PMC:7571312 / 1155-2827 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T54374","span":{"begin":34,"end":51},"obj":"Body_part"},{"id":"T26446","span":{"begin":205,"end":211},"obj":"Body_part"},{"id":"T37694","span":{"begin":774,"end":780},"obj":"Body_part"},{"id":"T78312","span":{"begin":910,"end":918},"obj":"Body_part"},{"id":"T72980","span":{"begin":1024,"end":1032},"obj":"Body_part"},{"id":"T62636","span":{"begin":1199,"end":1207},"obj":"Body_part"}],"attributes":[{"id":"A21684","pred":"fma_id","subj":"T54374","obj":"http://purl.org/sig/ont/fma/fma265130"},{"id":"A33537","pred":"fma_id","subj":"T26446","obj":"http://purl.org/sig/ont/fma/fma84116"},{"id":"A30951","pred":"fma_id","subj":"T37694","obj":"http://purl.org/sig/ont/fma/fma84116"},{"id":"A96217","pred":"fma_id","subj":"T78312","obj":"http://purl.org/sig/ont/fma/fma82751"},{"id":"A85018","pred":"fma_id","subj":"T72980","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A65071","pred":"fma_id","subj":"T62636","obj":"http://purl.org/sig/ont/fma/fma82751"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T1","span":{"begin":34,"end":51},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000065"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T10","span":{"begin":34,"end":61},"obj":"Disease"},{"id":"T11","span":{"begin":52,"end":61},"obj":"Disease"},{"id":"T12","span":{"begin":139,"end":143},"obj":"Disease"},{"id":"T13","span":{"begin":265,"end":269},"obj":"Disease"},{"id":"T14","span":{"begin":305,"end":338},"obj":"Disease"},{"id":"T15","span":{"begin":340,"end":344},"obj":"Disease"},{"id":"T16","span":{"begin":368,"end":372},"obj":"Disease"},{"id":"T17","span":{"begin":441,"end":445},"obj":"Disease"},{"id":"T18","span":{"begin":568,"end":572},"obj":"Disease"},{"id":"T19","span":{"begin":616,"end":620},"obj":"Disease"},{"id":"T20","span":{"begin":691,"end":701},"obj":"Disease"},{"id":"T21","span":{"begin":763,"end":767},"obj":"Disease"},{"id":"T22","span":{"begin":1074,"end":1078},"obj":"Disease"},{"id":"T23","span":{"begin":1268,"end":1272},"obj":"Disease"},{"id":"T24","span":{"begin":1305,"end":1309},"obj":"Disease"},{"id":"T25","span":{"begin":1320,"end":1324},"obj":"Disease"},{"id":"T26","span":{"begin":1563,"end":1567},"obj":"Disease"},{"id":"T27","span":{"begin":1619,"end":1623},"obj":"Disease"}],"attributes":[{"id":"A10","pred":"mondo_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MONDO_0024355"},{"id":"A11","pred":"mondo_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A12","pred":"mondo_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A13","pred":"mondo_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A14","pred":"mondo_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A15","pred":"mondo_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A16","pred":"mondo_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A17","pred":"mondo_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A18","pred":"mondo_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A19","pred":"mondo_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A20","pred":"mondo_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A21","pred":"mondo_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A22","pred":"mondo_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A23","pred":"mondo_id","subj":"T23","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A24","pred":"mondo_id","subj":"T24","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A25","pred":"mondo_id","subj":"T25","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A26","pred":"mondo_id","subj":"T26","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A27","pred":"mondo_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T83605","span":{"begin":229,"end":234},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T83875","span":{"begin":244,"end":245},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T73484","span":{"begin":579,"end":582},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T36915","span":{"begin":636,"end":637},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T8644","span":{"begin":900,"end":904},"obj":"http://purl.obolibrary.org