Compounds > beta-methylene thiazole-4-carboxamide adenine dinucleotide
Page last updated: 2024-09-03

beta-methylene thiazole-4-carboxamide adenine dinucleotide and nad

beta-methylene thiazole-4-carboxamide adenine dinucleotide has been researched along with nad in 3 studies

Compound Research Comparison

Studies
(beta-methylene thiazole-4-carboxamide adenine dinucleotide)		Trials
(beta-methylene thiazole-4-carboxamide adenine dinucleotide)		Recent Studies (post-2010)
(beta-methylene thiazole-4-carboxamide adenine dinucleotide)		Studies
(nad)		Trials
(nad)		Recent Studies (post-2010) (nad)
60030,121885,663

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (66.67)18.2507
2000's1 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Colby, TD; Goldstein, BM; Jones, JP; Pankiewicz, KW; Zatorski, A1
Benhar, I; Davies, DR; Dyda, F; Li, M; Pastan, I1
Gan, L; Hedstrom, L; Petsko, GA1

Other Studies

3 other study(ies) available for beta-methylene thiazole-4-carboxamide adenine dinucleotide and nad

ArticleYear
Potent inhibitors of human inosine monophosphate dehydrogenase type II. Fluorine-substituted analogues of thiazole-4-carboxamide adenine dinucleotide.
    Journal of medicinal chemistry, 1995, Mar-31, Volume: 38, Issue:7

    Topics: Adenine Nucleotides; Adenosine Diphosphate; Animals; Fluorine; Horses; Humans; IMP Dehydrogenase; NAD; Recombinant Proteins; Thiazoles

1995
Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: implications for the activation process and for ADP ribosylation.
    Proceedings of the National Academy of Sciences of the United States of America, 1996, Jul-09, Volume: 93, Issue:14

    Topics: Adenosine Diphosphate; Adenosine Diphosphate Ribose; ADP Ribose Transferases; Bacterial Toxins; Binding Sites; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Exotoxins; Models, Molecular; NAD; Poly(ADP-ribose) Polymerases; Protein Conformation; Protein Structure, Secondary; Pseudomonas aeruginosa; Pseudomonas aeruginosa Exotoxin A; Recombinant Proteins; Thiazoles; Virulence Factors

1996
Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase: NAD+ orients the active site loop for catalysis.
    Biochemistry, 2002, Nov-05, Volume: 41, Issue:44

    Topics: Adenosine Diphosphate; Animals; Binding Sites; Catalytic Domain; Cations, Monovalent; Crystallization; Crystallography, X-Ray; Enzyme Activation; Enzyme Activators; Hydrogen Bonding; IMP Dehydrogenase; Inosine Monophosphate; Macromolecular Substances; Models, Molecular; Mutagenesis, Site-Directed; NAD; Potassium; Protein Structure, Tertiary; Protozoan Proteins; Thiazoles; Tritrichomonas foetus

2002