Evidence map›Paper›PMID 14603321›Full record

ArticleNature2003

Methylation at lysine 4 of histone H3 in ecdysone-dependent development of Drosophila.

Yurii Sedkov, Elizabeth Cho, Svetlana Petruk, Lucy Cherbas, Sheryl T Smith, Richard S Jones, Peter Cherbas, Eli Canaani, James B Jaynes, Alexander Mazo

Open access · greenAbstract read
In one paragraph

Article in Nature, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing 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

80 citing papers in PubMed, 180 citations in OpenAlex.

  1. Article
  2. Review
  3. bioRxiv : the preprint server for biology · 2025
    Article
  4. Loss-of-function in RBBP5 results in a syndromic neurodevelopmental disorder associated with microcephaly.Genetics in medicine : official journal of the American College of Medical Genetics · 2024
    Article
  5. Review
  6. Article
  7. Coregulators Reside withinInternational journal of molecular sciences · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Reprogramming of the epigenome in neurodevelopmental disorders.Critical reviews in biochemistry and molecular biology · 2022
    Review
  12. Article
  13. Article
  14. The MLL/SET family and haematopoiesis.Biochimica et biophysica acta. Gene regulatory mechanisms · 2020
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

20 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

10 authors at 5 institutions in 2 countries.

Yurii SedkovKimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
Elizabeth Cho
Svetlana Petruk
Lucy Cherbas
Sheryl T Smith
Richard S Jones
Peter Cherbas
Eli Canaani
James B Jaynes
Alexander Mazo
Sidney Kimmel Cancer Center · USThomas Jefferson University · USIndiana University Bloomington · USSouthern Methodist University · USWeizmann Institute of Science · IL

Funding

TRANSCRIPTIONAL REGULATORY MECHANISMS DURING DEVELOPMENTR01GM050231 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI JAYNES, JAMES B · 1995 to 2013
$3.3M
NIGMS NIH HHS R01 GM050231
6 · The paper itself

Abstract

Steroid hormones fulfil important functions in animal development. In Drosophila, ecdysone triggers moulting and metamorphosis through its effects on gene expression. Ecdysone works by binding to a nuclear receptor, EcR, which heterodimerizes with the retinoid X receptor homologue Ultraspiracle. Both partners are required for binding to ligand or DNA. Like most DNA-binding transcription factors, nuclear receptors activate or repress gene expression by recruiting co-regulators, some of which function as chromatin-modifying complexes. For example, p160 class coactivators associate with histone acetyltransferases and arginine histone methyltransferases. The Trithorax-related gene of Drosophila encodes the SET domain protein TRR. Here we report that TRR is a histone methyltransferases capable of trimethylating lysine 4 of histone H3 (H3-K4). trr acts upstream of hedgehog (hh) in progression of the morphogenetic furrow, and is required for retinal differentiation. Mutations in trr interact in eye development with EcR, and EcR and TRR can be co-immunoprecipitated on ecdysone treatment. TRR, EcR and trimethylated H3-K4 are detected at the ecdysone-inducible promoters of hh and BR-C in cultured cells, and H3-K4 trimethylation at these promoters is decreased in embryos lacking a functional copy of trr. We propose that TRR functions as a coactivator of EcR by altering the chromatin structure at ecdysone-responsive promoters.

Indexed as

AnimalsChromatin Assembly and DisassemblyDrosophilaDrosophila ProteinsEcdysoneEyeFemaleGene Expression Regulation, DevelopmentalHedgehog ProteinsHistone-Lysine N-MethyltransferaseHistonesLysineMaleMethylationPromoter Regions, GeneticProtein BindingDrosophila ProteinsEcdysoneecdysone receptorHedgehog Proteinshh protein, DrosophilaHistone-Lysine N-MethyltransferaseHistonesLysineReceptors, SteroidTRR protein, Drosophila

Identifiers

PMID14603321
PMCPMC2743927
OpenAlexW2003491070

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.