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Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica

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Synthesis and Biophysical Analysis of Porous Bi-Phase Calcium Phosphate/Gelatin-Pva Matrices Loaded with Silver Nanoparticles and Methotrexate for Osteogenic Engineering
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Folic acid and folates: the feasibility for nutritional enhancement in plant foods
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Metabolic Consequences of Enzyme Interactions
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Purification and immunochemical characterization of a dihydrofolate reductase—thymidylate synthase enzyme complex from wild‐carrot cells
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Substrate channeling between the human dihydrofolate reductase and thymidylate synthase
inferred← citeshttps://doi.org/10.1006/expr.1997.4221openalex-snapshot
Plasmodium falciparum:Asparagine Mutant at Residue 108 of Dihydrofolate Reductase Is an Optimal Antifolate-Resistant Single Mutant
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Dihydrofolate reductase
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Recent Advance on Thymidylate Synthase-Dihydrofolate Reductase from Plasmodium falciparum
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Malaria Chemotherapy: Paradigms from Pyrimidine Metabolism
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The Leishmania
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Fresh Paradigms for Curative Antimetabolites
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Dihydrofolate Reductase
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Dihydrofolate reductase
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The metabolism of nucleotides
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The metabolism of nucleotides
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Folate synthesis and compartmentation in higher plants
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Molecular cloning and analysis of a cDNA coding for the bifunctional dihydrofolate reductase-thymidylate synthase of Daucus carota
inferred← citeshttps://doi.org/10.1007/bf00016070openalex-snapshot
Proteolytic and partial sequencing studies of the bifunctional dihydrofolate reductase-thymidylate synthase from Daucus carota
inferred← citeshttps://doi.org/10.1007/bf00029883openalex-snapshot
Daucus carota cells contain a dihydrofolate reductase: thymidylate synthase bifunctional polypeptide
inferred← citeshttps://doi.org/10.1007/s00253-007-1023-8openalex-snapshot
Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase
inferred← citeshttps://doi.org/10.1007/s10295-008-0342-9openalex-snapshot
Bifunctional xylanases and their potential use in biotechnology
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Formation of catalytically active cross-species heterodimers of thymidylate synthase from Plasmodium falciparum and Plasmodium vivax
inferred← citeshttps://doi.org/10.1016/0003-9861(87)90442-5openalex-snapshot
Deoxyribonucleotide biosynthesis in green algae: Characterization of thymidylate synthase-dihydrofolate reductase in Scenedesmus obliquus
inferred← citeshttps://doi.org/10.1016/0003-9861(89)90120-3openalex-snapshot
Interaction of folylpolyglutamates with enzymes in one-carbon metabolism
inferred← citeshttps://doi.org/10.1016/0003-9861(92)90547-aopenalex-snapshot
Characteristics of NADPH-dependent thymidylate synthetase purified from Streptomyces aureofaciens
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Thymidylate synthase-dihydrofolate reductase in protozoa
inferred← citeshttps://doi.org/10.1016/0014-4894(91)90136-kopenalex-snapshot
Purification and characterization of dihydrofolate reductase from wild-type and trimethoprim-resistant Mycobacterium smegmatis
inferred← citeshttps://doi.org/10.1016/0020-7519(86)90084-6openalex-snapshot
Alteration in properties of thymidylate synthetase from pyrimethamine-resistant Plasmodium chabaudi
inferred← citeshttps://doi.org/10.1016/0065-2571(89)90098-8openalex-snapshot
Methotrexate 5-aminoallyl-2′-deoxyuridine 5′-monophosphate: A potential bifunctional inhibitor of thymidylate synthase
