Evidence map›Paper›PMID 29743234›Full record

ArticleThe Journal of biological chemistry2018

The ribosome: A hot spot for the identification of new types of protein methyltransferases.

Steven G Clarke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  7. Review
  8. Review
  9. Arginine Methylation Regulates Ribosome CAR Function.International journal of molecular sciences · 2021
    Article
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  11. Review
  12. Article
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  15. 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

1 author at 1 institution in 1 country.

Steven G ClarkeFrom the Department of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, Los Angeles, California 90095 clarke@mbi.ucla.edu.ORCID 0000-0002-7303-6632
UCLA Medical Center · US

Funding

CONTROL OF EUCARYOTIC FUNCTION BY METHYLATIONR37GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 2000 to 2009
$5.0M
CONTROL OF EUKARYOTIC MEMBRANE FUNCTION BY METHYLATIONR01GM026020 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, STEVEN G · 1985 to 2013
$2.1M
NIGMS NIH HHS R01 GM026020NIGMS NIH HHS R37 GM026020
6 · The paper itself

Abstract

Cellular physiology depends on the alteration of protein structures by covalent modification reactions. Using a combination of bioinformatic, genetic, biochemical, and mass spectrometric approaches, it has been possible to probe ribosomal proteins from the yeast

Indexed as

Awards and PrizesProtein BiosynthesisProtein Processing, Post-TranslationalHistonesMethylationProtein MethyltransferasesRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHistonesProtein MethyltransferasesRibosomal ProteinsSaccharomyces cerevisiae Proteinspost-translational modification (PTM)protein methylationprotein methyltransferaseribosomeribosome structuretranslation elongation factor

Identifiers

PMID29743234
PMCPMC6036201
OpenAlexW2802476942

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.