Evidence map›Paper›PMID 30209287›Full record

ArticleScientific reports2018

First evidence of octacalcium phosphate@osteocalcin nanocomplex as skeletal bone component directing collagen triple-helix nanofibril mineralization.

Paul Simon, Daniel Grüner, Hartmut Worch, Wolfgang Pompe, Hannes Lichte, Thaqif El Khassawna, Christian Heiss, Sabine Wenisch, Rüdiger Kniep

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

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  16. Role of carboxylic organic molecules in interfibrillar collagen mineralization.Frontiers in bioengineering and biotechnology · 2023
    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

9 authors.

Paul SimonMax-Planck-Institut für Chemische Physik fester Stoffe, Nöthnitzer Str. 40, 01187, Dresden, Germany. Paul.Simon@cpfs.mpg.de.
Daniel GrünerForschungszentrum Jülich GmbH, Institute of Energy and Climate Research, IEK-2, 52425, Jülich, Germany.
Hartmut WorchInstitute of Materials Science, Technical University of Dresden, Helmholtzstr. 7, 01069, Dresden, Germany.
Wolfgang PompeInstitute of Materials Science, Technical University of Dresden, Helmholtzstr. 7, 01069, Dresden, Germany.
Hannes LichteInstitute of Structure Physics, Technical University of Dresden, Zum Triebenberg 50, 01328, Dresden Zaschendorf, Germany.
Thaqif El KhassawnaExperimental Trauma Surgery, Faculty of Medicine, Justus-Liebig University of Giessen, Aulweg 128, Giessen, 35392, Germany.ORCID 0000-0002-1187-8578
Christian HeissExperimental Trauma Surgery, Faculty of Medicine, Justus-Liebig University of Giessen, Aulweg 128, Giessen, 35392, Germany.
Sabine WenischClinic of Small animals, c/o Institute of Veterinary Anatomy, Justus-Liebig University of Giessen, Giessen, Germany.
Rüdiger KniepMax-Planck-Institut für Chemische Physik fester Stoffe, Nöthnitzer Str. 40, 01187, Dresden, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tibia trabeculae and vertebrae of rats as well as human femur were investigated by high-resolution TEM at the atomic scale in order to reveal snapshots of the morphogenetic processes of local bone ultrastructure formation. By taking into account reflections of hydroxyapatite for Fourier filtering the appearance of individual alpha-chains within the triple-helix clearly shows that bone bears the feature of an intergrowth composite structure extending from the atomic to the nanoscale, thus representing a molecular composite of collagen and apatite. Careful Fourier analysis reveals that the non-collagenous protein osteocalcin is present directly combined with octacalcium phosphate. Besides single spherical specimen of about 2 nm in diameter, osteocalcin is spread between and over collagen fibrils and is often observed as pearl necklace strings. In high-resolution TEM, the three binding sites of the γ-carboxylated glutamic acid groups of the mineralized osteocalcin were successfully imaged, which provide the chemical binding to octacalcium phosphate. Osteocalcin is attached to the collagen structure and interacts with the Ca-sites on the (100) dominated hydroxyapatite platelets with Ca-Ca distances of about 9.5 Å. Thus, osteocalcin takes on the functions of Ca-ion transport and suppression of hydroxyapatite expansion.

Indexed as

AnimalsApatitesBinding SitesBlood PlateletsCalcification, PhysiologicCalciumCalcium PhosphatesCollagenDurapatiteFemaleFemurGlutamic AcidOsteocalcinRatsRats, Sprague-DawleyTibiaApatitesCalciumCalcium PhosphatesCollagenDurapatiteGlutamic Acidoctacalcium phosphateOsteocalcin

Identifiers

PMID30209287
PMCPMC6135843

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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.