Evidence map›Paper›PMID 32267882›Full record

ArticlePloS one2020

Molecular characterization of a whirlin-like protein with biomineralization-related functions from the shell of Mytilus coruscus.

Yuting Jiang, Qi Sun, Meihua Fan, Xiaolin Zhang, Wang Shen, Huanzhi Xu, Zhi Liao

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

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
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 1 institution in 1 country.

Yuting JiangLaboratory of Marine Biological Source and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan, Zhejiang, P.R. China.
Qi SunLaboratory of Marine Biological Source and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan, Zhejiang, P.R. China.
Meihua FanLaboratory of Marine Biological Source and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan, Zhejiang, P.R. China.
Xiaolin ZhangLaboratory of Marine Biological Source and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan, Zhejiang, P.R. China.
Wang ShenLaboratory of Marine Biological Source and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan, Zhejiang, P.R. China.
Huanzhi XuLaboratory of Marine Biological Source and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan, Zhejiang, P.R. China.
Zhi LiaoLaboratory of Marine Biological Source and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan, Zhejiang, P.R. China.ORCID 0000-0003-0688-7346
Zhejiang Ocean University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mollusc shells are produced from calcified skeletons and have excellent mechanical properties. Shell matrix proteins (SMPs) have important functions in shell formation. A 16.6 kDa whirlin-like protein (WLP) with a PDZ domain was identified in the shell of Mytilus coruscus as a novel SMP. In this study, the expression, function, and location of WLP were analysed. The WLP gene was highly expressed and specifically located in the adductor muscle and mantle. The expression of recombinant WLP (rWLP) was associated with morphological change, polymorphic change, binding ability, and crystallization rate inhibition of the calcium carbonate crystals in vitro. In addition, an anti-rWLP antibody was prepared, and the results from immunohistochemistry and immunofluorescence analyses revealed the specific location of the WLP in the mantle, adductor muscle, and myostracum layer of the shell, suggesting multiple functions for WLP in biomineralization, muscle-shell attachment, and muscle attraction. Furthermore, results from a pull-down analysis revealed 10 protein partners of WLP in the shell matrices and a possible network of interacting WLPs in the shell. In addition, in this study, one of the WLP partners, actin, was confirmed to have the ability to bind WLP. These results expand the understanding of the functions of PDZ-domain-containing proteins in biomineralization and provide clues for determining the mechanisms of myostracum formation and muscle-shell attachment.

Indexed as

Amino Acid SequenceAnimalsAnimal ShellsBiomineralizationCalcium CarbonateImmunohistochemistryIn Situ HybridizationMembrane ProteinsMicroscopy, Electron, ScanningMicroscopy, FluorescenceMytilusProtein BindingProtein Structure, SecondaryProteomicsRecombinant ProteinsCalcium CarbonateMembrane ProteinsRecombinant Proteins

Identifiers

PMID32267882
PMCPMC7141649
OpenAlexW3014483857

What OpenQuestion holds

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LicenceCC BY
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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.