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contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"bionlp-st-ge-2016-coref","denotations":[{"id":"T1029","span":{"begin":216,"end":220},"obj":"Antecedent"},{"id":"T1028","span":{"begin":272,"end":277},"obj":"Anaphor"}],"relations":[{"id":"R593","pred":"boundBy","subj":"T1028","obj":"T1029"}],"namespaces":[{"prefix":"_base","uri":"https://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"bionlp-st-ge-2016-test-proteins","denotations":[{"id":"T1079","span":{"begin":1481,"end":1486},"obj":"Protein"},{"id":"T1078","span":{"begin":1465,"end":1471},"obj":"Protein"},{"id":"T1077","span":{"begin":1454,"end":1458},"obj":"Protein"},{"id":"T1076","span":{"begin":1412,"end":1416},"obj":"Protein"},{"id":"T1075","span":{"begin":1403,"end":1407},"obj":"Protein"},{"id":"T1074","span":{"begin":1241,"end":1246},"obj":"Protein"},{"id":"T1073","span":{"begin":1232,"end":1236},"obj":"Protein"},{"id":"T1072","span":{"begin":1201,"end":1208},"obj":"Protein"},{"id":"T1071","span":{"begin":1187,"end":1191},"obj":"Protein"},{"id":"T1070","span":{"begin":1021,"end":1024},"obj":"Protein"},{"id":"T1069","span":{"begin":949,"end":953},"obj":"Protein"},{"id":"T1068","span":{"begin":938,"end":942},"obj":"Protein"},{"id":"T1067","span":{"begin":859,"end":864},"obj":"Protein"},{"id":"T1066","span":{"begin":838,"end":842},"obj":"Protein"},{"id":"T1065","span":{"begin":796,"end":801},"obj":"Protein"},{"id":"T1064","span":{"begin":775,"end":780},"obj":"Protein"},{"id":"T1063","span":{"begin":699,"end":704},"obj":"Protein"},{"id":"T1062","span":{"begin":644,"end":650},"obj":"Protein"},{"id":"T1061","span":{"begin":628,"end":634},"obj":"Protein"},{"id":"T1060","span":{"begin":541,"end":546},"obj":"Protein"},{"id":"T1059","span":{"begin":430,"end":434},"obj":"Protein"},{"id":"T1058","span":{"begin":247,"end":253},"obj":"Protein"},{"id":"T1057","span":{"begin":241,"end":245},"obj":"Protein"},{"id":"T1056","span":{"begin":234,"end":239},"obj":"Protein"},{"id":"T1055","span":{"begin":216,"end":220},"obj":"Protein"},{"id":"T1054","span":{"begin":172,"end":177},"obj":"Protein"},{"id":"T1053","span":{"begin":0,"end":5},"obj":"Protein"}],"namespaces":[{"prefix":"_base","uri":"http://bionlp.dbcls.jp/ontology/ge.owl#"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"bionlp-st-ge-2016-uniprot","denotations":[{"id":"T3667","span":{"begin":1481,"end":1486},"obj":"http://www.uniprot.org/uniprot/Q9BYM8"},{"id":"T3666","span":{"begin":1241,"end":1246},"obj":"http://www.uniprot.org/uniprot/Q13114"},{"id":"T3665","span":{"begin":796,"end":801},"obj":"http://www.uniprot.org/uniprot/Q13114"},{"id":"T3664","span":{"begin":775,"end":780},"obj":"http://www.uniprot.org/uniprot/Q9Y4K3"},{"id":"T3659","span":{"begin":1412,"end":1416},"obj":"http://www.uniprot.org/uniprot/Q92985"},{"id":"T3656","span":{"begin":1403,"end":1407},"obj":"http://www.uniprot.org/uniprot/Q14653"},{"id":"T3655","span":{"begin":838,"end":842},"obj":"http://www.uniprot.org/uniprot/Q14653"}],"namespaces":[{"prefix":"_base","uri":"http://www.uniprot.org/uniprot/"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"GO-BP","denotations":[{"id":"T1129","span":{"begin":1271,"end":1282},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T1128","span":{"begin":1375,"end":1388},"obj":"http://purl.obolibrary.org/obo/GO_0000209"},{"id":"T1127","span":{"begin":1071,"end":1084},"obj":"http://purl.obolibrary.org/obo/GO_0000209