The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Assembly mechanism of recombinant spider silk proteins
Open accessAbstract
Spider silk threads are formed by the irreversible aggregation of silk proteins in a spinning duct with dimensions of only a few micrometers. Here, we present a microfluidic device in which engineered and recombinantly produced spider dragline silk proteins eADF3 (engineered Araneus diadematus fibroin) and eADF4 are assembled into fibers. Our approach allows the direct observation and identification of the essential parameters of dragline silk assembly. Changes in ionic conditions and pH result in aggregation of the two proteins. Assembly of eADF3 fibers was induced only in the presence of an elongational flow component. Strikingly, eADF4 formed fibers only in combination with eADF3. On the basis of these results, we propose a model for dragline silk aggregation and early steps of fiber assembly in the microscopic regime.
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Cites
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Mechanism of silk processing in insects and spiders
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Primary Structure Elements of Spider Dragline Silks and Their Contribution to Protein Solubility
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Self-citationRousseau, M.-E., Lefèvre, T., Beaulieu, L., Asakura, T., & Pézolet, M. (2004) · Biomacromolecules · doi:10.1021/bm049717v · Cited by 303
Biotechnological Production of Spider‐Silk Proteins Enables New Applications
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Self-citationModels of shear-thickening behavior in physically crosslinked networks
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Cited by
Xia, X.-X., Qian, Z.-G., Ki, C. S., Park, Y. H., Kaplan, D. L., & Lee, S. Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003366107 · Cited by 561
Controlling silk fibroin particle features for drug delivery
Lammel, A. S., Hu, X., Park, S.-H., Kaplan, D. L., & Scheibel, T. R. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.02.024 · Cited by 538
Self-citationNext-generation synthetic gene networks
Lu, T. K., Khalil, A. S., & Collins, J. J. (2009) · Nature Biotechnology · doi:10.1038/nbt.1591 · Cited by 365
Decoding the secrets of spider silk
Eisoldt, L., Smith, A., & Scheibel, T. (2011) · Materials Today · doi:10.1016/s1369-7021(11)70057-8 · Cited by 342
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Metadata
- Authors
- Rammensee, S., Slotta, U., Scheibel, T., & Bausch, A. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-05-06
- Volume
- 105
- Issue
- 18
- Pages
- 6590-6595
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2151881328
- Cited by
- 363
- References
- 20
- FWCI
- 11.70
- Type
- journal article
- Language
- en
- Open access
- green
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- Rammensee, S., Slotta, U., Scheibel, T., & Bausch, A. R. (2008). Assembly mechanism of recombinant spider silk proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0709246105
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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