Page last updated: 2024-08-17

nad and adenosine 2',5'-diphosphate

nad has been researched along with adenosine 2',5'-diphosphate in 2 studies

Research

Studies (2)

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

Authors	Studies
MacKenzie, RE; Pawelek, PD	1
Abell, C; Blundell, TL; Ciulli, A; Smith, AG; Williams, G	1

Other Studies

2 other study(ies) available for nad and adenosine 2',5'-diphosphate

Article	Year
Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes. Biochemistry, 1998, Jan-27, Volume: 37, Issue:4 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. Journal of medicinal chemistry, 2006, Aug-10, Volume: 49, Issue:16 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

Article

Year

Methenyltetrahydrofolate cyclohydrolase is rate limiting for the enzymatic conversion of 10-formyltetrahydrofolate to 5,10-methylenetetrahydrofolate in bifunctional dehydrogenase-cyclohydrolase enzymes.

Biochemistry, 1998, Jan-27, Volume: 37, Issue:4

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.

Journal of medicinal chemistry, 2006, Aug-10, Volume: 49, Issue:16

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