ArticleHeredity2018
Conservation of a pH-sensitive structure in the C-terminal region of spider silk extends across the entire silk gene family.
Article in Heredity, 2018. 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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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.
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Who cites it
11 citing papers in PubMed.
- From fibres to adhesives: evolution of spider capture threads from web anchors by radical changes in silk gland function.Journal of the Royal Society, Interface · 2024Article
- Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers.Nature communications · 2024Article
- Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection.Molecules (Basel, Switzerland) · 2024Review
- Domain swap facilitates structural transitions of spider silk protein C-terminal domains.Protein science : a publication of the Protein Society · 2023Article
- Silk Assembly against Hydrophobic Surfaces─Modeling and Imaging of Formation of Nanofibrils.ACS applied bio materials · 2023Article
- 1000 spider silkomes: Linking sequences to silk physical properties.Science advances · 2022Article
- Complexity of Spider Dragline Silk.Biomacromolecules · 2022Review
- Golden orb-weaving spider (Trichonephila clavipes) silk genes with sex-biased expression and atypical architectures.G3 (Bethesda, Md.) · 2021Article
- Towards engineering and production of artificial spider silk using tools of synthetic biology.Engineering biology · 2020Review
- Spidroins and Silk Fibers of Aquatic Spiders.Scientific reports · 2019Article
- Two-step self-assembly of a spider silk molecular clamp.Nature communications · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Spiders produce multiple silks with different physical properties that allow them to occupy a diverse range of ecological niches, including the underwater environment. Despite this functional diversity, past molecular analyses show a high degree of amino acid sequence similarity between C-terminal regions of silk genes that appear to be independent of the physical properties of the resulting silks; instead, this domain is crucial to the formation of silk fibers. Here, we present an analysis of the C-terminal domain of all known types of spider silk and include silk sequences from the spider Argyroneta aquatica, which spins the majority of its silk underwater. Our work indicates that spiders have retained a highly conserved mechanism of silk assembly, despite the extraordinary diversification of species, silk types and applications of silk over 350 million years. Sequence analysis of the silk C-terminal domain across the entire gene family shows the conservation of two uncommon amino acids that are implicated in the formation of a salt bridge, a functional bond essential to protein assembly. This conservation extends to the novel sequences isolated from A. aquatica. This finding is relevant to research regarding the artificial synthesis of spider silk, suggesting that synthesis of all silk types will be possible using a single process.
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Registered trials
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