PMC:7556165 / 71123-72259
Annnotations
LitCovid-sample-CHEBI
{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T195","span":{"begin":120,"end":127},"obj":"Chemical"},{"id":"T196","span":{"begin":334,"end":341},"obj":"Chemical"}],"attributes":[{"id":"A195","pred":"chebi_id","subj":"T195","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A196","pred":"chebi_id","subj":"T196","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-PD-NCBITaxon
{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T397","span":{"begin":12,"end":17},"obj":"Species"},{"id":"T398","span":{"begin":272,"end":280},"obj":"Species"},{"id":"T399","span":{"begin":652,"end":662},"obj":"Species"},{"id":"T400","span":{"begin":652,"end":656},"obj":"Species"},{"id":"T401","span":{"begin":688,"end":693},"obj":"Species"},{"id":"T402","span":{"begin":721,"end":726},"obj":"Species"},{"id":"T403","span":{"begin":882,"end":892},"obj":"Species"},{"id":"T404","span":{"begin":882,"end":886},"obj":"Species"},{"id":"T405","span":{"begin":989,"end":999},"obj":"Species"},{"id":"T406","span":{"begin":989,"end":993},"obj":"Species"}],"attributes":[{"id":"A397","pred":"ncbi_taxonomy_id","subj":"T397","obj":"NCBItxid:9606"},{"id":"A405","pred":"ncbi_taxonomy_id","subj":"T405","obj":"NCBItxid:2697049"},{"id":"A406","pred":"ncbi_taxonomy_id","subj":"T406","obj":"NCBItxid:694009"},{"id":"A403","pred":"ncbi_taxonomy_id","subj":"T403","obj":"NCBItxid:2697049"},{"id":"A399","pred":"ncbi_taxonomy_id","subj":"T399","obj":"NCBItxid:2697049"},{"id":"A401","pred":"ncbi_taxonomy_id","subj":"T401","obj":"NCBItxid:9606"},{"id":"A400","pred":"ncbi_taxonomy_id","subj":"T400","obj":"NCBItxid:694009"},{"id":"A404","pred":"ncbi_taxonomy_id","subj":"T404","obj":"NCBItxid:694009"},{"id":"A402","pred":"ncbi_taxonomy_id","subj":"T402","obj":"NCBItxid:9606"},{"id":"A398","pred":"ncbi_taxonomy_id","subj":"T398","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-sentences
{"project":"LitCovid-sample-sentences","denotations":[{"id":"T421","span":{"begin":0,"end":204},"obj":"Sentence"},{"id":"T422","span":{"begin":205,"end":560},"obj":"Sentence"},{"id":"T423","span":{"begin":561,"end":767},"obj":"Sentence"},{"id":"T424","span":{"begin":768,"end":929},"obj":"Sentence"},{"id":"T425","span":{"begin":930,"end":1136},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-PD-UBERON
{"project":"LitCovid-sample-PD-UBERON","denotations":[{"id":"T151","span":{"begin":694,"end":706},"obj":"Body_part"},{"id":"T152","span":{"begin":727,"end":733},"obj":"Body_part"}],"attributes":[{"id":"A151","pred":"uberon_id","subj":"T151","obj":"http://purl.obolibrary.org/obo/UBERON_0001981"},{"id":"A152","pred":"uberon_id","subj":"T152","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-Pubtator
{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"1960","span":{"begin":118,"end":127},"obj":"Gene"},{"id":"1961","span":{"begin":820,"end":825},"obj":"Gene"},{"id":"1962","span":{"begin":973,"end":977},"obj":"Gene"},{"id":"1963","span":{"begin":1087,"end":1091},"obj":"Gene"},{"id":"1965","span":{"begin":281,"end":289},"obj":"Species"},{"id":"1966","span":{"begin":521,"end":529},"obj":"Species"},{"id":"1967","span":{"begin":688,"end":693},"obj":"Species"},{"id":"1968","span":{"begin":721,"end":726},"obj":"Species"},{"id":"1969","span":{"begin":882,"end":892},"obj":"Species"},{"id":"1970","span":{"begin":989,"end":999},"obj":"Species"},{"id":"1971","span":{"begin":415,"end":421},"obj":"Chemical"},{"id":"1972","span":{"begin":601,"end":607},"obj":"Chemical"},{"id":"1973","span":{"begin":272,"end":280},"obj":"Disease"},{"id":"1974","span":{"begin":535,"end":539},"obj":"Disease"},{"id":"1975","span":{"begin":652,"end":673},"obj":"Disease"}],"attributes":[{"id":"A1965","pred":"pubann:denotes","subj":"1965","obj":"Tax:9606"},{"id":"A1961","pred":"pubann:denotes","subj":"1961","obj":"Gene:59272"},{"id":"A1963","pred":"pubann:denotes","subj":"1963","obj":"Gene:59272"},{"id":"A1968","pred":"pubann:denotes","subj":"1968","obj":"Tax:9606"},{"id":"A1973","pred":"pubann:denotes","subj":"1973","obj":"MESH:C000657245"},{"id":"A1969","pred":"pubann:denotes","subj":"1969","obj":"Tax:2697049"},{"id":"A1975","pred":"pubann:denotes","subj":"1975","obj":"MESH:C000657245"},{"id":"A1962","pred":"pubann:denotes","subj":"1962","obj":"Gene:59272"},{"id":"A1967","pred":"pubann:denotes","subj":"1967","obj":"Tax:9606"},{"id":"A1970","pred":"pubann:denotes","subj":"1970","obj":"Tax:2697049"},{"id":"A1960","pred":"pubann:denotes","subj":"1960","obj":"Gene:43740568"},{"id":"A1966","pred":"pubann:denotes","subj":"1966","obj":"Tax:9606"},{"id":"A1974","pred":"pubann:denotes","subj":"1974","obj":"MESH:D012128"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-UniProt
