Evidence map›Paper›PMID 18538672›Full record

ArticleFEBS letters2008

Structural and functional mapping of the archaeal multi-aminoacyl-tRNA synthetase complex.

Corinne D Hausmann, Michael Ibba

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020
    Review
  5. Aminoacyl-tRNA synthetase complexes in evolution.International journal of molecular sciences · 2015
    Review
  6. Article
  7. Architecture and metamorphosis.Topics in current chemistry · 2014
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

2 authors at 1 institution in 1 country.

Corinne D HausmannDepartment of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA.
Michael Ibba
The Ohio State University · US

Funding

Mechanisms of translational controlR01GM065183 · NIGMS · OHIO STATE UNIVERSITY · PI DUNHAM, CHRISTINE M, FREDRICK, KURT L · 2003 to 2020
$4.9M
NIGMS NIH HHS GM 65183NIGMS NIH HHS R01 GM065183
6 · The paper itself

Abstract

Methanothermobacter thermautotrophicus contains a multi-aminoacyl-tRNA synthetase complex (MSC) of LysRS, LeuRS and ProRS. Elongation factor (EF) 1A also associates to the MSC, with LeuRS possibly acting as a core protein. Analysis of the MSC revealed that LysRS and ProRS specifically interact with the idiosyncratic N- and C- termini of LeuRS, respectively. EF-1A instead interacts with the inserted CP1 proofreading domain, consistent with models for post-transfer editing by class I synthetases such as LeuRS. Together with previous genetic data, these findings show that LeuRS plays a central role in mediating interactions within the archaeal MSC by acting as a core scaffolding protein.

Indexed as

Amino Acyl-tRNA SynthetasesArchaeal ProteinsLeucine-tRNA LigaseLysine-tRNA LigaseMethanobacteriaceaeMultienzyme ComplexesPeptide Elongation Factor 1Protein ConformationAmino Acyl-tRNA SynthetasesArchaeal ProteinsLeucine-tRNA LigaseLysine-tRNA LigaseMultienzyme ComplexesPeptide Elongation Factor 1prolyl T RNA synthetase

Identifiers

PMID18538672
PMCPMC2486338
OpenAlexW1975085856

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.