inferred← citeshttps://doi.org/10.1016/0163-7258(90)90017-vopenalex-snapshot
The dihydrofolate reductase-thymidylate synthetase gene in the drug resistance of malaria parasites
inferred← citeshttps://doi.org/10.1016/0166-6851(85)90129-xopenalex-snapshot
Selection and properties of Leishmania tropica resistant to 10-propargyl-5,8-dideazafolate, an inhibitor of thymidylate synthetase
inferred← citeshttps://doi.org/10.1016/0166-6851(86)90066-6openalex-snapshot
Altered dihydrofolate reductase in pyrimethamine-resistant Plasmodium falciparum
inferred← citeshttps://doi.org/10.1016/0166-6851(87)90149-6openalex-snapshot
Folate utilisation by Leishmania species and the identification of intracellular derivatives and folate-metabolising enzymes
inferred← citeshttps://doi.org/10.1016/0166-6851(88)90147-8openalex-snapshot
Selective inhibition of Leishmania dihydrofolate reductase and Leishmania growth by 5-benzyl-2,4-diaminopyrimidines
inferred← citeshttps://doi.org/10.1016/0166-6851(89)90007-8openalex-snapshot
Structure, genomic organization and transcription of the bifunctional dihydrofolate reductase-thymidylate synthase gene from Crithidia fasciculata
inferred← citeshttps://doi.org/10.1016/0166-6851(90)90147-eopenalex-snapshot
Nutritional requirements of wild-type and folate transport-deficient Leishmania donovani for pterins and folates
inferred← citeshttps://doi.org/10.1016/0166-6851(91)90100-kopenalex-snapshot
Functional expression of the dihydrofolate reductase and thymidylate synthetase activities of the human malaria parasite Plasmodium falciparum in Escherichia coli
inferred← citeshttps://doi.org/10.1016/0166-6851(91)90126-qopenalex-snapshot
Biopterin conversion to reduced folates byLeishmania donovani promastigotes
inferred← citeshttps://doi.org/10.1016/0166-6851(94)90076-0openalex-snapshot
Cloning and expression of the dihydrofolate reductase-thymidylate synthase gene from Trypanosoma cruzi
inferred← citeshttps://doi.org/10.1016/0166-6851(95)00059-aopenalex-snapshot
Trypanosoma brucei dihydrofolate reductase-thymidylate synthase: gene isolation and expression and characterization of the enzyme
inferred← citeshttps://doi.org/10.1016/0166-6851(95)02557-xopenalex-snapshot
Expression and characterization of the Trypanosoma cruzi dihydrofolate reductase domain
inferred← citeshttps://doi.org/10.1016/0167-4838(90)90258-hopenalex-snapshot
The purification of dihydrofolate reductase from Drosophila melanogaster
inferred← citeshttps://doi.org/10.1016/0378-1097(88)90240-6openalex-snapshot
Purine and pyrimidine metabolism in parasitic protozoa
inferred← citeshttps://doi.org/10.1016/0925-4439(94)90094-9openalex-snapshot
Amplification of the H locus in Leishmania infantum
inferred← citeshttps://doi.org/10.1016/1046-5928(91)90088-zopenalex-snapshot
Purification and properties of recombinant Pneumocystis carinii dihydrofolate reductase
inferred← citeshttps://doi.org/10.1016/b978-012437551-2/50024-0openalex-snapshot
Development and Application of an Engineered Dihydrofolate Reductase and Cytidine-Deaminase-Based Fusion Genes in Myeloprotection-Based Gene Therapy Strategies
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Comparative mapping of on-targets and off-targets for the discovery of anti-trypanosomatid folate pathway inhibitors
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A kinetic model for analysis of physical tunnels in sequentially acting enzymes with direct proximity channeling
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Design, synthesis and biological activity of novel substituted 3-benzoic acid derivatives as MtDHFR inhibitors
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Synthesis of N-(5,7-diamino-3-phenyl-quinoxalin-2-yl)-3,4,5-substituted anilines and N-[4[(5,7-diamino-3-phenylquinoxalin-2-yl)amino]benzoyl]-l-glutamic acid diethyl ester: Evaluation of in vitro anti-cancer and anti-folate activities
inferred← citeshttps://doi.org/10.1016/j.ejmech.2020.112986openalex-snapshot
Exploring the ability of dihydropyrimidine-5-carboxamide and 5-benzyl-2,4-diaminopyrimidine-based analogues for the selective inhibition of L. major dihydrofolate reductase
inferred← citeshttps://doi.org/10.1016/j.ijpara.2006.12.017openalex-snapshot
