Evidence map›Paper›PMID 30670594›Full record

ReviewThe Journal of biological chemistry2019

Progress and challenges in aminoacyl-tRNA synthetase-based therapeutics.

Christopher S Francklyn, Patrick Mullen

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed, 2 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

74 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Suppression rather than activation of the integrated stress response (GCN2-ATF4) pathway extends lifespan in the fly.Proceedings of the National Academy of Sciences of the United States of America · 2026
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14 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Christopher S FrancklynFrom the Department of Biochemistry, College of Medicine, University of Vermont, Burlington, Vermont 05405 christopher.francklyn@uvm.edu.
Patrick MullenFrom the Department of Biochemistry, College of Medicine, University of Vermont, Burlington, Vermont 05405.

Funding

Structure and Mechanism of Class II tRNA SynthetasesR01GM054899 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI FRANCKLYN, CHRISTOPHER S · 1997 to 2017
$5.7M
NIGMS NIH HHS R01 GM054899
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases (ARSs) are universal enzymes that catalyze the attachment of amino acids to the 3' ends of their cognate tRNAs. The resulting aminoacylated tRNAs are escorted to the ribosome where they enter protein synthesis. By specifically matching amino acids to defined anticodon sequences in tRNAs, ARSs are essential to the physical interpretation of the genetic code. In addition to their canonical role in protein synthesis, ARSs are also involved in RNA splicing, transcriptional regulation, translation, and other aspects of cellular homeostasis. Likewise, aminoacylated tRNAs serve as amino acid donors for biosynthetic processes distinct from protein synthesis, including lipid modification and antibiotic biosynthesis. Thanks to the wealth of details on ARS structures and functions and the growing appreciation of their additional roles regulating cellular homeostasis, opportunities for the development of clinically useful ARS inhibitors are emerging to manage microbial and parasite infections. Exploitation of these opportunities has been stimulated by the discovery of new inhibitor frameworks, the use of semi-synthetic approaches combining chemistry and genome engineering, and more powerful techniques for identifying leads from the screening of large chemical libraries. Here, we review the inhibition of ARSs by small molecules, including the various families of natural products, as well as inhibitors developed by either rational design or high-throughput screening as antibiotics and anti-parasitic therapeutics.

Indexed as

Amino Acyl-tRNA SynthetasesAnti-Bacterial AgentsAntiparasitic AgentsEnzyme InhibitorsInfectionsParasitic DiseasesAnimalsHumansRNA SplicingRNA, TransferAmino Acyl-tRNA SynthetasesAnti-Bacterial AgentsAntiparasitic AgentsEnzyme InhibitorsRNA, Transferaminoacyl sulfamateaminoacyl tRNA synthetaseantibiotic actioninhibitormalariamupirocinpeptidyl transferasetransfer RNA (tRNA)translationTrojan horse approach

Identifiers

PMID30670594
PMCPMC6462538

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.