PMC:7200337 / 9095-10644 JSONTXT

{"project":"2_test","denotations":[{"id":"32505227-25135833-46575232","span":{"begin":668,"end":672},"obj":"25135833"},{"id":"32505227-19380580-46575233","span":{"begin":930,"end":934},"obj":"19380580"},{"id":"32505227-26631542-46575234","span":{"begin":974,"end":978},"obj":"26631542"},{"id":"32505227-17761676-46575235","span":{"begin":1113,"end":1117},"obj":"17761676"},{"id":"32505227-17108024-46575236","span":{"begin":1144,"end":1148},"obj":"17108024"},{"id":"32505227-19369340-46575237","span":{"begin":1238,"end":1242},"obj":"19369340"},{"id":"32505227-29370303-46575238","span":{"begin":1288,"end":1292},"obj":"29370303"},{"id":"32505227-19838190-46575240","span":{"begin":1383,"end":1387},"obj":"19838190"},{"id":"32505227-26311885-46575241","span":{"begin":1427,"end":1431},"obj":"26311885"},{"id":"T99744","span":{"begin":668,"end":672},"obj":"25135833"},{"id":"T89021","span":{"begin":930,"end":934},"obj":"19380580"},{"id":"T58194","span":{"begin":974,"end":978},"obj":"26631542"},{"id":"T64611","span":{"begin":1113,"end":1117},"obj":"17761676"},{"id":"T46471","span":{"begin":1144,"end":1148},"obj":"17108024"},{"id":"T33023","span":{"begin":1238,"end":1242},"obj":"19369340"},{"id":"T71391","span":{"begin":1288,"end":1292},"obj":"29370303"},{"id":"T25270","span":{"begin":1383,"end":1387},"obj":"19838190"},{"id":"T42335","span":{"begin":1427,"end":1431},"obj":"26311885"}],"text":"Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses nonspecifically."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T62070","span":{"begin":247,"end":256},"obj":"Body_part"},{"id":"T34871","span":{"begin":343,"end":351},"obj":"Body_part"},{"id":"T98576","span":{"begin":416,"end":424},"obj":"Body_part"},{"id":"T56607","span":{"begin":862,"end":869},"obj":"Body_part"},{"id":"T85573","span":{"begin":987,"end":995},"obj":"Body_part"},{"id":"T13179","span":{"begin":1182,"end":1190},"obj":"Body_part"}],"attributes":[{"id":"A75885","pred":"fma_id","subj":"T62070","obj":"http://purl.org/sig/ont/fma/fma84050"},{"id":"A76407","pred":"fma_id","subj":"T34871","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A41956","pred":"fma_id","subj":"T98576","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A67508","pred":"fma_id","subj":"T56607","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A23168","pred":"fma_id","subj":"T85573","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A30012","pred":"fma_id","subj":"T13179","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses nonspecifically."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T62","span":{"begin":332,"end":340},"obj":"Disease"},{"id":"T63","span":{"begin":453,"end":461},"obj":"Disease"},{"id":"T64","span":{"begin":612,"end":620},"obj":"Disease"},{"id":"T65","span":{"begin":688,"end":696},"obj":"Disease"},{"id":"T66","span":{"begin":849,"end":857},"obj":"Disease"},{"id":"T67","span":{"begin":1007,"end":1015},"obj":"Disease"},{"id":"T68","span":{"begin":1206,"end":1214},"obj":"Disease"},{"id":"T69","span":{"begin":1328,"end":1336},"obj":"Disease"}],"attributes":[{"id":"A62","pred":"mondo_id","subj":"T62","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A63","pred":"mondo_id","subj":"T63","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A64","pred":"mondo_id","subj":"T64","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A65","pred":"mondo_id","subj":"T65","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A66","pred":"mondo_id","subj":"T66","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A67","pred":"mondo_id","subj":"T67","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A68","pred":"mondo_id","subj":"T68","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A69","pred":"mondo_id","subj":"T69","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses nonspecifically."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T46552","span":{"begin":10,"end":20},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T26255","span":{"begin":42,"end":51},"obj":"http://purl.obolibrary.org/obo/SO_0000418"},{"id":"T87993","span":{"begin":130,"end":132},"obj":"http://purl.obolibrary.org/obo/CLO_0007074"},{"id":"T52388","span":{"begin":130,"end":132},"obj":"http://purl.obolibrary.org/obo/CLO_0051988"},{"id":"T27533","span":{"begin":433,"end":442},"obj":"http://purl.obolibrary.org/obo/SO_0000418"},{"id":"T78168","span":{"begin":500,"end":509},"obj":"http://purl.obolibrary.org/obo/SO_0000418"},{"id":"T65422","span":{"begin":645,"end":654},"obj":"http://purl.obolibrary.org/obo/SO_0000418"},{"id":"T77228","span":{"begin":720,"end":729},"obj":"http://purl.obolibrary.org/obo/SO_0000418"},{"id":"T35185","span":{"begin":788,"end":797},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T5869","span":{"begin":899,"end":908},"obj":"http://purl.obolibrary.org/obo/SO_0000418"},{"id":"T15916","span":{"begin":1154,"end":1156},"obj":"http://purl.obolibrary.org/obo/CLO_0007074"},{"id":"T55083","span":{"begin":1154,"end":1156},"obj":"http://purl.obolibrary.org/obo/CLO_0051988"},{"id":"T42053","span":{"begin":1288,"end":1292},"obj":"http://purl.obolibrary.org/obo/CLO_0001185"}],"text":"Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses nonspecifically."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T27","span":{"begin":127,"end":129},"obj":"Chemical"},{"id":"T30","span":{"begin":141,"end":151},"obj":"Chemical"},{"id":"T31","span":{"begin":343,"end":351},"obj":"Chemical"},{"id":"T32","span":{"begin":416,"end":424},"obj":"Chemical"},{"id":"T33","span":{"begin":862,"end":869},"obj":"Chemical"},{"id":"T34","span":{"begin":987,"end":995},"obj":"Chemical"},{"id":"T35","span":{"begin":1018,"end":1021},"obj":"Chemical"},{"id":"T36","span":{"begin":1151,"end":1153},"obj":"Chemical"},{"id":"T39","span":{"begin":1182,"end":1190},"obj":"Chemical"},{"id":"T40","span":{"begin":1217,"end":1220},"obj":"Chemical"},{"id":"T41","span":{"begin":1514,"end":1523},"obj":"Chemical"}],"attributes":[{"id":"A27","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_141424"},{"id":"A28","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_25573"},{"id":"A29","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_1224"},{"id":"A30","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_52999"},{"id":"A31","pred":"chebi_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A32","pred":"chebi_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A33","pred":"chebi_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A34","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A35","pred":"chebi_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/CHEBI_18405"},{"id":"A36","pred":"chebi_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/CHEBI_141424"},{"id":"A37","pred":"chebi_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/CHEBI_25573"},{"id":"A38","pred":"chebi_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/CHEBI_1224"},{"id":"A39","pred":"chebi_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A40","pred":"chebi_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/CHEBI_18405"},{"id":"A41","pred":"chebi_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/CHEBI_22587"}],"text":"Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses nonspecifically."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T37","span":{"begin":42,"end":60},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T38","span":{"begin":42,"end":51},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T39","span":{"begin":77,"end":92},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T40","span":{"begin":96,"end":117},"obj":"http://purl.obolibrary.org/obo/GO_0000981"},{"id":"T41","span":{"begin":96,"end":109},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T42","span":{"begin":206,"end":219},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T43","span":{"begin":433,"end":451},"obj":"http://purl.obolibrary.org/obo/GO_0007165"},{"id":"T44","span":{"begin":433,"end":442},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T45","span":{"begin":500,"end":509},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T46","span":{"begin":645,"end":654},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T47","span":{"begin":720,"end":729},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T48","span":{"begin":743,"end":747},"obj":"http://purl.obolibrary.org/obo/GO_0008384"},{"id":"T49","span":{"begin":801,"end":805},"obj":"http://purl.obolibrary.org/obo/GO_0008384"},{"id":"T50","span":{"begin":894,"end":898},"obj":"http://purl.obolibrary.org/obo/GO_0008384"},{"id":"T51","span":{"begin":899,"end":908},"obj":"http://purl.obolibrary.org/obo/GO_0023052"},{"id":"T52","span":{"begin":1054,"end":1069},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T53","span":{"begin":1469,"end":1482},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T54","span":{"begin":1487,"end":1498},"obj":"http://purl.obolibrary.org/obo/GO_0006412"}],"text":"Following activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses nonspecifically."}

