Evidence map›Paper›PMID 23066109›Full record

ArticleNucleic acids research2012

Recognition of asymmetrically dimethylated arginine by TDRD3.

Tomas Sikorsky, Fruzsina Hobor, Eva Krizanova, Josef Pasulka, Karel Kubicek, Richard Stefl

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Contribution of Electrostatic CHJournal of the American Chemical Society · 2024
    Article
  3. Review
  4. Effectors and effects of arginine methylation.Biochemical Society transactions · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Targeting non-bromodomain chromatin readers.Nature structural & molecular biology · 2019
    Review
  14. Review
  15. Article
  16. Different phosphoisoforms of RNA polymerase II engage the Rtt103 termination factor in a structurally analogous manner.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Effect of methylation on the side-chain pKa value of arginine.Protein science : a publication of the Protein Society · 2016
    Article
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Tomas SikorskyCEITEC-Central European Institute of Technology, Masaryk University, CZ-62500 Brno, Czech Republic.
Fruzsina Hobor
Eva Krizanova
Josef Pasulka
Karel Kubicek
Richard Stefl
Central European Institute of Technology · CZCentral European Institute of Technology – Masaryk University · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Asymmetric dimethylarginine (aDMA) marks are placed on histones and the C-terminal domain (CTD) of RNA Polymerase II (RNAP II) and serve as a signal for recruitment of appropriate transcription and processing factors in coordination with transcription cycle. In contrast to other Tudor domain-containing proteins, Tudor domain-containing protein 3 (TDRD3) associates selectively with the aDMA marks but not with other methylarginine motifs. Here, we report the solution structure of the Tudor domain of TDRD3 bound to the asymmetrically dimethylated CTD. The structure and mutational analysis provide a molecular basis for how TDRD3 recognizes the aDMA mark. The unique aromatic cavity of the TDRD3 Tudor domain with a tyrosine in position 566 creates a selectivity filter for the aDMA residue. Our work contributes to the understanding of substrate selectivity rules of the Tudor aromatic cavity, which is an important structural motif for reading of methylation marks.

Indexed as

Amino AcidsAmino Acid SequenceArginineHydrogen BondingModels, MolecularMolecular Sequence DataMutationProteinsProtein Structure, TertiarySequence AlignmentAmino AcidsArginineN,N-dimethylarginineProteinsTdrd3 protein, human

Identifiers

PMID23066109
PMCPMC3526276
OpenAlexW2135449167

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.