{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670320738945152.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1046/j.1432-1033.2002.03112.x"}},{"identifier":{"@type":"URI","@value":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1033.2002.03112.x"}},{"identifier":{"@type":"URI","@value":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1033.2002.03112.x"}}],"dc:title":[{"@value":"Amyloidogenic nature of spider silk"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>In spiders soluble proteins are converted to form insoluble silk fibres, stronger than steel. The final fibre product has long been the subject of study; however, little is known about the conversion process in the silk‐producing gland of the spider. Here we describe a study of the conversion of the soluble form of the major spider‐silk protein, spidroin, directly extracted from the silk gland, to a β‐sheet enriched state using circular dichroism (CD) spectroscopy. Combined with electron microscopy (EM) data showing fibril formation in the β‐sheet rich region of the gland and amino‐acid sequence analyses linking spidroin and amyloids, these results lead us to suggest that the refolding conversion is amyloid like. We also propose that spider silk could be a valuable model system for testing hypotheses concerning β‐sheet formation in other fibrilogenic systems, including amyloids.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383670320738945155","@type":"Researcher","foaf:name":[{"@value":"John M. Kenney"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320738945154","@type":"Researcher","foaf:name":[{"@value":"David Knight"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320738945153","@type":"Researcher","foaf:name":[{"@value":"Michael J. Wise"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670320738945152","@type":"Researcher","foaf:name":[{"@value":"Fritz Vollrath"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00142956"},{"@type":"EISSN","@value":"14321033"}],"prism:publicationName":[{"@value":"European Journal of Biochemistry"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"2002-08","prism:volume":"269","prism:number":"16","prism:startingPage":"4159","prism:endingPage":"4163"},"reviewed":"false","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1033.2002.03112.x"},{"@id":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1033.2002.03112.x"}],"createdAt":"2003-03-11","modifiedAt":"2023-10-16","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360004232188460416","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Determination of the elastic modulus of β-lactoglobulin amyloid fibrils by measuring the Debye-Waller factor"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283691581212032","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Transformation of Coiled α-Helices into <i>Cross</i>-β-Sheets Superstructure"}]},{"@id":"https://cir.nii.ac.jp/crid/1360567180013395840","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Conformation change of hornet silk proteins in the solid phase in response to external stimulation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360845539041350272","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Poly(amino acid)s/polypeptides as potential functional and structural materials"}]},{"@id":"https://cir.nii.ac.jp/crid/1360846644363474816","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"A Structure-Toxicity Study of Aß42 Reveals a New Anti-Parallel Aggregation Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679238091520","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Structural Transition of <i>Bombyx mori</i> Liquid Silk Studied with Vibrational Circular Dichroism Spectroscopy"},{"@value":"Structural Transition of Bombyx mori Liquid Silk Studied with Vibrational Circular Dichroism Spectroscopy"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1046/j.1432-1033.2002.03112.x"},{"@type":"CROSSREF","@value":"10.1021/acs.biomac.7b00920_references_DOI_GL8lP1bcuzRC2C3rR3tqVzr32CM"},{"@type":"CROSSREF","@value":"10.1002/chir.22824_references_DOI_GL8lP1bcuzRC2C3rR3tqVzr32CM"},{"@type":"CROSSREF","@value":"10.2116/analsci.31.763_references_DOI_GL8lP1bcuzRC2C3rR3tqVzr32CM"},{"@type":"CROSSREF","@value":"10.1038/pj.2015.35_references_DOI_GL8lP1bcuzRC2C3rR3tqVzr32CM"},{"@type":"CROSSREF","@value":"10.1371/journal.pone.0080262_references_DOI_GL8lP1bcuzRC2C3rR3tqVzr32CM"},{"@type":"CROSSREF","@value":"10.1016/j.ijbiomac.2016.07.011_references_DOI_GL8lP1bcuzRC2C3rR3tqVzr32CM"}]}