ArticleNature communications2022
Micro and nano-scale compartments guide the structural transition of silk protein monomers into silk fibers.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed.
- A Dopamine Driven Dual-Amplifier Strategy for High Performance Bioorganic Piezoelectrics via Secondary-Structure Modulation and Synergistic Molecular Dipoles.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Diverging Liquid-Liquid Phase Separation Behavior of Different Recombinant Major Ampullate Spidroins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The stage-wise macromolecular assembly and structure evolution of silk along the silk gland.Nature communications · 2026Article
- Silk-Inspired Design and Manufacturing of Robust Plantymers.Nature communications · 2026Article
- Cryo-ET comparison of the hierarchical ultrastructure of silkworm, spider, and artificial silk fibers.Nature communications · 2026Article
- The cGAS-STING pathway at the crossroads of neuroimmunology: bridging innate immunity to aging and neurodegeneration.Biomarker research · 2026Review
- pH-triggered clustering regulates β-sheet activation in silk assembly.Communications chemistry · 2026Article
- Spider silk-based structural proteins as tough, biodegradable, and sustainable polymers.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2026Review
- Transient infrared nanoscopy resolves the millisecond photoswitching dynamics of single lipid vesicles in water.Nature communications · 2025Article
- Manipulating the Assembly and Architecture of Fibrillar Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Immobilization of KR-12 on a Titanium Alloy Surface Using Linking Arms Improves Antimicrobial Activity and Supports Osteoblast Cytocompatibility.ACS applied bio materials · 2025Article
- Spontaneous Hollow Coacervate Transition of Silk Fibroin via Dilution and Its Transition to Microcapsules.Biomacromolecules · 2025Article
- Probing the Interplay of Protein Self-Assembly and Covalent Bond Formation in Photo-Crosslinked Silk Fibroin Hydrogels.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Fine Structural Analysis of Degummed Fibroin Fibers Reveals Its Superior Mechanical Capabilities.ChemSusChem · 2025Article
- Calcium ion-triggered liquid-liquid phase separation of silk fibroin and spinning through acidification and shear stress.Nature communications · 2024Article
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
- Two-dimensional silk.Science advances · 2024Article
- Metal ions guide the production of silkworm silk fibers.Nature communications · 2024Article
- Molecular organization of fibroin heavy chain and mechanism of fibre formation in Bombyx mori.Communications biology · 2024Article
- In-situ observation of silk nanofibril assembly via graphene plasmonic infrared sensor.Nature communications · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Silk is a unique, remarkably strong biomaterial made of simple protein building blocks. To date, no synthetic method has come close to reproducing the properties of natural silk, due to the complexity and insufficient understanding of the mechanism of the silk fiber formation. Here, we use a combination of bulk analytical techniques and nanoscale analytical methods, including nano-infrared spectroscopy coupled with atomic force microscopy, to probe the structural characteristics directly, transitions, and evolution of the associated mechanical properties of silk protein species corresponding to the supramolecular phase states inside the silkworm's silk gland. We found that the key step in silk-fiber production is the formation of nanoscale compartments that guide the structural transition of proteins from their native fold into crystalline β-sheets. Remarkably, this process is reversible. Such reversibility enables the remodeling of the final mechanical characteristics of silk materials. These results open a new route for tailoring silk processing for a wide range of new material formats by controlling the structural transitions and self-assembly of the silk protein's supramolecular phases.
Indexed as
Identifiers
What OpenQuestion holds
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.