The role of tryptophan-48 in catalysis and binding of inhibitors of Plasmodium falciparum dihydrofolate reductase
inferred← citeshttps://doi.org/10.1016/j.molbiopara.2004.09.010openalex-snapshot
Subunit complementation of thymidylate synthase in Plasmodium falciparum bifunctional dihydrofolate reductase-thymidylate synthase
inferred← citeshttps://doi.org/10.1016/j.molp.2025.06.016openalex-snapshot
Structural insights into a plant-conserved DHFR-TS reveal a selective herbicide target
inferred← citeshttps://doi.org/10.1016/j.molstruc.2024.138329openalex-snapshot
Synthesis and biophysical characterization of porous bi-phase calcium phosphate/gelatin-PVA scaffold: Enhanced antibacterial, osteoconductivity and anticancer activity via silver nanoparticles and methotrexate incorporation
inferred← citeshttps://doi.org/10.1016/j.parint.2011.12.004openalex-snapshot
Cloning and heterologous expression of Plasmodium ovale dihydrofolate reductase-thymidylate synthase gene
inferred← citeshttps://doi.org/10.1016/s0014-827x(02)00005-8openalex-snapshot
Quinoxaline chemistry. Part 15. 4-[2-Quinoxalylmethylenimino]-benzoylglutamates and -benzoates, 4-[2-quinoxalylmethyl-N-methylamino]-benzoylglutamates as analogues of classical antifolate agents. Synthesis, elucidation of structures and in vitro evaluation of antifolate and anticancer activities
inferred← citeshttps://doi.org/10.1016/s0014-827x(98)00054-8openalex-snapshot
Quinoxaline chemistry. Part 11. 3-Phenyl-2 [phenoxy- and phenoxymethyl]-6(7) or 6,8-substituted quinoxalines and N-[4-(6(7)-substituted or 6,8-disubstituted-3-phenylquinoxalin-2-yl)hydroxy or hydroxymethyl]benzoylglutamates. Synthesis and evaluation of in vitro anticancer activity and enzymatic…
inferred← citeshttps://doi.org/10.1016/s0020-7519(01)00346-0openalex-snapshot
Pterin transport and metabolism in Leishmania and related trypanosomatid parasites
inferred← citeshttps://doi.org/10.1016/s0021-9258(17)34100-5openalex-snapshot
Isolation and characterization of a mutant dihydrofolate reductase-thymidylate synthase from methotrexate-resistant Leishmania cells.
inferred← citeshttps://doi.org/10.1016/s0021-9258(17)39522-4openalex-snapshot
DNA amplification in antifolate-resistant Leishmania. The thymidylate synthase-dihydrofolate reductase gene and abundant mRNAs.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)48048-9openalex-snapshot
A stable binary complex between Leishmania major thymidylate synthase and the substrate deoxyuridylate. A slow-binding interaction.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)52346-2openalex-snapshot
Amplification and molecular cloning of the IMP dehydrogenase gene of Leishmania donovani
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)52956-2openalex-snapshot
Cloning, expression, and characterization of Cryptococcus neoformans dihydrofolate reductase.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)53249-xopenalex-snapshot
Primary structure of the dihydrofolate reductase-thymidylate synthase gene from Toxoplasma gondii.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)61074-9openalex-snapshot
Biochemistry and regulation of folate and methotrexate transport in Leishmania major.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)68598-9openalex-snapshot
Methotrexate-resistant Leishmania donovani genetically deficient in the folate-methotrexate transporter.
inferred← citeshttps://doi.org/10.1016/s0021-9258(18)71573-1openalex-snapshot
Wild-type and Drug-resistant Leishmania major Hydrolyze Methotrexate to N-10-Methyl-4-deoxy-4-aminopteroate without Accumulation of Methotrexate Polyglutamates
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)35410-9openalex-snapshot
Aspartate transcarbamylase from Leishmania donovani. A discrete, nonregulatory enzyme as a potential chemotherapeutic site.
inferred← citeshttps://doi.org/10.1016/s0021-9258(19)76455-2openalex-snapshot
Reductions in methotrexate and folate influx in methotrexate-resistant lines of Leishmania major are independent of R or H region amplification.
inferred← citeshttps://doi.org/10.1016/s0021-9258(20)80589-4openalex-snapshot
The dihydrofolate reductase domain of Plasmodium falciparum thymidylate synthase-dihydrofolate reductase. Gene synthesis, expression, and anti-folate-resistant mutants.
