Evidence map›Paper›PMID 12435631›Full record

ArticleGenes & development2002

Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein.

Andrei Kuzmichev, Kenichi Nishioka, Hediye Erdjument-Bromage, Paul Tempst, Danny Reinberg

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 856 papers.

0numbers the graph read from it
0cells of the map it votes in
856citing papers in PubMed
–field-weighted citation impact
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

856 citing papers in PubMed, 1,597 citations in OpenAlex.

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  18. Liquid-liquid phase separation in neural development.Cellular and molecular life sciences : CMLS · 2026
    Review
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  20. Article

796 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

5 authors at 2 institutions in 1 country.

Andrei KuzmichevHoward Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
Kenichi Nishioka
Hediye Erdjument-Bromage
Paul Tempst
Danny Reinberg
Howard Hughes Medical Institute · USMemorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Initiation of Transcription of Protein Coding GenesR37GM037120 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI REINBERG, DANNY · 2004 to 2013
$4.5M
INITIATION OF TRANSCRIPTION OF PROTEIN CODING GENESR01GM037120 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI REINBERG, DANNY F · 1986 to 2001
$634k
NCI NIH HHS P30 CA008748NCI NIH HHS P30 CA08748NIGMS NIH HHS GM-37120NIGMS NIH HHS R01 GM037120NIGMS NIH HHS R37 GM037120
6 · The paper itself

Abstract

Enhancer of Zeste [E(z)] is a Polycomb-group transcriptional repressor and one of the founding members of the family of SET domain-containing proteins. Several SET-domain proteins possess intrinsic histone methyltransferase (HMT) activity. However, recombinant E(z) protein was found to be inactive in a HMT assay. Here we report the isolation of a multiprotein E(z) complex that contains extra sex combs, suppressor of zeste-12 [Su(z)12], and the histone binding proteins RbAp46/RbAp48. This complex, which we termed Polycomb repressive complex (PRC) 2, possesses HMT activity with specificity for Lys 9 (K9) and Lys 27 (K27) of histone H3. The HMT activity of PRC2 is dependent on an intact SET domain in the E(z) protein. We hypothesize that transcriptional repression by the E(z) protein involves methylation-dependent recruitment of PRC1. The presence of Su(z)12, a strong suppressor of position effect variegation, in PRC2 suggests that PRC2 may play a widespread role in heterochromatin-mediated silencing.

Indexed as

Histone-Lysine N-MethyltransferaseAmino Acid SequenceCarrier ProteinsDrosophila ProteinsHeLa CellsHistone Deacetylase 1Histone DeacetylasesHistone MethyltransferasesHistonesHumansLysineMacromolecular SubstancesMethyltransferasesMolecular Sequence DataMultiprotein ComplexesNuclear ProteinsCarrier ProteinsDrosophila Proteinsesc protein, DrosophilaE(z) protein, DrosophilaHDAC1 protein, humanHistone Deacetylase 1Histone DeacetylasesHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysineMacromolecular SubstancesMethyltransferasesMultiprotein ComplexesNuclear ProteinsPc protein, DrosophilaPolycomb Repressive Complex 1Polycomb Repressive Complex 2PRC2 protein, DrosophilaProtein MethyltransferasesRBBP4 protein, humanRbbp4 protein, mouseRBBP7 protein, humanRepressor ProteinsRetinoblastoma-Binding Protein 4Retinoblastoma-Binding Protein 7Su(z)12 protein, Drosophila

Identifiers

PMID12435631
PMCPMC187479
OpenAlexW2165894156

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.