Evidence map›Paper›PMID 15156183›Full record

ReviewOncogene2004

ETO interacting proteins.

Bruce A Hug, Mitchell A Lazar

Abstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

62 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Review
  3. LYL1 facilitates AETFC assembly and gene activation by recruiting CARM1 in t(8;21) AML.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Therapeutic siRNA targeting the cancer cell stemness regulator PRDI-BF1 and RIZ domain zinc finger protein 14.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. RUNX1-ETO: Attacking the Epigenome for Genomic Instable Leukemia.International journal of molecular sciences · 2019
    Review
  18. Review
  19. Dual Inhibition of HDAC and Tyrosine Kinase Signaling Pathways with CUDC-907 Inhibits Thyroid Cancer Growth and Metastases.Clinical cancer research : an official journal of the American Association for Cancer Research · 2017
    Article
  20. Article

2 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

2 authors at 1 institution in 1 country.

Bruce A HugDivision of Endocrinology, Diabetes, and Metabolism, Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. brucehug@mail.med.upenn.edu
Mitchell A Lazar
University of Pennsylvania · US

Funding

REV-ERB Nuclear Receptors in Circadian Rhythm and MetabolismR01DK045586 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1992 to 2026
$12.0M
THYROID HORMONE RECEPTORS-REGULATION AND FUNCTIONR37DK043806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI LAZAR, MITCHELL A. · 1998 to 2017
$8.8M
THYROID HORMONE RECEPTORS--REGULATION AND FUNCTIONR01DK043806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI MITCHELL A. LAZAR · 1991 to 2026
$4.9M
MECHANISMS OF TRANSCRIPTIONAL REPRESSION BY AML1-ETOK08HL004339 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI HUG, BRUCE A · 2000 to 2004
$648k
NHLBI NIH HHS HL004339NIDDK NIH HHS DK43806NIDDK NIH HHS DK45586
6 · The paper itself

Abstract

The 8;21 translocation produces a fusion between the ETO gene and that encoding the myeloid transcription factor AML1. The AML1-ETO fusion substitutes the majority of the ETO protein for the coregulator recruitment domains of AML1. Biochemical analyses of ETO have led to the identification of numerous interacting proteins including many corepressors. Importantly, the proteins interacting with ETO are different from those of wild-type AML1, suggesting that altered coregulator recruitment underlies the oncogenic properties of AML1-ETO. The list of corepressors capable of binding ETO includes histone deacetylases (HDACs) and components of distinct HDAC core complexes. These investigations have provided mechanistic insight into corepressor recruitment by ETO and clues to the leukemogenic activity of AML1-ETO.

Indexed as

Core Binding Factor Alpha 2 SubunitDNA-Binding ProteinsHistone DeacetylasesHumansNuclear ProteinsNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2Oncogene Proteins, FusionProtein Structure, TertiaryRepressor ProteinsRUNX1 Translocation Partner 1 ProteinSin3 Histone Deacetylase and Corepressor ComplexTranscription FactorsAML1-ETO fusion protein, humanCore Binding Factor Alpha 2 SubunitDNA-Binding ProteinsHistone DeacetylasesNCOR1 protein, humanNCOR2 protein, humanNuclear ProteinsNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2Oncogene Proteins, FusionRepressor ProteinsRUNX1 Translocation Partner 1 ProteinSin3 Histone Deacetylase and Corepressor ComplexTranscription Factors

Identifiers

PMID15156183
OpenAlexW2020677165

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.