inferred← citeshttps://doi.org/10.1016/s0074-7696(08)60529-xopenalex-snapshot
Macromolecular Compartmentation and Channeling
inferred← citeshttps://doi.org/10.1016/s0075-7535(08)70122-0openalex-snapshot
References
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[6] Fundamental mechanisms of substrate channeling
inferred← citeshttps://doi.org/10.1016/s0163-7258(97)00099-5openalex-snapshot
Thymidylate synthase: Structure, inhibition, and strained conformations during catalysis
inferred← citeshttps://doi.org/10.1016/s0166-6851(01)00213-4openalex-snapshot
Pteridine salvage throughout the Leishmania infectious cycle: implications for antifolate chemotherapy
inferred← citeshttps://doi.org/10.1016/s0166-6851(01)00402-9openalex-snapshot
Molecular characterization of dihydrofolate reductase in relation to antifolate resistance in Plasmodium vivax
inferred← citeshttps://doi.org/10.1016/s0166-6851(01)00440-6openalex-snapshot
Novel antifolate resistant mutations of Plasmodium falciparum dihydrofolate reductase selected in Escherichia coli
inferred← citeshttps://doi.org/10.1016/s0166-6851(02)00035-xopenalex-snapshot
Mutational analysis of Plasmodium falciparum dihydrofolate reductase: the role of aspartate 54 and phenylalanine 223 on catalytic activity and antifolate binding
inferred← citeshttps://doi.org/10.1016/s0166-6851(02)00240-2openalex-snapshot
Effect of N-terminal truncation of Plasmodium falciparum dihydrofolate reductase on dihydrofolate reductase and thymidylate synthase activity
inferred← citeshttps://doi.org/10.1016/s0166-6851(96)02756-9openalex-snapshot
Chemical synthesis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene
inferred← citeshttps://doi.org/10.1016/s0176-1617(11)81515-4openalex-snapshot
Biochemical Evidence for the Presence of a Bifunctional Dihydrofolate Reductase-Thymidylate Synthase in Plant Species
inferred← citeshttps://doi.org/10.1016/s0925-4439(02)00088-1openalex-snapshot
Inhibitors of dihydrofolate reductase in leishmania and trypanosomes
inferred← citeshttps://doi.org/10.1021/acssynbio.0c00368openalex-snapshot
Synthetic Virus-like Particles for Glutathione Biosynthesis
inferred← citeshttps://doi.org/10.1021/bi00035a030openalex-snapshot
Stereospecificity of folate binding to DNA photolyase from Escherichia coli
inferred← citeshttps://doi.org/10.1021/bi00101a004openalex-snapshot
Opposite facial specificity for two hydroquinone epoxidases: (3-si,4-re)-2,5-dihydroxyacetanilide epoxidase from Streptomyces LL-C10037 and (3-re,4-si)-2,5-dihydroxyacetanilide epoxidase from Streptomyces MPP 3051
inferred← citeshttps://doi.org/10.1021/bi00255a028openalex-snapshot
Crystal Structure of Thymidylate Synthase from T4 Phage: Component of a Deoxynucleoside Triphosphate-Synthesizing Complex
inferred← citeshttps://doi.org/10.1021/bi00383a026openalex-snapshot
Carbamoyl-phosphate synthetase II of the mammalian CAD protein: kinetic mechanism and elucidation of reaction intermediates by positional isotope exchange
inferred← citeshttps://doi.org/10.1021/bi00410a039openalex-snapshot
Heterologous expression of the bifunctional thymidylate synthase-dihydrofolate reductase from Leishmania major
inferred← citeshttps://doi.org/10.1021/bi00500a009openalex-snapshot
Heterologous expression of active thymidylate synthase-dihydrofolate reductase from Plasmodium falciparum
