{"@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/1362825893897362944.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1046/j.1432-1327.1999.00422.x"}},{"identifier":{"@type":"URI","@value":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.1999.00422.x"}},{"identifier":{"@type":"URI","@value":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.1999.00422.x"}},{"identifier":{"@type":"PMID","@value":"10231387"}},{"identifier":{"@type":"NAID","@value":"30014353882"}}],"dc:title":[{"@value":"Structural requirements of <i>para</i>‐alkylphenols to bind to estrogen receptor"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>Octyl‐ and nonylphenols in the environment have been proposed to function as estrogens. To gain insight into their structural essentials in binding to the estrogen receptor, a series of phenols with saturated alkyl groups at the <jats:italic>para</jats:italic> position, HO‐C<jats:sub>6</jats:sub>H<jats:sub>4</jats:sub>‐C<jats:sub>n</jats:sub>H<jats:sub>2n+1</jats:sub> (<jats:italic>n</jats:italic> = 0–12), were examined for their ability to displace [<jats:sup>3</jats:sup>H]17β‐estradiol in the recombinant human estrogen receptor, which was expressed in Sf9 cells using the vaculovirus expression system. All tested <jats:italic>para</jats:italic>‐alkylphenols were found to bind fully to the estrogen receptors in a dose‐dependent manner. The interaction of alkylphenols with the receptor became stronger with increase in the number of the alkyl carbons and the activity was maximized with <jats:italic>n</jats:italic> = 9 of nonylphenol. Phenol (<jats:italic>n</jats:italic> = 0) exhibited weak but full binding to the receptor, whereas anisole with a protected phenolic hydroxyl group was completely inactive. Also, alkanes such as <jats:italic>n</jats:italic>‐octane, 2,2,4‐trimethylpentane corresponding to <jats:italic>tert</jats:italic>‐octane, and <jats:italic>n</jats:italic>‐nonane exhibited no binding. The results indicate that the binding of <jats:italic>para</jats:italic>‐alkylphenols to the estrogen receptor is due to the effect of covalent bonding of two constituents of the phenol and alkyl groups, which correspond to the A‐ring and hydrophobic moiety of the steroid structure, respectively. When alkylphenols were examined for their receptor binding conformation by <jats:sup>1</jats:sup>H‐NMR measurements and <jats:italic>ab initio</jats:italic> molecular orbital calculations, it was suggested that nonbranched alkyl groups are in an extended conformation, while branched alkyl groups are in a folded conformation. These results suggest that branched and nonbranched alkyl moieties of alkylphenols interact differently with the lipophilic ligand binding cavity of the estrogen receptor when compared to the binding of 17β‐estradiol.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1382825893897362947","@type":"Researcher","foaf:name":[{"@value":"Yukiko Tabira"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362951","@type":"Researcher","foaf:name":[{"@value":"Makoto Nakai"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362952","@type":"Researcher","foaf:name":[{"@value":"Daisuke Asai"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362946","@type":"Researcher","foaf:name":[{"@value":"Yoshikuni Yakabe"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362948","@type":"Researcher","foaf:name":[{"@value":"Yoshiko Tahara"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362944","@type":"Researcher","foaf:name":[{"@value":"Teruo Shinmyozu"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362950","@type":"Researcher","foaf:name":[{"@value":"Masato Noguchi"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362945","@type":"Researcher","foaf:name":[{"@value":"Mineo Takatsuki"}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893897362949","@type":"Researcher","foaf:name":[{"@value":"Yasuyuki Shimohigashi"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00142956"},{"@type":"EISSN","@value":"14321033"}],"prism:publicationName":[{"@value":"European Journal of Biochemistry"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"1999-05-15","prism:volume":"262","prism:number":"1","prism:startingPage":"240","prism:endingPage":"245"},"reviewed":"false","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.1999.00422.x"},{"@id":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.1999.00422.x"}],"createdAt":"2003-03-11","modifiedAt":"2023-10-17","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Chromatography,%20Gas","dc:title":"Chromatography, Gas"},{"@id":"https://cir.nii.ac.jp/all?q=Magnetic%20Resonance%20Spectroscopy","dc:title":"Magnetic Resonance Spectroscopy"},{"@id":"https://cir.nii.ac.jp/all?q=Molecular%20Structure","dc:title":"Molecular Structure"},{"@id":"https://cir.nii.ac.jp/all?q=Recombinant%20Proteins","dc:title":"Recombinant Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Structure-Activity%20Relationship","dc:title":"Structure-Activity Relationship"},{"@id":"https://cir.nii.ac.jp/all?q=Phenols","dc:title":"Phenols"},{"@id":"https://cir.nii.ac.jp/all?q=Receptors,%20Estrogen","dc:title":"Receptors, Estrogen"},{"@id":"https://cir.nii.ac.jp/all?q=Humans","dc:title":"Humans"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Binding","dc:title":"Protein Binding"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1390001204496979712","@type":"Article","relationType":["isReferencedBy","isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Several Environmental Pollutants Have Binding Affinities for Both Androgen Receptor and Estrogen Receptor .ALPHA.."},{"@value":"Several Environmental Pollutants Have Binding Affinities for Both Androgen Receptor and Estrogen Receptorα"},{"@language":"ja-Kana","@value":"Several Environmental Pollutants Have Binding Affinities for Both Androgen Receptor and Estrogen Receptor アルファ"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204498188288","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Androgenic and Antiandrogenic Effects of Alkylphenols and Parabens Assessed Using the Reporter Gene Assay with Stably Transfected CHO-K1 Cells (AR-EcoScreen System)"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206472722304","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy","isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Isolation of Bacterial Strains that Produce the Endocrine Disruptor, Octylphenol Diethoxylates, in Paddy Fields."}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679234782848","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Migration Behavior of Alkylphenols, Bisphenol A and Bisphenol S Studied by Capillary Electrophoresis Using Sulfated .BETA.-Cyclodextrin."},{"@value":"Migration Behavior of Alkylphenols, Bisphenol A and Bisphenol S Studied by Capillary Electrophoresis Using Sulfated β-Cyclodextrin"},{"@language":"ja-Kana","@value":"Migration Behavior of Alkylphenols Bisphenol A and Bisphenol S Studied by Capillary Electrophoresis Using Sulfated ベータ Cyclodextrin"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679476168576","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Estrogenic Activity of Branched 4-Nonylphenol Isomers Examined by Yeast Two-Hybrid 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