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LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T397","span":{"begin":64,"end":69},"obj":"Body_part"},{"id":"T398","span":{"begin":368,"end":372},"obj":"Body_part"},{"id":"T399","span":{"begin":374,"end":379},"obj":"Body_part"},{"id":"T400","span":{"begin":506,"end":512},"obj":"Body_part"},{"id":"T401","span":{"begin":829,"end":834},"obj":"Body_part"},{"id":"T402","span":{"begin":922,"end":937},"obj":"Body_part"}],"attributes":[{"id":"A397","pred":"fma_id","subj":"T397","obj":"http://purl.org/sig/ont/fma/fma9670"},{"id":"A398","pred":"fma_id","subj":"T398","obj":"http://purl.org/sig/ont/fma/fma256135"},{"id":"A399","pred":"fma_id","subj":"T399","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A400","pred":"fma_id","subj":"T400","obj":"http://purl.org/sig/ont/fma/fma62970"},{"id":"A401","pred":"fma_id","subj":"T401","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A402","pred":"fma_id","subj":"T402","obj":"http://purl.org/sig/ont/fma/fma63841"}],"text":"CaNa2EDTA was approved by FDA in chelation therapy for lowering blood lead levels a long time ago (1953). Then, different (commercially available) iron chelating agents, expected to work in chelating zinc ion as well, were approved by FDA. Chelation therapy comprises intravenous or oral administration of chelating agents that remove metal ions such as zinc from the body. Cells synthesising high amounts of ACE or ACE2 needs of high amounts of bioavailable (free) zinc. Therefore, it is conceivable that plasma levels of free zinc may influence not only ACE and ACE2 activities but also their cellular synthesis. Indeed, both ACE and ACE2 synthesis might be particularly sensitive to reduction of free zinc levels in case of their upregulation. In addition, metal chelating agents, by limiting the availability of free zinc to cells, might have effects on both ACE2/ACE synthesis and conformation (when assembled on the plasma membrane). Indeed, the closed conformer of ACE2 homodimer that is the preferential conformation for virus binding [28], needs the presence of both zinc and substrate/inhibitor in the catalytic site [90], suggesting that zinc chelation (differently from MLN-4760) might also inhibit ACE2-mediated viral entry."}

LitCovid-PD-UBERON

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T133","span":{"begin":64,"end":69},"obj":"Body_part"}],"attributes":[{"id":"A133","pred":"uberon_id","subj":"T133","obj":"http://purl.obolibrary.org/obo/UBERON_0000178"}],"text":"CaNa2EDTA was approved by FDA in chelation therapy for lowering blood lead levels a long time ago (1953). Then, different (commercially available) iron chelating agents, expected to work in chelating zinc ion as well, were approved by FDA. Chelation therapy comprises intravenous or oral administration of chelating agents that remove metal ions such as zinc from the body. Cells synthesising high amounts of ACE or ACE2 needs of high amounts of bioavailable (free) zinc. Therefore, it is conceivable that plasma levels of free zinc may influence not only ACE and ACE2 activities but also their cellular synthesis. Indeed, both ACE and ACE2 synthesis might be particularly sensitive to reduction of free zinc levels in case of their upregulation. In addition, metal chelating agents, by limiting the availability of free zinc to cells, might have effects on both ACE2/ACE synthesis and conformation (when assembled on the plasma membrane). Indeed, the closed conformer of ACE2 homodimer that is the preferential conformation for virus binding [28], needs the presence of both zinc and substrate/inhibitor in the catalytic site [90], suggesting that zinc chelation (differently from MLN-4760) might also inhibit ACE2-mediated viral entry."}

