Evidence map›Paper›PMID 19166478›Full record

ArticleJournal of anatomy2009

Morphological and biochemical analyses of otoliths of the ice-fish Chionodraco hamatus confirm a common origin with red-blooded species.

Chiara Maria Motta, Bice Avallone, Giuseppina Balassone, Giuseppe Balsamo, Umberto Fascio, Palma Simoniello, Stefania Tammaro, Francesco Marmo

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of anatomy, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 93% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. Embryogenesis and early skeletogenesis in the antarctic bullhead notothen, Notothenia coriiceps.Developmental dynamics : an official publication of the American Association of Anatomists · 2016
    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 2 institutions in 1 country.

Chiara Maria MottaDepartment of Biological Sciences, University of Naples Federico II, Naples, Italy. mottacm@unina.it
Bice Avallone
Giuseppina Balassone
Giuseppe Balsamo
Umberto Fascio
Palma Simoniello
Stefania Tammaro
Francesco Marmo
University of Naples Federico II · ITUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The morphology and composition of the three otoliths of the Antarctic ice-fish Chionodraco hamatus were studied by scanning electron microscopy and X-ray diffraction. The composition of the sagitta, lapillus and asteriscus protein matrices was also analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, western blots and confocal laser scanning microscopy to reveal the presence of and to localize the calcium-binding proteins calmodulin, calbindin and S-100. Morphological results indicated that the otoliths in this ice-fish were similar to those of Trematomus bernacchii, a red-blooded Antarctic species [B. Avallone et al. (2003) J. Submicrosc. Cytol. Pathol. 35, 69-76], but rather different from those of other teleosts. These two Antarctic species possessed a completely vateritic asteriscus, whereas their sagitta and lapillus were made mostly of aragonite. Parallel analysis of protein patterns in C. hamatus and T. bernacchii revealed that the sagitta significantly differed from the lapillus and asteriscus in both species. The sagitta did not contain the S-100 protein and showed calmodulin and calbindin located in discontinuous or incremental zones, respectively. These results demonstrate that the otoliths of C. hamatus and T. bernacchii share more resemblances than differences and support the idea of a common origin of these species.

Indexed as

Biological EvolutionAbsorptiometry, PhotonAnimalsBlotting, WesternCalbindinsCalcification, PhysiologicCalcium-Binding ProteinsCalmodulinCold TemperatureElectrophoresis, Polyacrylamide GelFemaleMicroscopy, ConfocalMicroscopy, Electron, ScanningOtolithic MembranePerciformesS100 Calcium Binding Protein GCalbindinsCalcium-Binding ProteinsCalmodulinS100 Calcium Binding Protein GS100 Proteins

Identifiers

PMID19166478
PMCPMC2667923
OpenAlexW1982295595

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.