Chemicals and Drugs

Jumonji Domain-Containing Histone Demethylases

A family of histone demethylases that share a conserved Jumonji C domain. The enzymes function via an iron-dependent dioxygenase mechanism that couples the conversion of 2-oxoglutarate to succinate to the hydroxylation of N-methyl groups.

National Library of MedicineMedical Subject Headings2026

Structured Summary

Abstract

A family of histone demethylases that share a conserved Jumonji C domain. The enzymes function via an iron-dependent dioxygenase mechanism that couples the conversion of 2-oxoglutarate to succinate to the hydroxylation of N-methyl groups.

MeSH Record

Classification

Related Concepts

Knowledge Graph

Loading graph…

Drag nodes to rearrange; hover to trace links; click a node to open its page.

MeSH Record

Synonyms

3 entry terms
  • JmjC Domain-Containing Histone Demethylases
  • JmjC Domain Containing Histone Demethylases
  • Jumonji Domain Containing Histone Demethylases

MeSH Record

Aspects Covered

29 allowable subheadings

Indexed with the subheadings administration & dosage, adverse effects, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.

MeSH Record

History Note

2010

MeSH Hierarchy

Tree Numbers

AMA Style

References

  1. National Library of Medicine. Jumonji Domain-Containing Histone Demethylases. Medical Subject Headings (MeSH). 2026. Unique ID D056484. http://id.nlm.nih.gov/mesh/2026/D056484
  2. Jumonji Domain-Containing Histone Demethylases. In: Wikidata. https://www.wikidata.org/wiki/Q77922055