Evidence map›Paper›PMID 29476076›Full record

ArticleScientific reports2018

fam20C participates in the shell formation in the pearl oyster, Pinctada fucata.

Jinzhe Du, Chuang Liu, Guangrui Xu, Jun Xie, Liping Xie, Rongqing Zhang

Open access · goldAbstract 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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. The Gln-rich protein twip1 promotes high-density {110} twins formation in the shell of the limpetProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. The cement of the tube-dwelling polychaeteBeilstein journal of nanotechnology · 2025
    Article
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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

6 authors at 1 institution in 1 country.

Jinzhe DuInstitute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Chuang LiuDepartment of Biotechnology and Biomedicine, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, Zhejiang Province, 314006, China.
Guangrui XuDepartment of Biotechnology and Biomedicine, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, Zhejiang Province, 314006, China.
Jun XieInstitute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Liping XieInstitute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Rongqing ZhangInstitute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing, 100084, China. rqzhanglab@mail.tsinghua.edu.cn.
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinase-family with sequence similarity 20, member C (Fam20C) is a protein kinase, which can phosphorylate biomineralization related proteins in vertebrate animals. However, the function of Fam20C in invertebrate animals especially the role in biomineralization is still unknown. Herein, we cloned the cDNA of fam20C from the pearl oyster, Pinctada fucata. It is showed that the expression of fam20C in the mantle edge was much higher than other tissues. In situ hybridization showed that fam20C was expressed mostly in the outer epithelial cells of the middle fold, indicating it may play important roles in the shell formation. Besides, fam20C expression increased greatly in the D-shape stage of pearl oyster development, when the shell was first formed. During the shell repair process, the expression level of fam20C increased 1.5 times at 6 h after shell notching. Knockdown of fam20C in vivo by RNA interference resulted in abnormally stacking of calcium carbonate crystals at the edges of nacre tablets, showing direct evidence that fam20C participates in the shell formation. This study provides an insight into the role of kinase protein in the shell formation in mollusk and broaden our understanding of biomineralization mechanism.

Indexed as

AnimalsAnimal ShellsBiomineralizationCalcification, PhysiologicCalcium-Binding ProteinsCasein Kinase ICloning, MolecularDNA, ComplementaryExtracellular Matrix ProteinsGene Expression Regulation, DevelopmentalGene Knockdown TechniquesIn Situ HybridizationPinctadaProtein TransportRNA InterferenceCalcium-Binding ProteinsCasein Kinase IDNA, ComplementaryExtracellular Matrix ProteinsFAM20C protein, mouse

Identifiers

PMID29476076
PMCPMC5824888
OpenAlexW2807298392

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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.