{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T6198","span":{"begin":18,"end":21},"obj":"Protein"},{"id":"T6223","span":{"begin":118,"end":127},"obj":"Protein"},{"id":"T6234","span":{"begin":893,"end":896},"obj":"Protein"},{"id":"T6243","span":{"begin":973,"end":977},"obj":"Protein"},{"id":"T6244","span":{"begin":1000,"end":1003},"obj":"Protein"},{"id":"T6253","span":{"begin":1087,"end":1091},"obj":"Protein"}],"attributes":[{"id":"A6198","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q9GLN7"},{"id":"A6199","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q9GLN6"},{"id":"A6200","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q9EQM9"},{"id":"A6201","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q8CFN1"},{"id":"A6202","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q7TMC6"},{"id":"A6203","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q7M4L4"},{"id":"A6204","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q6GTS2"},{"id":"A6205","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q59GY8"},{"id":"A6206","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q53YX9"},{"id":"A6207","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q50JE5"},{"id":"A6208","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q10751"},{"id":"A6209","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q0GA41"},{"id":"A6210","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P47820"},{"id":"A6211","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P22968"},{"id":"A6212","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P22967"},{"id":"A6213","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P22966"},{"id":"A6214","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P12822"},{"id":"A6215","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P12821"},{"id":"A6216","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P12820"},{"id":"A6217","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/P09470"},{"id":"A6218","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/O02852"},{"id":"A6219","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/E7EU16"},{"id":"A6220","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/B4DXI3"},{"id":"A6221","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/B0LPF0"},{"id":"A6222","pred":"uniprot_id","subj":"T6198","obj":"https://www.uniprot.org/uniprot/Q9VJV3"},{"id":"A6223","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/Q9D080"},{"id":"A6224","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/Q9BSH7"},{"id":"A6225","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/Q91X32"},{"id":"A6226","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/Q8VII4"},{"id":"A6227","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/Q5SYG4"},{"id":"A6228","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/P48819"},{"id":"A6229","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/P29788"},{"id":"A6230","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/P22458"},{"id":"A6231","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/P04004"},{"id":"A6232","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/P01141"},{"id":"A6233","pred":"uniprot_id","subj":"T6223","obj":"https://www.uniprot.org/uniprot/B2R7G0"},{"id":"A6234","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/Q63492"},{"id":"A6235","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/Q63491"},{"id":"A6236","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/Q62815"},{"id":"A6237","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/Q62691"},{"id":"A6238","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/Q01542"},{"id":"A6239","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