ArticleJournal of the Royal Society, Interface2017
A cohort of new adhesive proteins identified from transcriptomic analysis of mussel foot glands.
Article in Journal of the Royal Society, Interface, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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Who cites it
30 citing papers in PubMed, 91 citations in OpenAlex.
- Biomedical Potential of the Deep-Sea Vent MusselMarine drugs · 2026Review
- Investigating byssus self-assembly ofMarine life science & technology · 2026Article
- Identification and characterization of a wet adhesive protein extracted fromProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Histidine-rich coiled-coils promote zinc-dependent self-assembly and curing of porous mussel glues.Nature communications · 2026Article
- Intertidal Warfare: Synergistic Allelopathy Mediates Spatial Competition between Two Marine Calcareous-Shelled Sessile Organisms.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The Redox Properties of Polyphenols and Their Role in ROS Generation for Biomedical Applications.Angewandte Chemie (International ed. in English) · 2026Review
- Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials.Advanced healthcare materials · 2026Review
- De novo transcriptome analysis of Perna perna L. (Bivalve) with functional and metabolic pathway analysis.Scientific data · 2025Article
- Development of a decellularized extracellular matrix-derived wet adhesive for sustained drug delivery and enhanced wound healing.Materials today. Bio · 2025Article
- Catechol redox maintenance in mussel adhesion.Nature reviews. Chemistry · 2025Review
- Pharmacological effects and application prospects of mussel adhesive proteins.Frontiers in pharmacology · 2025Review
- Diversity and evolution of tyrosinase enzymes involved in the adhesive systems of mussels and tubeworms.iScience · 2024Article
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Recent advances in biomimetic hemostatic materials.Materials today. Bio · 2023Review
- Protein-Based Biological Materials: Molecular Design and Artificial Production.Chemical reviews · 2023Review
- Glycoproteins Involved in Sea Urchin Temporary Adhesion.Marine drugs · 2023Article
- Hydrogen-bonds mediate liquid-liquid phase separation of mussel derived adhesive peptides.Nature communications · 2022Article
- Exploration of sea anemone-inspired high-performance biomaterials with enhanced antioxidant activity.Bioactive materials · 2022Article
- Decoding the byssus fabrication by spatiotemporal secretome analysis of scallop foot.Computational and structural biotechnology journal · 2022Article
- From Natural Xanthones to Synthetic C-1 Aminated 3,4-Dioxygenated Xanthones as Optimized Antifouling Agents.Marine drugs · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The adaptive attachment of marine mussels to a wide range of substrates in a high-energy, saline environment has been explored for decades and is a significant driver of bioinspired wet adhesion research. Mussel attachment relies on a fibrous holdfast known as the byssus, which is made by a specialized appendage called the foot. Multiple adhesive and structural proteins are rapidly synthesized, secreted and moulded by the foot into holdfast threads. About 10 well-characterized proteins, namely the mussel foot proteins (Mfps), the preCols and the thread matrix proteins, are reported as representing the bulk of these structures. To explore how robust this proposition is, we sequenced the transcriptome of the glandular tissues that produce and secrete the various holdfast components using next-generation sequencing methods. Surprisingly, we found around 15 highly expressed genes that have not previously been characterized, but bear key similarities to the previously defined mussel foot proteins, suggesting additional contribution to byssal function. We verified the validity of these transcripts by polymerase chain reaction, cloning and Sanger sequencing as well as confirming their presence as proteins in the byssus. These newly identified proteins greatly expand the palette of mussel holdfast biochemistry and provide new targets for investigation into bioinspired wet adhesion.
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Registered trials
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.