adenosine 2',5'-diphosphate has been researched along with nad in 2 studies
Studies (adenosine 2',5'-diphosphate) | Trials (adenosine 2',5'-diphosphate) | Recent Studies (post-2010) (adenosine 2',5'-diphosphate) | Studies (nad) | Trials (nad) | Recent Studies (post-2010) (nad) |
---|---|---|---|---|---|
29 | 0 | 2 | 30,121 | 88 | 5,663 |
7 | 0 | 0 | 21 | 0 | 8 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (50.00) | 18.2507 |
2000's | 1 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
MacKenzie, RE; Pawelek, PD | 1 |
Abell, C; Blundell, TL; Ciulli, A; Smith, AG; Williams, G | 1 |
2 other study(ies) available for adenosine 2',5'-diphosphate and nad
Article | Year |
---|---|
Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes.
Topics: Adenosine Diphosphate; Aminohydrolases; Bacterial Proteins; Formate-Tetrahydrofolate Ligase; Humans; Kinetics; Leucovorin; Methylenetetrahydrofolate Dehydrogenase (NADP); Mitochondria; Models, Chemical; Multienzyme Complexes; NAD; NADP; Photobacterium; Tetrahydrofolates | 1998 |
Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods.
Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Binding Sites; Biophysical Phenomena; Biophysics; Calorimetry; Escherichia coli; Ligands; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nucleotides; Protein Binding; Structure-Activity Relationship; Thermodynamics | 2006 |