Evidence map›Paper›PMID 8657149›Full record

ArticleMolecular and cellular biology1996

Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus.

C P Chang, L Brocchieri, W F Shen, C Largman, M L Cleary

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

109 citing papers in PubMed, 273 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. The role of HOXA1 in cancer and targeted therapy.Medical oncology (Northwood, London, England) · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Molecular processes involved in B cell acute lymphoblastic leukaemia.Cellular and molecular life sciences : CMLS · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Article

49 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

5 authors at 3 institutions in 1 country.

C P ChangDepartment of Pathology, Stanford University, California 94305, USA.
L Brocchieri
W F Shen
C Largman
M L Cleary
Stanford University · USSan Francisco VA Medical Center · USUniversity of California, San Francisco · US

Funding

MOLECULAR PATHOLOGY OF LYMPHOID MALIGNANCIESR37CA042971 · NCI · STANFORD UNIVERSITY · PI CLEARY, MICHAEL L · 1999 to 2006
$3.6M
THEORY &APPLIED STUDIES IN EVOLUTIONARY GENETICSR01GM010452 · NIGMS · STANFORD UNIVERSITY · PI KARLIN, SAMUEL · 1985 to 2006
$2.1M
MOLECULAR PATHOLOGY OF LYMPHOID MALIGNANCIESR01CA042971 · NCI · STANFORD UNIVERSITY · PI CLEARY, MICHAEL L · 1986 to 1998
–
NCI NIH HHS CA42971NIGMS NIH HHS GM10452-31
6 · The paper itself

Abstract

Pbx cofactors are implicated to play important roles in modulating the DNA-binding properties of heterologous homeodomain proteins, including class I Hox proteins. To assess how Pbx proteins influence Hox DNA-binding specificity, we used a binding-site selection approach to determine high-affinity target sites recognized by various Pbx-Hox homeoprotein complexes. Pbx-Hox heterodimers preferred to bind a bipartite sequence 5'-ATGATTNATNN-3' consisting of two adjacent half sites in which the Pbx component of the heterodimer contacted the 5' half (ATGAT) and the Hox component contacted the more variable 3' half (TNATNN). Binding sites matching the consensus were also obtained for Pbx1 complexed with HoxA10, which lacks a hexapeptide but requires a conserved tryptophan-containing motif for cooperativity with Pbx. Interactions with Pbx were found to play an essential role in modulating Hox homeodomain amino-terminal arm contact with DNA in the core of the Hox half site such that heterodimers of different compositions could distinguish single nucleotide alterations in the Hox half site both in vitro and in cellular assays measuring transactivation. When complexed with Pbx, Hox proteins B1 through B9 and A10 showed stepwise differences in their preferences for nucleotides in the Hox half site core (TTAT to TGAT, 5' to 3') that correlated with the locations of their respective genes in the Hox cluster. These observations demonstrate previously undetected DNA-binding specificity for the amino-terminal arm of the Hox homeodomain and suggest that different binding activities of Pbx-Hox complexes are at least part of the position-specific activities of the Hox genes.

Indexed as

Drosophila ProteinsGenes, HomeoboxAnimalsBase SequenceDNADNA-Binding ProteinsDrosophilaHomeodomain ProteinsMacromolecular SubstancesModels, MolecularMolecular Sequence DataPre-B-Cell Leukemia Transcription Factor 1Proto-Oncogene ProteinsTranscription FactorsDNADNA-Binding ProteinsDrosophila Proteinsexd protein, DrosophilaHomeodomain ProteinsMacromolecular SubstancesPBX1 protein, humanPre-B-Cell Leukemia Transcription Factor 1Proto-Oncogene ProteinsTranscription Factors

Identifiers

PMID8657149
PMCPMC231160
OpenAlexW1941286715

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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.