Evidence map›Paper›PMID 20101264›Full record

ArticleCell research2010

AOF1 is a histone H3K4 demethylase possessing demethylase activity-independent repression function.

Ze Yang, Jun Jiang, M David Stewart, David M Stewart, Shankang Qi, Kenichi Yamane, Jiwen Li, Yi Zhang, Jiemin Wong

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Cell research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Discovery and structural studies of histone demethylases.Frontiers in epigenetics and epigenomics · 2025
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. LSD1: more than demethylation of histone lysine residues.Experimental & molecular medicine · 2020
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
    Stewart, David M [corrected to Stewart, M David]
5 · Who and what money

Authors and funding

9 authors at 5 institutions in 2 countries.

Ze YangThe Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, China.
Jun Jiang
M David Stewart
David M Stewart
Shankang Qi
Kenichi Yamane
Jiwen Li
Yi Zhang
Jiemin Wong
East China Normal University · CNDaping Hospital · CNHoward Hughes Medical Institute · USThe University of Texas MD Anderson Cancer Center · USUniversity of North Carolina at Chapel Hill · US

Funding

Mechanisms of Polycomb SilencingR01GM068804 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YI · 2003 to 2010
$2.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM068804
6 · The paper itself

Abstract

LSD1 (KDM1 under the new nomenclature) was the first identified lysine-specific histone demethylase belonging to the flavin-dependent amine oxidase family. Here, we report that AOF1 (KDM1B under the new nomenclature), a mammalian protein related to LSD1, also possesses histone demethylase activity with specificity for H3K4me1 and H3K4me2. Like LSD1, the highly conserved SWIRM domain is required for its enzymatic activity. However, AOF1 differs from LSD1 in several aspects. First, AOF1 does not appear to form stable protein complexes containing histone deacetylases. Second, AOF1 is found to localize to chromosomes during the mitotic phase of the cell cycle, whereas LSD1 does not. Third, AOF1 represses transcription when tethered to DNA and this repression activity is independent of its demethylase activity. Structural and functional analyses identified its unique N-terminal Zf-CW domain as essential for the demethylase activity-independent repression function. Collectively, our study identifies AOF1 as the second histone demethylase in the family of flavin-dependent amine oxidases and reveals a demethylase-independent repression function of AOF1.

Indexed as

AnimalsChromosomesHistone DeacetylasesHistonesMiceMitosisOocytesOxidoreductases, N-DemethylatingProtein Structure, TertiaryRepressor ProteinsTranscription, GeneticXenopusZinc FingersHistone DeacetylasesHistoneskdm1b protein, mouseOxidoreductases, N-DemethylatingRepressor Proteins

Identifiers

PMID20101264
PMCPMC4106039
OpenAlexW2005867783

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.