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LitCovid-PubTator

LitCovid-PD-FMA-UBERON

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T5","span":{"begin":60,"end":83},"obj":"Body_part"},{"id":"T6","span":{"begin":66,"end":83},"obj":"Body_part"}],"attributes":[{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001558"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000065"}],"text":"Coronavirus replication and pathogenesis\nACE2, found in the lower respiratory tract of humans, is known as cell receptor for SARS-CoV [27] and regulates both the cross-species and human-to-human transmission [28]. Isolated from the bronchoalveolar lavage fluid (BALF) of a COVID-19 patient, Zhou et al. [8] have confirmed that the SARS-CoV-2 uses the same cellular entry receptor, ACE2, as SARS-CoV. The virion S-glycoprotein on the surface of coronavirus can attach to the receptor, ACE2 on the surface of human cells [29]. S glycoprotein includes two subunits, S1 and S2 [30]. S1 determines the virus-host range and cellular tropism with the key function domain − RBD, while S2 mediates virus-cell membrane fusion by two tandem domains, heptad repeats 1 (HR1) [31] and HR2 [32]. After membrane fusion, the viral genome RNA is released into the cytoplasm, and the uncoated RNA translates two polyproteins, pp1a and pp1ab [33], which encode non-structural proteins, and form replication-transcription complex (RTC) in double-membrane vesicle [34]. Continuously RTC replicate and synthesize a nested set of subgenomic RNAs [35], which encode accessory proteins and structural proteins. Mediating endoplasmic reticulum (ER) and Golgi [36], newly formed genomic RNA, nucleocapsid proteins and envelope glycoproteins assemble and form viral particle buds. Lastly, the virion-containing vesicles fuse with the plasma membrane to release the virus.\nBecause the binding of SARS-CoV-2 Spike (S) glycoprotein and ACE2 receptor is a critical step for virus entry, virus-receptor binding affinity is under intensive study through different approaches. Systematic detection of β-CoV receptors showed that human cells expressing ACE2, but not human Dipeptidyl peptidase-4 (DPP4) or APN (Aminopeptidase N), were enhanced entry of SARS-CoV-2 [37]. While, another study showed that S-protein and ACE2 binding efficiency is 10- to 20- fold higher than that of SARS-CoV, evidenced by Cryo-EM Structure of the SARS-CoV-2 Spike in the prefusion conformation [38]. For SARS-CoV, the cleavage of trimer S protein is triggered by the cell surface-associated transmembrane protease serine 2 (TMPRSS2) [39] and cathepsin [40], while the possible molecules facilitated membrane invagination for SARS-CoV-2 endocytosis are still unclear. Up to the date this review paper was prepared, reports showed that the SARS-CoV-2 may readily transmit, while cause less serious human infection rather than human SARS-CoV. Based on the latest WHO report, the number of infected people (over 80,000 globally, updated on 1 March 2020). The global outbreak may due to the following factors: firstly, the unknown pneumonia outbroke at the time of China Spring Festival, when the mass population flowing. Secondly, more detailed molecular mechanisms of viral binding and entry manners await to be elucidated, which may hamper the development of targeted therapy. Thirdly, available data suggested that the SARS-CoV-2 may be less virulent than the SARS-CoV and MERS-CoV, with the currently analyzed mortality of COVID-19 is 3.4%, lower than death rate of SARS (9.6%) and MERS (around 35%), respectively [19]. Thus, the potential mechanisms for human-to-human transmission and pathogenic mechanisms of the SARS-CoV-2 are under extensively studied."}

