ArticleScientific reports2017
A Novel Matrix Protein, PfY2, Functions as a Crucial Macromolecule during Shell Formation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- CRISPR/Cas9 Knockout of Shell Matrix Protein 1 in the Slipper-Snail Crepidula atrasolea.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2025Article
- Exploring proteins within the coccolith matrix.Scientific reports · 2024Article
- The First High-Quality Genome Assembly of Freshwater Pearl MusselInternational journal of molecular sciences · 2024Article
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- Shell Matrix Protein N38 of Pinctada fucata, Inducing Vaterite Formation, Extends the DING Protein to the Mollusca World.Marine biotechnology (New York, N.Y.) · 2022Article
- PU14, a Novel Matrix Protein, Participates in Pearl Oyster, Pinctada Fucata, Shell Formation.Marine biotechnology (New York, N.Y.) · 2021Article
- A species-specific miRNA participates in biomineralization by targeting CDS regions of Prisilkin-39 and ACCBP in Pinctada fucata.Scientific reports · 2020Article
- A basic protein, N25, from a mollusk modifies calcium carbonate morphology and shell biomineralization.The Journal of biological chemistry · 2019Article
- PfmPif97-like regulated by Pfm-miR-9b-5p participates in shell formation in Pinctada fucata martensii.PloS one · 2019Article
- Hemocytes in the extrapallial space of Pinctada fucata are involved in immunity and biomineralization.Scientific reports · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biomineralization, including shell formation, is dedicatedly regulated by matrix proteins. PfY2, a matrix protein detected in the ethylene diamine tetraacetic acid (EDTA)-soluble fraction from both prismatic layer and nacreous layer, was discovered by our group using microarray. It may play dual roles during biomineralization. However, the molecular mechanism is still unclear. In this research, we studied the function of PfY2 on crystallization in vivo and in vitro, revealing that it might be a negative regulator during shell formation. Notching experiment indicated that PfY2 was involved in shell repairing and regenerating process. Repression of PfY2 gene affected the structure of prismatic and nacreous layer simultaneously, confirming its dual roles in shell formation. Recombinant protein rPfY2 significantly suppressed CaCO
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