Evidence map›Paper›PMID 28326729›Full record

ArticleHua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology2017

[Study of human leucine-rich amelogenin peptide and its regulation of mineralization by cryogenic transmission electron microscopy].

Tian Kun, Feng Xiaoyun, Du Qin, Liao Chuhang, Ren Xiaohua

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 1 institution in 1 country.

Tian KunDept. of Stomatology, Hospital of University of Electronic Science and Technology of China UESTC & Sichuan Provincial People's Hosptial, Chengdu 610072, China.
Feng XiaoyunDept. of Stomatology, Hospital of University of Electronic Science and Technology of China UESTC & Sichuan Provincial People's Hosptial, Chengdu 610072, China.
Du QinDept. of Stomatology, Hospital of University of Electronic Science and Technology of China UESTC & Sichuan Provincial People's Hosptial, Chengdu 610072, China.
Liao ChuhangDept. of Stomatology, Hospital of University of Electronic Science and Technology of China UESTC & Sichuan Provincial People's Hosptial, Chengdu 610072, China.
Ren XiaohuaDept. of Stomatology, Hospital of University of Electronic Science and Technology of China UESTC & Sichuan Provincial People's Hosptial, Chengdu 610072, China.
University of Electronic Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveRecombinant human leucine-rich amelogenin peptide (LRAP) was studied by cryogenic transmission electron microscopy (TEM); evaluation focused on its self-assembly and crystal growth in vitro.

methodsHuman LRAP was recombined through prokaryotic expression vector pCold-SUMO and transformed into Escherichia coli BL21plys to acquire purified proteins. Cryogen TEM recorded assembly and self-assembling of LRAP from pH 3.5 to pH 8.0, and the hydroxyapatite crystal growth in the mixture of LRAP protein solution and artificial saliva was observed using TEM and selected area electron diffraction.

resultsMore than 90% purity LRAP was expressed, purified and identified as described in methods. LRAP linked into oligomers, nanospheres, nanochains, and microribbons, whereas pH value increased from 3.5 to 8.0. Mature hydroxyapatite crystal growth was guided in artificial saliva filled with calcium phosphate.

conclusionsLRAP is simplified amelogenin functional domain and conserved the basic characters of amelogenin such as self-assembling and inducing crystallization along c axis. In the area of acellular synthesis of hydroxyapatite using extracellular enamel matrix protein, LRAP is one of candidate repair materials for irregular hard tissue defection.
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Indexed as

Bone DensityAmelogeninCalcium PhosphatesCrystallizationDental EnamelDental Enamel ProteinsDurapatiteHumansMicroscopy, Electron, TransmissionAmelogenincalcium phosphateCalcium PhosphatesDental Enamel ProteinsDurapatiteenamel matrix proteinsleucine-rich amelogenin peptideamelogenincryogenic transmission electron microscopyhydroxyapatiteleucine-rich amelogenin peptide

Identifiers

PMID28326729
PMCPMC7030201
OpenAlexW2998849030

What OpenQuestion holds

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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.