{"@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/1361699996345838080.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1126/science.1191714"}},{"identifier":{"@type":"URI","@value":"https://www.science.org/doi/pdf/10.1126/science.1191714"}}],"dc:title":[{"@value":"Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>M2 Out of the Envelope</jats:title>\n          <jats:p>\n            The M2 protein from influenza A virus forms an acid-activated tetrameric proton channel in the viral envelope and is essential for viral replication. Two manuscripts shed light on the functional mechanism of this channel.\n            <jats:bold>\n              Sharma\n              <jats:italic>et al.</jats:italic>\n            </jats:bold>\n            (p.\n            <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"509\" related-article-type=\"in-this-issue\" vol=\"330\" xlink:href=\"10.1126/science.1191750\">509</jats:related-article>\n            ; see the Perspective by\n            <jats:bold>\n              <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" issue=\"6003\" page=\"456\" related-article-type=\"in-this-issue\" vol=\"330\" xlink:href=\"10.1126/science.1197748\">\n                Fiorin\n                <jats:italic>et al.</jats:italic>\n              </jats:related-article>\n            </jats:bold>\n            ) determined the structure of the conductance domain in a lipid bilayer and propose that a histidine and tryptophan from each monomer form a cluster that guides protons through the channel in a mechanism that involves forming and breaking hydrogen bonds between adjacent pairs of histidines.\n            <jats:bold>\n              Hu\n              <jats:italic>et al.</jats:italic>\n            </jats:bold>\n            (p.\n            <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" page=\"505\" related-article-type=\"in-this-issue\" vol=\"330\" xlink:href=\"10.1126/science.1191714\">505</jats:related-article>\n            ; see the Perspective by\n            <jats:bold>\n              <jats:related-article xmlns:xlink=\"http://www.w3.org/1999/xlink\" ext-link-type=\"doi\" issue=\"6003\" page=\"456\" related-article-type=\"in-this-issue\" vol=\"330\" xlink:href=\"10.1126/science.1197748\">\n                Fiorin\n                <jats:italic>et al.</jats:italic>\n              </jats:related-article>\n            </jats:bold>\n            ) focused on the structure and dynamics of the proton-selective histidine at high and low pH, proposing that proton conduction involves histidine deprotonation and reprotonation.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381699996345838082","@type":"Researcher","foaf:name":[{"@value":"Fanghao Hu"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry, Iowa State University, Ames, IA 50011, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699996345838080","@type":"Researcher","foaf:name":[{"@value":"Wenbin Luo"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry, Iowa State University, Ames, IA 50011, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1381699996345838081","@type":"Researcher","foaf:name":[{"@value":"Mei Hong"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry, Iowa State University, Ames, IA 50011, USA."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00368075"},{"@type":"EISSN","@value":"10959203"}],"prism:publicationName":[{"@value":"Science"}],"dc:publisher":[{"@value":"American Association for the Advancement of Science (AAAS)"}],"prism:publicationDate":"2010-10-22","prism:volume":"330","prism:number":"6003","prism:startingPage":"505","prism:endingPage":"508"},"reviewed":"false","url":[{"@id":"https://www.science.org/doi/pdf/10.1126/science.1191714"}],"createdAt":"2010-10-21","modifiedAt":"2024-01-10","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002214425561984","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Thermally Induced Intra‐Carboxyl Proton Shuttle in a Molecular Rack‐and‐Pinion Cascade Achieving Macroscopic Crystal Deformation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004235446645760","@type":"Article","resourceType":"学術雑誌論文(journal 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Formation at High Temperature in a Pt(II)-Based Metallo-Supramolecular Polymer and Imidazole System"}]},{"@id":"https://cir.nii.ac.jp/crid/1360579820397808640","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Proton Conduction at High Temperature in High‐Symmetry Hydrogen‐Bonded Molecular Crystals of Ru<sup>III</sup> Complexes with Six Imidazole‐Imidazolate Ligands"}]},{"@id":"https://cir.nii.ac.jp/crid/1360588380133084288","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Raman signatures of type A and B influenza viruses: molecular origin of the “\n                    <i>catch and kill</i>\n                    ” inactivation mechanism mediated by micrometric silicon nitride powder"}]},{"@id":"https://cir.nii.ac.jp/crid/1360853567829436288","@type":"Article","resourceType":"学術雑誌論文(journal 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