inferred← citeshttps://doi.org/10.1021/bi200499mopenalex-snapshot
A Tale of Two Subunits: How the Neomorphic R132H IDH1 Mutation Enhances Production of αHG
inferred← citeshttps://doi.org/10.1021/bi400576topenalex-snapshot
First Three-Dimensional Structure of Toxoplasma gondii Thymidylate Synthase–Dihydrofolate Reductase: Insights for Catalysis, Interdomain Interactions, and Substrate Channeling
inferred← citeshttps://doi.org/10.1021/bi701624uopenalex-snapshot
Probing the Role of Parasite-Specific, Distant Structural Regions on Communication and Catalysis in the Bifunctional Thymidylate Synthase−Dihydrofolate Reductase from Plasmodium falciparum
inferred← citeshttps://doi.org/10.1021/cb400007kopenalex-snapshot
Structure of Mycobacterial β-Oxidation Trifunctional Enzyme Reveals Its Altered Assembly and Putative Substrate Channeling Pathway
inferred← citeshttps://doi.org/10.1021/jm030781popenalex-snapshot
Docking and Database Screening Reveal New Classes ofPlasmodiumfalciparumDihydrofolate Reductase Inhibitors
inferred← citeshttps://doi.org/10.1021/jm1010572openalex-snapshot
Virtual Screening Identification of Nonfolate Compounds, Including a CNS Drug, as Antiparasitic Agents Inhibiting Pteridine Reductase
inferred← citeshttps://doi.org/10.1034/j.1399-3054.1993.880317.xopenalex-snapshot
Dihydrofolate reductase and thymidylate synthase in plants: an open problem
inferred← citeshttps://doi.org/10.1038/nsb0394-131openalex-snapshot
An electrostatic highway
inferred← citeshttps://doi.org/10.1038/nsb0394-186openalex-snapshot
Structure of and kinetic channelling in bifunctional dihydrofolate reductase–thymidylate synthase
inferred← citeshttps://doi.org/10.1038/nsb921openalex-snapshot
Insights into antifolate resistance from malarial DHFR-TS structures
inferred← citeshttps://doi.org/10.1046/j.1365-313x.1993.03050657.xopenalex-snapshot
The origin of the bifunctional dihydrofolate reductase-thymidylate synthase isogenes of Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.03044.xopenalex-snapshot
Fusion of farnesyldiphosphate synthase and epi‐aristolochene synthase, a sesquiterpene cyclase involved in capsidiol biosynthesis in Nicotiana tabacum
inferred← citeshttps://doi.org/10.1063/1.4867286openalex-snapshot
A model study of sequential enzyme reactions and electrostatic channeling
inferred← citeshttps://doi.org/10.1073/pnas.0704384105openalex-snapshot
Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development
inferred← citeshttps://doi.org/10.1073/pnas.0906101107openalex-snapshot
Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum
inferred← citeshttps://doi.org/10.1073/pnas.82.21.7188openalex-snapshot
Limited proteolysis of the bifunctional thymidylate synthase-dihydrofolate reductase from Leishmania tropica.
inferred← citeshttps://doi.org/10.1073/pnas.83.15.5387openalex-snapshot
Bifunctional thymidylate synthase-dihydrofolate reductase from Leishmania tropica: sequence homology with the corresponding monofunctional proteins.
inferred← citeshttps://doi.org/10.1073/pnas.83.8.2584openalex-snapshot
Primary structure of the gene encoding the bifunctional dihydrofolate reductase-thymidylate synthase of Leishmania major.
inferred← citeshttps://doi.org/10.1073/pnas.91.24.11442openalex-snapshot
PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major.
