Results 71 to 80 of about 324,922 (336)

Enhancing Specificity, Precision, Accessibility, Flexibility, and Safety to Overcome Traditional CRISPR/Cas Editing Challenges and Shape Future Innovations

open access: yesAdvanced Science, EarlyView.
CRISPR/Cas9, while transformative, faces challenges in specificity, precision, delivery, accessibility, flexibility, and safety. This review addresses these limitations by highlighting strategies to reduce off‐target effects, exploring HDR‐based and alternative editing approaches, and evaluating advanced delivery mechanisms.
Muna Alariqi   +8 more
wiley   +1 more source

Uncharged tRNA Activates GCN2 by Displacing the Protein Kinase Moiety from a Bipartite tRNA-Binding Domain [PDF]

open access: yes, 2000
Protein kinase GCN2 regulates translation in amino acid–starved cells by phosphorylating eIF2. GCN2 contains a regulatory domain related to histidyl-tRNA synthetase (HisRS) postulated to bind multiple deacylated tRNAs as a general sensor of starvation ...
Anderson, James T.   +4 more
core   +1 more source

15N NMR study of a mixture of uniformly labeled tRNAs [PDF]

open access: yes, 1982
15N NMR spectra were taken of 15N-enriched tRNA extracted from bakers yeast; ammonium sulfate was used as a nitrogen source. The increase in the degree of denaturation of tRNA, which occurs with increase in temperature from 30 degrees C to 70 degrees C ...
Birdseye, Theresa R.   +3 more
core   +1 more source

Small RNA Toxin‐Assisted Evolution of GC‐Preferred ErCas12a for Enhanced Genome Targeting Range

open access: yesAdvanced Science, EarlyView.
ErCas12a is engineered to target GC‐rich PAMs using a small RNA toxin‐aided positive screening system. The resulting variant, enErCas12a, exhibits an expanded PAM profile and facilitates efficient gene editing in both bacterial and mammalian cells, while preserving high targeting specificity for both canonical and non‐canonical PAM targets.
Zehua Chen   +8 more
wiley   +1 more source

Aminoacyl-tRNA synthetase-induced cleavage of tRNA

open access: yesNucleic Acids Research, 1992
Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutaminyl-tRNA synthetase destabilizes tRNA(Gln) causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends.
Sergey Beresten   +2 more
openaire   +4 more sources

Drugging tRNA aminoacylation [PDF]

open access: yesRNA Biology, 2018
Inhibition of tRNA aminoacylation has proven to be an effective antimicrobial strategy, impeding an essential step of protein synthesis. Mupirocin, the well-known selective inhibitor of bacterial isoleucyl-tRNA synthetase, is one of three aminoacylation inhibitors now approved for human or animal use.
Joanne M. Ho   +3 more
openaire   +3 more sources

A eubacterial origin for the human tRNA nucleotidyltransferase? [PDF]

open access: yes, 2001
tRNA CCA-termini are generated and maintained by tRNA nucleotidyltransferases. Together with poly(A) polymerases and other enzymes they belong to the nucleotidyltransferase superfamily.
Aebi M.   +12 more
core   +1 more source

Hosts and Commensal Bacteria Synergistically Antagonize Opportunistic Pathogens at the Single‐Cell Resolution

open access: yesAdvanced Science, EarlyView.
In the tripartite‐species model, Drosophila larvae stimulate lactate production through excreting digestion enzymes. S. marcescens population senses a cue of lactate and tends to diverge into virulent and reduced virulence subclusters with remarkable heterogeneity to metabolize carbon metabolism and counter colonization resistance, giving a fitness ...
Sheng Zhang   +10 more
wiley   +1 more source

tRNA-tRNA interactions within cellular ribosomes. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1989
We describe an assay that converts the effects of tRNA-tRNA contacts at two particular codons into a quantitative effect on beta-galactosidase level. The assay measures the separate and combined efficiency of suppression at adjacent nonsense codons in vivo using a set of specially created homologous messages.
Michael Yarus, Drew Smith
openaire   +3 more sources

Role of the Bifunctional Aminoacyl-tRNA Synthetase EPRS in Human Disease [PDF]

open access: yes, 2020
Aminoacyl-tRNA synthetases (AARS) are a class of enzymes that catalyze the charging of tRNAs with cognate amino acids, a critical step that contributes to the fidelity of protein synthesis.
Kudlapur, Nathan
core  

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