{"@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/1361137043667440640.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1016/j.febslet.2005.12.030"}},{"identifier":{"@type":"URI","@value":"http://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2005.12.030"}},{"identifier":{"@type":"URI","@value":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2005.12.030"}}],"dc:title":[{"@value":"Phosphorylation and concomitant structural changes in human 2‐Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>The H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub>‐catabolizing peroxidase activity of human peroxiredoxin I (hPrxI) was previously shown to be regulated by phosphorylation of Thr<jats:sup>90</jats:sup>. Here, we show that hPrxI forms multiple oligomers with distinct secondary structures. HPrxI is a dual function protein, since it can behave either as a peroxidase or as a molecular chaperone. The effects of phosphorylation of hPrxI on its protein structure and dual functions were determined using site‐directed mutagenesis, in which the phosphorylation site was substituted with aspartate to mimic the phosphorylated status of the protein (T90D‐hPrxI). Phosphorylation of the protein induces significant changes in its protein structure from low molecular weight (MW) protein species to high MW protein complexes as well as its dual functions. In contrast to the wild type (WT)‐ and T90A‐hPrxI, the T90D‐hPrxI exhibited a markedly reduced peroxidase activity, but showed about sixfold higher chaperone activity than WT‐hPrxI.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381137043667440651","@type":"Researcher","foaf:name":[{"@value":"Ho Hee Jang"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440652","@type":"Researcher","foaf:name":[{"@value":"Sun Young Kim"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440653","@type":"Researcher","foaf:name":[{"@value":"Soo Kwon Park"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440649","@type":"Researcher","foaf:name":[{"@value":"Hye Sook Jeon"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440648","@type":"Researcher","foaf:name":[{"@value":"Young Mee Lee"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440646","@type":"Researcher","foaf:name":[{"@value":"Ji Hyun Jung"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440642","@type":"Researcher","foaf:name":[{"@value":"Sun Yong Lee"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440641","@type":"Researcher","foaf:name":[{"@value":"Ho Byoung Chae"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440647","@type":"Researcher","foaf:name":[{"@value":"Young Jun Jung"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440654","@type":"Researcher","foaf:name":[{"@value":"Kyun Oh Lee"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440640","@type":"Researcher","foaf:name":[{"@value":"Chae Oh Lim"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440643","@type":"Researcher","foaf:name":[{"@value":"Woo Sik Chung"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440645","@type":"Researcher","foaf:name":[{"@value":"Jeong Dong Bahk"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440655","@type":"Researcher","foaf:name":[{"@value":"Dae-Jin Yun"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440650","@type":"Researcher","foaf:name":[{"@value":"Moo Je Cho"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137043667440644","@type":"Researcher","foaf:name":[{"@value":"Sang Yeol Lee"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00145793"},{"@type":"EISSN","@value":"18733468"}],"prism:publicationName":[{"@value":"FEBS Letters"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"2005-12-19","prism:volume":"580","prism:number":"1","prism:startingPage":"351","prism:endingPage":"355"},"reviewed":"false","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"http://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2005.12.030"},{"@id":"https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2005.12.030"}],"createdAt":"2005-12-23","modifiedAt":"2023-10-12","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002216022916736","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Negatively Charged Lipids Are Essential for Functional and Structural Switch of Human 2-Cys Peroxiredoxin II"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282680192027392","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Improvement of Chaperone Activity of 2-Cys Peroxiredoxin Using Gamma Ray"}]},{"@id":"https://cir.nii.ac.jp/crid/2051433317034866432","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"PRDX1 is essential for the viability and maintenance of reactive oxygen species in chicken DT40"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1016/j.febslet.2005.12.030"},{"@type":"CROSSREF","@value":"10.1269/jrr.11046_references_DOI_GvxNIrDsitNXN0lb8KsrHBFHBDT"},{"@type":"CROSSREF","@value":"10.1186/s41021-021-00211-4_references_DOI_GvxNIrDsitNXN0lb8KsrHBFHBDT"},{"@type":"CROSSREF","@value":"10.1016/j.jmb.2017.12.020_references_DOI_GvxNIrDsitNXN0lb8KsrHBFHBDT"}]}