Evidence map›Paper›PMID 25490041›Full record

ArticlePloS one2014

Intrinsically disordered and pliable Starmaker-like protein from medaka (Oryzias latipes) controls the formation of calcium carbonate crystals.

Mirosława Różycka, Magdalena Wojtas, Michał Jakób, Christian Stigloher, Mikołaj Grzeszkowiak, Maciej Mazur, Andrzej Ożyhar

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

12 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
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  6. Review
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  8. Article
  9. Single-molecule electrometry.Nature nanotechnology · 2017
    Article
  10. Article
  11. Article
  12. Intrinsically disordered proteins and biomineralization.Matrix biology : journal of the International Society for Matrix Biology
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Mirosława RóżyckaDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Magdalena WojtasDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Michał JakóbDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Christian StigloherDivision of Electron Microscopy, Biocenter, University of Würzburg, Würzburg, Germany.
Mikołaj GrzeszkowiakNanoBioMedical Centre and Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University, Poznań, Poland.
Maciej MazurDepartment of Chemistry, University of Warsaw, Warsaw, Poland.
Andrzej OżyharDepartment of Biochemistry, Faculty of Chemistry, Wrocław University of Technology, Wrocław, Poland.
Wrocław University of Science and Technology · PLAdam Mickiewicz University in Poznań · PLUniversity of Warsaw · PLUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fish otoliths, biominerals composed of calcium carbonate with a small amount of organic matrix, are involved in the functioning of the inner ear. Starmaker (Stm) from zebrafish (Danio rerio) was the first protein found to be capable of controlling the formation of otoliths. Recently, a gene was identified encoding the Starmaker-like (Stm-l) protein from medaka (Oryzias latipes), a putative homologue of Stm and human dentine sialophosphoprotein. Although there is no sequence similarity between Stm-l and Stm, Stm-l was suggested to be involved in the biomineralization of otoliths, as had been observed for Stm even before. The molecular properties and functioning of Stm-l as a putative regulatory protein in otolith formation have not been characterized yet. A comprehensive biochemical and biophysical analysis of recombinant Stm-l, along with in silico examinations, indicated that Stm-l exhibits properties of a coil-like intrinsically disordered protein. Stm-l possesses an elongated and pliable structure that is able to adopt a more ordered and rigid conformation under the influence of different factors. An in vitro assay of the biomineralization activity of Stm-l indicated that Stm-l affected the size, shape and number of calcium carbonate crystals. The functional significance of intrinsically disordered properties of Stm-l and the possible role of this protein in controlling the formation of calcium carbonate crystals is discussed.

Indexed as

OryziasAnimalsCalcium CarbonateComputer SimulationFish ProteinsHydrodynamicsIntrinsically Disordered ProteinsMineralsProtein Structure, SecondaryProtein UnfoldingZebrafish ProteinsCalcium CarbonateFish ProteinsIntrinsically Disordered ProteinsMineralsstm protein, zebrafishZebrafish Proteins

Identifiers

PMID25490041
PMCPMC4260845
OpenAlexW2088482451

What OpenQuestion holds

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LicenceCC BY
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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.