LitCovid_AGAC

{"project":"LitCovid_AGAC","denotations":[{"id":"p13914s6","span":{"begin":1866,"end":1875},"obj":"Protein"},{"id":"p13914s10","span":{"begin":1880,"end":1884},"obj":"Protein"},{"id":"p13914s11","span":{"begin":1885,"end":1892},"obj":"Interaction"}],"text":"Coronavirus replication and pathogenesis\nACE2, found in the lower respiratory tract of humans, is known as cell receptor for SARS-CoV [27] and regulates both the cross-species and human-to-human transmission [28]. Isolated from the bronchoalveolar lavage fluid (BALF) of a COVID-19 patient, Zhou et al. [8] have confirmed that the SARS-CoV-2 uses the same cellular entry receptor, ACE2, as SARS-CoV. The virion S-glycoprotein on the surface of coronavirus can attach to the receptor, ACE2 on the surface of human cells [29]. S glycoprotein includes two subunits, S1 and S2 [30]. S1 determines the virus-host range and cellular tropism with the key function domain − RBD, while S2 mediates virus-cell membrane fusion by two tandem domains, heptad repeats 1 (HR1) [31] and HR2 [32]. After membrane fusion, the viral genome RNA is released into the cytoplasm, and the uncoated RNA translates two polyproteins, pp1a and pp1ab [33], which encode non-structural proteins, and form replication-transcription complex (RTC) in double-membrane vesicle [34]. Continuously RTC replicate and synthesize a nested set of subgenomic RNAs [35], which encode accessory proteins and structural proteins. Mediating endoplasmic reticulum (ER) and Golgi [36], newly formed genomic RNA, nucleocapsid proteins and envelope glycoproteins assemble and form viral particle buds. Lastly, the virion-containing vesicles fuse with the plasma membrane to release the virus.\nBecause the binding of SARS-CoV-2 Spike (S) glycoprotein and ACE2 receptor is a critical step for virus entry, virus-receptor binding affinity is under intensive study through different approaches. Systematic detection of β-CoV receptors showed that human cells expressing ACE2, but not human Dipeptidyl peptidase-4 (DPP4) or APN (Aminopeptidase N), were enhanced entry of SARS-CoV-2 [37]. While, another study showed that S-protein and ACE2 binding efficiency is 10- to 20- fold higher than that of SARS-CoV, evidenced by Cryo-EM Structure of the SARS-CoV-2 Spike in the prefusion conformation [38]. For SARS-CoV, the cleavage of trimer S protein is triggered by the cell surface-associated transmembrane protease serine 2 (TMPRSS2) [39] and cathepsin [40], while the possible molecules facilitated membrane invagination for SARS-CoV-2 endocytosis are still unclear. Up to the date this review paper was prepared, reports showed that the SARS-CoV-2 may readily transmit, while cause less serious human infection rather than human SARS-CoV. Based on the latest WHO report, the number of infected people (over 80,000 globally, updated on 1 March 2020). The global outbreak may due to the following factors: firstly, the unknown pneumonia outbroke at the time of China Spring Festival, when the mass population flowing. Secondly, more detailed molecular mechanisms of viral binding and entry manners await to be elucidated, which may hamper the development of targeted therapy. Thirdly, available data suggested that the SARS-CoV-2 may be less virulent than the SARS-CoV and MERS-CoV, with the currently analyzed mortality of COVID-19 is 3.4%, lower than death rate of SARS (9.6%) and MERS (around 35%), respectively [19]. Thus, the potential mechanisms for human-to-human transmission and pathogenic mechanisms of the SARS-CoV-2 are under extensively studied."}

