Evidence map›Paper›PMID 26780236›Full record

ArticleEuropean biophysics journal : EBJ2016

Structural studies of hydrated samples of amorphous calcium phosphate and phosphoprotein nanoclusters.

Samuel Lenton, Tommy Nylander, Carl Holt, Lindsay Sawyer, Michael Härtlein, Harrald Müller, Susana C M Teixeira

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Article in European biophysics journal : EBJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

4 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
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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

7 authors at 6 institutions in 3 countries.

Samuel LentonEPSAM, Keele University, Staffordshire, ST5 5BG, UK.
Tommy NylanderDivision of Physical Chemistry, Department of Chemistry, Lund University, 124, Lund, S221 00, Sweden.
Carl HoltInstitute of Molecular, Cell, and Systems Biology, University of Glasgow, Glasgow, G12 8QQ, UK.
Lindsay SawyerStructural Biochemistry Group, University of Edinburgh, Roger Land Building, The King's Buildings, Mayfield Road, EH9 3JR, Edinburgh, UK.
Michael HärtleinInstitut Laue-Langevin, 71 Avenue des Martyrs, 38042, Grenoble Cedex 9, France.
Harrald MüllerEuropean Synchrotron Radiation Facility, CS 40220, 38043, Grenoble, France.
Susana C M TeixeiraEPSAM, Keele University, Staffordshire, ST5 5BG, UK. teixeira@ill.fr.ORCID http://orcid.org/0000-0002-1967-0026
Institut Laue-Langevin · FREuropean Synchrotron Radiation Facility · FRLund University · SEUniversity of Edinburgh · GBUniversity of Glasgow · GBUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There are abundant examples of nanoclusters and inorganic microcrystals in biology. Their study under physiologically relevant conditions remains challenging due to their heterogeneity, instability, and the requirements of sample preparation. Advantages of using neutron diffraction and contrast matching to characterize biomaterials are highlighted in this article. We have applied these and complementary techniques to search for nanocrystals within clusters of calcium phosphate sequestered by bovine phosphopeptides, derived from osteopontin or casein. The neutron diffraction patterns show broad features that could be consistent with hexagonal hydroxyapatite crystallites smaller than 18.9 Å. Such nanocrystallites are, however, undetected by the complementary X-ray and FTIR data, collected on the same samples. The absence of a distinct diffraction pattern from the nanoclusters supports the generally accepted amorphous calcium phosphate structure of the mineral core.

Indexed as

AnimalsCalcium PhosphatesCattleNanoparticlesOsteopontinPhosphopeptidesPhosphoproteinsWateramorphous calcium phosphateCalcium PhosphatesOsteopontinPhosphopeptidesPhosphoproteinsWaterAmorphous calcium phosphateBiomineralizationCaseinNeutron diffractionOsteopontinPhosphoproteins

Identifiers

PMID26780236
OpenAlexW2270069018

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.