Evidence map›Paper›PMID 9343407›Full record

ArticleMolecular and cellular biology1997

AbdB-like Hox proteins stabilize DNA binding by the Meis1 homeodomain proteins.

W F Shen, J C Montgomery, S Rozenfeld, J J Moskow, H J Lawrence, A M Buchberg, C Largman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

108 citing papers in PubMed, 275 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Diversification and Functional Evolution of HOX Proteins.Frontiers in cell and developmental biology · 2022
    Review
  9. MEIS1 and its potential as a cancer therapeutic target (Review).International journal of molecular medicine · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

48 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

7 authors at 2 institutions in 1 country.

W F ShenDepartment of Medicine, University of California VA Medical Center, San Francisco 94121, USA.
J C Montgomery
S Rozenfeld
J J Moskow
H J Lawrence
A M Buchberg
C Largman
San Francisco VA Medical Center · USSidney Kimmel Cancer Center · US

Funding

THE ROLE OF HOX HOMEOBOX GENES IN NORMAL HEMATOPOIESISR01DK048642 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI LAWRENCE, HUGH JEFFREY · 1996 to 2003
$1.0M
VIROLOGY AND GENETICS OF CANCERP01CA021124 · NCI · WISTAR INSTITUTE · PI KOPROWSKI, HILARY · 1985 to 1999
–
NCI NIH HHS P01CA 21124NIDDK NIH HHS N44DK-3-2219NIDDK NIH HHS R01 DK48642
6 · The paper itself

Abstract

Recent studies show that Hox homeodomain proteins from paralog groups 1 to 10 gain DNA binding specificity and affinity through cooperative binding with the divergent homeodomain protein Pbx1. However, the AbdB-like Hox proteins from paralogs 11, 12, and 13 do not interact with Pbx1a, raising the possibility of different protein partners. The Meis1 homeobox gene has 44% identity to Pbx within the homeodomain and was identified as a common site of viral integration in myeloid leukemias arising in BXH-2 mice. These integrations result in constitutive activation of Meis1. Furthermore, the Hoxa-9 gene is frequently activated by viral integration in the same BXH-2 leukemias, suggesting a biological synergy between these two distinct classes of homeodomain proteins in causing malignant transformation. We now show that the Hoxa-9 protein physically interacts with Meis1 proteins by forming heterodimeric binding complexes on a DNA target containing a Meis1 site (TGACAG) and an AbdB-like Hox site (TTTTACGAC). Hox proteins from the other AbdB-like paralogs, Hoxa-10, Hoxa-11, Hoxd-12, and Hoxb-13, also form DNA binding complexes with Meis1b, while Hox proteins from other paralogs do not appear to interact with Meis1 proteins. DNA binding complexes formed by Meis1 with Hox proteins dissociate much more slowly than DNA complexes with Meis1 alone, suggesting that Hox proteins stabilize the interactions of Meis1 proteins with their DNA targets.

Indexed as

Drosophila ProteinsAnimalsCell Transformation, NeoplasticDNADNA-Binding ProteinsHomeodomain ProteinsLeukemia, MyeloidMiceMyeloid Ecotropic Viral Integration Site 1 ProteinNeoplasm ProteinsProtein BindingAbd-B proteins, DrosophilaDNADNA-Binding ProteinsDrosophila Proteinshomeobox protein HOXA9Homeodomain ProteinsMeis1 protein, mouseMyeloid Ecotropic Viral Integration Site 1 ProteinNeoplasm Proteins

Identifiers

PMID9343407
PMCPMC232497
OpenAlexW2147751805

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.