proline has been researched along with anticodon in 12 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 5 (41.67) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 4 (33.33) | 29.6817 |
2010's | 2 (16.67) | 24.3611 |
2020's | 1 (8.33) | 2.80 |
Authors | Studies |
---|---|
Buckingham, RH | 1 |
Culbertson, MR; Cummins, CM; Knapp, G | 1 |
Hasegawa, T; Ishikura, H; Murao, K | 1 |
Barrett, JC; Miller, PS; Ts'o, PO | 1 |
Kawakami, M; Kondo, T; Ogawa, K; Takemura, S | 1 |
O'Connor, M | 1 |
Hou, YM; Lipman, RS; Sowers, KR; Wang, J | 1 |
Feng, L; Söll, D; Toogood, H; Tumbula-Hansen, D; Yuan, J | 1 |
Christian, T; Evilia, C; Hou, YM | 1 |
Bacusmo, JM; Cantara, WA; Goto, Y; Kuzmishin, AB; Musier-Forsyth, K; Suga, H | 1 |
Akinpelu, IC; Berg, MD; Brandl, CJ; Duennwald, ML; Heinemann, IU; Hoffman, KS; Lant, JT; O'Donoghue, P; Sze, DHW; Turk, MA | 1 |
Christian, T; Detroja, R; Frenkel-Morgenstern, M; Hou, YM; Lowe, TM; Maharjan, S; Masuda, I; Matsubara, R; Moore, H; Nakano, Y; Tagore, S; Yamaki, Y | 1 |
12 other study(ies) available for proline and anticodon
Article | Year |
---|---|
Anticodon conformation and accessibility in wild-type and suppressor tryptophan tRNA from E. coli.
Topics: Anticodon; Base Sequence; Binding Sites; Escherichia coli; Nucleic Acid Conformation; Proline; RNA, Bacterial; RNA, Transfer; Tryptophan | 1976 |
Frameshift suppressor mutations outside the anticodon in yeast proline tRNAs containing an intervening sequence.
Topics: Anticodon; Base Sequence; Codon; DNA, Fungal; DNA, Recombinant; Genes, Fungal; Mutation; Nucleic Acid Conformation; Proline; Repetitive Sequences, Nucleic Acid; RNA Processing, Post-Transcriptional; RNA, Transfer; Saccharomyces cerevisiae; Suppression, Genetic | 1985 |
The nucleotide sequence of proline tRNAmo5UGG from Bacillus subtilis.
Topics: Anticodon; Bacillus subtilis; Base Sequence; Nucleic Acid Conformation; Proline; RNA, Transfer | 1985 |
Inhibitory effect of complex formation with oligodeoxyribonucleotide ethyl phosphotriesters on transfer ribonucleic acid aminoacylation.
Topics: Amino Acyl-tRNA Synthetases; Anticodon; Base Sequence; Binding Sites; Deoxyribonucleotides; Diphosphates; Escherichia coli; Kinetics; Leucine; Lysine; Oligonucleotides; Phenylalanine; Phosphorus Radioisotopes; Proline; Protein Binding; RNA, Bacterial; RNA, Transfer; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Time Factors; Tritium; Tyrosine | 1974 |
A modified nucleoside located in the anticodon of proline tRNA from Torulopsis utilis is 5-carbamoylmethyluridine.
Topics: Anticodon; Candida; Magnetic Resonance Spectroscopy; Mass Spectrometry; Proline; RNA, Transfer; Spectrophotometry, Ultraviolet; Uridine | 1983 |
Imbalance of tRNA(Pro) isoacceptors induces +1 frameshifting at near-cognate codons.
Topics: Alcohol Oxidoreductases; Anticodon; Bacterial Proteins; Base Sequence; beta-Galactosidase; Codon; Frameshift Mutation; Frameshifting, Ribosomal; Gene Expression Regulation, Bacterial; Genes, Bacterial; Genes, Reporter; Mutation; Nucleic Acid Conformation; Plasmids; Proline; RNA, Bacterial; RNA, Transfer, Pro; Salmonella typhimurium; Suppression, Genetic; Transaminases | 2002 |
Prevention of mis-aminoacylation of a dual-specificity aminoacyl-tRNA synthetase.
Topics: Acylation; Adenosine Triphosphate; Amino Acyl-tRNA Synthetases; Anticodon; Base Sequence; Binding Sites; Cysteine; Genetic Engineering; Kinetics; Methanococcus; Molecular Sequence Data; Mutation; Nucleic Acid Conformation; Proline; RNA Editing; RNA, Transfer, Cys; RNA, Transfer, Pro; Substrate Specificity; Thermodynamics; Transcription, Genetic | 2002 |
Aspartyl-tRNA synthetase requires a conserved proline in the anticodon-binding loop for tRNA(Asn) recognition in vivo.
Topics: Acylation; Amino Acid Sequence; Anticodon; Aspartate-tRNA Ligase; Aspartic Acid; Binding Sites; Conserved Sequence; Deinococcus; DNA, Bacterial; Escherichia coli; Gene Expression; Molecular Sequence Data; Mutagenesis; Proline; Protein Conformation; Recombinant Proteins; RNA, Transfer, Asn; Sequence Alignment; Structure-Activity Relationship; Substrate Specificity; Transformation, Bacterial | 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 |
Quality control by trans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate.
Topics: Alanine; Amino Acyl-tRNA Synthetases; Aminobutyrates; Anticodon; Binding Sites; Codon; Escherichia coli; Kinetics; Molecular Docking Simulation; Mutation; Nucleic Acid Conformation; Proline; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Rhodopseudomonas; RNA Processing, Post-Transcriptional; RNA, Transfer, Pro; Substrate Specificity; Transfer RNA Aminoacylation | 2018 |
Visualizing tRNA-dependent mistranslation in human cells.
Topics: Alanine; Amino Acyl-tRNA Synthetases; Aminoacylation; Anticodon; Cell Survival; Codon; Culture Media; Escherichia coli; Genes, Reporter; Glucose; Green Fluorescent Proteins; HEK293 Cells; Humans; Mutation; Plasmids; Proline; Proteasome Endopeptidase Complex; Protein Biosynthesis; RNA Processing, Post-Transcriptional; RNA, Transfer, Pro; Transfection | 2018 |
tRNA methylation resolves codon usage bias at the limit of cell viability.
Topics: Anticodon; Cell Survival; Codon; Codon Usage; Escherichia coli; Guanosine; Methylation; Proline; RNA, Transfer | 2022 |