LitCovid-PD-MONDO

LitCovid-PD-CLO

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T13","span":{"begin":28,"end":40},"obj":"http://purl.obolibrary.org/obo/GO_0009405"},{"id":"T14","span":{"begin":627,"end":634},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T15","span":{"begin":700,"end":715},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T16","span":{"begin":787,"end":802},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T17","span":{"begin":987,"end":1000},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T18","span":{"begin":2243,"end":2264},"obj":"http://purl.obolibrary.org/obo/GO_0010324"},{"id":"T19","span":{"begin":2280,"end":2291},"obj":"http://purl.obolibrary.org/obo/GO_0006897"}],"text":"Coronavirus replication and pathogenesis\nACE2, found in the lower respiratory tract of humans, is known as cell receptor for SARS-CoV [27] and regulates both the cross-species and human-to-human transmission [28]. Isolated from the bronchoalveolar lavage fluid (BALF) of a COVID-19 patient, Zhou et al. [8] have confirmed that the SARS-CoV-2 uses the same cellular entry receptor, ACE2, as SARS-CoV. The virion S-glycoprotein on the surface of coronavirus can attach to the receptor, ACE2 on the surface of human cells [29]. S glycoprotein includes two subunits, S1 and S2 [30]. S1 determines the virus-host range and cellular tropism with the key function domain − RBD, while S2 mediates virus-cell membrane fusion by two tandem domains, heptad repeats 1 (HR1) [31] and HR2 [32]. After membrane fusion, the viral genome RNA is released into the cytoplasm, and the uncoated RNA translates two polyproteins, pp1a and pp1ab [33], which encode non-structural proteins, and form replication-transcription complex (RTC) in double-membrane vesicle [34]. Continuously RTC replicate and synthesize a nested set of subgenomic RNAs [35], which encode accessory proteins and structural proteins. Mediating endoplasmic reticulum (ER) and Golgi [36], newly formed genomic RNA, nucleocapsid proteins and envelope glycoproteins assemble and form viral particle buds. Lastly, the virion-containing vesicles fuse with the plasma membrane to release the virus.\nBecause the binding of SARS-CoV-2 Spike (S) glycoprotein and ACE2 receptor is a critical step for virus entry, virus-receptor binding affinity is under intensive study through different approaches. Systematic detection of β-CoV receptors showed that human cells expressing ACE2, but not human Dipeptidyl peptidase-4 (DPP4) or APN (Aminopeptidase N), were enhanced entry of SARS-CoV-2 [37]. While, another study showed that S-protein and ACE2 binding efficiency is 10- to 20- fold higher than that of SARS-CoV, evidenced by Cryo-EM Structure of the SARS-CoV-2 Spike in the prefusion conformation [38]. For SARS-CoV, the cleavage of trimer S protein is triggered by the cell surface-associated transmembrane protease serine 2 (TMPRSS2) [39] and cathepsin [40], while the possible molecules facilitated membrane invagination for SARS-CoV-2 endocytosis are still unclear. Up to the date this review paper was prepared, reports showed that the SARS-CoV-2 may readily transmit, while cause less serious human infection rather than human SARS-CoV. Based on the latest WHO report, the number of infected people (over 80,000 globally, updated on 1 March 2020). The global outbreak may due to the following factors: firstly, the unknown pneumonia outbroke at the time of China Spring Festival, when the mass population flowing. Secondly, more detailed molecular mechanisms of viral binding and entry manners await to be elucidated, which may hamper the development of targeted therapy. Thirdly, available data suggested that the SARS-CoV-2 may be less virulent than the SARS-CoV and MERS-CoV, with the currently analyzed mortality of COVID-19 is 3.4%, lower than death rate of SARS (9.6%) and MERS (around 35%), respectively [19]. Thus, the potential mechanisms for human-to-human transmission and pathogenic mechanisms of the SARS-CoV-2 are under extensively studied."