Evidence map›Paper›PMID 8413232›Full record

ArticleMolecular and cellular biology1993

Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO) as sequence-specific DNA-binding proteins: the runt homology domain is required for DNA binding and protein-protein interactions.

S Meyers, J R Downing, S W Hiebert

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 168 papers.

0numbers the graph read from it
0cells of the map it votes in
168citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

168 citing papers in PubMed, 475 citations in OpenAlex.

  1. Article
  2. Article
  3. C/EBPα activatesScience immunology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. RUNX1-ETO: Attacking the Epigenome for Genomic Instable Leukemia.International journal of molecular sciences · 2019
    Review
  17. RUNX1 and the endothelial origin of blood.Experimental hematology · 2018
    Review
  18. Article
  19. Article
  20. HumanBlood · 2018
    Article

108 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.

S MeyersDepartment of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
J R Downing
S W Hiebert
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
CSF-1 RECEPTOR TYROSINE KINASEK08CA001429 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI DOWNING, JAMES R · 1989 to 1993
–
NCI NIH HHS 5 P30 CA 21765NCI NIH HHS CA 01429
6 · The paper itself

Abstract

The AML1 gene on chromosome 21 is disrupted in the (8;21)(q22;q22) translocation associated with acute myelogenous leukemia and encodes a protein with a central 118-amino-acid domain with 69% homology to the Drosophila pair-rule gene, runt. We demonstrate that AML-1 is a DNA-binding protein which specifically interacts with a sequence belonging to the group of enhancer core motifs, TGT/cGGT. Electrophoretic mobility shift analysis of cell extracts identified two AML-1-containing protein-DNA complexes whose electrophoretic mobilities were slower than those of complexes formed with AML-1 produced in vitro. Mixing of in vitro-produced AML-1 with cell extracts prior to gel mobility shift analysis resulted in the formation of higher-order complexes. Deletion mutagenesis of AML-1 revealed that the runt homology domain mediates both sequence-specific DNA binding and protein-protein interactions. The hybrid product, AML-1/ETO, which results from the (8;21) translocation and retains the runt homology domain, both recognizes the AML-1 consensus sequence and interacts with other cellular proteins.

Indexed as

Chromosomes, Human, Pair 21Proto-Oncogene ProteinsTranscription FactorsTranscription, GeneticTranslocation, GeneticAnimalsBase SequenceCell LineCore Binding Factor Alpha 2 SubunitDNADNA-Binding ProteinsDrosophilaDrosophila ProteinsEnhancer Elements, GeneticHumansLeukemia, Myeloid, AcuteCore Binding Factor Alpha 2 SubunitDNADNA-Binding ProteinsDrosophila ProteinsNeoplasm ProteinsNuclear ProteinsProto-Oncogene ProteinsRecombinant Fusion Proteinsrun protein, DrosophilaRUNX1 protein, humanTranscription Factors

Identifiers

PMID8413232
PMCPMC364692
OpenAlexW1945687446

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.