Evidence map›Paper›PMID 31241793›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019

Lattice Shrinkage by Incorporation of Recombinant Starmaker-Like Protein within Bioinspired Calcium Carbonate Crystals.

Mirosława Różycka, Ismael Coronado, Katarzyna Brach, Joanna Olesiak-Bańska, Marek Samoć, Mirosław Zarębski, Jerzy Dobrucki, Maciej Ptak, Eva Weber, Iryna Polishchuk and 3 more

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

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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

13 authors.

Mirosława RóżyckaDepartment of Biochemistry, Faculty of Chemistry, Wroclaw University of Science and Technology, Wroclaw, 50-370, Poland.ORCID http://orcid.org/0000-0002-8008-6689
Ismael CoronadoInstitute of Paleobiology, Polish Academy of Sciences, Warsaw, 00-818, Poland.
Katarzyna BrachAdvanced Materials Engineering and Modelling Group, Faculty of Chemistry, Wroclaw University of Science and Technology, Wroclaw, 50-370, Poland.
Joanna Olesiak-BańskaAdvanced Materials Engineering and Modelling Group, Faculty of Chemistry, Wroclaw University of Science and Technology, Wroclaw, 50-370, Poland.
Marek SamoćAdvanced Materials Engineering and Modelling Group, Faculty of Chemistry, Wroclaw University of Science and Technology, Wroclaw, 50-370, Poland.
Mirosław ZarębskiDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, 30-387, Poland.
Jerzy DobruckiDepartment of Cell Biophysics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, 30-387, Poland.
Maciej PtakInstitute of Low Temperature and Structure Research, Polish Academy of Sciences, Wroclaw, 50-422, Poland.
Eva WeberDepartment of Materials Science and Engineering and the Russell Berrie Nanotechnology Institute, Technion Israel Institute of Technology, Haifa, 32000, Israel.
Iryna PolishchukDepartment of Materials Science and Engineering and the Russell Berrie Nanotechnology Institute, Technion Israel Institute of Technology, Haifa, 32000, Israel.
Boaz PokroyDepartment of Materials Science and Engineering and the Russell Berrie Nanotechnology Institute, Technion Israel Institute of Technology, Haifa, 32000, Israel.
Jarosław StolarskiInstitute of Paleobiology, Polish Academy of Sciences, Warsaw, 00-818, Poland.
Andrzej OżyharDepartment of Biochemistry, Faculty of Chemistry, Wroclaw University of Science and Technology, Wroclaw, 50-370, Poland.

Funding

National Science Centre UMO-2015/19/B/ST10/02148Statutory activity subsidy from the Polish Ministry of Science and Higher Education for the Faculty of Chemistry of Wroclaw University of Science and Technology 0401/0143/18
6 · The paper itself

Abstract

The biological mediation of mineral formation (biomineralization) is realized through diverse organic macromolecules that guide this process in a spatial and temporal manner. Although the role of these molecules in biomineralization is being gradually revealed, the molecular basis of their regulatory function is still poorly understood. In this study, the incorporation and distribution of the model intrinsically disordered starmaker-like (Stm-l) protein, which is active in fish otoliths biomineralization, within calcium carbonate crystals, is revealed. Stm-l promotes crystal nucleation and anisotropic tailoring of crystal morphology. Intracrystalline incorporation of Stm-l protein unexpectedly results in shrinkage (and not expansion, as commonly described in biomineral and bioinspired crystals) of the crystal lattice volume, which is described herein, for the first time, for bioinspired mineralization. A ring pattern was observed in crystals grown for 48 h; this was composed of a protein-enriched region flanked by protein-depleted regions. It can be explained as a result of the Ostwald-like ripening process and intrinsic properties of Stm-l, and bears some analogy to the daily growth layers of the otolith.

Indexed as

AnimalsCalcium CarbonateFishesMineralsOtolithic MembraneRecombinant ProteinsCalcium CarbonateMineralsRecombinant Proteinsbiomineralscalciumcrystal growthproteinsX-ray diffraction

Identifiers

PMID31241793
PMCPMC6790713

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Registered trials

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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.