{"@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/1363670318964805760.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1146/annurev-biophys-070816-033928"}},{"identifier":{"@type":"URI","@value":"https://www.annualreviews.org/doi/pdf/10.1146/annurev-biophys-070816-033928"}}],"dc:title":[{"@value":"Geometric Principles for Designing Highly Symmetric Self-Assembling Protein Nanomaterials"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p> Emerging protein design strategies are enabling the creation of diverse, self-assembling supramolecular structures with precision on the atomic scale. The design possibilities include various types of architectures: finite cages or shells, essentially unbounded two-dimensional and three-dimensional arrays (i.e., crystals), and linear or tubular filaments. In nature, structures of those types are generally symmetric, and, accordingly, symmetry provides a powerful guide for developing new design approaches. Recent design studies have produced numerous protein assemblies in close agreement with geometric specifications. For certain design approaches, a complete list of allowable symmetry combinations that can be used for construction has been articulated, opening a path to a rich diversity of geometrically defined protein materials. Future challenges include improving and elaborating on current strategies and endowing designed protein nanomaterials with properties useful in nanomedicine and material science applications. </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383670318964805760","@type":"Researcher","foaf:name":[{"@value":"Todd O. Yeates"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095"},{"@value":"UCLA-DOE Institute for Genomics and Proteomics, Los Angeles, California 90095;"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"1936122X"},{"@type":"EISSN","@value":"19361238"}],"prism:publicationName":[{"@value":"Annual Review of Biophysics"}],"dc:publisher":[{"@value":"Annual Reviews"}],"prism:publicationDate":"2017-05-22","prism:volume":"46","prism:number":"1","prism:startingPage":"23","prism:endingPage":"42"},"reviewed":"false","url":[{"@id":"https://www.annualreviews.org/doi/pdf/10.1146/annurev-biophys-070816-033928"}],"createdAt":"2017-03-16","modifiedAt":"2021-10-06","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050014359399263872","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Construction of a Triangle‐Shaped Trimer and a Tetrahedron Using an α‐Helix‐Inserted Circular Permutant of Cytochrome c555"},{"@value":"Construction of a Triangle‐Shaped Trimer and a Tetrahedron Using an α‐Helix‐Inserted Circular Permutant of Cytochrome <i>c</i><sub>555</sub>"},{"@value":"Construction of a triangle-shaped trimer and a tetrahedron using an α-helix-lnserted circular permutant of cytochrome c555"},{"@value":"Construction of a triangle-shaped trimer and a tetrahedron using an alpha-helix-inserted circular permutant of cytochrome c555"},{"@value":"Construction of a triangle-shaped trimer and a tetrahedron using an α-helix-inserted circular permutant of cytochrome c555"}]},{"@id":"https://cir.nii.ac.jp/crid/1050577309352683136","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Construction of a Quadrangular Tetramer and a Cage-Like Hexamer from Three-Helix Bundle-Linked Fusion Proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004229926182144","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Design of Hollow Protein Nanoparticles with Modifiable Interior and Exterior Surfaces"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092434100096","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Enzyme-Directed Functionalization of Designed, Two-Dimensional Protein Lattices"}]},{"@id":"https://cir.nii.ac.jp/crid/1360588380613502720","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Construction of ligand-binding controlled hemoprotein assemblies utilizing 3D domain swapping"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1146/annurev-biophys-070816-033928"},{"@type":"CROSSREF","@value":"10.1002/anie.201805565_references_DOI_7pDjWJGKu8TB6SA20THJsDHD58K"},{"@type":"CROSSREF","@value":"10.1002/asia.201800252_references_DOI_7pDjWJGKu8TB6SA20THJsDHD58K"},{"@type":"CROSSREF","@value":"10.1021/acs.biochem.0c00363_references_DOI_7pDjWJGKu8TB6SA20THJsDHD58K"},{"@type":"CROSSREF","@value":"10.1039/d4cc03129f_references_DOI_7pDjWJGKu8TB6SA20THJsDHD58K"},{"@type":"CROSSREF","@value":"10.1021/acssynbio.9b00019_references_DOI_7pDjWJGKu8TB6SA20THJsDHD58K"}]}