CORD-19:120bd6eed7e254029455aec25478a4860a46764e / 87851-88192 JSONTXT

{"project":"CORD-19-SciBite-sentences","denotations":[{"id":"T1428","span":{"begin":0,"end":341},"obj":"http://www.genenames.org/cgi-bin/gene_symbol_report?match=TRADD"},{"id":"T1443","span":{"begin":0,"end":341},"obj":"http://www.genenames.org/cgi-bin/gene_symbol_report?match=RIPK1"},{"id":"T1445","span":{"begin":0,"end":341},"obj":"http://www.genenames.org/cgi-bin/gene_symbol_report?match=FADD"},{"id":"T1458","span":{"begin":0,"end":341},"obj":"http://purl.obolibrary.org/obo/GO0097153"},{"id":"T1473","span":{"begin":0,"end":341},"obj":"http://purl.obolibrary.org/obo/GO0097190"},{"id":"T1486","span":{"begin":0,"end":341},"obj":"http://purl.obolibrary.org/obo/GO0030693"},{"id":"T1507","span":{"begin":0,"end":341},"obj":"http://purl.obolibrary.org/obo/GO0097300"},{"id":"T1525","span":{"begin":0,"end":341},"obj":"http://purl.obolibrary.org/obo/GO0004197"},{"id":"T1562","span":{"begin":0,"end":341},"obj":"https://id.nlm.nih.gov/mesh/D009336"}],"attributes":[{"id":"A1428","pred":"class","subj":"T1428","obj":"GENE"},{"id":"A1445","pred":"class","subj":"T1445","obj":"GENE"},{"id":"A1443","pred":"class","subj":"T1443","obj":"GENE"},{"id":"A1473","pred":"class","subj":"T1473","obj":"GOONTOL"},{"id":"A1507","pred":"class","subj":"T1507","obj":"GOONTOL"},{"id":"A1486","pred":"class","subj":"T1486","obj":"GOONTOL"},{"id":"A1458","pred":"class","subj":"T1458","obj":"GOONTOL"},{"id":"A1525","pred":"class","subj":"T1525","obj":"GOONTOL"},{"id":"A1562","pred":"class","subj":"T1562","obj":"INDICATION"}],"text":"Remember that RIPK1, depending on its ubiquitination status, can associate with the trimerized DR and direct the cell toward regulated necrosis (if caspases are inhibited) or toward survival via activation of NFκB, and has an N-terminal death domain (DD) that links it to the apoptotic pathway through adaptor proteins such as TRADD or FADD."}

{"project":"CORD-19_Custom_license_subset","denotations":[{"id":"T247","span":{"begin":0,"end":341},"obj":"Sentence"}],"text":"Remember that RIPK1, depending on its ubiquitination status, can associate with the trimerized DR and direct the cell toward regulated necrosis (if caspases are inhibited) or toward survival via activation of NFκB, and has an N-terminal death domain (DD) that links it to the apoptotic pathway through adaptor proteins such as TRADD or FADD."}

{"project":"CORD-19-Sentences","denotations":[{"id":"TextSentencer_T556","span":{"begin":0,"end":341},"obj":"Sentence"},{"id":"TextSentencer_T556","span":{"begin":0,"end":341},"obj":"Sentence"},{"id":"T52944","span":{"begin":0,"end":341},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Remember that RIPK1, depending on its ubiquitination status, can associate with the trimerized DR and direct the cell toward regulated necrosis (if caspases are inhibited) or toward survival via activation of NFκB, and has an N-terminal death domain (DD) that links it to the apoptotic pathway through adaptor proteins such as TRADD or FADD."}

{"project":"CORD-19-PD-MONDO","denotations":[{"id":"T248","span":{"begin":251,"end":253},"obj":"Disease"}],"attributes":[{"id":"A248","pred":"mondo_id","subj":"T248","obj":"http://purl.obolibrary.org/obo/MONDO_0009107"},{"id":"A249","pred":"mondo_id","subj":"T248","obj":"http://purl.obolibrary.org/obo/MONDO_0015613"}],"text":"Remember that RIPK1, depending on its ubiquitination status, can associate with the trimerized DR and direct the cell toward regulated necrosis (if caspases are inhibited) or toward survival via activation of NFκB, and has an N-terminal death domain (DD) that links it to the apoptotic pathway through adaptor proteins such as TRADD or FADD."}