Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetase

31 Mar 2015

Abstract excerpt

The polyketide natural product borrelidin displays antibacterial, antifungal, antimalarial, anticancer, insecticidal and herbicidal activities through the selective inhibition of threonyl-tRNA synthetase (ThrRS). How borrelidin simultaneously attenuates bacterial growth and suppresses a variety of infections in plants and animals is not known. Here we show, using X-ray crystal structures and functional analyses,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Genomics and Phylogenetic Studies
Share to Microbial Natural Products and Biosynthesis
Share to RNA and protein synthesis mechanisms

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25824639
DOI: 10.1038/ncomms7402

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetasePMID 25824639Read ↗

Aminoacyl-tRNA synthetases: Structure, function, and drug discovery.Semantic proximity Read ↗

Aminoacyl-tRNA synthetases in medicine and disease.Semantic proximity Read ↗

Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design.Semantic proximity Read ↗

Structural analyses of the malaria parasite aminoacyl‐tRNA synthetases provide new avenues for antimalarial drug discoverySemantic proximity Read ↗

Identification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.Semantic proximity Read ↗

Coordination between aminoacylation and editing to protect against proteotoxicity.Semantic proximity Read ↗

Recent Development of Aminoacyl-tRNA Synthetase Inhibitors for Human Diseases: A Future PerspectiveSemantic proximity Read ↗

Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote.Semantic proximity Read ↗

Tryptophanyl-tRNA Synthetase as a Potential Therapeutic TargetSemantic proximity Read ↗

Nucleotidyltransferase toxin MenT targets and extends the aminoacyl acceptor ends of serine tRNAs <i>in vivo</i> to control <i>Mycobacterium tuberculosis</i> growthSemantic proximity Read ↗

Stereochemical basis for engineered pyrrolysyl-tRNA synthetase and the efficient in vivo incorporation of structurally divergent non-native amino acids.Semantic proximity Read ↗

High-Throughput Screening for Protein Synthesis Inhibitors Targeting Aminoacyl-tRNA Synthetases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.