/obo/CLO_0053943"},{"id":"T48219","span":{"begin":1099,"end":1100},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T88436","span":{"begin":1417,"end":1423},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T85651","span":{"begin":1431,"end":1432},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T20594","span":{"begin":1522,"end":1530},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T11","span":{"begin":910,"end":918},"obj":"Chemical"},{"id":"T12","span":{"begin":1024,"end":1032},"obj":"Chemical"},{"id":"T13","span":{"begin":1199,"end":1207},"obj":"Chemical"},{"id":"T14","span":{"begin":1637,"end":1647},"obj":"Chemical"},{"id":"T15","span":{"begin":1653,"end":1662},"obj":"Chemical"}],"attributes":[{"id":"A11","pred":"chebi_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CHEBI_15356"},{"id":"A12","pred":"chebi_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A13","pred":"chebi_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CHEBI_15356"},{"id":"A14","pred":"chebi_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_22587"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T75111","span":{"begin":495,"end":504},"obj":"http://purl.obolibrary.org/obo/GO_0007585"},{"id":"T3","span":{"begin":1050,"end":1067},"obj":"http://purl.obolibrary.org/obo/GO_0019079"},{"id":"T4","span":{"begin":1050,"end":1067},"obj":"http://purl.obolibrary.org/obo/GO_0019058"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-sentences","denotations":[{"id":"T9","span":{"begin":0,"end":98},"obj":"Sentence"},{"id":"T10","span":{"begin":99,"end":553},"obj":"Sentence"},{"id":"T11","span":{"begin":554,"end":937},"obj":"Sentence"},{"id":"T12","span":{"begin":938,"end":1286},"obj":"Sentence"},{"id":"T13","span":{"begin":1287,"end":1672},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-PD-HP","denotations":[{"id":"T1","span":{"begin":34,"end":61},"obj":"Phenotype"},{"id":"T2","span":{"begin":463,"end":468},"obj":"Phenotype"},{"id":"T3","span":{"begin":470,"end":478},"obj":"Phenotype"},{"id":"T4","span":{"begin":484,"end":504},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/HP_0011947"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/HP_0001945"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/HP_0012735"},{"id":"A4","pred":"hp_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/HP_0002098"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"LitCovid-PubTator","denotations":[{"id":"59","span":{"begin":816,"end":820},"obj":"Gene"},{"id":"60","span":{"begin":121,"end":138},"obj":"Species"},{"id":"61","span":{"begin":139,"end":149},"obj":"Species"},{"id":"62","span":{"begin":265,"end":273},"obj":"Species"},{"id":"63","span":{"begin":281,"end":292},"obj":"Species"},{"id":"64","span":{"begin":368,"end":376},"obj":"Species"},{"id":"65","span":{"begin":441,"end":451},"obj":"Species"},{"id":"66","span":{"begin":568,"end":578},"obj":"Species"},{"id":"67","span":{"begin":616,"end":624},"obj":"Species"},{"id":"68","span":{"begin":763,"end":771},"obj":"Species"},{"id":"69","span":{"begin":1074,"end":1082},"obj":"Species"},{"id":"70","span":{"begin":1179,"end":1190},"obj":"Species"},{"id":"71","span":{"begin":1221,"end":1230},"obj":"Species"},{"id":"72","span":{"begin":1235,"end":1239},"obj":"Species"},{"id":"73","span":{"begin":1268,"end":1278},"obj":"Species"},{"id":"74","span":{"begin":1305,"end":1313},"obj":"Species"},{"id":"75","span":{"begin":1320,"end":1330},"obj":"Species"},{"id":"76","span":{"begin":1563,"end":1571},"obj":"Species"},{"id":"77","span":{"begin":1619,"end":1629},"obj":"Species"},{"id":"78","span":{"begin":34,"end":61},"obj":"Disease"},{"id":"79","span":{"begin":192,"end":200},"obj":"Disease"},{"id":"80","span":{"begin":312,"end":338},"obj":"Disease"},{"id":"81","span":{"begin":402,"end":408},"obj":"Disease"},{"id":"82","span":{"begin":463,"end":468},"obj":"Disease"},{"id":"83","span":{"begin":470,"end":478},"obj":"Disease"},{"id":"84","span":{"begin":691,"end":701},"obj":"Disease"},{"id":"85","span":{"begin":731,"end":737},"obj":"Disease"}],"attributes":[{"id":"A59","pred":"tao:has_database_id","subj":"59","obj":"Gene:5499"},{"id":"A60","pred":"tao:has_database