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 11703-11707
    • Donald, R.1
  • 37
    • 0035178430 scopus 로고    scopus 로고
    • Dicyclic and tricyclic diaminopyrimidine derivatives as potent inhibitors of Cryptosporidium parvum dihydrofolate reductase: Structure-activity and structure-selectivity correlations
    • Nelson R., et al. Dicyclic and tricyclic diaminopyrimidine derivatives as potent inhibitors of Cryptosporidium parvum dihydrofolate reductase: structure-activity and structure-selectivity correlations. Antimicrob. Agents Chemother. 45:2001;3293-3303
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 3293-3303
    • Nelson, R.1
  • 38
    • 0030221884 scopus 로고    scopus 로고
    • Potential antifolate resistance determinants and genotypic variation in the bifunctional dihydrofolate reductase-thymidylate synthase gene from human and bovine isolates of Cryptosporidium parvum
    • Vasquez J., et al. Potential antifolate resistance determinants and genotypic variation in the bifunctional dihydrofolate reductase-thymidylate synthase gene from human and bovine isolates of Cryptosporidium parvum. Mol. Biochem. Parasitol. 79:1996;153-165
    • (1996) Mol. Biochem. Parasitol , vol.79 , pp. 153-165
    • Vasquez, J.1
  • 39
    • 0347993050 scopus 로고    scopus 로고
    • Phylogenetic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase-thymidylate synthase
    • O'Neil R., et al. Phylogenetic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase-thymidylate synthase. J. Biol. Chem. 278:2003;52980-52987
    • (2003) J. Biol. Chem. , vol.278 , pp. 52980-52987
    • O'Neil, R.1
  • 40
    • 0028403267 scopus 로고
    • Structure of and kinetic channeling in bifunctional dihydrofolate reductase-thymidylate synthase
    • Knighton D., et al. Structure of and kinetic channeling in bifunctional dihydrofolate reductase-thymidylate synthase. Nat. Struct. Biol. 1:1994;186-194
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 186-194
    • Knighton, D.1
  • 41
    • 0033528719 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+
    • Cody V., et al. Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+. Biochemistry. 38:1999;4303-4312
    • (1999) Biochemistry , vol.38 , pp. 4303-4312
    • Cody, V.1
  • 42
    • 0027080589 scopus 로고
    • Crystal structure determination at 2.3 Å of recombinant human dihydrofolate reductase ternary complex with NADPH and methotrexate-γ- tetrazole
    • Cody V., et al. Crystal structure determination at 2.3 Å of recombinant human dihydrofolate reductase ternary complex with NADPH and methotrexate-γ-tetrazole. Anticancer Drug Des. 7:1992;483-491
    • (1992) Anticancer Drug Des. , vol.7 , pp. 483-491
    • Cody, V.1
  • 43
    • 0028774337 scopus 로고
    • The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 Å resolution
    • Champness J., et al. The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 Å resolution. Structure. 2:1994;915-924
    • (1994) Structure , vol.2 , pp. 915-924
    • Champness, J.1
  • 44
    • 0034645774 scopus 로고    scopus 로고
    • Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs
    • Li R., et al. Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs. J. Mol. Biol. 295:2000;307-323
    • (2000) J. Mol. Biol. , vol.295 , pp. 307-323
    • Li, R.1
  • 45
    • 0023931977 scopus 로고
    • Crystal structure of human dihydrofolate reductase complexed with folate
    • Oefner C., et al. Crystal structure of human dihydrofolate reductase complexed with folate. Eur. J. Biochem. 174:1988;377-385
