ArticleNature communications2024
Structural conversion of the spidroin C-terminal domain during assembly of spider silk fibers.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- The temperature dependence of amyloidProceedings of the National Academy of Sciences of the United States of America · 2026Article
- A Mini-Spidroin Forms High-Performance Artificial Spider Silk via Edge-Cysteine-Locked β-Sheet Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Recombinant production of spider silk protein in Physcomitrella photobioreactors.Plant cell reports · 2025Article
- Silk Protein Gene Engineering and Its Applications: Recent Advances in Biomedicine Driven by Molecular Biotechnology.Drug design, development and therapy · 2025Review
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
The major ampullate Spidroin 1 (MaSp1) is the main protein of the dragline spider silk. The C-terminal (CT) domain of MaSp1 is crucial for the self-assembly into fibers but the details of how it contributes to the fiber formation remain unsolved. Here we exploit the fact that the CT domain can form silk-like fibers by itself to gain knowledge about this transition. Structural investigations of fibers from recombinantly produced CT domain from E. australis MaSp1 reveal an α-helix to β-sheet transition upon fiber formation and highlight the helix N
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Registered trials
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