Evidence map›Paper›PMID 21239497›Full record

ArticleThe Journal of biological chemistry2011

Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism.

Sojin An, Kwon Joo Yeo, Young Ho Jeon, Ji-Joon Song

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 8% 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

84 citing papers in PubMed, 1 synthesis or guideline pooled it, 137 citations in OpenAlex.

  1. Pooled it
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  5. Review
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  12. Chromatin modifiers in neurodevelopment.Frontiers in molecular neuroscience · 2025
    Review
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  20. Review

24 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

4 authors at 2 institutions in 1 country.

Sojin AnFrom the Structural Biology Laboratory of Epigenetics, Department of Biological Sciences, Graduate school of Nanoscience and Technology (World Class University), KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), 335 Gwahangno, Yuseong-gu, Daejeon 305-701 and.
Kwon Joo Yeothe Division of Magnetic Resonance, Korea Basic Science Institute (KBSI) and University of Science and Technology, 804-1, Yangcheong-Ri, Ochang, Chungbuk 363-883, Korea.
Young Ho Jeonthe Division of Magnetic Resonance, Korea Basic Science Institute (KBSI) and University of Science and Technology, 804-1, Yangcheong-Ri, Ochang, Chungbuk 363-883, Korea.
Ji-Joon SongFrom the Structural Biology Laboratory of Epigenetics, Department of Biological Sciences, Graduate school of Nanoscience and Technology (World Class University), KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), 335 Gwahangno, Yuseong-gu, Daejeon 305-701 and. Electronic address: songj@kaist.ac.kr.
Korea Advanced Institute of Science and Technology · KRKorea University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Absent, small, or homeotic disc1 (Ash1) is a trithorax group histone methyltransferase that is involved in gene activation. Although there are many known histone methyltransferases, their regulatory mechanisms are poorly understood. Here, we present the crystal structure of the human ASH1L catalytic domain, showing its substrate binding pocket blocked by a loop from the post-SET domain. In this configuration, the loop limits substrate access to the active site. Mutagenesis of the loop stimulates ASH1L histone methyltransferase activity, suggesting that ASH1L activity may be regulated through the loop from the post-SET domain. In addition, we show that human ASH1L specifically methylates histone H3 Lys-36. Our data implicate that there may be a regulatory mechanism of ASH1L histone methyltransferases.

Indexed as

Crystallography, X-RayDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansMethylationMutagenesisProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipSubstrate SpecificityTranscription FactorsASH1L protein, humanDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesTranscription Factors

Identifiers

PMID21239497
PMCPMC3048721
OpenAlexW2042871128

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.