ArticleFrontiers in physiology2018
Characterization of an Atypical Metalloproteinase Inhibitors Like Protein (Sbp8-1) From Scallop Byssus.
Article in Frontiers in physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials.Advanced healthcare materials · 2026Review
- Article
- 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
- Identification and characterization of protein phosphorylation in the soluble protein fraction of scallop (Chlamys farreri) byssus.Molecular biology reports · 2019Article
- In Silico Analysis of Pacific Oyster (International journal of molecular sciences · 2019Article
- The discovered chimeric protein plays the cohesive role to maintain scallop byssal root structural integrity.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adhesion is a vital physiological process for many marine molluscs, including the mussel and scallop, and therefore it is important to characterize the proteins involved in these adhesives. Although several mussel byssal proteins were identified and characterized, the study for scallop byssal proteins remains scarce. Our previous study identified two foot-specific proteins (Sbp7, Sbp8-1), which were annotated as the tissue inhibitors of metalloproteinases (TIMPs). Evolutionary analysis suggests that the
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