{"@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/1363388844753076480.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1038/sj.cdd.4401373"}},{"identifier":{"@type":"URI","@value":"http://www.nature.com/articles/4401373.pdf"}},{"identifier":{"@type":"URI","@value":"http://www.nature.com/articles/4401373"}},{"identifier":{"@type":"PMID","@value":"14685163"}},{"identifier":{"@type":"NAID","@value":"30014053448"}}],"dc:title":[{"@value":"Roles of CHOP/GADD153 in endoplasmic reticulum stress"}],"description":[{"notation":[{"@value":"Endoplasmic reticulum (ER) is the site of synthesis and folding of secretory proteins. Perturbations of ER homeostasis affect protein folding and cause ER stress. ER can sense the stress and respond to it through translational attenuation, upregulation of the genes for ER chaperones and related proteins, and degradation of unfolded proteins by a quality-control system. However, when the ER function is severely impaired, the organelle elicits apoptotic signals. ER stress has been implicated in a variety of common diseases such as diabetes, ischemia and neurodegenerative disorders. One of the components of the ER stress-mediated apoptosis pathway is C/EBP homologous protein (CHOP), also known as growth arrest- and DNA damage-inducible gene 153 (GADD153). Here, we summarize the current understanding of the roles of CHOP/GADD153 in ER stress-mediated apoptosis and in diseases including diabetes, brain ischemia and neurodegenerative disease."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1582824500903195136","@type":"Researcher","foaf:name":[{"@value":"S Oyadomari"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388844753076480","@type":"Researcher","foaf:name":[{"@value":"M Mori"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"13509047"},{"@type":"EISSN","@value":"14765403"},{"@type":"PISSN","@value":"https://id.crossref.org/issn/13509047"}],"prism:publicationName":[{"@value":"Cell Death & Differentiation"}],"dc:publisher":[{"@value":"Springer Science and Business Media LLC"}],"prism:publicationDate":"2003-12-19","prism:volume":"11","prism:number":"4","prism:startingPage":"381","prism:endingPage":"389"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["http://www.springer.com/tdm"],"url":[{"@id":"http://www.nature.com/articles/4401373.pdf"},{"@id":"http://www.nature.com/articles/4401373"}],"createdAt":"2003-12-19","modifiedAt":"2024-01-11","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Apoptosis","dc:title":"Apoptosis"},{"@id":"https://cir.nii.ac.jp/all?q=Cell%20Differentiation","dc:title":"Cell Differentiation"},{"@id":"https://cir.nii.ac.jp/all?q=Endoplasmic%20Reticulum","dc:title":"Endoplasmic Reticulum"},{"@id":"https://cir.nii.ac.jp/all?q=Mice","dc:title":"Mice"},{"@id":"https://cir.nii.ac.jp/all?q=Stress,%20Physiological","dc:title":"Stress, Physiological"},{"@id":"https://cir.nii.ac.jp/all?q=CCAAT-Enhancer-Binding%20Proteins","dc:title":"CCAAT-Enhancer-Binding Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Humans","dc:title":"Humans"},{"@id":"https://cir.nii.ac.jp/all?q=Disease","dc:title":"Disease"},{"@id":"https://cir.nii.ac.jp/all?q=Cell%20Division","dc:title":"Cell Division"},{"@id":"https://cir.nii.ac.jp/all?q=Transcription%20Factor%20CHOP","dc:title":"Transcription Factor CHOP"},{"@id":"https://cir.nii.ac.jp/all?q=Transcription%20Factors","dc:title":"Transcription Factors"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050003824925902208","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Rescue from Stx2-Producing E.coli-Associated Encephalopathy by Intravenous Injection of Muse Cells in NOD-SCID Mice"}]},{"@id":"https://cir.nii.ac.jp/crid/1050005822275014144","@type":"Article","resourceType":"学術雑誌論文(journal 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KDM6 inhibitor potently induces ATF4 and its target gene expression through HRI activation and by UTX inhibition"}]},{"@id":"https://cir.nii.ac.jp/crid/1050307501845302656","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Selenoprotein P-neutralizing antibodies improve insulin secretion and glucose sensitivity in type 2 diabetes mouse models"}]},{"@id":"https://cir.nii.ac.jp/crid/1050568772216313472","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"CHOP deletion does not impact the development of diabetes but suppresses the early production of insulin autoantibody in the NOD mouse."}]},{"@id":"https://cir.nii.ac.jp/crid/1360002214577278592","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"An ATF4‐Signal‐Modulating Machine Other Than GADD34 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