ArticleScientific reports2018
The discovered chimeric protein plays the cohesive role to maintain scallop byssal root structural integrity.
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 3 papers.
What it found
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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.
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.
Who cites it
3 citing papers in PubMed.
- Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials.Advanced healthcare materials · 2026Review
- Extensible and self-recoverable proteinaceous materials derived from scallop byssal thread.Nature communications · 2022Article
- Decoding the byssus fabrication by spatiotemporal secretome analysis of scallop foot.Computational and structural biotechnology journal · 2022Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Adhesion is essential for many marine sessile organisms. Unraveling the compositions and assembly of marine bioadheisves is the fundamental to understand their physiological roles. Despite the remarkable diversity of animal bioadhesion, our understanding of this biological process remains limited to only a few animal lineages, leaving the majority of lineages remain enigmatic. Our previous study demonstrated that scallop byssus had distinct protein composition and unusual assembly mechanism apart from mussels. Here a novel protein (Sbp9) was discovered from the key part of the byssus (byssal root), which contains two Calcium Binding Domain (CBD) and 49 tandem Epidermal Growth Factor-Like (EGFL) domain repeats. Modular architecture of Sbp9 represents a novel chimeric gene family resulting from a gene fusion event through the acquisition of CBD2 domain by tenascin like (TNL) gene from Na
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Registered trials
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