"},{"id":"T1126","span":{"begin":897,"end":921},"obj":"http://purl.obolibrary.org/obo/GO_0004843"},{"id":"T1125","span":{"begin":1525,"end":1537},"obj":"http://purl.obolibrary.org/obo/GO_0009293"},{"id":"T1124","span":{"begin":563,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0009293"},{"id":"T1123","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0090520"},{"id":"T1122","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0038008"},{"id":"T1121","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0007266"},{"id":"T1120","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0048015"},{"id":"T1119","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0019933"},{"id":"T1118","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0007265"},{"id":"T1117","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0007263"},{"id":"T1116","span":{"begin":547,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0016601"},{"id":"T1102","span":{"begin":1417,"end":1430},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T1099","span":{"begin":1518,"end":1537},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T1098","span":{"begin":556,"end":575},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T1093","span":{"begin":1319,"end":1328},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T1092","span":{"begin":1105,"end":1114},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T1091","span":{"begin":1025,"end":1034},"obj":"http://purl.obolibrary.org/obo/GO_0023052"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"GO-MF","denotations":[{"id":"T1181","span":{"begin":897,"end":921},"obj":"http://purl.obolibrary.org/obo/GO_0004843"},{"id":"T1178","span":{"begin":1160,"end":1169},"obj":"http://purl.obolibrary.org/obo/GO_0031386"},{"id":"T1177","span":{"begin":749,"end":758},"obj":"http://purl.obolibrary.org/obo/GO_0031386"},{"id":"T1176","span":{"begin":595,"end":604},"obj":"http://purl.obolibrary.org/obo/GO_0031386"},{"id":"T1175","span":{"begin":466,"end":475},"obj":"http://purl.obolibrary.org/obo/GO_0031386"},{"id":"T1174","span":{"begin":143,"end":150},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T1173","span":{"begin":136,"end":142},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T1172","span":{"begin":78,"end":84},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"GO-CC","denotations":[{"id":"T1226","span":{"begin":1251,"end":1261},"obj":"http://purl.obolibrary.org/obo/GO_0000502"},{"id":"T1225","span":{"begin":374,"end":387},"obj":"http://purl.obolibrary.org/obo/GO_0044214"},{"id":"T1224","span":{"begin":374,"end":387},"obj":"http://purl.obolibrary.org/obo/GO_0016021"},{"id":"T1223","span":{"begin":346,"end":354},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T1222","span":{"begin":332,"end":354},"obj":"http://purl.obolibrary.org/obo/GO_0031966"},{"id":"T1221","span":{"begin":326,"end":354},"obj":"http://purl.obolibrary.org/obo/GO_0031315"},{"id":"T1220","span":{"begin":326,"end":354},"obj":"http://purl.obolibrary.org/obo/GO_0031307"},{"id":"T1219","span":{"begin":326,"end":354},"obj":"http://purl.obolibrary.org/obo/GO_0031306"},{"id":"T1218","span":{"begin":326,"end":354},"obj":"http://purl.obolibrary.org/obo/GO_0005741"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"sentences","denotations":[{"id":"T933","span":{"begin":1330,"end":1538},"obj":"Sentence"},{"id":"T932","span":{"begin":1126,"end":1329},"obj":"Sentence"},{"id":"T931","span":{"begin":