ArticleJournal of the Royal Society, Interface2021
Correlation between protein secondary structure and mechanical performance for the ultra-tough dragline silk of Darwin's bark spider.
Article in Journal of the Royal Society, Interface, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- 3D-printed soy protein and microalga films: A sustainable approach with antioxidant functionality.Current research in food science · 2026Article
- Triangle weaver spiders construct spring-loaded webs using a novel set of genes for exceptionally proline-rich silk.PNAS nexus · 2025Article
- Characterization of the secondary structure, renaturation and physical ageing of gelatine adhesives.Scientific reports · 2025Article
- Article
- Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection.Molecules (Basel, Switzerland) · 2024Review
- Influence of experimental methods on the mechanical properties of silk fibers: A systematic literature review and future road map.Biophysics reviews · 2023Review
- Molecular mechanisms of the high performance of spider silks revealed through multi-omics analysis.Biophysics and physicobiology · 2023Article
- An Image-Analysis-Based Method for the Prediction of Recombinant Protein Fiber Tensile Strength.Materials (Basel, Switzerland) · 2022Article
- Characterization of the genome and silk-gland transcriptomes of Darwin's bark spider (Caerostris darwini).PloS one · 2022Article
- Recombinant Spider Silk: Promises and Bottlenecks.Frontiers in bioengineering and biotechnology · 2022Review
- Darwin's bark spider shares a spidroin repertoire withOpen biology · 2021Article
- Correlation between protein secondary structure and mechanical performance for the ultra-tough dragline silk of Darwin's bark spider.Journal of the Royal Society, Interface · 2021Article
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spider major ampullate (MA) silk exhibits high tensile strength and extensibility and is typically a blend of MaSp1 and MaSp2 proteins with the latter comprising glycine-proline-glycine-glycine-X repeating motifs that promote extensibility and supercontraction. The MA silk from Darwin's bark spider (
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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.