Evidence map›Paper›PMID 22345066›Full record

ReviewMolecular reproduction and development2012

Arginine methylation of RNA-binding proteins regulates cell function and differentiation.

Ernest Blackwell, Stephanie Ceman

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular reproduction and development, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

41 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  5. Article
  6. Article
  7. Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023
    Review
  8. Article
  9. Article
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  11. Review
  12. Article
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  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Cellular consequences of arginine methylation.Cellular and molecular life sciences : CMLS · 2019
    Review
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.

Ernest BlackwellDepartment of Cell and Developmental Biology, Neuroscience Program and College of Medicine, University of Illinois, Urbana-Champaign, Illlinois, USA.
Stephanie Ceman
University of Illinois Urbana-Champaign · US

Funding

DEVELOPMENT PSYCHOBIOLOGY AND NEUROBIOLOGYT32HD007333 · NICHD · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI JURASKA, JANICE M · 1987 to 2011
$3.0M
NICHD NIH HHS 2T32HD007333-21NICHD NIH HHS T32 HD007333
6 · The paper itself

Abstract

Arginine methylation is a post-translational modification that regulates protein function. RNA-binding proteins are an important class of cell-function mediators, some of which are methylated on arginine. Early studies of RNA-binding proteins and arginine methylation are briefly introduced, and the enzymes that mediate this post-translational modification are described. We review the most common RNA-binding domains and briefly discuss how they associate with RNAs. We address the following groups of RNA-binding proteins: hnRNP, Sm, Piwi, Vasa, FMRP, and HuD. hnRNPs were the first RNA-binding proteins found to be methylated on arginine. The Sm proteins function in RNA processing and germ cell specification. The Piwi proteins are largely germ cell specific and are also required for germ cell production, as is Vasa. FMRP participates in germ cell formation in Drosophila, but is more widely known for its neuronal function. Similarly, HuD plays a role in nervous system development and function. We review the effects of arginine methylation on the function of each protein, then conclude by addressing remaining questions and future directions of arginine methylation as an important and emerging area of regulation.

Indexed as

AnimalsArginineCell DifferentiationDrosophilaGerm CellsMethylationProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalRNA-Binding ProteinsArginineProtein-Arginine N-MethyltransferasesRNA-Binding Proteins

Identifiers

PMID22345066
PMCPMC3286031
OpenAlexW2028721495

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.