ReviewNature chemical biology2015
Toward spinning artificial spider silk.
Review in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 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
129 citing papers in PubMed, 374 citations in OpenAlex.
- Ultratight Binding of a Capture Spiral Spider Silk Protein through Electrostatic Forces.ACS bio & med chem Au · 2026Article
- Liquid-liquid phase separation enables chromatography-free purification and high-performance spidroin-amyloid hybrid silk fibers.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Spider Silk-Like Nanodomain Spacings Enable Mechanically Robust and Healable Elastomers with Record-High Puncture Resistance.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Scalable hierarchical textile fibers toward personalized wearable atmospheric water harvesting.Science advances · 2026Article
- The stage-wise macromolecular assembly and structure evolution of silk along the silk gland.Nature communications · 2026Article
- Transition From Land to Sea: Comparative Genomics Illuminates the Adaptive Evolution of the Intertidal Spider.Molecular ecology resources · 2026Article
- Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026Article
- Post-translational modifications of silk proteins.RSC chemical biology · 2026Review
- Spider Silk Inspired Processing of Liquid Crystalline Complex Coacervates.ACS macro letters · 2026Article
- Arg-Tyr cation-π interactions drive phase separation and β-sheet assembly in native spider dragline silk.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Seed Oligomers Regulate Sequence Development through a Templating Effect in Simulated Irreversible Step-Growth Copolymerization.Macromolecules · 2025Article
- Distinct Dimerization Mechanisms in Silkworm and Spider Silk Proteins Revealed by Mass Photometry.The journal of physical chemistry letters · 2025Article
- Physics-informed deep learning for plasmonic sensing of nanoscale protein dynamics in solution.Science advances · 2025Article
- Crosslinking, salt-induced aging, and secondary structure formation in Peptide-containing coacervates inspired by spider silk.Communications chemistry · 2025Article
- Effect of Poly(l-serine) Additives with Different Primary Structures on the Mechanical Properties of Poly(vinyl alcohol) Films.Biomacromolecules · 2025Article
- The Biology of Natural Polymers Accelerates and Expands the Science of Biomacromolecules: A Focus on Structural Proteins.Biomacromolecules · 2025Review
- Artificial Spidroin Nanogenerator-Based Articulus Wound Dressing.ChemistryOpen · 2025Article
- High-yield spidroin mimics for bioinspired fibers via computational design.Frontiers in bioengineering and biotechnology · 2025Article
- Liquid-liquid crystalline phase separation of spider silk proteins.Communications chemistry · 2024Review
- Coupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.ACS nano · 2024Article
69 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spider silk is strong and extensible but still biodegradable and well tolerated when implanted, making it the ultimate biomaterial. Shortcomings that arise in replicating spider silk are due to the use of recombinant spider silk proteins (spidroins) that lack native domains, the use of denaturing conditions under purification and spinning and the fact that the understanding of how spiders control silk formation is incomplete. Recent progress has unraveled the molecular mechanisms of the spidroin N- and C-terminal nonrepetitive domains (NTs and CTs) and revealed the pH and ion gradients in spiders' silk glands, clarifying how spidroin solubility is maintained and how silk is formed in a fraction of a second. Protons and CO2, generated by carbonic anhydrase, affect the stability and structures of the NT and CT in different ways. These insights should allow the design of conditions and devices for the spinning of recombinant spidroins into native-like silk.
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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.