s-adenosylmethionine has been researched along with anticodon in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (10.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (30.00) | 29.6817 |
| 2010's | 6 (60.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Kennedy, TD; Lane, BG | 1 |
| Bonnerot, C; Bujnicki, JM; Grosjean, H; Lapeyre, B; Lecointe, F; Pintard, L | 1 |
| Gabruzsk, J; Holmes, WM; Watts, JM | 1 |
| Christian, T; Evilia, C; Hou, YM | 1 |
| Christian, T; Hou, YM; Lahoud, G; Liu, C | 1 |
| D'Silva, S; Haider, SJ; Phizicky, EM | 1 |
| Fang, ZP; Liu, RJ; Long, T; Wang, ED; Zhou, M; Zhou, XL | 1 |
| Goto-Ito, S; Hou, YM; Ito, T; Masuda, I; Sekine, S; Suh, SW; Yokoyama, S; Yoshida, K | 1 |
| Boal, AK; Booker, SJ; Grove, TL; Schwalm, EL | 1 |
| Al Refaii, A; Barraud, P; Brachet, F; Caillet, J; Dégut, C; Droogmans, L; Feller, A; Larue, V; Roovers, M; Tisné, C | 1 |
10 other study(ies) available for s-adenosylmethionine and anticodon
| Article | Year |
|---|---|
Selective labelling ot the methyl carboxylate substituents found in the anticodon sequences of some species of yeast transfer RNA.
Topics: Alkaline Phosphatase; Anticodon; Carboxylic Acids; Chromatography, DEAE-Cellulose; Escherichia coli; Isotope Labeling; Oligonucleotides; Plants; Ribonucleases; Ribonucleosides; RNA, Transfer; S-Adenosylmethionine; Saccharomyces cerevisiae; tRNA Methyltransferases | 1975 |
Trm7p catalyses the formation of two 2'-O-methylriboses in yeast tRNA anticodon loop.
Topics: Amino Acid Sequence; Animals; Anticodon; Base Sequence; Catalysis; Cell Cycle Proteins; Escherichia coli; Eukaryotic Cells; Humans; Methyltransferases; Molecular Sequence Data; Mutagenesis; Nucleic Acid Conformation; Protein Biosynthesis; Protein Structure, Tertiary; Recombinant Fusion Proteins; Ribose; RNA, Fungal; RNA, Messenger; RNA, Transfer; S-Adenosylmethionine; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; tRNA Methyltransferases | 2002 |
Ligand-mediated anticodon conformational changes occur during tRNA methylation by a TrmD methyltransferase.
Topics: Adenosine; Amino Acid Sequence; Anticodon; Base Sequence; Escherichia coli Proteins; Fluorescence Resonance Energy Transfer; Ligands; Methylation; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Protein Conformation; Protein Footprinting; RNA-Binding Proteins; RNA, Transfer, Leu; S-Adenosylmethionine; Sequence Alignment; Thermotoga maritima; tRNA Methyltransferases | 2005 |
Catalysis by the second class of tRNA(m1G37) methyl transferase requires a conserved proline.
Topics: Amino Acid Sequence; Amino Acid Substitution; Anticodon; Archaeal Proteins; Catalysis; Conserved Sequence; DNA Mutational Analysis; Endoribonucleases; Escherichia coli; Kinetics; Models, Molecular; Molecular Sequence Data; Proline; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; S-Adenosylmethionine; Sequence Homology, Amino Acid; Substrate Specificity; tRNA Methyltransferases | 2006 |
Control of catalytic cycle by a pair of analogous tRNA modification enzymes.
Topics: Amino Acyl-tRNA Synthetases; Anticodon; Catalysis; Catalytic Domain; Escherichia coli Proteins; Methanococcus; Models, Molecular; Protein Conformation; Protein Multimerization; RNA, Transfer; S-Adenosylmethionine; Spectrometry, Fluorescence; tRNA Methyltransferases | 2010 |
A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop.
Topics: Anticodon; Cytidine; Microfilament Proteins; Nucleic Acid Conformation; Protein Structure, Tertiary; RNA, Transfer; S-Adenosylmethionine; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; tRNA Methyltransferases | 2011 |
Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2'-O-methyltransferase.
Topics: Alkenes; Anticodon; Base Sequence; Binding Sites; Biocatalysis; Codon; Escherichia coli Proteins; Kinetics; Methylation; Methyltransferases; Models, Molecular; Molecular Sequence Data; Mutation; Nucleic Acid Conformation; Protein Multimerization; Pyrimidines; RNA, Transfer, Leu; S-Adenosylmethionine; Substrate Specificity | 2015 |
Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD.
Topics: Adenosine; Amino Acid Sequence; Anticodon; Base Sequence; Binding Sites; Biocatalysis; Crystallography, X-Ray; Escherichia coli Proteins; Guanine; Haemophilus influenzae; Kinetics; Methylation; Models, Molecular; Molecular Sequence Data; RNA, Transfer; S-Adenosylmethionine; Sequence Alignment; Structure-Activity Relationship; Substrate Specificity; Thermotoga maritima; tRNA Methyltransferases | 2015 |
Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.
Topics: Adenosine; Alanine; Amino Acid Substitution; Anticodon; Catalytic Domain; Crystallography, X-Ray; Cysteine; Escherichia coli Proteins; Methylation; Methyltransferases; Nucleic Acid Conformation; Protein Structure, Tertiary; RNA, Bacterial; RNA, Transfer, Glu; S-Adenosylmethionine | 2016 |
Structural characterization of B. subtilis m1A22 tRNA methyltransferase TrmK: insights into tRNA recognition.
Topics: Anticodon; Bacillus subtilis; Catalytic Domain; Crystallography, X-Ray; Methylation; Protein Conformation; RNA Recognition Motif Proteins; RNA, Transfer; S-Adenosylmethionine; Substrate Specificity; tRNA Methyltransferases | 2019 |