scholarly article | Q13442814 |
P50 | author | Janusz Bujnicki | Q11720088 |
P2093 | author name string | Daniel S Sem | |
James T Anderson | |||
Sarah G Ozanick | |||
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GCD14p, a repressor of GCN4 translation, cooperates with Gcd10p and Lhp1p in the maturation of initiator methionyl-tRNA in Saccharomyces cerevisiae | Q33652039 | ||
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Modulation of tRNA(iMet), eIF-2, and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNA(iMet) ternary complexes | Q36555932 | ||
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The bipartite structure of the tRNA m1A58 methyltransferase from S. cerevisiae is conserved in humans | Q41869952 | ||
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GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3. | Q42675542 | ||
Structural alterations of the tRNA(m1G37)methyltransferase from Salmonella typhimurium affect tRNA substrate specificity | Q43206406 | ||
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Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme | Q44828360 | ||
Sequence-structure-function relationships of a tRNA (m7G46) methyltransferase studied by homology modeling and site-directed mutagenesis | Q46403152 | ||
Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes. | Q51135032 | ||
Effect of modified nucleotides on Escherichia coli tRNAGlu structure and on its aminoacylation by glutamyl-tRNA synthetase. Predominant and distinct roles of the mnm5 and s2 modifications of U34 | Q73231471 | ||
Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy | Q88519866 | ||
P433 | issue | 20 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Saccharomyces cerevisiae | Q719725 |
P304 | page(s) | 6808-6819 | |
P577 | publication date | 2007-10-10 | |
P1433 | published in | Nucleic Acids Research | Q135122 |
P1476 | title | Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding | |
P478 | volume | 35 |