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activation, RLR and TLRs induce signaling cascades, leading to the phosphorylation of transcription factors, such as NF-kB and the interferon-regulatory factor family (IRF), ultimately leading to transcription of IFN and proinflammatory cytokines. Although no experimental studies have delineated the precise functions of SARS-CoV-2 proteins, proteomic studies have demonstrated interactions between viral proteins and PRR signaling cascades. SARS-CoV-2 ORF9b indirectly interacts with the signaling adaptor MAVS via its association with Tom70 (Gordon et al., 2020), consistent with prior reports that SARS-CoV-1 ORF9b suppresses MAVS signaling (Shi et al., 2014). Furthermore, SARS-CoV-2 NSP13 interacts with signaling intermediate TBK1, and NSP15 is associated with RNF41, an activator of TBK1 and IRF3 (Gordon et al., 2020). Similarly, SARS-CoV-1 M protein is known to inhibit the TBK1 signaling complex (Siu et al., 2009), as does MERS-CoV ORF4b (Yang et al., 2015). Other proteins, including SARS-CoV-1 PLP, N, ORF3b, and ORF6, block IRF3 phosphorylation and nuclear translocation (Devaraj et al., 2007, Kopecky-Bromberg et al., 2007). NF-kB is also inhibited by CoV proteins. These include SARS-CoV-1 PLP (Frieman et al., 2009) and MERS-CoV ORF4b and ORF5 (Canton et al., 2018, Menachery et al., 2017). Finally, SARS-CoV-1 NSP1 (Huang et al., 2011a, Kamitani et al., 2009) and MERS-CoV NSP1 (Lokugamage et al., 2015) initiate general inhibition of host transcription and translation, thus limiting antiviral defenses nonspecifically."}

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