Evidence map›Paper›PMID 39247978›Full record

ArticleIUBMB life2024

AARS Online: A collaborative database on the structure, function, and evolution of the aminoacyl-tRNA synthetases.

Jordan Douglas, Haissi Cui, John J Perona, Oscar Vargas-Rodriguez, Henna Tyynismaa, Claudia Alvarez Carreño, Jiqiang Ling, Lluís Ribas de Pouplana, Xiang-Lei Yang, Michael Ibba and 5 more

Abstract read
In one paragraph

Article in IUBMB life, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–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

12 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Protein Structural Phylogenetics.Genome biology and evolution · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Article
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

15 authors.

Jordan DouglasDepartment of Physics, University of Auckland, New Zealand.ORCID 0000-0003-0371-9961
Haissi CuiDepartment of Chemistry, University of Toronto, Canada.
John J PeronaDepartment of Chemistry, Portland State University, Portland, Oregon, USA.
Oscar Vargas-RodriguezDepartment of Molecular Biology and Biophysics, University of Connecticut, Storrs, Connecticut, USA.ORCID 0000-0002-2301-2800
Henna TyynismaaStem Cells and Metabolism Research Program, Faculty of Medicine, University of Helsinki, Finland.
Claudia Alvarez CarreñoInstitute of Structural and Molecular Biology, University College of London, UK.
Jiqiang LingDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland, USA.ORCID 0000-0003-4466-8304
Lluís Ribas de PouplanaInstitute for Research in Biomedicine, The Barcelona Institute of Science and Technology, Barcelona, Catalonia, Spain.
Xiang-Lei YangDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, California, USA.
Michael IbbaBiological Sciences, Chapman University, Orange, California, USA.
Hubert BeckerGénétique Moléculaire, Génomique Microbiologique, University of Strasbourg, France.
Frédéric FischerGénétique Moléculaire, Génomique Microbiologique, University of Strasbourg, France.
Marie SisslerGénétique Moléculaire, Génomique Microbiologique, University of Strasbourg, France.
Charles W CarterDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.ORCID 0000-0002-2653-4452
Peter R WillsDepartment of Physics, University of Auckland, New Zealand.

Funding

Link extracellular function of tRNA synthetase with pathological mechanism of diseaseR35GM139627 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI YANG, XIANG-LEI · 2021 to 2025
$2.3M
Regulation and Physiological Roles of Translational FidelityR35GM136213 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI LING, JIQIANG · 2020 to 2024
$2.0M
Academy of FinlandAlfred P. Sloan Foundation G-2021-16944CIHRNatural Sciences and Engineering Research Council of CanadaNIGMS NIH HHS R35 GM136213NIGMS NIH HHS R35 GM139627Royal SocietySigrid Juselius Foundation
6 · The paper itself

Abstract

The aminoacyl-tRNA synthetases (aaRS) are a large group of enzymes that implement the genetic code in all known biological systems. They attach amino acids to their cognate tRNAs, moonlight in various translational and non-translational activities beyond aminoacylation, and are linked to many genetic disorders. The aaRS have a subtle ontology characterized by structural and functional idiosyncrasies that vary from organism to organism, and protein to protein. Across the tree of life, the 22 coded amino acids are handled by 16 evolutionary families of Class I aaRS and 21 families of Class II aaRS. We introduce AARS Online, an interactive Wikipedia-like tool curated by an international consortium of field experts. This platform systematizes existing knowledge about the aaRS by showcasing a taxonomically diverse selection of aaRS sequences and structures. Through its graphical user interface, AARS Online facilitates a seamless exploration between protein sequence and structure, providing a friendly introduction to the material for non-experts and a useful resource for experts. Curated multiple sequence alignments can be extracted for downstream analyses. Accessible at www.aars.online, AARS Online is a free resource to delve into the world of the aaRS.

Indexed as

Amino Acyl-tRNA SynthetasesEvolution, MolecularAmino Acid SequenceAnimalsDatabases, ProteinHumansInternetUser-Computer InterfaceAmino Acyl-tRNA Synthetasesaminoacyl‐tRNA synthetasesdatabaseprotein structure

Identifiers

PMID39247978
PMCPMC11580382

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.