folic acid has been researched along with 10-formyl-5,8-dideazafolate in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 6 (60.00) | 18.2507 |
| 2000's | 3 (30.00) | 29.6817 |
| 2010's | 1 (10.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cook, RJ; Krupenko, SA; Wagner, C | 1 |
| Huang, T; Kim, DW; Schirch, D; Schirch, V | 1 |
| Cook, RJ | 1 |
| Almassy, R; Bartlett, C; Boritzki, T; Ferre, R; Howland, EJ; Janson, CA; Margosiak, SA; Palmer, CL; Romines, WH; Varney, MD | 1 |
| Barra, D; Fu, TF; Maras, B; Schirch, V | 1 |
| Benkovic, SJ; Shim, JH | 1 |
| Krupenko, SA; Vlasov, AP; Wagner, C | 1 |
| Benkovic, SJ; Lee, SG; Lutz, S | 1 |
| Caperelli, CA; Dahms, TE; Giroux, EL; Sainz, G; Smith, JL | 1 |
| Horita, DA; Krupenko, SA | 1 |
10 other study(ies) available for folic acid and 10-formyl-5,8-dideazafolate
| Article | Year |
|---|---|
Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate.
Topics: Enzyme Activation; Folic Acid; Hydrolases; Mercaptoethanol; Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors; Recombinant Fusion Proteins; Substrate Specificity | 1995 |
Properties of tetrahydropteroylpentaglutamate bound to 10-formyltetrahydrofolate dehydrogenase.
Topics: Aminohydrolases; Animals; Chromatography, Gel; Fluorescence; Folic Acid; Formate-Tetrahydrofolate Ligase; Glycine Hydroxymethyltransferase; Kinetics; Leucovorin; Liver; Methylenetetrahydrofolate Dehydrogenase (NADP); Models, Chemical; Multienzyme Complexes; NADP; Oxidoreductases Acting on CH-NH Group Donors; Protein Binding; Pteroylpolyglutamic Acids; Rabbits; Spectrophotometry | 1996 |
Use of 10-formyl-5,8-dideazafolate as substrate for rat 10-formyltetrahydrofolate dehydrogenase.
Topics: Acyltransferases; Animals; Folic Acid; Hydrolysis; Hydroxymethyl and Formyl Transferases; Leucovorin; Molecular Structure; NADP; Oxidoreductases Acting on CH-NH Group Donors; Phosphoribosylglycinamide Formyltransferase; Quinazolines; Rats; Spectrophotometry; Stereoisomerism | 1997 |
Protein structure-based design, synthesis, and biological evaluation of 5-thia-2,6-diamino-4(3H)-oxopyrimidines: potent inhibitors of glycinamide ribonucleotide transformylase with potent cell growth inhibition.
Topics: Acyltransferases; Animals; Antineoplastic Agents; Cell Division; Crystallography, X-Ray; Drug Design; Escherichia coli; Folic Acid; Humans; Hydroxymethyl and Formyl Transferases; Mice; Models, Molecular; Phosphoribosylaminoimidazolecarboxamide Formyltransferase; Phosphoribosylglycinamide Formyltransferase; Protein Conformation; Pyrimidines; Recombinant Proteins; Stereoisomerism; Tumor Cells, Cultured | 1997 |
A noncatalytic tetrahydrofolate tight binding site is on the small domain of 10-formyltetrahydrofolate dehydrogenase.
Topics: Amino Acid Sequence; Animals; Binding Sites; Catalytic Domain; Chromatography; Folic Acid; Humans; Liver; Mice; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Rabbits; Sequence Homology, Amino Acid; Tetrahydrofolates; Time Factors | 1999 |
Catalytic mechanism of Escherichia coli glycinamide ribonucleotide transformylase probed by site-directed mutagenesis and pH-dependent studies.
Topics: Binding Sites; Catalysis; Deuterium Oxide; Escherichia coli; Folic Acid; Hydrogen-Ion Concentration; Hydroxymethyl and Formyl Transferases; Kinetics; Mutagenesis, Site-Directed; Phosphoribosylglycinamide Formyltransferase; Plasmids; Protein Conformation; Recombinant Proteins; Solvents | 1999 |
On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis: connection between hydrolase and dehydrogenase mechanisms.
Topics: Amino Acid Sequence; Animals; Binding Sites; Catalysis; Conserved Sequence; Folic Acid; Histidine; Hydrogen Bonding; Hydrolases; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidoreductases Acting on CH-NH Group Donors; Protein Folding; Protein Structure, Tertiary; Quinazolines; Sequence Homology, Amino Acid | 2001 |
On the structural and functional modularity of glycinamide ribonucleotide formyltransferases.
Topics: Catalysis; Catalytic Domain; DNA Shuffling; Escherichia coli; Folic Acid; Gene Expression Regulation, Enzymologic; Humans; Hydrolysis; Hydroxymethyl and Formyl Transferases; Kinetics; Models, Molecular; Phosphoribosylglycinamide Formyltransferase; Protein Binding; Protein Engineering; Recombinant Fusion Proteins; Structural Homology, Protein; Structure-Activity Relationship; Temperature | 2003 |
The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase.
Topics: Apoproteins; Binding Sites; Catalysis; Crystallography, X-Ray; Drug Design; Enzyme Inhibitors; Escherichia coli Proteins; Folic Acid; Humans; Hydrogen-Ion Concentration; Hydroxymethyl and Formyl Transferases; Models, Molecular; Phosphoribosylglycinamide Formyltransferase; Protein Binding; Protein Structure, Tertiary; Quinazolines; Substrate Specificity | 2005 |
Modeling of interactions between functional domains of ALDH1L1.
Topics: Aldehyde Dehydrogenase; Binding Sites; Biocatalysis; Folic Acid; Humans; Hydroxymethyl and Formyl Transferases; Molecular Docking Simulation; Oxidoreductases Acting on CH-NH Group Donors; Protein Binding; Protein Domains | 2017 |