Evidence map›Paper›PMID 29447067›Full record

ArticleRNA biology2018

Regulation of eukaryotic elongation factor 1 alpha (eEF1A) by dynamic lysine methylation.

Magnus E Jakobsson, Jędrzej Małecki, Pål Ø Falnes

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 64 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 2 countries.

Magnus E Jakobssona Department of Biosciences , Faculty of Mathematics and Natural Sciences, University of Oslo , Oslo , Norway.
Jędrzej Małeckia Department of Biosciences , Faculty of Mathematics and Natural Sciences, University of Oslo , Oslo , Norway.
Pål Ø Falnesa Department of Biosciences , Faculty of Mathematics and Natural Sciences, University of Oslo , Oslo , Norway.
University of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine methylation is a frequent post-translational protein modification, which has been intensively studied in the case of histone proteins. Lysine methylations are also found on many non-histone proteins, and one prominent example is eukaryotic elongation factor 1 alpha (eEF1A). Besides its essential role in the protein synthesis machinery, a number of non-canonical functions have also been described for eEF1A, such as regulation of the actin cytoskeleton and the promotion of viral replication. The functional significance of the extensive lysine methylations on eEF1A, as well as the identity of the responsible lysine methyltransferases (KMTs), have until recently remained largely elusive. However, recent discoveries and characterizations of human eEF1A-specific KMTs indicate that lysine methylation of eEF1A can be dynamic and inducible, and modulates mRNA translation in a codon-specific fashion. Here, we give a general overview of eEF1A lysine methylation and discuss its possible functional and regulatory significance, with particular emphasis on newly discovered human KMTs.

Indexed as

Actin CytoskeletonEukaryotic Initiation Factor-1Histone-Lysine N-MethyltransferaseHumansLysineMethylationModels, MolecularProtein ConformationProtein Processing, Post-TranslationalVirus ReplicationEukaryotic Initiation Factor-1eukaryotic peptide initiation factor-1AHistone-Lysine N-MethyltransferaseLysineEukaryotic elongation factor 1 alphalysine methylationmethyltransferaseprotein synthesis

Identifiers

PMID29447067
PMCPMC5927720
OpenAlexW2792754462

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.