/P27732"},{"id":"A6240","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/O09024"},{"id":"A6241","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/O09023"},{"id":"A6242","pred":"uniprot_id","subj":"T6234","obj":"https://www.uniprot.org/uniprot/O09022"},{"id":"A6243","pred":"uniprot_id","subj":"T6243","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"},{"id":"A6244","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/Q63492"},{"id":"A6245","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/Q63491"},{"id":"A6246","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/Q62815"},{"id":"A6247","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/Q62691"},{"id":"A6248","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/Q01542"},{"id":"A6249","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/P27732"},{"id":"A6250","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/O09024"},{"id":"A6251","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/O09023"},{"id":"A6252","pred":"uniprot_id","subj":"T6244","obj":"https://www.uniprot.org/uniprot/O09022"},{"id":"A6253","pred":"uniprot_id","subj":"T6253","obj":"https://www.uniprot.org/uniprot/Q9UFZ6"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-PD-IDO
{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T290","span":{"begin":143,"end":147},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T291","span":{"begin":663,"end":676},"obj":"http://purl.obolibrary.org/obo/IDO_0000586"},{"id":"T292","span":{"begin":694,"end":699},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"T293","span":{"begin":913,"end":917},"obj":"http://purl.obolibrary.org/obo/CL_0000000"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-PD-FMA
{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T458","span":{"begin":120,"end":127},"obj":"Body_part"},{"id":"T459","span":{"begin":334,"end":341},"obj":"Body_part"},{"id":"T460","span":{"begin":694,"end":706},"obj":"Body_part"},{"id":"T461","span":{"begin":727,"end":733},"obj":"Body_part"},{"id":"T462","span":{"begin":913,"end":917},"obj":"Body_part"}],"attributes":[{"id":"A458","pred":"fma_id","subj":"T458","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A459","pred":"fma_id","subj":"T459","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A460","pred":"fma_id","subj":"T460","obj":"http://purl.org/sig/ont/fma/fma63183"},{"id":"A461","pred":"fma_id","subj":"T461","obj":"http://purl.org/sig/ont/fma/fma7203"},{"id":"A462","pred":"fma_id","subj":"T462","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-PD-MONDO
{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T420","span":{"begin":272,"end":280},"obj":"Disease"},{"id":"T421","span":{"begin":535,"end":539},"obj":"Disease"},{"id":"T422","span":{"begin":652,"end":662},"obj":"Disease"},{"id":"T423","span":{"begin":652,"end":656},"obj":"Disease"},{"id":"T424","span":{"begin":663,"end":676},"obj":"Disease"},{"id":"T425","span":{"begin":882,"end":892},"obj":"Disease"},{"id":"T426","span":{"begin":882,"end":886},"obj":"Disease"},{"id":"T427","span":{"begin":989,"end":999},"obj":"Disease"},{"id":"T428","span":{"begin":989,"end":993},"obj":"Disease"}],"attributes":[{"id":"A423","pred":"mondo_id","subj":"T423","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A426","pred":"mondo_id","subj":"T426","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A422","pred":"mondo_id","subj":"T422","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A428","pred":"mondo_id","subj":"T428","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A424","pred":"mondo_id","subj":"T424","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A421","pred":"mondo_id","subj":"T421","obj":"http://purl.obolibrary.org/obo/MONDO_0006502"},{"id":"A427","pred":"mondo_id","subj":"T427","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A425","pred":"mondo_id","subj":"T425","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A420","pred":"mondo_id","subj":"T420","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sample-PD-MAT
