Evidence map›Paper›PMID 11842107›Full record

ArticleNucleic acids research2002

The MT domain of the proto-oncoprotein MLL binds to CpG-containing DNA and discriminates against methylation.

Marco Birke, Silke Schreiner, María-Paz García-Cuéllar, Kerstin Mahr, Fritz Titgemeyer, Robert K Slany

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 5% 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

124 citing papers in PubMed, 1 synthesis or guideline pooled it, 216 citations in OpenAlex.

  1. Pooled it
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  13. An enhancer RNA recruits MLL1 to regulate transcription ofbioRxiv : the preprint server for biology · 2023
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64 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

6 authors at 1 institution in 1 country.

Marco BirkeDepartment of Genetics, University of Erlangen, Staudtstrasse 5, 91058 Erlangen, Germany.
Silke Schreiner
María-Paz García-Cuéllar
Kerstin Mahr
Fritz Titgemeyer
Robert K Slany
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alterations of the proto-oncogene MLL (mixed lineage leukemia) are characteristic for a high proportion of acute leukemias, especially those occurring in infants. The activation of MLL is achieved either by an internal tandem duplication of 5' MLL exons or by chromosomal translocations that create chimeric proteins with the N-terminus of MLL fused to a variety of different partner proteins. A domain of MLL with significant homology to the eukaryotic DNA methyltransferases (MT domain) has been found to be essential for the transforming potential of the oncogenic MLL derivatives. Here we demonstrate that this domain specifically recognizes DNA with unmethylated CpG sequences. In gel mobility shifts, the presence of CpG was sufficient for binding of recombinant GST-MT protein to DNA. The introduction of 5-methylCpG on one or both DNA strands precluded an efficient interaction. In surface plasmon resonance a KD of approximately 3.3 x 10(-8) M was determined for the GST-MT/DNA complex formation. Site selection experiments and DNase I footprinting confirmed CpG as the target of the MT domain. Finally, this interaction was corroborated in vivo in reporter assays utilizing the DNA-binding properties of the MT domain in a hybrid MT-VP16 transactivator construct.

Indexed as

Proto-OncogenesTranscription FactorsAmino Acid SequenceBase SequenceBinding SitesDeoxyribonuclease IDNA-Binding ProteinsDNA FootprintingDNA MethylationDNA Modification MethylasesElectrophoretic Mobility Shift AssayGlutathione TransferaseHistone-Lysine N-MethyltransferaseHumansMolecular Sequence DataMyeloid-Lymphoid Leukemia ProteinCPG-oligonucleotideDeoxyribonuclease IDNA-Binding ProteinsDNA Modification MethylasesGlutathione TransferaseHistone-Lysine N-MethyltransferaseKMT2A protein, humanMAS1 protein, humanMyeloid-Lymphoid Leukemia ProteinOligodeoxyribonucleotidesProto-Oncogene MasProto-Oncogene ProteinsRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID11842107
PMCPMC100340
OpenAlexW1985171686

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.