Evidence map›Paper›PMID 27909912›Full record

ArticleMarine biotechnology (New York, N.Y.)2016

Identification and Characterization of the Lysine-Rich Matrix Protein Family in Pinctada fucata: Indicative of Roles in Shell Formation.

Jian Liang, Jun Xie, Jing Gao, Chao-Qun Xu, Yi Yan, Gan-Chu Jia, Liang Xiang, Li-Ping Xie, Rong-Qing Zhang

Abstract read
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In one paragraph

Article in Marine biotechnology (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

6 citing papers in PubMed, 22 citations in OpenAlex.

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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 at 2 institutions in 1 country.

Jian LiangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Jun XieInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Jing GaoInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Chao-Qun XuInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Yi YanInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Gan-Chu JiaInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Liang XiangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Li-Ping XieInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China. lpxie@mail.tsinghua.edu.cn.
Rong-Qing ZhangInstitute of Marine Biotechnology, Collaborative Innovation Center of Deep Sea Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China. rqzhang@mail.tsinghua.edu.cn.
Tsinghua University · CNQinghai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mantle can secret matrix proteins playing key roles in regulating the process of shell formation. The genes encoding lysine-rich matrix proteins (KRMPs) are one of the most highly expressed matrix genes in pearl oysters. However, the expression pattern of KRMPs is limited and the functions of them still remain unknown. In this study, we isolated and identified six new members of lysine-rich matrix proteins, rich in lysine, glycine and tyrosine, and all of them are basic matrix proteins. Combined with four members of the KRMPs previously reported, all these proteins can be divided into three subclasses according to the results of phylogenetic analyses: KRMP1-3 belong to subclass KPI, KRMP4-5 belong to KPII, and KRMP6-10 belong to KPIII. Three subcategories of lysine-rich matrix proteins are highly expressed in the D-phase, the larvae and adult mantle. Lysine-rich matrix proteins are involved in the shell repairing process and associated with the formation of the shell and pearl. What's more, they can cause abnormal shell growth after RNA interference. In detail, KPI subgroup was critical for the beginning formation of the prismatic layer; both KPII and KPIII subgroups participated in the formation of prismatic layer and nacreous layer. Compared with different temperatures and salinity stimulation treatments, the influence of changes in pH on KRMPs gene expression was the greatest. Recombinant KRMP7 significantly inhibited CaCO

Indexed as

Multigene FamilyAmino Acid SequenceAnimalsAnimal ShellsCalcium CarbonateCloning, MolecularEscherichia coliExtracellular Matrix ProteinsGene Expression Regulation, DevelopmentalHydrogen-Ion ConcentrationLarvaNacrePhylogenyPinctadaRecombinant ProteinsSalinityCalcium CarbonateExtracellular Matrix ProteinsNacreRecombinant ProteinsBiomineralizationGene expressionGene familyKRMPMollusk

Identifiers

PMID27909912
OpenAlexW2558802633

What OpenQuestion holds

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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.