arginine has been researched along with cytidine monophosphate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 2 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Assairi, L; Bârzu, O; Bertrand, T; Briozzo, P; Bucurenci, N; Gilles, AM; Golinelli-Pimpaneau, B; Munier-Lehmann, H; Ofiteru, A | 1 |
| Frosch, M; Gerardy-Schahn, R; Gotza, B; Muhlenhoff, M; Munster, AK; Weinhold, B | 1 |
| Gea-Mallorqui, E; Goring, ME; Hanic-Joyce, PJ; Joyce, PB; Karls, S; Leibovitch, M; Richard, F | 1 |
| Deng, Z; Han, T; He, X; Liu, G; Wu, G; Zhang, Y; Zhao, G | 1 |
4 other study(ies) available for arginine and cytidine monophosphate
| Article | Year |
|---|---|
Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme.
Topics: Amino Acid Sequence; Arabinonucleotides; Arginine; Binding Sites; Catalysis; Crystallography, X-Ray; Cytidine Diphosphate; Cytidine Monophosphate; Deoxycytidine Monophosphate; Deoxycytosine Nucleotides; Dideoxynucleotides; Drug Design; Escherichia coli; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Nucleoside-Phosphate Kinase; Pentoses; Phosphorylation; Protein Binding; Protein Conformation; Sequence Alignment; Serine; Structure-Activity Relationship; Substrate Specificity | 2002 |
Nuclear localization signal of murine CMP-Neu5Ac synthetase includes residues required for both nuclear targeting and enzymatic activity.
Topics: 3T3 Cells; Amino Acid Motifs; Amino Acid Sequence; Amino Acids; Animals; Arginine; Base Sequence; Blotting, Western; Cell Nucleus; CHO Cells; Conserved Sequence; Cricetinae; Cytidine Monophosphate; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Evolution, Molecular; Glutamine; Green Fluorescent Proteins; Luminescent Proteins; Mice; Microscopy, Fluorescence; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; N-Acylneuraminate Cytidylyltransferase; Nuclear Localization Signals; Plasmids; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Homology, Amino Acid | 2002 |
The ability of an arginine to tryptophan substitution in Saccharomyces cerevisiae tRNA nucleotidyltransferase to alleviate a temperature-sensitive phenotype suggests a role for motif C in active site organization.
Topics: Adenosine Monophosphate; Amino Acid Motifs; Amino Acid Substitution; Arginine; Aspartic Acid; Catalytic Domain; Cytidine Monophosphate; Hot Temperature; Molecular Dynamics Simulation; Molecular Sequence Data; Phenotype; Protein Structure, Secondary; RNA Nucleotidyltransferases; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Tryptophan | 2013 |
Structure of the N-glycosidase MilB in complex with hydroxymethyl CMP reveals its Arg23 specifically recognizes the substrate and controls its entry.
Topics: Arginine; Catalytic Domain; Cytidine Monophosphate; Glycoside Hydrolases; Models, Molecular; Point Mutation; Protein Binding; Substrate Specificity | 2014 |