nad has been researched along with n(1)-guanyl-1,7-diaminoheptane in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (25.00) | 18.2507 |
2000's | 1 (25.00) | 29.6817 |
2010's | 1 (25.00) | 24.3611 |
2020's | 1 (25.00) | 2.80 |
Authors | Studies |
---|---|
Dimitriadis, EK; Joe, YA; Lee, YB; Park, MH; Wolff, EC | 1 |
Davies, DR; Park, MH; Umland, TC; Wolff, EC | 1 |
Mandal, A; Mandal, S; Park, MH; Wolff, EC | 1 |
Ambrus-Aikelin, G; Imamura, S; Kimura, H; Kitazawa, S; Klein, MG; Kurasawa, O; Matsumoto, S; Morishita, D; Ogawa, K; Okaniwa, M; Ono, K; Saito, B; Tanaka, Y; Uchiyama, N; Yokota, A | 1 |
4 other study(ies) available for nad and n(1)-guanyl-1,7-diaminoheptane
Article | Year |
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Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor.
Topics: Cell Extracts; Chromatography, Affinity; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Eukaryotic Translation Initiation Factor 5A; Guanine; Humans; Hydrogen-Ion Concentration; Molecular Weight; NAD; Oxidoreductases Acting on CH-NH Group Donors; Peptide Initiation Factors; Protein Binding; Protein Precursors; Protons; Recombinant Fusion Proteins; RNA-Binding Proteins; Sequence Analysis; Spermidine; Temperature; Thermodynamics; Ultracentrifugation | 1999 |
A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex.
Topics: Alkyl and Aryl Transferases; Amino Acid Motifs; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Dimerization; Electrons; Eukaryotic Translation Initiation Factor 5A; Guanine; Humans; Hydrogen-Ion Concentration; Ions; Models, Molecular; NAD; Oxidoreductases Acting on CH-NH Group Donors; Peptide Initiation Factors; Protein Binding; Protein Conformation; Protein Structure, Secondary; RNA-Binding Proteins; Spermidine; X-Ray Diffraction | 2004 |
A new non-radioactive deoxyhypusine synthase assay adaptable to high throughput screening.
Topics: Biosynthetic Pathways; Enzyme Assays; Enzyme Inhibitors; Guanine; High-Throughput Screening Assays; Humans; Hydrogen-Ion Concentration; Kinetics; Luminescent Measurements; NAD; Oxidoreductases Acting on CH-NH Group Donors; Small Molecule Libraries; Spermidine; Substrate Specificity; Time Factors | 2017 |
Discovery of Novel Allosteric Inhibitors of Deoxyhypusine Synthase.
Topics: Allosteric Site; Crystallography, X-Ray; Drug Discovery; Enzyme Assays; Enzyme Inhibitors; Guanine; High-Throughput Screening Assays; Humans; Indoles; Molecular Structure; NAD; Oxidoreductases Acting on CH-NH Group Donors; Protein Binding; Protein Conformation; Spermidine; Structure-Activity Relationship; Thiophenes | 2020 |