inferred← citeshttps://doi.org/10.1073/pnas.94.20.10931openalex-snapshot
Transformation with human dihydrofolate reductase renders malaria parasites insensitive to WR99210 but does not affect the intrinsic activity of proguanil
inferred← citeshttps://doi.org/10.1073/pnas.94.4.1124openalex-snapshot
Antifolate-resistant mutants of Plasmodium falciparum dihydrofolate reductase
inferred← citeshttps://doi.org/10.1074/jbc.271.16.9466openalex-snapshot
Mitochondria Are a Major Site for Folate and Thymidylate Synthesis in Plants
inferred← citeshttps://doi.org/10.1074/jbc.272.21.13883openalex-snapshot
The Roles of Pteridine Reductase 1 and Dihydrofolate Reductase-Thymidylate Synthase in Pteridine Metabolism in the Protozoan Parasite Leishmania major
inferred← citeshttps://doi.org/10.1074/jbc.274.18.12193openalex-snapshot
The Molecular Basis of Substrate Channeling
inferred← citeshttps://doi.org/10.1074/jbc.274.53.37781openalex-snapshot
Essential Protein-Protein Interactions between Plasmodium falciparum Thymidylate Synthase and Dihydrofolate Reductase Domains
inferred← citeshttps://doi.org/10.1074/jbc.m109.064683openalex-snapshot
Crystal Structure of Albaflavenone Monooxygenase Containing a Moonlighting Terpene Synthase Active Site
inferred← citeshttps://doi.org/10.1074/jbc.m114.625483openalex-snapshot
First Evidence for Substrate Channeling between Proline Catabolic Enzymes
inferred← citeshttps://doi.org/10.1074/jbc.m116.756965openalex-snapshot
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function
inferred← citeshttps://doi.org/10.1074/jbc.m206523200openalex-snapshot
Mechanistic Characterization of Toxoplasma gondiiThymidylate Synthase (TS-DHFR)-Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1074/jbc.m212689200openalex-snapshot
Probing Electrostatic Channeling in Protozoal Bifunctional Thymidylate Synthase-Dihydrofolate Reductase Using Site-directed Mutagenesis
inferred← citeshttps://doi.org/10.1074/jbc.m212690200openalex-snapshot
A Molecular Docking Strategy Identifies Eosin B as a Non-active Site Inhibitor of Protozoal Bifunctional Thymidylate Synthase-Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1074/jbc.m400009200openalex-snapshot
Kinetic Characterization of Bifunctional Thymidylate Synthase-Dihydrofolate Reductase (TS-DHFR) from Cryptosporidium hominis
inferred← citeshttps://doi.org/10.1074/jbc.m409264200openalex-snapshot
Growth Phase Regulation of the Main Folate Transporter of Leishmania infantum and Its Role in Methotrexate Resistance
inferred← citeshttps://doi.org/10.1080/07391102.2016.1186560openalex-snapshot
Human dihydrofolate reductase and thymidylate synthase form a complexin vitroand co-localize in normal and cancer cells
inferred← citeshttps://doi.org/10.1080/11263509009428141openalex-snapshot
Methotrexate-resistance in plants: genetic, molecular and cytological analyses
inferred← citeshttps://doi.org/10.1080/14756366.2019.1651311openalex-snapshot
Dual and selective inhibitors of pteridine reductase 1 (PTR1) and dihydrofolate reductase-thymidylate synthase (DHFR-TS) from Leishmania chagasi
inferred← citeshttps://doi.org/10.1089/omi.1.1998.3.1openalex-snapshot
First Report on the Systematic Sequencing of the Small Genome of Encephalitozoon cuniculi (Protozoa, Microspora): Gene Organization of a 4.3 kbp Region on Chromosome I
inferred← citeshttps://doi.org/10.1093/gbe/evu213openalex-snapshot
Complex Patterns of Gene Fission in the Eukaryotic Folate Biosynthesis Pathway
inferred← citeshttps://doi.org/10.1093/protein/gzx004openalex-snapshot
Understanding the molecular mechanism of substrate channeling and domain communication in protozoal bifunctional TS-DHFR
inferred← citeshttps://doi.org/10.1096/fasebj.4.6.2180768openalex-snapshot
Bifunctional thymidylate synthase‐dihydrofolate reductase in protozoa
inferred← citeshttps://doi.org/10.1096/fasebj.5.12.1916088openalex-snapshot
Compartmentation of folate‐mediated one‐carbon metabolism in eukaryotes
inferred← citeshttps://doi.org/10.1104/pp.91.3.1168openalex-snapshot
Coregulation of Dihydrofolate Reductase and Thymidylate Synthase in Overproducer Cell Lines of Wild Carrot