878,"end":1125},"obj":"Sentence"},{"id":"T930","span":{"begin":717,"end":877},"obj":"Sentence"},{"id":"T929","span":{"begin":582,"end":716},"obj":"Sentence"},{"id":"T928","span":{"begin":406,"end":581},"obj":"Sentence"},{"id":"T927","span":{"begin":131,"end":405},"obj":"Sentence"},{"id":"T926","span":{"begin":0,"end":130},"obj":"Sentence"},{"id":"T37","span":{"begin":0,"end":130},"obj":"Sentence"},{"id":"T38","span":{"begin":131,"end":405},"obj":"Sentence"},{"id":"T39","span":{"begin":406,"end":581},"obj":"Sentence"},{"id":"T40","span":{"begin":582,"end":716},"obj":"Sentence"},{"id":"T41","span":{"begin":717,"end":877},"obj":"Sentence"},{"id":"T42","span":{"begin":878,"end":1125},"obj":"Sentence"},{"id":"T43","span":{"begin":1126,"end":1329},"obj":"Sentence"},{"id":"T44","span":{"begin":1330,"end":1538},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"simple1","denotations":[{"id":"T1332","span":{"begin":1481,"end":1486},"obj":"Protein"},{"id":"T1331","span":{"begin":1465,"end":1471},"obj":"Protein"},{"id":"T1330","span":{"begin":1454,"end":1458},"obj":"Protein"},{"id":"T1329","span":{"begin":1412,"end":1416},"obj":"Protein"},{"id":"T1328","span":{"begin":1403,"end":1407},"obj":"Protein"},{"id":"T1327","span":{"begin":1241,"end":1246},"obj":"Protein"},{"id":"T1326","span":{"begin":1232,"end":1236},"obj":"Protein"},{"id":"T1325","span":{"begin":1201,"end":1208},"obj":"Protein"},{"id":"T1324","span":{"begin":1187,"end":1191},"obj":"Protein"},{"id":"T1323","span":{"begin":1021,"end":1024},"obj":"Protein"},{"id":"T1322","span":{"begin":949,"end":953},"obj":"Protein"},{"id":"T1321","span":{"begin":938,"end":942},"obj":"Protein"},{"id":"T1320","span":{"begin":859,"end":864},"obj":"Protein"},{"id":"T1319","span":{"begin":838,"end":842},"obj":"Protein"},{"id":"T1318","span":{"begin":796,"end":801},"obj":"Protein"},{"id":"T1317","span":{"begin":775,"end":780},"obj":"Protein"},{"id":"T1316","span":{"begin":699,"end":704},"obj":"Protein"},{"id":"T1315","span":{"begin":644,"end":650},"obj":"Protein"},{"id":"T1314","span":{"begin":628,"end":634},"obj":"Protein"},{"id":"T1313","span":{"begin":541,"end":546},"obj":"Protein"},{"id":"T1312","span":{"begin":430,"end":434},"obj":"Protein"},{"id":"T1311","span":{"begin":247,"end":253},"obj":"Protein"},{"id":"T1310","span":{"begin":241,"end":245},"obj":"Protein"},{"id":"T1309","span":{"begin":234,"end":239},"obj":"Protein"},{"id":"T1308","span":{"begin":216,"end":220},"obj":"Protein"},{"id":"T1307","span":{"begin":172,"end":177},"obj":"Protein"},{"id":"T1306","span":{"begin":0,"end":5},"obj":"Protein"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

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contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"bionlp-st-ge-2016-test-tees","denotations":[{"id":"T3968","span":{"begin":1481,"end":1486},"obj":"Protein"},{"id":"T3967","span":{"begin":1412,"end":1438},"obj":"Protein"},{"id":"T3966","span":{"begin":1403,"end":1407},"obj":"Protein"},{"id":"T3965","span":{"begin":1362,"end":1395},"obj":"Protein"},{"id":"T3964","span":{"begin":1271,"end":1282},"obj":"Protein_catabolism"},{"id":"T3963","span":{"begin":1271,"end":1282},"obj":"Protein_catabolism"},{"id":"T3962","span":{"begin":1241,"end":1246},"obj":"Protein"},{"id":"T3961","span":{"begin":1147,"end":1177},"obj":"Protein"},{"id":"T3960","span":{"begin":1071,"end":1084},"obj":"Protein"},{"id":"T3959","span":{"begin":807,"end":814},"obj":"Positive_regulation"},{"id":"T3958","span":{"begin":807,"end":814},"obj":"Positive_regulation"},{"id":"T3957","span":{"begin":843,"end":853},"obj":"Positive_regulation"},{"id":"T3956","span":{"begin":843,"end":853},"obj":"Positive_regulation"},{"id":"T3946","span":{"begin":582,"end":612},"obj":"Protein"},{"id":"T3945","span":{"begin":541,"end":546},"obj":"Protein"},{"id":"T3944","span":{"begin":466,"end":475},"obj":"Protein"},{"id":"T3943","span":{"begin":430,"end":434},"obj":"Protein"},{"id":"T3942","span":{"begin":178,"end":187},"obj":"Binding"},{"id":"T3941","span":{"begin":143,"end":150},"obj":"Binding"},{"id":"T3940","span":{"begin":143,"end":150},"obj":"Binding"},{"id":"T3939","span":{"begin":143,"end":150},"obj":"Binding"},{"id":"T3938","span":{"begin":197,"end":208},"obj":"Protein"},{"id":"T3937","span":{"begin":172,"end":177},"obj":"Protein"},{"id":"T3936","span":{"begin":156,"end":168},"obj":"Protein"},{"id":"T3935","span":{"begin":28,"end":47},"obj":"Protein"},{"id":"T3955","span":{"begin":859,"end":864},"obj":"Protein"},{"id":"T3954","span":{"begin":838,"end":842},"obj":"Protein"},{"id":"T3953","span":{"begin":828,"end":833},"obj":"Protein"},{"id":"T3952","span":{"begin":749,"end":766},"obj":"Protein"},{"id":"T3951","span":{"begin":705,"end":715},"obj":"Positive_regulation"},{"id":"T3950","span":{"begin":691,"end":698},"obj":"Gene_expression"},{"id":"T3949","span":{"begin":691,"end":698},"obj":"Gene_expression"},{"id":"T3948","span":{"begin":699,"end":704},"obj":"Protein"},{"id":"T3947","span":{"begin":614,"end":617},"obj":"Protein"}],"relations":[{"id":"R3013","pred":"themeOf","subj":"T3936","obj":"T3939"},{"id":"R3014","pred":"themeOf","subj":"T3936","obj":"T3941"},{"id":"R3015","pred":"themeOf","subj":"T3937","obj":"T3940"},{"id":"R3016","pred":"themeOf","subj":"T3937","obj":"T3941"},{"id":"R3017","pred":"themeOf","subj":"T3937","obj":"T3942"},{"id":"R3018","pred":"themeOf","subj":"T3938","obj":"T3942"},{"id":"R3022","pred":"themeOf","subj":"T3946","obj":"T3949"},{"id":"R3023","pred":"themeOf","subj":"T3947","obj":"T3950"},{"id":"R3025","pred":"themeOf","subj":"T3948","obj":"T3951"},{"id":"R3028","pred":"themeOf","subj":"T3953","obj":"T3956"},{"id":"R3029","pred":"themeOf","subj":"T3954","obj":"T3957"},{"id":"R3030","pred":"themeOf","subj":"T3956","obj":"T3958"},{"id":"R3031","pred":"themeOf","subj":"T3957","obj":"T3959"},{"id":"R3032","pred":"Cause","subj":"T3958","obj":"T3952"},{"id":"R3033","pred":"Cause","subj":"T3959","obj":"T3952"},{"id":"R3034","pred":"themeOf","subj":"T3961","obj":"T3963"},{"id":"R3035","pred":"themeOf","subj":"T3962","obj":"T3964"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}

{"project":"testone","denotations":[{"id":"T782","span":{"begin":1271,"end":1282},"obj":"Protein_catabolism"},{"id":"T781","span":{"begin":843,"end":853},"obj":"Positive_regulation"},{"id":"T780","span":{"begin":388,"end":394},"obj":"Entity"},{"id":"T779","span":{"begin":291,"end":303},"obj":"Localization"},{"id":"T778","span":{"begin":202,"end":208},"obj":"Entity"},{"id":"T777","span":{"begin":178,"end":187},"obj":"Binding"},{"id":"T776","span":{"begin":161,"end":168},"obj":"Entity"},{"id":"T775","span":{"begin":143,"end":150},"obj":"Binding"},{"id":"T765","span":{"begin":1481,"end":1486},"obj":"Protein"},{"id":"T764","span":{"begin":1465,"end":1471},"obj":"Protein"},{"id":"T763","span":{"begin":1454,"end":1458},"obj":"Protein"},{"id":"T762","span":{"begin":1412,"end":1416},"obj":"Protein"},{"id":"T761","span":{"begin":1403,"end":1407},"obj":"Protein"},{"id":"T760","span":{"begin":1241,"end":1246},"obj":"Protein"},{"id":"T759","span":{"begin":1232,"end":1236},"obj":"Protein"},{"id":"T758","span":{"begin":1201,"end":1208},"obj":"Protein"},{"id":"T757","span":{"begin":1187,"end":1191},"obj":"Protein"},{"id":"T756","span":{"begin":1021,"end":1024},"obj":"Protein"},{"id":"T755","span":{"begin":949,"end":953},"obj":"Protein"},{"id":"T754","span":{"begin":938,"end":942},"obj":"Protein"},{"id":"T753","span":{"begin":859,"end":864},"obj":"Protein"},{"id":"T752","span":{"begin":838,"end":842},"obj":"Protein"},{"id":"T751","span":{"begin":796,"end":801},"obj":"Protein"},{"id":"T750","span":{"begin":775,"end":780},"obj":"Protein"},{"id":"T749","span":{"begin":699,"end":704},"obj":"Protein"},{"id":"T748","span":{"begin":644,"end":650},"obj":"Protein"},{"id":"T747","span":{"begin":628,"end":634},"obj":"Protein"},{"id":"T746","span":{"begin":541,"end":546},"obj":"Protein"},{"id":"T745","span":{"begin":430,"end":434},"obj":"Protein"},{"id":"T744","span":{"begin":247,"end":253},"obj":"Protein"},{"id":"T743","span":{"begin":241,"end":245},"obj":"Protein"},{"id":"T742","span":{"begin":234,"end":239},"obj":"Protein"},{"id":"T741","span":{"begin":216,"end":220},"obj":"Protein"},{"id":"T740","span":{"begin":172,"end":177},"obj":"Protein"},{"id":"T739","span":{"begin":0,"end":5},"obj":"Protein"}],"relations":[{"id":"R526","pred":"themeOf","subj":"T752","obj":"T781"},{"id":"R523","pred":"themeOf","subj":"T742","obj":"T779"},{"id":"R524","pred":"themeOf","subj":"T743","obj":"T779"},{"id":"R525","pred":"themeOf","subj":"T744","obj":"T779"},{"id":"R527","pred":"causeOf","subj":"T753","obj":"T781"},{"id":"R528","pred":"themeOf","subj":"T757","obj":"T782"},{"id":"R529","pred":"themeOf","subj":"T758","obj":"T782"},{"id":"R530","pred":"themeOf","subj":"T759","obj":"T782"}],"text":"RIG-I contains a C-terminal DExD/H box helicase domain, which is required for ligand recognition, and two N-terminal CARD domains. Upon ligand binding, the CARD domains of RIG-I associate with the CARD domain of the MAVS (also termed IPS-1, VISA, Cardif) adaptor protein, which subsequently translocates to and inserts in the outer mitochondrial membrane via its C-terminal transmembrane domain [17]–[20]. Signaling downstream of MAVS requires the action of various ubiquitin modifying enzymes, which both positively and negatively regulate RIG-I mediated signal transduction [21]. K63-specific ubiquitin ligases (E3s), such as TRIM25 [22] and Riplet [23], [24], have been shown to directly promote RIG-I activation. In addition, well characterized ubiquitin ligases such as TRAF6 [25], [26] and TRAF3 [27] mediate respectively NF-κB and IRF3 activation upon RIG-I stimulation. On the other hand, deubiquitinating enzymes (DUBs), such as DUBA [28], CYLD [29], [30] and OTUB1/2 [31] have been shown to negatively regulate RLR signaling by specifically removing K63-linked polyubiquitin chains from several signaling molecules. Furthermore, various K48-specific ubiquitin ligases, such as AIP4 [32] and TRIAD3A [33] mark respectively MAVS and TRAF3 for proteasome mediated degradation, thus inhibiting further downstream signaling. Additionally, the attachment of K48-specific polyubiquitin chains to the IRF3 and IRF7 transcription factors by E3s such as RAUL [34], TRIM21 [35] and RBCK1 [36] further dampens antiviral signal transduction."}