Evidence map›Paper›PMID 19932696›Full record

ReviewFEBS letters2010

Functional expansion of human tRNA synthetases achieved by structural inventions.

Min Guo, Paul Schimmel, Xiang-Lei Yang

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

66 citing papers in PubMed, 104 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Tryptophanyl-tRNA Synthetase as a Potential Therapeutic Target.International journal of molecular sciences · 2021
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

6 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 1 institution in 1 country.

Min GuoThe Skaggs Institute for Chemical Biology, Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Paul Schimmel
Xiang-Lei Yang
Scripps Research Institute · US

Funding

SCRIPPS TRANSLATIONAL SCIENCE INSTITUTE (UL1)UL1RR025774 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI TOPOL, ERIC JEFFREY · 2008 to 2011
$16.3M
INVESTIGATIONS OF REACTIONS OF PHYSIOLOGICAL IMPORTANCER01GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2011
$6.6M
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
REACTIONS OF PHYSIOLOGICAL IMPORTANCER37GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI SCHIMMEL, PAUL R · 1989 to 1998
–
NCI NIH HHS CA92577NCI NIH HHS R01 CA092577NCRR NIH HHS U54RR025204NCRR NIH HHS UL1 RR025774NIGMS NIH HHS GM 15539NIGMS NIH HHS GM 23562NIGMS NIH HHS R01 GM015539NIGMS NIH HHS R01 GM023562
6 · The paper itself

Abstract

Known as an essential component of the translational apparatus, the aminoacyl-tRNA synthetase family catalyzes the first step reaction in protein synthesis, that is, to specifically attach each amino acid to its cognate tRNA. While preserving this essential role, tRNA synthetases developed other roles during evolution. Human tRNA synthetases, in particular, have diverse functions in different pathways involving angiogenesis, inflammation and apoptosis. The functional diversity is further illustrated in the association with various diseases through genetic mutations that do not affect aminoacylation or protein synthesis. Here we review the accumulated knowledge on how human tRNA synthetases used structural inventions to achieve functional expansions.

Indexed as

Protein BiosynthesisAmino Acyl-tRNA SynthetasesCatalytic DomainHumansAmino Acyl-tRNA Synthetases

Identifiers

PMID19932696
PMCPMC2826164
OpenAlexW1967509044

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.