Evidence map›Paper›PMID 26223266›Full record

ArticleBMC evolutionary biology2015

Evolutionary analysis of selective constraints identifies ameloblastin (AMBN) as a potential candidate for amelogenesis imperfecta.

Frédéric Delsuc, Barbara Gasse, Jean-Yves Sire

Open access · goldAbstract read
In one paragraph

Article in BMC evolutionary biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Functions of secretory calcium-binding phosphoproteins in dental mineralization.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025
    Review
  4. Article
  5. Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Review
  6. Article
  7. Article
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  9. Article
  10. PeerJ · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The Expression and Purification of Recombinant Mouse Ameloblastin in E. coli.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

3 authors at 2 institutions in 1 country.

Frédéric DelsucInstitut des Sciences de l'Evolution, UMR 5554, CNRS, IRD, EPHE, Université de Montpellier, Montpellier, France.
Barbara GasseUniversité Pierre et Marie Curie, UMR 7138 Evolution Paris-Seine, Paris, France.
Jean-Yves SireUniversité Pierre et Marie Curie, UMR 7138 Evolution Paris-Seine, Paris, France. jean-yves.sire@upmc.fr.
Sorbonne Université · FRÉcole Pratique des Hautes Études · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAmeloblastin (AMBN) is a phosphorylated, proline/glutamine-rich protein secreted during enamel formation. Previous studies have revealed that this enamel matrix protein was present early in vertebrate evolution and certainly plays important roles during enamel formation although its precise functions remain unclear. We performed evolutionary analyses of AMBN in order to (i) identify residues and motifs important for the protein function, (ii) predict mutations responsible for genetic diseases, and (iii) understand its molecular evolution in mammals.

resultsIn silico searches retrieved 56 complete sequences in public databases that were aligned and analyzed computationally. We showed that AMBN is globally evolving under moderate purifying selection in mammals and contains a strong phylogenetic signal. In addition, our analyses revealed codons evolving under significant positive selection. Evidence for positive selection acting on AMBN was observed in catarrhine primates and the aye-aye. We also found that (i) an additional translation initiation site was recruited in the ancestral placental AMBN, (ii) a short exon was duplicated several times in various species including catarrhine primates, and (iii) several polyadenylation sites are present.

conclusionsAMBN possesses many positions, which have been subjected to strong selective pressure for 200 million years. These positions correspond to several cleavage sites and hydroxylated, O-glycosylated, and phosphorylated residues. We predict that these conserved positions would be potentially responsible for enamel disorder if substituted. Some motifs that were previously identified as potentially important functionally were confirmed, and we found two, highly conserved, new motifs, the function of which should be tested in the near future. This study illustrates the power of evolutionary analyses for characterizing the functional constraints acting on proteins with yet uncharacterized structure.

Indexed as

Amelogenesis ImperfectaAmino Acid SequenceAnimalsConserved SequenceDental EnamelDental Enamel ProteinsEvolution, MolecularHumansMammalsMolecular Sequence DataMutationPhylogenyProtein BiosynthesisProtein Sorting SignalsSequence AlignmentAMBN protein, humanDental Enamel ProteinsProtein Sorting Signals

Identifiers

PMID26223266
PMCPMC4518657
OpenAlexW1954645890

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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.