The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
EVOLUTION OF ARTHROPOD SILKS
Abstract
▪ Abstract Silks belong to the class of molecules called structural proteins. The ability to produce silk proteins has evolved multiple times in the arthropods, and silk secreting glands have evolved via two different pathways. The comparative data and phylogenetic analyses in this review suggest that the silk-secreting systems of spiders and insects are homologous and linked to the crural gland (origin of systemic pathway to silk production) and cuticular secretions (origin of surficial pathway to silk production) of an onychophoran-like ancestor. The evolution of silk secreting organs via a surficial pathway is possible in adult and larval hexapods, regardless of their developmental mode. Silk secretion via a systemic pathway is possible in either adult or larval hexapods, but only larval insects have dedicated silk producing glands. Spiders, however, have evolved silk producing systems via both systemic pathway and surficial pathways, and a single individual retains both throughout its lifespan. Early in the evolution of spiders, silk glands were undifferentiated, suggesting that the number of silk secreting glands of any individual was related to the spider's energetic need to produce large quantities of protein. However, the complex silk-producing systems that characterize the aerial web–building spiders and the diverse types of proteins they produce suggest that their silks reflect the diverse and increasing number of ways in which spiders use them. Because the muscular and innervated spinnerets and spigots of spiders allow them to control fiber functional properties, silk proteins represent an avenue through which animal behavior may directly affect the molecular properties of a protein.
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An investigation of the structure of silk fibroin
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Molecular Orientation and Two-Component Nature of the Crystalline Fraction of Spider Dragline Silk
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The structure and properties of spider silk
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“Cross-β” conformation in proteins
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Cited by
Liquid crystalline spinning of spider silk
Vollrath, F., & Knight, D. P. (2001) · Nature · doi:10.1038/35069000 · Cited by 1,610
Silk fibroin as a functional biomaterial for tissue engineering
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Protein Secondary Structure and Orientation in Silk as Revealed by Raman Spectromicroscopy
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Spider and mulberry silkworm silks as compatible biomaterials
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Metadata
- Authors
- Craig, C. L.
- Venue
- Annual Review of Entomology
- Publisher
- Annual Reviews
- Published
- 1997-01
- Volume
- 42
- Issue
- 1
- Pages
- 231-267
- ISSN
- 0066-4170 (ISSN-L)
- 1545-4487
- OpenAlex
- W2098863487
- Cited by
- 375
- References
- 36
- FWCI
- 1.12
- Type
- journal article
- Language
- en
- Open access
- closed
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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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