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T76","span":{"begin":0,"end":40},"obj":"Sentence"},{"id":"T77","span":{"begin":41,"end":213},"obj":"Sentence"},{"id":"T78","span":{"begin":214,"end":399},"obj":"Sentence"},{"id":"T79","span":{"begin":400,"end":524},"obj":"Sentence"},{"id":"T80","span":{"begin":525,"end":578},"obj":"Sentence"},{"id":"T81","span":{"begin":579,"end":780},"obj":"Sentence"},{"id":"T82","span":{"begin":781,"end":1047},"obj":"Sentence"},{"id":"T83","span":{"begin":1048,"end":1184},"obj":"Sentence"},{"id":"T84","span":{"begin":1185,"end":1351},"obj":"Sentence"},{"id":"T85","span":{"begin":1352,"end":1442},"obj":"Sentence"},{"id":"T86","span":{"begin":1443,"end":1640},"obj":"Sentence"},{"id":"T87","span":{"begin":1641,"end":1832},"obj":"Sentence"},{"id":"T88","span":{"begin":1833,"end":2043},"obj":"Sentence"},{"id":"T89","span":{"begin":2044,"end":2310},"obj":"Sentence"},{"id":"T90","span":{"begin":2311,"end":2483},"obj":"Sentence"},{"id":"T91","span":{"begin":2484,"end":2594},"obj":"Sentence"},{"id":"T92","span":{"begin":2595,"end":2760},"obj":"Sentence"},{"id":"T93","span":{"begin":2761,"end":2918},"obj":"Sentence"},{"id":"T94","span":{"begin":2919,"end":3163},"obj":"Sentence"},{"id":"T95","span":{"begin":3164,"end":3301},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Coronavirus replication and pathogenesis\nACE2, found in the lower respiratory tract of humans, is known as cell receptor for SARS-CoV [27] and regulates both the cross-species and human-to-human transmission [28]. Isolated from the bronchoalveolar lavage fluid (BALF) of a COVID-19 patient, Zhou et al. [8] have confirmed that the SARS-CoV-2 uses the same cellular entry receptor, ACE2, as SARS-CoV. The virion S-glycoprotein on the surface of coronavirus can attach to the receptor, ACE2 on the surface of human cells [29]. S glycoprotein includes two subunits, S1 and S2 [30]. S1 determines the virus-host range and cellular tropism with the key function domain − RBD, while S2 mediates virus-cell membrane fusion by two tandem domains, heptad repeats 1 (HR1) [31] and HR2 [32]. After membrane fusion, the viral genome RNA is released into the cytoplasm, and the uncoated RNA translates two polyproteins, pp1a and pp1ab [33], which encode non-structural proteins, and form replication-transcription complex (RTC) in double-membrane vesicle [34]. Continuously RTC replicate and synthesize a nested set of subgenomic RNAs [35], which encode accessory proteins and structural proteins. Mediating endoplasmic reticulum (ER) and Golgi [36], newly formed genomic RNA, nucleocapsid proteins and envelope glycoproteins assemble and form viral particle buds. Lastly, the virion-containing vesicles fuse with the plasma membrane to release the virus.\nBecause the binding of SARS-CoV-2 Spike (S) glycoprotein and ACE2 receptor is a critical step for virus entry, virus-receptor binding affinity is under intensive study through different approaches. Systematic detection of β-CoV receptors showed that human cells expressing ACE2, but not human Dipeptidyl peptidase-4 (DPP4) or APN (Aminopeptidase N), were enhanced entry of SARS-CoV-2 [37]. While, another study showed that S-protein and ACE2 binding efficiency is 10- to 20- fold higher than that of SARS-CoV, evidenced by Cryo-EM Structure of the SARS-CoV-2 Spike in the prefusion conformation [38]. For SARS-CoV, the cleavage of trimer S protein is triggered by the cell surface-associated transmembrane protease serine 2 (TMPRSS2) [39] and cathepsin [40], while the possible molecules facilitated membrane invagination for SARS-CoV-2 endocytosis are still unclear. Up to the date this review paper was prepared, reports showed that the SARS-CoV-2 may readily transmit, while cause less serious human infection rather than human SARS-CoV. Based on the latest WHO report, the number of infected people (over 80,000 globally, updated on 1 March 2020). The global outbreak may due to the following factors: firstly, the unknown pneumonia outbroke at the time of China Spring Festival, when the mass population flowing. Secondly, more detailed molecular mechanisms of viral binding and entry manners await to be elucidated, which may hamper the development of targeted therapy. Thirdly, available data suggested that the SARS-CoV-2 may be less virulent than the SARS-CoV and MERS-CoV, with the currently analyzed mortality of COVID-19 is 3.4%, lower than death rate of SARS (9.6%) and MERS (around 35%), respectively [19]. Thus, the potential mechanisms for human-to-human transmission and pathogenic mechanisms of the SARS-CoV-2 are under extensively studied."}

