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Probing the Role of Parasite-Specific, Distant Structural Regions on Communication and Catalysis in the Bifunctional Thymidylate Synthase−Dihydrofolate Reductase from Plasmodium falciparum

https://doi.org/10.1021/bi701624u
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1016/0014-4894(90)90119-wopenalex-snapshot
Thymidylate synthase-dihydrofolate reductase in protozoa
inferredcites →https://doi.org/10.1016/0022-2836(90)90347-oopenalex-snapshot
Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitory ternary complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate
inferredcites →https://doi.org/10.1016/j.jmb.2006.05.009openalex-snapshot
Role of Solvation Barriers in Protein Kinetic Stability
inferredcites →https://doi.org/10.1016/j.molbiopara.2006.10.016openalex-snapshot
Cell-free production of functional Plasmodium falciparum dihydrofolate reductase-thymidylate synthase
inferredcites →https://doi.org/10.1016/s0021-9258(19)45476-8openalex-snapshot
Folate Coenzymes of Clostridium acidi-urici
inferredcites →https://doi.org/10.1016/s0021-9258(20)81357-xopenalex-snapshot
Enzymic Preparation of the l,l-Diastereoisomer of Tetrahydrofolic Acid
inferredcites →https://doi.org/10.1016/s0140-6736(05)66420-3openalex-snapshot
Malaria
inferredcites →https://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
inferredcites →https://doi.org/10.1016/s1286-4579(01)01525-8openalex-snapshot
Basis for antifolate action and resistance in malaria
inferredcites →https://doi.org/10.1017/s0033583506004240openalex-snapshot
Designing ligands to bind proteins
inferredcites →https://doi.org/10.1021/bi00324a021openalex-snapshot
Purification and characterization of the bifunctional thymidylate synthetase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica
inferredcites →https://doi.org/10.1021/bi027019uopenalex-snapshot
A Major Role for a Set of Non-Active Site Mutations in the Development of HIV-1 Protease Drug Resistance
inferredcites →https://doi.org/10.1021/bi700531ropenalex-snapshot
Nonconserved Residues Ala287 and Ser290 of the Cryptosporidium hominis Thymidylate Synthase Domain Facilitate Its Rapid Rate of Catalysis,
inferredcites →https://doi.org/10.1021/bi9803168openalex-snapshot
Substrate Channeling and Domain−Domain Interactions in Bifunctional Thymidylate Synthase−Dihydrofolate Reductase
inferredcites →https://doi.org/10.1038/nsb0394-186openalex-snapshot
Structure of and kinetic channelling in bifunctional dihydrofolate reductase–thymidylate synthase
inferredcites →https://doi.org/10.1038/nsb921openalex-snapshot
Insights into antifolate resistance from malarial DHFR-TS structures
inferredcites →https://doi.org/10.1073/pnas.0500699102openalex-snapshot
Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis
inferredcites →https://doi.org/10.1073/pnas.1230801100openalex-snapshot
Correlated motion and the effect of distal mutations in dihydrofolate reductase
inferredcites →https://doi.org/10.1073/pnas.90.24.11797openalex-snapshot
Methotrexate resistance in an in vivo mouse tumor due to a non-active-site dihydrofolate reductase mutation.
inferredcites →https://doi.org/10.1074/jbc.274.34.23699openalex-snapshot
Non-active Site Changes Elicit Broad-based Cross-resistance of the HIV-1 Protease to Inhibitors
inferredcites →https://doi.org/10.1074/jbc.274.53.37781openalex-snapshot
Essential Protein-Protein Interactions between Plasmodium falciparum Thymidylate Synthase and Dihydrofolate Reductase Domains
inferredcites →https://doi.org/10.1074/jbc.m310328200openalex-snapshot
Phylogenetic Classification of Protozoa Based on the Structure of the Linker Domain in the Bifunctional Enzyme, Dihydrofolate Reductase-Thymidylate Synthase
inferredcites →https://doi.org/10.1074/jbc.m400009200openalex-snapshot
Kinetic Characterization of Bifunctional Thymidylate Synthase-Dihydrofolate Reductase (TS-DHFR) from Cryptosporidium hominis
inferredcites →https://doi.org/10.1074/jbc.m500277200openalex-snapshot
Identification of Amino Acids Required for the Functional Up-regulation of Human Dihydrofolate Reductase Protein in Response to Antifolate Treatment
inferredcites →https://doi.org/10.1093/clinids/7.5.625openalex-snapshot
Pentamidine: A Review
inferredcites →https://doi.org/10.1096/fasebj.4.6.2180768openalex-snapshot
Bifunctional thymidylate synthase‐dihydrofolate reductase in protozoa
inferredcites →https://doi.org/10.1096/fasebj.7.8.8500692openalex-snapshot
Stereochemistry of a multistep/bipartite methyl transfer reaction: thymidylate synthase
inferredcites →https://doi.org/10.1107/s0907444904001544openalex-snapshot
Characterization, crystallization and preliminary X-ray analysis of bifunctional dihydrofolate reductase–thymidylate synthase from Plasmodium falciparum
inferredcites →https://doi.org/10.1111/j.1550-7408.2003.tb00627.xopenalex-snapshot
The Crystal Structure of Dihydrofolate Reductase‐Thymidylate Synthase from Cryptosporidium hominis Reveals a Novel Architecture for the Bifunctional Enzyme
inferredcites →https://doi.org/10.1111/j.1747-0285.2007.00519.xopenalex-snapshot