LitCovid-PubTator

{"project":"LitCovid-PubTator","denotations":[{"id":"2267","span":{"begin":409,"end":412},"obj":"Gene"},{"id":"2268","span":{"begin":416,"end":420},"obj":"Gene"},{"id":"2269","span":{"begin":556,"end":559},"obj":"Gene"},{"id":"2270","span":{"begin":564,"end":568},"obj":"Gene"},{"id":"2271","span":{"begin":628,"end":631},"obj":"Gene"},{"id":"2272","span":{"begin":636,"end":640},"obj":"Gene"},{"id":"2273","span":{"begin":863,"end":867},"obj":"Gene"},{"id":"2274","span":{"begin":868,"end":871},"obj":"Gene"},{"id":"2275","span":{"begin":972,"end":976},"obj":"Gene"},{"id":"2276","span":{"begin":1211,"end":1215},"obj":"Gene"},{"id":"2277","span":{"begin":1182,"end":1185},"obj":"Gene"},{"id":"2278","span":{"begin":0,"end":9},"obj":"Chemical"},{"id":"2279","span":{"begin":147,"end":151},"obj":"Chemical"},{"id":"2280","span":{"begin":335,"end":340},"obj":"Chemical"},{"id":"2281","span":{"begin":760,"end":765},"obj":"Chemical"}],"attributes":[{"id":"A2267","pred":"tao:has_database_id","subj":"2267","obj":"Gene:59272"},{"id":"A2268","pred":"tao:has_database_id","subj":"2268","obj":"Gene:59272"},{"id":"A2269","pred":"tao:has_database_id","subj":"2269","obj":"Gene:59272"},{"id":"A2270","pred":"tao:has_database_id","subj":"2270","obj":"Gene:59272"},{"id":"A2271","pred":"tao:has_database_id","subj":"2271","obj":"Gene:59272"},{"id":"A2272","pred":"tao:has_database_id","subj":"2272","obj":"Gene:59272"},{"id":"A2273","pred":"tao:has_database_id","subj":"2273","obj":"Gene:59272"},{"id":"A2274","pred":"tao:has_database_id","subj":"2274","obj":"Gene:59272"},{"id":"A2275","pred":"tao:has_database_id","subj":"2275","obj":"Gene:59272"},{"id":"A2276","pred":"tao:has_database_id","subj":"2276","obj":"Gene:59272"},{"id":"A2277","pred":"tao:has_database_id","subj":"2277","obj":"Gene:4295"},{"id":"A2279","pred":"tao:has_database_id","subj":"2279","obj":"MESH:D007501"},{"id":"A2280","pred":"tao:has_database_id","subj":"2280","obj":"MESH:D008670"},{"id":"A2281","pred":"tao:has_database_id","subj":"2281","obj":"MESH:D008670"}],"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":"CaNa2EDTA was approved by FDA in chelation therapy for lowering blood lead levels a long time ago (1953). Then, different (commercially available) iron chelating agents, expected to work in chelating zinc ion as well, were approved by FDA. Chelation therapy comprises intravenous or oral administration of chelating agents that remove metal ions such as zinc from the body. Cells synthesising high amounts of ACE or ACE2 needs of high amounts of bioavailable (free) zinc. Therefore, it is conceivable that plasma levels of free zinc may influence not only ACE and ACE2 activities but also their cellular synthesis. Indeed, both ACE and ACE2 synthesis might be particularly sensitive to reduction of free zinc levels in case of their upregulation. In addition, metal chelating agents, by limiting the availability of free zinc to cells, might have effects on both ACE2/ACE synthesis and conformation (when assembled on the plasma membrane). Indeed, the closed conformer of ACE2 homodimer that is the preferential conformation for virus binding [28], needs the presence of both zinc and substrate/inhibitor in the catalytic site [90], suggesting that zinc chelation (differently from MLN-4760) might also inhibit ACE2-mediated viral entry."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T794","span":{"begin":64,"end":69},"obj":"http://purl.obolibrary.org/obo/UBERON_0000178"},{"id":"T795","span":{"begin":64,"end":69},"obj":"http://www.ebi.ac.uk/efo/EFO_0000296"},{"id":"T796","span":{"begin":82,"end":83},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T797","span":{"begin":374,"end":379},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T798","span":{"begin":506,"end":512},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T799","span":{"begin":569,"end":579},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T800","span":{"begin":829,"end":834},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T801","span":{"begin":922,"end":928},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T802","span":{"begin":929,"end":937},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T803","span":{"begin":1029,"end":1034},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"CaNa2EDTA was approved by FDA in chelation therapy for lowering blood lead levels a long time ago (1953). Then, different (commercially available) iron chelating agents, expected to work in chelating zinc ion as well, were approved by FDA. Chelation therapy comprises intravenous or oral administration of chelating agents that remove metal ions such as zinc from the body. Cells synthesising high amounts of ACE or ACE2 needs of high amounts of bioavailable (free) zinc. Therefore, it is conceivable that plasma levels of free zinc may influence not only ACE and ACE2 activities but also their cellular synthesis. Indeed, both ACE and ACE2 synthesis might be particularly sensitive to reduction of free zinc levels in case of their upregulation. In addition, metal chelating agents, by limiting the availability of free zinc to cells, might have effects on both ACE2/ACE synthesis and conformation (when assembled on the plasma membrane). Indeed, the closed conformer of ACE2 homodimer that is the preferential conformation for virus binding [28], needs the presence of both zinc and substrate/inhibitor in the catalytic site [90], suggesting that zinc chelation (differently from MLN-4760) might also inhibit ACE2-mediated viral entry."}