LitCovid-PD-HP

{"project":"LitCovid-PD-HP","denotations":[{"id":"T14","span":{"begin":2670,"end":2679},"obj":"Phenotype"}],"attributes":[{"id":"A14","pred":"hp_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/HP_0002090"}],"text":"Coronavirus replication and pathogenesis\nACE2, found in the lower respiratory tract of humans, is known as cell receptor for SARS-CoV [27] and regulates both the cross-species and human-to-human transmission [28]. Isolated from the bronchoalveolar lavage fluid (BALF) of a COVID-19 patient, Zhou et al. [8] have confirmed that the SARS-CoV-2 uses the same cellular entry receptor, ACE2, as SARS-CoV. The virion S-glycoprotein on the surface of coronavirus can attach to the receptor, ACE2 on the surface of human cells [29]. S glycoprotein includes two subunits, S1 and S2 [30]. S1 determines the virus-host range and cellular tropism with the key function domain − RBD, while S2 mediates virus-cell membrane fusion by two tandem domains, heptad repeats 1 (HR1) [31] and HR2 [32]. After membrane fusion, the viral genome RNA is released into the cytoplasm, and the uncoated RNA translates two polyproteins, pp1a and pp1ab [33], which encode non-structural proteins, and form replication-transcription complex (RTC) in double-membrane vesicle [34]. Continuously RTC replicate and synthesize a nested set of subgenomic RNAs [35], which encode accessory proteins and structural proteins. Mediating endoplasmic reticulum (ER) and Golgi [36], newly formed genomic RNA, nucleocapsid proteins and envelope glycoproteins assemble and form viral particle buds. Lastly, the virion-containing vesicles fuse with the plasma membrane to release the virus.\nBecause the binding of SARS-CoV-2 Spike (S) glycoprotein and ACE2 receptor is a critical step for virus entry, virus-receptor binding affinity is under intensive study through different approaches. Systematic detection of β-CoV receptors showed that human cells expressing ACE2, but not human Dipeptidyl peptidase-4 (DPP4) or APN (Aminopeptidase N), were enhanced entry of SARS-CoV-2 [37]. While, another study showed that S-protein and ACE2 binding efficiency is 10- to 20- fold higher than that of SARS-CoV, evidenced by Cryo-EM Structure of the SARS-CoV-2 Spike in the prefusion conformation [38]. For SARS-CoV, the cleavage of trimer S protein is triggered by the cell surface-associated transmembrane protease serine 2 (TMPRSS2) [39] and cathepsin [40], while the possible molecules facilitated membrane invagination for SARS-CoV-2 endocytosis are still unclear. Up to the date this review paper was prepared, reports showed that the SARS-CoV-2 may readily transmit, while cause less serious human infection rather than human SARS-CoV. Based on the latest WHO report, the number of infected people (over 80,000 globally, updated on 1 March 2020). The global outbreak may due to the following factors: firstly, the unknown pneumonia outbroke at the time of China Spring Festival, when the mass population flowing. Secondly, more detailed molecular mechanisms of viral binding and entry manners await to be elucidated, which may hamper the development of targeted therapy. Thirdly, available data suggested that the SARS-CoV-2 may be less virulent than the SARS-CoV and MERS-CoV, with the currently analyzed mortality of COVID-19 is 3.4%, lower than death rate of SARS (9.6%) and MERS (around 35%), respectively [19]. Thus, the potential mechanisms for human-to-human transmission and pathogenic mechanisms of the SARS-CoV-2 are under extensively studied."}

