PMC:7571312 / 424-975 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T35139","span":{"begin":48,"end":56},"obj":"Body_part"},{"id":"T8747","span":{"begin":270,"end":277},"obj":"Body_part"}],"attributes":[{"id":"A24141","pred":"fma_id","subj":"T35139","obj":"http://purl.org/sig/ont/fma/fma82751"},{"id":"A77659","pred":"fma_id","subj":"T8747","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"hich are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4"}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T8","span":{"begin":394,"end":398},"obj":"Disease"}],"attributes":[{"id":"A8","pred":"mondo_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"hich are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4"}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T55568","span":{"begin":38,"end":42},"obj":"http://purl.obolibrary.org/obo/CLO_0053943"},{"id":"T24614","span":{"begin":78,"end":79},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T12954","span":{"begin":202,"end":209},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T9960","span":{"begin":288,"end":289},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T99506","span":{"begin":311,"end":318},"obj":"http://purl.obolibrary.org/obo/CLO_0009985"}],"text":"hich are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4"}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T2","span":{"begin":48,"end":56},"obj":"Chemical"},{"id":"T3","span":{"begin":270,"end":277},"obj":"Chemical"},{"id":"T4","span":{"begin":367,"end":373},"obj":"Chemical"},{"id":"T5","span":{"begin":380,"end":390},"obj":"Chemical"},{"id":"T6","span":{"begin":422,"end":428},"obj":"Chemical"}],"attributes":[{"id":"A2","pred":"chebi_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CHEBI_15356"},{"id":"A3","pred":"chebi_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A4","pred":"chebi_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CHEBI_17087"},{"id":"A5","pred":"chebi_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CHEBI_35222"},{"id":"A6","pred":"chebi_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CHEBI_52214"}],"text":"hich are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4"}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T30304","span":{"begin":85,"end":98},"obj":"http://purl.obolibrary.org/obo/GO_0006412"}],"text":"hich are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4"}

{"project":"LitCovid-sentences","denotations":[{"id":"T5","span":{"begin":161,"end":287},"obj":"Sentence"},{"id":"T6","span":{"begin":288,"end":518},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"hich are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4"}

{"project":"LitCovid-PubTator","denotations":[{"id":"22","span":{"begin":136,"end":147},"obj":"Species"},{"id":"23","span":{"begin":186,"end":189},"obj":"Species"},{"id":"24","span":{"begin":196,"end":201},"obj":"Species"},{"id":"25","span":{"begin":394,"end":402},"obj":"Species"},{"id":"27","span":{"begin":367,"end":373},"obj":"Chemical"}],"attributes":[{"id":"A22","pred":"tao:has_database_id","subj":"22","obj":"Tax:11118"},{"id":"A23","pred":"tao:has_database_id","subj":"23","obj":"Tax:11118"},{"id":"A24","pred":"tao:has_database_id","subj":"24","obj":"Tax:2697049"},{"id":"A25","pred":"tao:has_database_id","subj":"25","obj":"Tax:694009"},{"id":"A27","pred":"tao:has_database_id","subj":"27","obj":"MESH:D007659"}],"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":"hich are cleaved at specific sites by a 3C-like cysteine protease (3CLpro) in a post-translational processing step that is critical for coronavirus replication. The 3CLpro sequences for CoV-1 and CoV-2 viruses are 100% identical in the catalytic domain that carries out protein cleavage. A research effort that focused on the discovery of reversible and irreversible ketone-based inhibitors of SARS CoV-1 3CLpro employing ligand-protease structures solved by X-ray crystallography led to the identification of 3 and 4. Preclinical experiments reveal 4"}