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T127","span":{"begin":595,"end":613},"obj":"http://purl.obolibrary.org/obo/GO_0044249"},{"id":"T128","span":{"begin":604,"end":613},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T129","span":{"begin":641,"end":650},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T130","span":{"begin":872,"end":881},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"CaNa2EDTA was approved by FDA in chelation therapy for lowering blood lead levels a long time ago (1953). Then, different (commercially available) iron chelating agents, expected to work in chelating zinc ion as well, were approved by FDA. Chelation therapy comprises intravenous or oral administration of chelating agents that remove metal ions such as zinc from the body. Cells synthesising high amounts of ACE or ACE2 needs of high amounts of bioavailable (free) zinc. Therefore, it is conceivable that plasma levels of free zinc may influence not only ACE and ACE2 activities but also their cellular synthesis. Indeed, both ACE and ACE2 synthesis might be particularly sensitive to reduction of free zinc levels in case of their upregulation. In addition, metal chelating agents, by limiting the availability of free zinc to cells, might have effects on both ACE2/ACE synthesis and conformation (when assembled on the plasma membrane). Indeed, the closed conformer of ACE2 homodimer that is the preferential conformation for virus binding [28], needs the presence of both zinc and substrate/inhibitor in the catalytic site [90], suggesting that zinc chelation (differently from MLN-4760) might also inhibit ACE2-mediated viral entry."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T303","span":{"begin":0,"end":105},"obj":"Sentence"},{"id":"T304","span":{"begin":106,"end":239},"obj":"Sentence"},{"id":"T305","span":{"begin":240,"end":373},"obj":"Sentence"},{"id":"T306","span":{"begin":374,"end":471},"obj":"Sentence"},{"id":"T307","span":{"begin":472,"end":614},"obj":"Sentence"},{"id":"T308","span":{"begin":615,"end":746},"obj":"Sentence"},{"id":"T309","span":{"begin":747,"end":939},"obj":"Sentence"},{"id":"T310","span":{"begin":940,"end":1237},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"CaNa2EDTA was approved by FDA in chelation therapy for lowering blood lead levels a long time ago (1953). Then, different (commercially available) iron chelating agents, expected to work in chelating zinc ion as well, were approved by FDA. Chelation therapy comprises intravenous or oral administration of chelating agents that remove metal ions such as zinc from the body. Cells synthesising high amounts of ACE or ACE2 needs of high amounts of bioavailable (free) zinc. Therefore, it is conceivable that plasma levels of free zinc may influence not only ACE and ACE2 activities but also their cellular synthesis. Indeed, both ACE and ACE2 synthesis might be particularly sensitive to reduction of free zinc levels in case of their upregulation. In addition, metal chelating agents, by limiting the availability of free zinc to cells, might have effects on both ACE2/ACE synthesis and conformation (when assembled on the plasma membrane). Indeed, the closed conformer of ACE2 homodimer that is the preferential conformation for virus binding [28], needs the presence of both zinc and substrate/inhibitor in the catalytic site [90], suggesting that zinc chelation (differently from MLN-4760) might also inhibit ACE2-mediated viral entry."}

2_test

{"project":"2_test","denotations":[{"id":"32708755-32132184-20678873","span":{"begin":1044,"end":1046},"obj":"32132184"}],"text":"CaNa2EDTA was approved by FDA in chelation therapy for lowering blood lead levels a long time ago (1953). Then, different (commercially available) iron chelating agents, expected to work in chelating zinc ion as well, were approved by FDA. Chelation therapy comprises intravenous or oral administration of chelating agents that remove metal ions such as zinc from the body. Cells synthesising high amounts of ACE or ACE2 needs of high amounts of bioavailable (free) zinc. Therefore, it is conceivable that plasma levels of free zinc may influence not only ACE and ACE2 activities but also their cellular synthesis. Indeed, both ACE and ACE2 synthesis might be particularly sensitive to reduction of free zinc levels in case of their upregulation. In addition, metal chelating agents, by limiting the availability of free zinc to cells, might have effects on both ACE2/ACE synthesis and conformation (when assembled on the plasma membrane). Indeed, the closed conformer of ACE2 homodimer that is the preferential conformation for virus binding [28], needs the presence of both zinc and substrate/inhibitor in the catalytic site [90], suggesting that zinc chelation (differently from MLN-4760) might also inhibit ACE2-mediated viral entry."}

PMC:7408073 / 63262-64499 JSONTXT

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PMC:7408073 / 63262-64499 JSON TXT