PubMed:32264791 / 694-977 JSONTXT

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    LitCovid-OGER-BB

    {"project":"LitCovid-OGER-BB","denotations":[{"id":"T7984","span":{"begin":56,"end":64},"obj":"SP_10"},{"id":"T7985","span":{"begin":97,"end":107},"obj":"SP_7"},{"id":"T7986","span":{"begin":200,"end":205},"obj":"SP_6;PG_10"},{"id":"T7987","span":{"begin":206,"end":210},"obj":"PG_10"},{"id":"T7988","span":{"begin":255,"end":268},"obj":"BV_19"},{"id":"T7989","span":{"begin":272,"end":282},"obj":"SP_7"}],"namespaces":[{"prefix":"NCBITaxon","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"}],"text":"Although sharing a close evolutionary relationship with SARS-CoV, the receptor-binding domain of SARS-CoV-2 differs in several key amino acid residues, allowing for stronger binding affinity with the human ACE2 receptor, which may account for the greater pathogenicity of SARS-CoV-2."}

    LitCovid_AGAC

    {"project":"LitCovid_AGAC","denotations":[{"id":"p125237s33","span":{"begin":174,"end":181},"obj":"Interaction"},{"id":"p125237s34","span":{"begin":182,"end":190},"obj":"Interaction"}],"text":"Although sharing a close evolutionary relationship with SARS-CoV, the receptor-binding domain of SARS-CoV-2 differs in several key amino acid residues, allowing for stronger binding affinity with the human ACE2 receptor, which may account for the greater pathogenicity of SARS-CoV-2."}

    Inflammaging

    {"project":"Inflammaging","denotations":[{"id":"T5","span":{"begin":0,"end":283},"obj":"Sentence"},{"id":"T5","span":{"begin":0,"end":283},"obj":"Sentence"}],"text":"Although sharing a close evolutionary relationship with SARS-CoV, the receptor-binding domain of SARS-CoV-2 differs in several key amino acid residues, allowing for stronger binding affinity with the human ACE2 receptor, which may account for the greater pathogenicity of SARS-CoV-2."}

    PubMed_ArguminSci

    {"project":"PubMed_ArguminSci","denotations":[{"id":"T4","span":{"begin":0,"end":283},"obj":"DRI_Background"}],"text":"Although sharing a close evolutionary relationship with SARS-CoV, the receptor-binding domain of SARS-CoV-2 differs in several key amino acid residues, allowing for stronger binding affinity with the human ACE2 receptor, which may account for the greater pathogenicity of SARS-CoV-2."}