Compensating Enthalpic and Entropic Changes Hinder Binding Affinity Optimization
inferredcites →https://doi.org/10.1128/aac.41.10.2300openalex-snapshot
In vitro activities of the biguanide PS-15 and its metabolite, WR99210, against cycloguanil-resistant Plasmodium falciparum isolates from Thailand
inferredcites →https://doi.org/10.1146/annurev.biophys.33.110502.133613openalex-snapshot
Structure, Dynamics, and Catalytic Function of Dihydrofolate Reductase
inferredcites →https://doi.org/10.4269/ajtmh.1993.49.121openalex-snapshot
PS-15: a Potent, Orally Active Antimalarial from a New Class of Folic Acid Antagonists

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4852584openalex-extracted
The Characteristic Structural and Functional Dynamics of P. Falciparum Dhfr Binding with Pyrimidine Chemotypes Implicate Malaria Therapy Design
inferred← citeshttps://doi.org/10.1002/9783527670383.ch24openalex-snapshot
Targeting the Trypanosomatidic Enzymes Pteridine Reductase and Dihydrofolate Reductase
inferred← citeshttps://doi.org/10.1002/pro.2300openalex-snapshot
Selective peptide inhibitors of bifunctional thymidylate synthase‐dihydrofolate reductase from Toxoplasma gondii provide insights into domain–domain communication and allosteric regulation
inferred← citeshttps://doi.org/10.1007/s10822-008-9254-zopenalex-snapshot
Interactions between cycloguanil derivatives and wild type and resistance-associated mutant Plasmodium falciparum dihydrofolate reductases
inferred← citeshttps://doi.org/10.1007/s11033-010-0199-7openalex-snapshot
Formation of catalytically active cross-species heterodimers of thymidylate synthase from Plasmodium falciparum and Plasmodium vivax
inferred← citeshttps://doi.org/10.1007/s44371-026-00905-0openalex-snapshot
Review on benzothiazole as a privileged nucleus for Plasmodium DHFR inhibition with structure guided comprehensive analysis
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Artificial intelligence and machine learning in antiparasitic drug discovery
inferred← citeshttps://doi.org/10.1016/j.bioorg.2024.107663openalex-snapshot
Intersite communication in dimeric enzymes highlighted by structural and thermodynamic analysis of didansyltyrosine binding to thymidylate synthases
inferred← citeshttps://doi.org/10.1016/j.chphi.2024.100703openalex-snapshot
The characteristic structural and functional dynamics of P. falciparum DHFR binding with pyrimidine chemotypes implicate malaria therapy design
inferred← citeshttps://doi.org/10.1016/j.chphi.2025.100990openalex-snapshot
In Silico Design of Isoindolinone-Hydrazide Hybrid Compounds as Antiplasmodium Through Molecular Docking, Molecular Dynamics Simulation, and MM-PBSA Calculation
inferred← citeshttps://doi.org/10.1016/j.micpath.2024.106978openalex-snapshot
Analysis of diagnostic biomarkers for malaria: Prospects on rapid diagnostic test (RDT) development
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/10.1021/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/cb8002804openalex-snapshot
Exploiting Structural Analysis, in Silico Screening, and Serendipity To Identify Novel Inhibitors of Drug-Resistant Falciparum Malaria
inferred← citeshttps://doi.org/10.1038/s41598-024-72427-7openalex-snapshot
Computational approach for decoding malaria drug targets from single-cell transcriptomics and finding potential drug molecule
inferred← citeshttps://doi.org/10.1039/c3md00141eopenalex-snapshot
Exploring novel strategies for AIDS protozoal pathogens: α-helix mimetics targeting a key allosteric protein–protein interaction in C. hominis thymidylate synthase-dihydrofolate reductase (TS-DHFR)
inferred← citeshttps://doi.org/10.1042/bj20081247openalex-snapshot
Disruption of the crossover helix impairs dihydrofolate reductase activity in the bifunctional enzyme TS–DHFR from Cryptosporidium hominis
inferred← citeshttps://doi.org/10.1080/14756360802201223openalex-snapshot
Particular interaction between pyrimethamine derivatives and quadruple mutant type dihydrofolate reductase of Plasmodium falciparum: CoMFA and quantum chemical calculations studies
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/10.1107/s090744490901230xopenalex-snapshot
Structures of dihydrofolate reductase-thymidylate synthase ofTrypanosoma cruziin the folate-free state and in complex with two antifolate drugs, trimetrexate and methotrexate
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/10.1371/journal.pmed.1000055openalex-snapshot
Multiple Origins and Regional Dispersal of Resistant dhps in African Plasmodium falciparum Malaria
inferred← citeshttps://doi.org/10.20935/acaddrug8499openalex-snapshot
Targeting Plasmodium falciparum pathways to overcome antimalarial resistance
inferred← citeshttps://doi.org/10.2174/156802611796575948openalex-snapshot
Purine and Pyrimidine Pathways as Targets in Plasmodium falciparum
inferred← citeshttps://doi.org/10.3390/ph18091318openalex-snapshot
Exploring Subtilisin Inhibition to Discover Antimalarial Drugs: Insights into Medicinal Chemistry and Drug Discovery
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