Compounds > cytidine triphosphate
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cytidine triphosphate and cobamamide

cytidine triphosphate has been researched along with cobamamide in 3 studies

Research

Studies (3)

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

Authors

AuthorsStudies
Barbé, J; Eliasson, R; Gibert, I; Hellman, U; Jeanthon, C; Jordan, A; Reichard, P; Torrents, E; Wernstedt, C1
Gerfen, GJ; Lohman, GJ; Stubbe, J1
Lohman, GJ; Stubbe, J1

Other Studies

3 other study(ies) available for cytidine triphosphate and cobamamide

ArticleYear
B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli.
    Proceedings of the National Academy of Sciences of the United States of America, 1997, Dec-09, Volume: 94, Issue:25

    Topics: Amino Acid Sequence; Bacteria; Base Sequence; Binding Sites; Chromosome Mapping; Cloning, Molecular; Cobamides; Cytidine Diphosphate; Cytidine Triphosphate; DNA Primers; Escherichia coli; Genes, Bacterial; Gram-Negative Anaerobic Bacteria; Gram-Positive Cocci; Molecular Sequence Data; Polymerase Chain Reaction; Ribonucleotide Reductases; Sequence Homology, Amino Acid; Substrate Specificity; Temperature

1997
Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2',2'-difluoro-2'-deoxycytidine 5'-triphosphate: adenosylcobalamin destruction and formation of a nucleotide-based radical.
    Biochemistry, 2010, Feb-23, Volume: 49, Issue:7

    Topics: Bacterial Proteins; Cobamides; Cytidine Triphosphate; Enzyme Activation; Enzyme Inhibitors; Free Radicals; Lactobacillus leichmannii; Models, Chemical; Nucleosides; Nucleotides; Ribonucleotide Reductases; Ribose

2010
Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2',2'-difluoro-2'-deoxycytidine 5'-triphosphate: covalent modification.
    Biochemistry, 2010, Feb-23, Volume: 49, Issue:7

    Topics: Alkylation; Amino Acid Sequence; Bacterial Proteins; Cobamides; Cytidine Triphosphate; Cytosine Deaminase; Enzyme Inhibitors; Humans; Lactobacillus leichmannii; Molecular Sequence Data; Peptide Fragments; Protein Binding; Protein Conformation; Ribonucleotide Reductases; Tandem Mass Spectrometry

2010