Evidence map›Paper›PMID 15367676›Full record

ArticleMolecular and cellular biology2004

Loss of function but no gain of function caused by amino acid substitutions in the hexapeptide of Hoxa1 in vivo.

Sophie Remacle, Leïla Abbas, Olivier De Backer, Nathalie Pacico, Anthony Gavalas, Françoise Gofflot, Jacques J Picard, René Rezsöhazy

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

  1. Homeodomain Involvement in Nuclear HOX Protein Homo- and Heterodimerization.International journal of molecular sciences · 2025
    Article
  2. Article
  3. Diversification and Functional Evolution of HOX Proteins.Frontiers in cell and developmental biology · 2022
    Review
  4. Article
  5. Hindbrain induction and patterning during early vertebrate development.Cellular and molecular life sciences : CMLS · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Hox transcription factors influence motoneuron identity through the integrated actions of both homeodomain and non-homeodomain regions.Developmental dynamics : an official publication of the American Association of Anatomists · 2012
    Article
  11. Review
  12. Article
  13. Pbx homeodomain proteins: TALEnted regulators of limb patterning and outgrowth.Developmental dynamics : an official publication of the American Association of Anatomists · 2011
    Review
  14. Article
  15. Selection of distinct Hox-Extradenticle interaction modes fine-tunes Hox protein activity.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. A unique Extradenticle recruitment mode in the Drosophila Hox protein Ultrabithorax.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Article
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

8 authors at 3 institutions in 2 countries.

Sophie RemacleUnit of Developmental Genetics, Université Catholique de Louvain, Brussels, Belgium.
Leïla Abbas
Olivier De Backer
Nathalie Pacico
Anthony Gavalas
Françoise Gofflot
Jacques J Picard
René Rezsöhazy
UCLouvain · BEKing's College London · GBLudwig Cancer Research · BE

Funding

Wellcome Trust
6 · The paper itself

Abstract

Homeodomain containing transcription factors of the Hox family play critical roles in patterning the anteroposterior embryonic body axis, as well as in controlling several steps of organogenesis. Several Hox proteins have been shown to cooperate with members of the Pbx family for the recognition and activation of identified target enhancers. Hox proteins contact Pbx via a conserved hexapeptide motif. Previous biochemical studies provided evidence that critical amino acid substitutions in the hexapeptide sequence of Hoxa1 abolish its interaction with Pbx. As a result, these substitutions also abolish Hoxa1 activity on known target enhancers in cellular models, suggesting that Hoxa1 activity relies on its capacity to interact with Pbx. Here, we show that mice with mutations in the Hoxa1 hexapeptide display hindbrain, cranial nerve, and skeletal defects highly reminiscent of those reported for the Hoxa1 loss of function. Since similar hexapeptide mutations in the mouse Hoxb8 and the Drosophila AbdA proteins result in activity modulation and gain of function, our data demonstrate that the functional importance of the hexapeptide in vivo differs according to the Hox proteins.

Indexed as

Amino Acid SubstitutionAnimalsBody PatterningCranial NervesEarHomeobox A1 ProteinHomeodomain ProteinsMiceMice, TransgenicMutationNeural CrestOccipital BonePeptide FragmentsRhombencephalonTranscription FactorsHomeobox A1 ProteinHomeodomain ProteinsPeptide FragmentsTranscription Factors

Identifiers

PMID15367676
PMCPMC516739
OpenAlexW1989071778

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.