Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3.

Proceedings of the National Academy of Sciences of the United States of America - 30 Sept 2003

Byrd Kristin Nastase, Shearn Allen

Abstract excerpt

Covalent modifications of histone tails modulate gene expression via chromatin organization. As examples, methylation of lysine 9 residues of histone H3 (H3) (H3-K9) is believed to repress transcription by compacting chromatin, whereas methylation of lysine 4 residues of H3 (H3-K4) is believed to activate transcription by relaxing chromatin. The Drosophila trithorax group protein absent, small, or homeotic discs...

Topics

Animals
DNA-Binding Proteins
Drosophila
Drosophila Proteins
Fluorescent Antibody Technique
Histones
Lysine
Methylation
Mutation
Transcription Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Open in PubMed Open full text

Identifiers

PMID: 13679578
DOI: 10.1073/pnas.1933593100
PMCID: PMC208793

Genes

SET

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-13679578-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3.PMID 13679578Read ↗

The Drosophila ash1 gene product, which is localized at specific sites on polytene chromosomes, contains a SET domain and a PHD finger.Semantic proximity Read ↗

Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1.Semantic proximity Read ↗

dSet1 is the main H3K4 di- and tri-methyltransferase throughout Drosophila development.Semantic proximity Read ↗

Functional dissection of the ash2 and ash1 transcriptomes provides insights into the transcriptional basis of wing phenotypes and reveals conserved protein interactions.Semantic proximity Read ↗

A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3.Semantic proximity Read ↗

Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism.Semantic proximity Read ↗

A unique histone 3 lysine 14 chromatin signature underlies tissue-specific gene regulation.Semantic proximity Read ↗

Transcription in the absence of histone H3.3.Semantic proximity Read ↗

ATX3, ATX4, and ATX5 Encode Putative H3K4 Methyltransferases and Are Critical for Plant Development.Semantic proximity Read ↗

Multiple SET methyltransferases are required to maintain normal heterochromatin domains in the genome of Drosophila melanogaster.Semantic proximity Read ↗

A homeotic mutation in the trithorax SET domain impedes histone binding.Semantic proximity Read ↗

The Histone Methyltransferase Gene Absent, Small, or Homeotic Discs-1 Like Is Required for Normal Hox Gene Expression and Fertility in Mice.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.