    • (1988) Eur. J. Biochem , vol.174 , pp. 377-385
    • Oefner, C.1
  • 46
    • 0031734331 scopus 로고    scopus 로고
    • Antimalarial drug discovery: Development of inhibitors of dihydrofolate reductase active in drug resistance
    • Warhurst D. Antimalarial drug discovery: development of inhibitors of dihydrofolate reductase active in drug resistance. Drug Discov. Today. 3:1998;538-546
    • (1998) Drug Discov. Today , vol.3 , pp. 538-546
    • Warhurst, D.1
  • 47
    • 15144349302 scopus 로고    scopus 로고
    • Rational drug design approach for overcoming drug resistance: Application to pyrimethamine resistance in malaria
    • McKie J., et al. Rational drug design approach for overcoming drug resistance: application to pyrimethamine resistance in malaria. J. Med. Chem. 41:1998;1367-1370
    • (1998) J. Med. Chem. , vol.41 , pp. 1367-1370
    • McKie, J.1
  • 48
    • 9144272211 scopus 로고    scopus 로고
    • Inhibitors of multiple mutants of Plasmodium falciparum dihydrofolate reductase and their antimalarial activities
    • Kamchonwongpaisan S., et al. Inhibitors of multiple mutants of Plasmodium falciparum dihydrofolate reductase and their antimalarial activities. J. Med. Chem. 47:2004;673-680
    • (2004) J. Med. Chem. , vol.47 , pp. 673-680
    • Kamchonwongpaisan, S.1
  • 49
    • 1542298076 scopus 로고    scopus 로고
    • New 2,4-Diamino-5-(2′,5′-substituted benzyl)pyrimidines as potential drugs against opportunistic infections of AIDS and other immune disorders. Synthesis and species-dependent antifolate activity
    • Rosowsky A., et al. New 2,4-Diamino-5-(2′,5′-substituted benzyl)pyrimidines as potential drugs against opportunistic infections of AIDS and other immune disorders. Synthesis and species-dependent antifolate activity. J. Med. Chem. 47:2004;1475-1486
    • (2004) J. Med. Chem. , vol.47 , pp. 1475-1486
    • Rosowsky, A.1
  • 50
    • 0037464497 scopus 로고    scopus 로고
    • Further studies on 2,4-diamino-5-(2′,5′-disubstituted benzyl)pyrimidines as potent and selective inhibitors of dihydrofolate reductases from three major opportunistic pathogens of AIDS
    • Rosowsky A., et al. Further studies on 2,4-diamino-5-(2′,5′- disubstituted benzyl)pyrimidines as potent and selective inhibitors of dihydrofolate reductases from three major opportunistic pathogens of AIDS. J. Med. Chem. 46:2003;1726-1736
    • (2003) J. Med. Chem. , vol.46 , pp. 1726-1736
    • Rosowsky, A.1
  • 51
    • 3042594465 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of 2,4-Diamino-5-methyl-6- substituted-pyrrolo[2,3-d]pyrimidines as dihydrofolate reductase inhibitors
    • Gangjee A., et al. Design, synthesis, and biological evaluation of 2,4-Diamino-5-methyl-6-substituted-pyrrolo[2,3-d]pyrimidines as dihydrofolate reductase inhibitors. J. Med. Chem. 47:2004;3689-3692
    • (2004) J. Med. Chem. , vol.47 , pp. 3689-3692
    • Gangjee, A.1
  • 52
    • 2342468066 scopus 로고    scopus 로고
    • Synthesis of 2,4-diamino-6-[2′-O-(ω-carboxyalkyl)oxydibenz[b, f]azepin-5-yl]-methylpteridines as potent and selective inhibitors of Pneumocystis carinii, Toxoplasma gondii, and Mycobacterium avium dihydrofolate reductase
    • Rosowsky A., et al. Synthesis of 2,4-diamino-6-[2′-O-(ω- carboxyalkyl)oxydibenz[b,f]azepin-5-yl]-methylpteridines as potent and selective inhibitors of Pneumocystis carinii, Toxoplasma gondii, and Mycobacterium avium dihydrofolate reductase. J. Med. Chem. 47:2004;2475-2485
    • (2004) J. Med. Chem. , vol.47 , pp. 2475-2485
    • Rosowsky, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.