PMC:7556165 / 9265-9575 JSONTXT

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T66","span":{"begin":93,"end":253},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"lusive of ACE2, α helices and a portion of β-sheet are located around the catalytic channel. The negative charge of the channel and the presence of distinct hydrophobic regions contribute to the specificity of the binding site (Prabakaran et al., 2004). The determination of the crystal structure of the extrac"}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"312","span":{"begin":10,"end":14},"obj":"Gene"}],"attributes":[{"id":"A312","pred":"pubann:denotes","subj":"312","obj":"Gene:59272"}],"text":"lusive of ACE2, α helices and a portion of β-sheet are located around the catalytic channel. The negative charge of the channel and the presence of distinct hydrophobic regions contribute to the specificity of the binding site (Prabakaran et al., 2004). The determination of the crystal structure of the extrac"}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T1454","span":{"begin":10,"end":14},"obj":"Protein"}],"attributes":[{"id":"A1454","pred":"uniprot_id","subj":"T1454","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"}],"text":"lusive of ACE2, α helices and a portion of β-sheet are located around the catalytic channel. The negative charge of the channel and the presence of distinct hydrophobic regions contribute to the specificity of the binding site (Prabakaran et al., 2004). The determination of the crystal structure of the extrac"}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T27","span":{"begin":222,"end":226},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"lusive of ACE2, α helices and a portion of β-sheet are located around the catalytic channel. The negative charge of the channel and the presence of distinct hydrophobic regions contribute to the specificity of the binding site (Prabakaran et al., 2004). The determination of the crystal structure of the extrac"}

{"project":"LitCovid-PubTator","denotations":[{"id":"312","span":{"begin":10,"end":14},"obj":"Gene"}],"attributes":[{"id":"A312","pred":"tao:has_database_id","subj":"312","obj":"Gene:59272"}],"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":"lusive of ACE2, α helices and a portion of β-sheet are located around the catalytic channel. The negative charge of the channel and the presence of distinct hydrophobic regions contribute to the specificity of the binding site (Prabakaran et al., 2004). The determination of the crystal structure of the extrac"}

{"project":"LitCovid-sentences","denotations":[{"id":"T66","span":{"begin":93,"end":253},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"lusive of ACE2, α helices and a portion of β-sheet are located around the catalytic channel. The negative charge of the channel and the presence of distinct hydrophobic regions contribute to the specificity of the binding site (Prabakaran et al., 2004). The determination of the crystal structure of the extrac"}