Evidence map›Paper›PMID 12481029›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

The DNA methyltransferase-like protein DNMT3L stimulates de novo methylation by Dnmt3a.

Frederic Chedin, Michael R Lieber, Chih-Lin Hsieh

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 225 papers.

0numbers the graph read from it
0cells of the map it votes in
225citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

225 citing papers in PubMed, 540 citations in OpenAlex.

  1. Multidomain interaction governs the filamentous assembly of the dominant-negative DNMT3A R882H mutant.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Epigenetic regulation of transgenes.Journal of biotechnology · 2026
    Review
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  10. Epigenetic remodeling during early embryonic development.Frontiers in cell and developmental biology · 2026
    Review
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165 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

3 authors at 1 institution in 1 country.

Frederic ChedinDepartments of Pathology, Biochemistry and Molecular Biology, and Urology, Norris Comprehensive Cancer Center, Room 5420, Keck School of Medicine, University of Southern California, Los Angeles, CA 90089, USA.
Michael R Lieber
Chih-Lin Hsieh
University of Southern California · US

Funding

TARGETS AND REQUIREMENTS OF METHYLATION IN HUMAN CELLSR01GM060237 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI HSIEH, CHIH-LIN · 2000 to 2004
$1.0M
NIGMS NIH HHS R01 GM060237NIGMS NIH HHS R01 GM60237
6 · The paper itself

Abstract

Dnmt3L is required for the establishment of maternal methylation imprints at imprinting centers (ICs). Dnmt3L, however, lacks the conserved catalytic domain common to DNA methyltransferases. In an attempt to define its function, we coexpressed DNMT3L with each of the two known de novo methyltransferases, Dnmt3a and DNMT3B, in human cells and monitored de novo methylation by using replicating minichromosomes carrying various ICs as targets. Coexpression of DNMT3L with DNMT3B led to little or no change in target methylation. However, coexpression of DNMT3L with Dnmt3a resulted in a striking stimulation of de novo methylation by Dnmt3a. Stimulation was observed at maternally methylated ICs such as small nuclear ribonucleoprotein polypeptide N (SNRPN), Snrpn, and Igf2rAir, as well as at various nonimprinted sequences present on the episomes. Stimulation of Dnmt3a by DNMT3L was also observed at endogenous sequences in the genome. Therefore, DNMT3L acts as a general stimulatory factor for de novo methylation by Dnmt3a. The implications of these findings for the function of DNMT3L and Dnmt3a in DNA methylation and genomic imprinting are discussed.

Indexed as

Cell LineCpG IslandsDNA (Cytosine-5-)-MethyltransferasesDNA MethylationDNA Methyltransferase 3AHumansTransfectionDNA (Cytosine-5-)-MethyltransferasesDNA Methyltransferase 3ADNMT3A protein, humanDNMT3L protein, human

Identifiers

PMID12481029
PMCPMC139244
OpenAlexW2114221123

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.