ArticleThe Journal of experimental biology2009
Hyperunstable matrix proteins in the byssus of Mytilus galloprovincialis.
Article in The Journal of experimental biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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Who cites it
21 citing papers in PubMed.
- Investigating byssus self-assembly ofMarine life science & technology · 2026Article
- Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials.Advanced healthcare materials · 2026Review
- Thermal tipping points in mediterranean mussel adhesion: molecular mechanisms and mechanical consequences of heatwave on byssus production in Mytilus galloprovincialis.Scientific reports · 2025Article
- Catechol redox maintenance in mussel adhesion.Nature reviews. Chemistry · 2025Review
- Diversity and evolution of tyrosinase enzymes involved in the adhesive systems of mussels and tubeworms.iScience · 2024Article
- Protein-Based Biological Materials: Molecular Design and Artificial Production.Chemical reviews · 2023Review
- Viscoelastic analysis of mussel threads reveals energy dissipative mechanisms.Journal of the Royal Society, Interface · 2022Article
- Structure-Antifouling Activity Relationship and Molecular Targets of Bio-Inspired(thio)xanthones.Biomolecules · 2020Article
- Fingerprinting of Proteins that Mediate Quagga Mussel Adhesion using a De Novo Assembled Foot Transcriptome.Scientific reports · 2019Article
- A cohort of new adhesive proteins identified from transcriptomic analysis of mussel foot glands.Journal of the Royal Society, Interface · 2017Article
- Rapid self-assembly of complex biomolecular architectures during mussel byssus biofabrication.Nature communications · 2017Article
- Mussel adhesion - essential footwork.The Journal of experimental biology · 2017Review
- Deep conservation of bivalve nacre proteins highlighted by shell matrix proteomics of the Unionoida Elliptio complanata and Villosa lienosa.Journal of the Royal Society, Interface · 2017Article
- Recombinant mussel proximal thread matrix protein promotes osteoblast cell adhesion and proliferation.BMC biotechnology · 2016Article
- Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins.Nature communications · 2015Article
- Crystallization and preliminary X-ray diffraction analysis of proximal thread matrix protein 1 (PTMP1) from Mytilus galloprovincialis.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Novel proteins identified in the insoluble byssal matrix of the freshwater zebra mussel.Marine biotechnology (New York, N.Y.) · 2014Article
- Changing environments and structure--property relationships in marine biomaterials.The Journal of experimental biology · 2012Review
- Mussel-Inspired Adhesives and Coatings.Annual review of materials research · 2011Article
- Mussel protein adhesion depends on interprotein thiol-mediated redox modulation.Nature chemical biology · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The marine mussel Mytilus galloprovincialis is tethered to rocks in the intertidal zone by a holdfast known as the byssus. Functioning as a shock absorber, the byssus is composed of threads, the primary molecular components of which are collagen-containing proteins (preCOLs) that largely dictate the higher order self-assembly and mechanical properties of byssal threads. The threads contain additional matrix components that separate and perhaps lubricate the collagenous microfibrils during deformation in tension. In this study, the thread matrix proteins (TMPs), a glycine-, tyrosine- and asparagine-rich protein family, were shown to possess unique repeated sequence motifs, significant transcriptional heterogeneity and were distributed throughout the byssal thread. Deamidation was shown to occur at a significant rate in a recombinant TMP and in the byssal thread as a function of time. Furthermore, charge heterogeneity presumably due to deamidation was observed in TMPs extracted from threads. The TMPs were localized to the preCOL-containing secretory granules in the collagen gland of the foot and are assumed to provide a viscoelastic matrix around the collagenous fibers in byssal threads.
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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.