{"project":"LitCovid-sample-PD-MAT","denotations":[{"id":"T137","span":{"begin":694,"end":706},"obj":"http://purl.obolibrary.org/obo/MAT_0000393"},{"id":"T138","span":{"begin":694,"end":699},"obj":"http://purl.obolibrary.org/obo/MAT_0000083"},{"id":"T139","span":{"begin":694,"end":699},"obj":"http://purl.obolibrary.org/obo/MAT_0000315"},{"id":"T140","span":{"begin":727,"end":733},"obj":"http://purl.obolibrary.org/obo/MAT_0000119"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-PubTator
{"project":"LitCovid-PubTator","denotations":[{"id":"1959","span":{"begin":18,"end":23},"obj":"Gene"},{"id":"1960","span":{"begin":118,"end":127},"obj":"Gene"},{"id":"1961","span":{"begin":820,"end":825},"obj":"Gene"},{"id":"1962","span":{"begin":973,"end":977},"obj":"Gene"},{"id":"1963","span":{"begin":1087,"end":1091},"obj":"Gene"},{"id":"1964","span":{"begin":12,"end":17},"obj":"Species"},{"id":"1965","span":{"begin":281,"end":289},"obj":"Species"},{"id":"1966","span":{"begin":521,"end":529},"obj":"Species"},{"id":"1967","span":{"begin":688,"end":693},"obj":"Species"},{"id":"1968","span":{"begin":721,"end":726},"obj":"Species"},{"id":"1969","span":{"begin":882,"end":892},"obj":"Species"},{"id":"1970","span":{"begin":989,"end":999},"obj":"Species"},{"id":"1971","span":{"begin":415,"end":421},"obj":"Chemical"},{"id":"1972","span":{"begin":601,"end":607},"obj":"Chemical"},{"id":"1973","span":{"begin":272,"end":280},"obj":"Disease"},{"id":"1974","span":{"begin":535,"end":539},"obj":"Disease"},{"id":"1975","span":{"begin":652,"end":673},"obj":"Disease"}],"attributes":[{"id":"A1959","pred":"tao:has_database_id","subj":"1959","obj":"Gene:59272"},{"id":"A1960","pred":"tao:has_database_id","subj":"1960","obj":"Gene:43740568"},{"id":"A1961","pred":"tao:has_database_id","subj":"1961","obj":"Gene:59272"},{"id":"A1962","pred":"tao:has_database_id","subj":"1962","obj":"Gene:59272"},{"id":"A1963","pred":"tao:has_database_id","subj":"1963","obj":"Gene:59272"},{"id":"A1964","pred":"tao:has_database_id","subj":"1964","obj":"Tax:9606"},{"id":"A1965","pred":"tao:has_database_id","subj":"1965","obj":"Tax:9606"},{"id":"A1966","pred":"tao:has_database_id","subj":"1966","obj":"Tax:9606"},{"id":"A1967","pred":"tao:has_database_id","subj":"1967","obj":"Tax:9606"},{"id":"A1968","pred":"tao:has_database_id","subj":"1968","obj":"Tax:9606"},{"id":"A1969","pred":"tao:has_database_id","subj":"1969","obj":"Tax:2697049"},{"id":"A1970","pred":"tao:has_database_id","subj":"1970","obj":"Tax:2697049"},{"id":"A1973","pred":"tao:has_database_id","subj":"1973","obj":"MESH:C000657245"},{"id":"A1974","pred":"tao:has_database_id","subj":"1974","obj":"MESH:D012128"},{"id":"A1975","pred":"tao:has_database_id","subj":"1975","obj":"MESH:C000657245"}],"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":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}
LitCovid-sentences
{"project":"LitCovid-sentences","denotations":[{"id":"T421","span":{"begin":0,"end":204},"obj":"Sentence"},{"id":"T422","span":{"begin":205,"end":560},"obj":"Sentence"},{"id":"T423","span":{"begin":561,"end":767},"obj":"Sentence"},{"id":"T424","span":{"begin":768,"end":929},"obj":"Sentence"},{"id":"T425","span":{"begin":930,"end":1136},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Recombinant human ACE 2, rhACE2 (hrsACE2, APN01, GSK2586881), sequesters circulating viral particles interfering with S-protein binding to its host target, beside its role in regulating the systemic RAAS. Taken together, these activities may offer therapeutic benefits in COVID-19 patients, although the large molecular weight of the protein may potentially limit its effects on local RAAS (Gheblawi et al., 2020). rhACE2 has already undergone phase 1 and 2 clinical trials in healthy volunteers and in a small cohort of patients with ARDS (Khan et al., 2017). Moreover, it has been demonstrated that rhACE2 can significantly block the early stages of SARS-CoV-2 infections in engineered human blood vessel organoids and human kidney organoids (Monteil et al., 2020). In this context, Procko (2020) was able to engineer hACE2 sequences to obtain soluble receptors able to sequester SARS-CoV-2 RBD and inhibit its cell attachment. Remarkably, combinatorial mutants enhanced ACE2 binding to SARS-CoV-2 RBD by an order of magnitude, as compared to the wild type receptor form, and targeted ACE2 mutations might provide further improvement."}