Evidence map›Paper›PMID 15856011›Full record

ArticleOncogene2005

The eleven-nineteen-leukemia protein ENL connects nuclear MLL fusion partners with chromatin.

Deniz T Zeisig, Claudia B Bittner, Bernd B Zeisig, Maria-Paz García-Cuéllar, Jay L Hess, Robert K Slany

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

71 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. Discovery of a Highly Potent and Selective ENL Degrader.Journal of medicinal chemistry · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Engineering an inducible leukemia-associated fusion protein enables large-scale ex vivo production of functional human phagocytes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Small-molecule tools for YEATS domain proteins.Current opinion in chemical biology · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Fragment-Based Discovery of AF9 YEATS Domain Inhibitors.International journal of molecular sciences · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Epigenetic Control of Infant B Cell Precursor Acute Lymphoblastic Leukemia.International journal of molecular sciences · 2021
    Review
  20. Article

11 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 2 institutions in 2 countries.

Deniz T ZeisigDepartment of Genetics, University Erlangen, Staudtstrasse 5, 91058 Erlangen, Germany.
Claudia B Bittner
Bernd B Zeisig
Maria-Paz García-Cuéllar
Jay L Hess
Robert K Slany
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversity of Pennsylvania · US

Funding

MECHANISMS OF HOX GENE REGULATION BY MLLR01CA078815 · NCI · WASHINGTON UNIVERSITY · PI HESS, JAY L. · 1998 to 2007
$2.3M
NCI NIH HHS CA78815NCI NIH HHS CA92251
6 · The paper itself

Abstract

Mixed lineage leukemia (MLL) fusion proteins are derived from translocations at 11q23 that occur in aggressive subtypes of leukemia. As a consequence, MLL is joined to different unrelated proteins to form oncogenic transcription factors. Here we demonstrate a direct interaction between several nuclear MLL fusion partners and present evidence for a role of these proteins in histone binding. In two-hybrid studies, ENL interacted with AF4 and AF5q31 as well as with a fragment of AF10. A structure-function analysis revealed that the AF4/AF5q31/AF10 binding domain in ENL coincided with the C-terminus that is essential for transformation by MLL-ENL. The ENL/AF4 association was corroborated by GST-pulldown experiments and by mutual coprecipitation. Both proteins colocalized in vivo in a nuclear speckled pattern. Moreover, AF4 and ENL coeluted on sizing columns together with the known ENL binding partner Polycomb3, suggesting the presence of a multiprotein complex. The overexpression of ENL alone activated a reporter construct and a mutational screen indicated the conserved YEATS domain as essential for this function. Overlay and pulldown-assays finally showed a specific and YEATS domain-dependent association of ENL with histones H3 and H1. In summary, our studies support a common role for nuclear MLL fusion partners in chromatin biology.

Indexed as

AnimalsChromatinDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistonesHumansMyeloid-Lymphoid Leukemia ProteinProtein BiosynthesisProto-OncogenesRecombinant Fusion ProteinsStructure-Activity RelationshipTranscriptional ActivationTranscription FactorsTwo-Hybrid System TechniquesChromatinDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistonesKMT2A protein, humanMyeloid-Lymphoid Leukemia ProteinRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID15856011
OpenAlexW2015469418

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.