ReviewPrion
Silks produced by insect labial glands.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 107 citations in OpenAlex.
- Protein Sequence and Structural Diversity inBiomacromolecules · 2026Article
- Morphological and compositional basis of silk fiber function inJournal of materials chemistry. B · 2026Article
- Evolution of Highly Repetitive Silk Genes in the Luna Moth, Actias luna.Genome biology and evolution · 2026Article
- Self-Assembly ofIndustrial & engineering chemistry research · 2025Article
- Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts:Chemical reviews · 2025Review
- Native Silk Fibers: Protein Sequence and Structure Influences on Thermal and Mechanical Properties.Biomacromolecules · 2025Review
- Transcriptome and Neuroendocrinome Responses to Environmental Stress in the Model and Pest InsectInternational journal of molecular sciences · 2025Article
- Article
- Exploring the functional properties ofMaterials today. Communications · 2025Article
- Characterization and comparative analysis of sericin protein 150 in Bombyx mori.Scientific reports · 2024Article
- Disentangling the Web: An Interdisciplinary Review on the Potential and Feasibility of Spider Silk Bioproduction.ACS biomaterials science & engineering · 2024Review
- De Novo Long-Read Genome Assembly and Annotation of the Luna Moth (Actias luna) Fully Resolves Repeat-Rich Silk Genes.Genome biology and evolution · 2024Article
- Article
- Flow-Induced Protein Chain Deformation, Segmental Orientation, and Phase Separation in Native Silk Feedstock.Biomacromolecules · 2023Article
- Negative phototaxis of jumping cocooned parasitoid wasp larvae against short wavelengths and physicochemical properties of the cocoon shell.Scientific reports · 2023Article
- Silk Sericin: A Promising Sustainable Biomaterial for Biomedical and Pharmaceutical Applications.Polymers · 2022Review
- An Ecological Profile ofInsects · 2022Article
- A Gland of Many Uses: a Diversity of Compounds in the Labial Glands of the Bumble Bee Bombus impatiens Suggests Multiple Signaling Functions.Journal of chemical ecology · 2022Article
- Bioselectivity of silk protein-based materials and their bio-inspired applications.Beilstein journal of nanotechnology · 2022Review
- RNA-Seq analysis of the blue light-emitting Orfelia fultoni (Diptera: Keroplatidae) suggest photoecological adaptations at the molecular level.Comparative biochemistry and physiology. Part D, Genomics & proteomics · 2021Article
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 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insect silks are secreted from diverse gland types; this chapter deals with the silks produced by labial glands of Holometabola (insects with pupa in their life cycle). Labial silk glands are composed of a few tens or hundreds of large polyploid cells that secrete polymerizing proteins which are stored in the gland lumen as a semi-liquid gel. Polymerization is based on weak molecular interactions between repetitive amino acid motifs present in one or more silk proteins; cross-linking by disulfide bonds may be important in the silks spun under water. The mechanism of long-term storage of the silk dope inside the glands and its conversion into the silk fiber during spinning is not fully understood. The conversion occurs within seconds at ambient temperature and pressure, under minimal drawing force and in some cases under water. The silk filament is largely built of proteins called fibroins and in Lepidoptera and Trichoptera coated by glue-type proteins known as sericins. Silks often contain small amounts of additional proteins of poorly known function. The silk components controlling dope storage and filament formation seem to be conserved at the level of orders, while the nature of polymerizing motifs in the fibroins, which determine the physical properties of silk, differ at the level of family and even genus. Most silks are based on fibroin beta-sheets interrupted with other structures such as alpha-helices but the silk proteins of certain sawflies have predominantly a collagen-like or polyglycine II arrangement and the silks of social Hymenoptera are formed from proteins in a coiled coil arrangement.
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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.