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At higher IPA concentrations translation remains inhibited.
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Here we report achievement of continuous D-amino acid elongation by the use of engineered tRNAs and optimized concentrations of translation factors, enabling us to incorporate up to ten consecutive D-Ser residues into a nascent peptide chain.
As polyamine concentrations influence translation [ 24, 28], we speculated that the time-dependent concentration changes of spermidine and spermine could be associated with the induction of the stress response.
Such sequences are playing an increasingly prominent role in post-transcriptional control devices: by serving as allosteric sites built into mRNA transcripts, they enable coupling between exogenous ligand concentrations and translation rates.
Overnight cultures grown in YPD or SC−Ura, were diluted to an absorbance at 600 nm (A600) of 0.25, followed by 5-fold serial dilutions, and 3 μl of each dilution was spotted on a YPD agar plate containing the indicated concentrations of translation inhibitors, or an SC−Ura agar plate, containing the indicated concentrations of 6AU.
Exquisite dependence on eIF4G concentration for translation initiation may result from reduced eIF4G binding affinity by an mRNA, or from more complex indirect effects on translation factors and ribosome affinity.
Likewise, environmental cues are known to be linked to PD [55], [56] and elicit significant effects on intraneuronal concentrations, post-translation modifications, conformational behavior, and aggregation of α-Syn [57].
Therefore, de novo synthesis of isoleucine was under a complex set of controls comprising antagonistic regulations of both the concentration and translation of mRNA.
They made the surprising observation that sublethal concentrations of translation-inhibiting antibiotics (tetracyclines, aminoglycoside, amphenicols, and macrolides) were effective biofilm-triggering agents.
Since no data are available in literature about the relationship between UCB intracellular concentration and translation rate, there is a compelling need for an accurate proteomic analysis of UCB effects in SH-SY5Y neuroblastoma cells.
This selection could be a result of differences in tRNA concentrations [ 33], translation kinetics [ 34], translation accuracy [ 35, 36], and protein folding [ 37] that are dependent on codon usage, as well as the existence of conserved exonic splicing enhancers and silencers [ 38, 39], or some other yet unknown factors.
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