Evidence map›Paper›PMID 21172665›Full record

ArticleMolecular cell2010

TDRD3 is an effector molecule for arginine-methylated histone marks.

Yanzhong Yang, Yue Lu, Alexsandra Espejo, Jiacai Wu, Wei Xu, Shoudan Liang, Mark T Bedford

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

147 citing papers in PubMed, 231 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Current aging science · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The emerging role of CARM1 in cancer.Cellular oncology (Dordrecht, Netherlands) · 2024
    Review
  19. Article
  20. Article

87 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

Yanzhong YangThe University of Texas MD Anderson Cancer Center, Science Park-Research Division, P.O. Box 389, Smithville, TX 78957, USA.
Yue Lu
Alexsandra Espejo
Jiacai Wu
Wei Xu
Shoudan Liang
Mark T Bedford
The University of Texas MD Anderson Cancer Center · USUniversity of Wisconsin–Madison · US

Funding

Pilot Project ProgramP30ES007784 · NIEHS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI SHEN, JIANJUN · 1996 to 2011
$16.4M
The Functional Analysis of the Coactivator CARM1R01DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T. · 2002 to 2015
$4.2M
Genome-wide Identification of Minor Histocompatibility AntigensK25CA123344 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI LIANG, SHOUDAN · 2008 to 2012
$734k
The Functional Analysis of the Coactivator CARM1R56DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T · 2007 to 2007
$77k
NCI NIH HHS K25 CA123344NIDDK NIH HHS DK62248NIDDK NIH HHS R01 DK062248NIDDK NIH HHS R56 DK062248NIEHS NIH HHS ES07784NIEHS NIH HHS P30 ES007784
6 · The paper itself

Abstract

Specific sites of histone tail methylation are associated with transcriptional activity at gene loci. These methyl marks are interpreted by effector molecules, which harbor protein domains that bind the methylated motifs and facilitate either active or inactive states of transcription. CARM1 and PRMT1 are transcriptional coactivators that deposit H3R17me2a and H4R3me2a marks, respectively. We used a protein domain microarray approach to identify the Tudor domain-containing protein TDRD3 as a "reader" of these marks. Importantly, TDRD3 itself is a transcriptional coactivator. This coactivator activity requires an intact Tudor domain. TDRD3 is recruited to an estrogen-responsive element in a CARM1-dependent manner. Furthermore, ChIP-seq analysis of TDRD3 reveals that it is predominantly localized to transcriptional start sites. Thus, TDRD3 is an effector molecule that promotes transcription by binding methylarginine marks on histone tails.

Indexed as

ArginineCARD Signaling Adaptor ProteinsGuanylate CyclaseHistonesHumansMethylationProtein-Arginine N-MethyltransferasesProtein Array AnalysisProteinsRepressor ProteinsTranscription, GeneticArginineCARD11 protein, humanCARD Signaling Adaptor ProteinsGuanylate CyclaseHistonesPRMT1 protein, humanProtein-Arginine N-MethyltransferasesProteinsRepressor ProteinsTdrd3 protein, human

Identifiers

PMID21172665
PMCPMC3090733
OpenAlexW2026081838

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.