_id","subj":"60","obj":"Tax:2697049"},{"id":"A61","pred":"tao:has_database_id","subj":"61","obj":"Tax:2697049"},{"id":"A62","pred":"tao:has_database_id","subj":"62","obj":"Tax:694009"},{"id":"A63","pred":"tao:has_database_id","subj":"63","obj":"Tax:11118"},{"id":"A64","pred":"tao:has_database_id","subj":"64","obj":"Tax:694009"},{"id":"A65","pred":"tao:has_database_id","subj":"65","obj":"Tax:2697049"},{"id":"A66","pred":"tao:has_database_id","subj":"66","obj":"Tax:2697049"},{"id":"A67","pred":"tao:has_database_id","subj":"67","obj":"Tax:694009"},{"id":"A68","pred":"tao:has_database_id","subj":"68","obj":"Tax:694009"},{"id":"A69","pred":"tao:has_database_id","subj":"69","obj":"Tax:694009"},{"id":"A70","pred":"tao:has_database_id","subj":"70","obj":"Tax:11118"},{"id":"A71","pred":"tao:has_database_id","subj":"71","obj":"Tax:11137"},{"id":"A72","pred":"tao:has_database_id","subj":"72","obj":"Tax:11149"},{"id":"A73","pred":"tao:has_database_id","subj":"73","obj":"Tax:2697049"},{"id":"A74","pred":"tao:has_database_id","subj":"74","obj":"Tax:694009"},{"id":"A75","pred":"tao:has_database_id","subj":"75","obj":"Tax:2697049"},{"id":"A76","pred":"tao:has_database_id","subj":"76","obj":"Tax:694009"},{"id":"A77","pred":"tao:has_database_id","subj":"77","obj":"Tax:2697049"},{"id":"A78","pred":"tao:has_database_id","subj":"78","obj":"MESH:D012141"},{"id":"A79","pred":"tao:has_database_id","subj":"79","obj":"MESH:C000657245"},{"id":"A80","pred":"tao:has_database_id","subj":"80","obj":"MESH:D012120"},{"id":"A81","pred":"tao:has_database_id","subj":"81","obj":"MESH:D003643"},{"id":"A82","pred":"tao:has_database_id","subj":"82","obj":"MESH:D005334"},{"id":"A83","pred":"tao:has_database_id","subj":"83","obj":"MESH:D003371"},{"id":"A84","pred":"tao:has_database_id","subj":"84","obj":"MESH:D007239"},{"id":"A85","pred":"tao:has_database_id","subj":"85","obj":"MESH:D003643"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}

{"project":"2_test","denotations":[{"id":"33054210-32015508-61913438","span":{"begin":201,"end":202},"obj":"32015508"},{"id":"33054210-32015507-61913439","span":{"begin":203,"end":204},"obj":"32015507"},{"id":"33054210-32015507-61913440","span":{"begin":359,"end":360},"obj":"32015507"},{"id":"33054210-12730500-61913441","span":{"begin":361,"end":362},"obj":"12730500"},{"id":"33054210-12917450-61913442","span":{"begin":1068,"end":1069},"obj":"12917450"},{"id":"33054210-32321856-61913443","span":{"begin":1671,"end":1672},"obj":"32321856"}],"text":"In late 2019, cases of an unknown respiratory tract infection were first reported in Wuhan, China. By February 2020, the novel coronavirus SARS CoV-2 was identified as the causative agent for COVID-19.1,2 Genome analysis of this virus revealed a high similarity to SARS CoV-1, the coronavirus that caused severe acute respiratory syndrome (SARS) in 2002–2003.2−4 Like SARS CoV-1, which resulted in 799 deaths among the 8464 probable cases,5 SARS CoV-2 can induce fever, coughing, and difficulty breathing that rapidly becomes more serious in some cases. The spread of SARS CoV-2 has been more extensive than that of SARS CoV-1, causing a global pandemic with the current number of worldwide infections surpassing eight million and deaths surpassing 400,000.6 The SARS CoV-1 genome encodes for two large polyproteins pp1a (∼450 kDa) and pp1ab (∼750 kDa) that contain overlapping sequences and include a 3C-like cysteine protease (3CLpro). The function of this internally encoded 3CLpro is integral to the processing of these proteins and critical for viral replication.7 The SARS CoV-1 3CLpro shares a high degree of structural homology and similar substrate specificity with the coronavirus 3C-like cysteine proteases of hCoV 229E and TGEV8 but is most similar to the SARS CoV-2 3CLpro. Specifically, the SARS CoV-1 and SARS CoV-2 share 96% identity between their respective 3CLpro sequences and 100% identity in the active site.8 A recent report by Dai et al. demonstrates that crystallographic information and structure–activity relationships obtained with the SARS CoV-1 3CLpro could facilitate the design of potent SARS CoV-2 3CLpro inhibitors with antiviral potency.9"}