2_test

{"project":"2_test","denotations":[{"id":"32169119-16282461-70132203","span":{"begin":135,"end":137},"obj":"16282461"},{"id":"32169119-32015507-70132204","span":{"begin":304,"end":305},"obj":"32015507"},{"id":"32169119-31522710-70132205","span":{"begin":520,"end":522},"obj":"31522710"},{"id":"32169119-24766432-70132206","span":{"begin":574,"end":576},"obj":"24766432"},{"id":"32169119-28643204-70132207","span":{"begin":923,"end":925},"obj":"28643204"},{"id":"32169119-15609508-70132208","span":{"begin":1043,"end":1045},"obj":"15609508"},{"id":"32169119-15827143-70132209","span":{"begin":1123,"end":1125},"obj":"15827143"},{"id":"32169119-31399512-70132210","span":{"begin":1233,"end":1235},"obj":"31399512"},{"id":"32169119-30102747-70132211","span":{"begin":2039,"end":2041},"obj":"30102747"},{"id":"32169119-25445340-70132212","span":{"begin":2178,"end":2180},"obj":"25445340"},{"id":"32169119-27344959-70132213","span":{"begin":3159,"end":3161},"obj":"27344959"}],"text":"Coronavirus replication and pathogenesis\nACE2, found in the lower respiratory tract of humans, is known as cell receptor for SARS-CoV [27] and regulates both the cross-species and human-to-human transmission [28]. Isolated from the bronchoalveolar lavage fluid (BALF) of a COVID-19 patient, Zhou et al. [8] have confirmed that the SARS-CoV-2 uses the same cellular entry receptor, ACE2, as SARS-CoV. The virion S-glycoprotein on the surface of coronavirus can attach to the receptor, ACE2 on the surface of human cells [29]. S glycoprotein includes two subunits, S1 and S2 [30]. S1 determines the virus-host range and cellular tropism with the key function domain − RBD, while S2 mediates virus-cell membrane fusion by two tandem domains, heptad repeats 1 (HR1) [31] and HR2 [32]. After membrane fusion, the viral genome RNA is released into the cytoplasm, and the uncoated RNA translates two polyproteins, pp1a and pp1ab [33], which encode non-structural proteins, and form replication-transcription complex (RTC) in double-membrane vesicle [34]. Continuously RTC replicate and synthesize a nested set of subgenomic RNAs [35], which encode accessory proteins and structural proteins. Mediating endoplasmic reticulum (ER) and Golgi [36], newly formed genomic RNA, nucleocapsid proteins and envelope glycoproteins assemble and form viral particle buds. Lastly, the virion-containing vesicles fuse with the plasma membrane to release the virus.\nBecause the binding of SARS-CoV-2 Spike (S) glycoprotein and ACE2 receptor is a critical step for virus entry, virus-receptor binding affinity is under intensive study through different approaches. Systematic detection of β-CoV receptors showed that human cells expressing ACE2, but not human Dipeptidyl peptidase-4 (DPP4) or APN (Aminopeptidase N), were enhanced entry of SARS-CoV-2 [37]. While, another study showed that S-protein and ACE2 binding efficiency is 10- to 20- fold higher than that of SARS-CoV, evidenced by Cryo-EM Structure of the SARS-CoV-2 Spike in the prefusion conformation [38]. For SARS-CoV, the cleavage of trimer S protein is triggered by the cell surface-associated transmembrane protease serine 2 (TMPRSS2) [39] and cathepsin [40], while the possible molecules facilitated membrane invagination for SARS-CoV-2 endocytosis are still unclear. Up to the date this review paper was prepared, reports showed that the SARS-CoV-2 may readily transmit, while cause less serious human infection rather than human SARS-CoV. Based on the latest WHO report, the number of infected people (over 80,000 globally, updated on 1 March 2020). The global outbreak may due to the following factors: firstly, the unknown pneumonia outbroke at the time of China Spring Festival, when the mass population flowing. Secondly, more detailed molecular mechanisms of viral binding and entry manners await to be elucidated, which may hamper the development of targeted therapy. Thirdly, available data suggested that the SARS-CoV-2 may be less virulent than the SARS-CoV and MERS-CoV, with the currently analyzed mortality of COVID-19 is 3.4%, lower than death rate of SARS (9.6%) and MERS (around 35%), respectively [19]. Thus, the potential mechanisms for human-to-human transmission and pathogenic mechanisms of the SARS-CoV-2 are under extensively studied."}

PMC:7068984 / 10719-14020 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7068984 / 10719-14020 JSON TXT