inferred← citeshttps://doi.org/10.1107/s0907444904001544openalex-snapshot
Characterization, crystallization and preliminary X-ray analysis of bifunctional dihydrofolate reductase–thymidylate synthase from Plasmodium falciparum
inferred← citeshttps://doi.org/10.1107/s1744309109041979openalex-snapshot
Crystallization and preliminary crystallographic studies of dihydrofolate reductase-thymidylate synthase fromTrypanosoma cruzi, the Chagas disease pathogen
inferred← citeshttps://doi.org/10.1111/j.1365-2958.2008.06305.xopenalex-snapshot
Chemical and genetic validation of dihydrofolate reductase–thymidylate synthase as a drug target in African trypanosomes
inferred← citeshttps://doi.org/10.1111/j.1365-313x.1993.00657.xopenalex-snapshot
The origin of the bifunctional dihydrofolate reductasethymidylate synthase isogenes of Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1111/j.1749-6632.1989.tb27370.xopenalex-snapshot
Recent Studies on Thymidylate Synthase
inferred← citeshttps://doi.org/10.1128/9781555817558.ch23openalex-snapshot
Mechanisms of Antimalarial Drug Action and Resistance
inferred← citeshttps://doi.org/10.1128/aac.33.11.1860openalex-snapshot
Antileishmanial activities of 2,4-diaminoquinazoline putative dihydrofolate reductase inhibitors
inferred← citeshttps://doi.org/10.1128/aac.36.4.704openalex-snapshot
Molecular targets of 5-fluoroorotate in the human malaria parasite, Plasmodium falciparum
inferred← citeshttps://doi.org/10.1128/aac.38.3.476openalex-snapshot
Susceptibility of Plasmodium falciparum to a combination of thymidine and ICI D1694, a quinazoline antifolate directed at thymidylate synthase
inferred← citeshttps://doi.org/10.1128/aem.66.11.4620-4624.2000openalex-snapshot
Trehalose Synthesis by Sequential Reactions of Recombinant Maltooligosyltrehalose Synthase and Maltooligosyltrehalose Trehalohydrolase from Brevibacterium helvolum
inferred← citeshttps://doi.org/10.1128/aem.66.6.2484-2490.2000openalex-snapshot
Characterization of a Bifunctional Enzyme Fusion of Trehalose-6-Phosphate Synthetase and Trehalose-6-Phosphate Phosphatase of Escherichia coli
inferred← citeshttps://doi.org/10.1128/jb.170.7.3040-3045.1988openalex-snapshot
Construction of a dihydrofolate reductase-deficient mutant of Escherichia coli by gene replacement
inferred← citeshttps://doi.org/10.1128/mcb.16.10.5655openalex-snapshot
Selection against the Dihydrofolate Reductase-Thymidylate Synthase ( DHFR-TS ) Locus as a Probe of Genetic Alterations in Leishmania major
inferred← citeshttps://doi.org/10.1134/s0006297907090039openalex-snapshot
Steady-state kinetics of bifunctional enzymes. Taking into account kinetic hierarchy of fast and slow catalytic cycles in a generalized model
inferred← citeshttps://doi.org/10.1146/annurev.biochem.70.1.149openalex-snapshot
Channeling of Substrates and Intermediates in Enzyme-Catalyzed Reactions
inferred← citeshttps://doi.org/10.1186/1475-2875-12-91openalex-snapshot
Insights into the role of the junctional region of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase
inferred← citeshttps://doi.org/10.1199/tab.0018openalex-snapshot
Purine and Pyrimidine Nucleotide Synthesis and Metabolism
inferred← citeshttps://doi.org/10.1371/journal.pntd.0004714openalex-snapshot
Trypanosoma brucei DHFR-TS Revisited: Characterisation of a Bifunctional and Highly Unstable Recombinant Dihydrofolate Reductase-Thymidylate Synthase
inferred← citeshttps://doi.org/10.2217/17460913.1.1.113openalex-snapshot
Folate Metabolism as a Source of Molecular Targets for Antimalarials
inferred← citeshttps://doi.org/10.25335/m0rm-hp68openalex-snapshot
Intermediate transport in nanoscale scaffolds for multistep catalytic reactions
inferred← citeshttps://doi.org/10.2741/3932openalex-snapshot
Substrate channeling in proline metabolism
inferred← citeshttps://doi.org/10.5772/intechopen.100821openalex-snapshot
Malaria - Recent Advances and New Perspectives
inferred← citeshttps://doi.org/10.5772/intechopen.106468openalex-snapshot
Purine and Pyrimidine Pathways as Antimalarial Targets
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