Evidence map›Paper›PMID 23416400›Full record

ReviewNature chemical biology2013

Essential nontranslational functions of tRNA synthetases.

Min Guo, Paul Schimmel

Abstract readReview
In one paragraph

Review in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 232 papers.

0numbers the graph read from it
0cells of the map it votes in
232citing papers in PubMed
13.8field-weighted citation impact, top 1% of its field
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

232 citing papers in PubMed, 355 citations in OpenAlex.

  1. Article
  2. Review
  3. The theory of the inflammatory ecosystem.Science China. Life sciences · 2026
    Review
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  5. Tyrosine Supplementation Rescues a Growth Defect in a HumanizedInternational journal of molecular sciences · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026
    Article
  13. Isoleucyl-tRNA synthetase 1 is essential for embryogenesis in mice.The Journal of veterinary medical science · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

172 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 at 1 institution in 1 country.

Min GuoDepartment of Cancer Biology, The Scripps Research Institute, Jupiter, Florida, USA.
Paul Schimmel
Scripps Research Institute · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
GENETIC APPROACHES TO PROTEIN/NUCLEIC ACID INTERACTIONSR01GM023562 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2012
$4.9M
Components of Translation in Signal TransductionR01CA092577 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 2001 to 2016
$4.5M
Structural and Functional Studies of LysRS in Mast Cell ActivationR01GM100136 · NIGMS · SCRIPPS FLORIDA · PI KODADEK, THOMAS J. · 2012 to 2016
$1.9M
NCI NIH HHS CA92577NCI NIH HHS R01 CA092577NCRR NIH HHS P41 RR001209NIGMS NIH HHS GM 100136NIGMS NIH HHS GM 23562NIGMS NIH HHS R01 GM023562NIGMS NIH HHS R01 GM100136
6 · The paper itself

Abstract

Nontranslational functions of vertebrate aminoacyl tRNA synthetases (aaRSs), which catalyze the production of aminoacyl-tRNAs for protein synthesis, have recently been discovered. Although these new functions were thought to be 'moonlighting activities', many are as critical for cellular homeostasis as their activity in translation. New roles have been associated with their cytoplasmic forms as well as with nuclear and secreted extracellular forms that affect pathways for cardiovascular development and the immune response and mTOR, IFN-γ and p53 signaling. The associations of aaRSs with autoimmune disorders, cancers and neurological disorders further highlight nontranslational functions of these proteins. New architecture elaborations of the aaRSs accompany their functional expansion in higher organisms and have been associated with the nontranslational functions for several aaRSs. Although a general understanding of how these functions developed is limited, the expropriation of aaRSs for essential nontranslational functions may have been initiated by co-opting the amino acid-binding site for another purpose.

Indexed as

Amino Acyl-tRNA SynthetasesAnimalsBiocatalysisHumansModels, MolecularProtein BiosynthesisRNA, Transfer, Amino AcylAmino Acyl-tRNA SynthetasesRNA, Transfer, Amino Acyl

Identifiers

PMID23416400
PMCPMC3773598
OpenAlexW2050299992

What OpenQuestion holds

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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.