Evidence map›Paper›PMID 33081015›Full record

ArticleGenes2020

Fine-Tuning of Alanyl-tRNA Synthetase Quality Control Alleviates Global Dysregulation of the Proteome.

Paul Kelly, Arundhati Kavoor, Michael Ibba

Open access · goldAbstract read
In one paragraph

Article in Genes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 54% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

3 authors at 1 institution in 1 country.

Paul KellyThe Ohio State University Molecular, Cellular and Developmental Biology Program, The Ohio State University, Columbus, OH 43210, USA.
Arundhati KavoorThe Ohio State University Molecular, Cellular and Developmental Biology Program, The Ohio State University, Columbus, OH 43210, USA.
Michael IbbaThe Ohio State University Molecular, Cellular and Developmental Biology Program, The Ohio State University, Columbus, OH 43210, USA.
The Ohio State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One integral step in the transition from a nucleic acid encoded-genome to functional proteins is the aminoacylation of tRNA molecules. To perform this activity, aminoacyl-tRNA synthetases (aaRSs) activate free amino acids in the cell forming an aminoacyl-adenylate before transferring the amino acid on to its cognate tRNA. These newly formed aminoacyl-tRNA (aa-tRNA) can then be used by the ribosome during mRNA decoding. In

Indexed as

MutationAlanine-tRNA LigaseAmino AcidsAmino Acid SequenceEscherichia coliEscherichia coli ProteinsProteomeQuality ControlRNA, Transfer, Amino AcylSequence HomologySubstrate SpecificityAlanine-tRNA LigaseAmino AcidsEscherichia coli ProteinsProteomeRNA, Transfer, Amino Acylaminoacyl-tRNA synthetasestranslational fidelitytRNA

Identifiers

PMID33081015
PMCPMC7603204
OpenAlexW3093461831

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.