Evidence map›Paper›PMID 24706556›Full record

ReviewWiley interdisciplinary reviews. RNA

tRNA synthetase: tRNA aminoacylation and beyond.

Yan Ling Joy Pang, Kiranmai Poruri, Susan A Martinis

Abstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

104 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Active transport of tRNAs facilitates distributed protein synthesis.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Structural basis of tRNA recognition by the mNature structural & molecular biology · 2024
    Article
  20. Article

44 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

3 authors at 2 institutions in 1 country.

Yan Ling Joy PangDepartment of Biochemistry, University of Illinois at Urbana, Urbana, IL, USA.
Kiranmai Poruri
Susan A Martinis
University of Illinois Urbana-Champaign · USUrbana University · US

Funding

YEAST RIBOSOMAL STALK COMPOSITION IN VIVO BY TWO-PHOTON FCS AND PCH ANALYSISP41RR003155 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GRATTON, ENRICO · 1986 to 2011
$14.9M
tRNA Synthetase Fidelity MechanismsR01GM063789 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MARTINIS, SUSAN A · 2001 to 2014
$3.3M
Leucyl-tRNA Synthetase Assisted Splicing MechanismsR01GM063107 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI MARTINIS, SUSAN A · 2001 to 2005
$1.1M
NCRR NIH HHS P41 RR003155NIGMS NIH HHS GM63789NIGMS NIH HHS R01 GM063107NIGMS NIH HHS R01 GM063789
6 · The paper itself

Abstract

The aminoacyl-tRNA synthetases are prominently known for their classic function in the first step of protein synthesis, where they bear the responsibility of setting the genetic code. Each enzyme is exquisitely adapted to covalently link a single standard amino acid to its cognate set of tRNA isoacceptors. These ancient enzymes have evolved idiosyncratically to host alternate activities that go far beyond their aminoacylation role and impact a wide range of other metabolic pathways and cell signaling processes. The family of aminoacyl-tRNA synthetases has also been suggested as a remarkable scaffold to incorporate new domains that would drive evolution and the emergence of new organisms with more complex function. Because they are essential, the tRNA synthetases have served as pharmaceutical targets for drug and antibiotic development. The recent unfolding of novel important functions for this family of proteins offers new and promising pathways for therapeutic development to treat diverse human diseases.

Indexed as

Transfer RNA AminoacylationAmino Acyl-tRNA SynthetasesHumansMolecular Targeted TherapyRNA, TransferAmino Acyl-tRNA SynthetasesRNA, Transfer

Identifiers

PMID24706556
PMCPMC4062602
OpenAlexW1489489167

What OpenQuestion holds

Textmetadata
LicenceTDM
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.