PMC:7271924 / 6793-7930 JSONTXT

{"project":"LitCovid-PMC-OGER-BB","denotations":[{"id":"T126","span":{"begin":11,"end":22},"obj":"NCBITaxon:1"},{"id":"T127","span":{"begin":40,"end":53},"obj":"GO:0005622"},{"id":"T128","span":{"begin":58,"end":69},"obj":"GO:0051235"},{"id":"T129","span":{"begin":107,"end":118},"obj":"CHEBI:4056;CHEBI:4056"},{"id":"T130","span":{"begin":180,"end":192},"obj":"CL:0000232"},{"id":"T131","span":{"begin":231,"end":242},"obj":"PR:000016261"},{"id":"T132","span":{"begin":258,"end":270},"obj":"CL:0000232"},{"id":"T133","span":{"begin":271,"end":275},"obj":"GO:0019835"},{"id":"T134","span":{"begin":424,"end":429},"obj":"UBERON:0001977"},{"id":"T135","span":{"begin":538,"end":549},"obj":"CHEBI:30808;CHEBI:30808"},{"id":"T136","span":{"begin":614,"end":625},"obj":"CHEBI:30808;CHEBI:30808"},{"id":"T137","span":{"begin":709,"end":717},"obj":"CHEBI:29191;CHEBI:29191"},{"id":"T138","span":{"begin":718,"end":726},"obj":"CHEBI:26519;CHEBI:26519"},{"id":"T139","span":{"begin":774,"end":782},"obj":"NCBITaxon:2"},{"id":"T140","span":{"begin":834,"end":842},"obj":"NCBITaxon:2"},{"id":"T141","span":{"begin":862,"end":874},"obj":"GO:0051235"},{"id":"T142","span":{"begin":919,"end":939},"obj":"NCBITaxon:139"},{"id":"T11033","span":{"begin":11,"end":22},"obj":"NCBITaxon:1"},{"id":"T96899","span":{"begin":40,"end":53},"obj":"GO:0005622"},{"id":"T45353","span":{"begin":58,"end":69},"obj":"GO:0051235"},{"id":"T6528","span":{"begin":107,"end":118},"obj":"CHEBI:4056;CHEBI:4056"},{"id":"T45565","span":{"begin":180,"end":192},"obj":"CL:0000232"},{"id":"T26527","span":{"begin":231,"end":242},"obj":"PR:000016261"},{"id":"T21144","span":{"begin":258,"end":270},"obj":"CL:0000232"},{"id":"T23591","span":{"begin":271,"end":275},"obj":"GO:0019835"},{"id":"T8872","span":{"begin":424,"end":429},"obj":"UBERON:0001977"},{"id":"T84052","span":{"begin":538,"end":549},"obj":"CHEBI:30808;CHEBI:30808"},{"id":"T54713","span":{"begin":614,"end":625},"obj":"CHEBI:30808;CHEBI:30808"},{"id":"T9722","span":{"begin":709,"end":717},"obj":"CHEBI:29191;CHEBI:29191"},{"id":"T47741","span":{"begin":718,"end":726},"obj":"CHEBI:26519;CHEBI:26519"},{"id":"T2039","span":{"begin":774,"end":782},"obj":"NCBITaxon:2"},{"id":"T61995","span":{"begin":834,"end":842},"obj":"NCBITaxon:2"},{"id":"T84319","span":{"begin":862,"end":874},"obj":"GO:0051235"},{"id":"T34249","span":{"begin":919,"end":939},"obj":"NCBITaxon:139"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-PubTator","denotations":[{"id":"193","span":{"begin":231,"end":242},"obj":"Gene"},{"id":"194","span":{"begin":631,"end":644},"obj":"Gene"},{"id":"195","span":{"begin":648,"end":659},"obj":"Gene"},{"id":"196","span":{"begin":365,"end":376},"obj":"Gene"},{"id":"197","span":{"begin":390,"end":399},"obj":"Gene"},{"id":"198","span":{"begin":492,"end":505},"obj":"Gene"},{"id":"199","span":{"begin":919,"end":939},"obj":"Species"},{"id":"200","span":{"begin":24,"end":28},"obj":"Chemical"},{"id":"201","span":{"begin":206,"end":210},"obj":"Chemical"},{"id":"202","span":{"begin":538,"end":549},"obj":"Chemical"},{"id":"203","span":{"begin":614,"end":625},"obj":"Chemical"},{"id":"204","span":{"begin":709,"end":726},"obj":"Chemical"},{"id":"205","span":{"begin":755,"end":759},"obj":"Chemical"},{"id":"206","span":{"begin":875,"end":879},"obj":"Chemical"},{"id":"207","span":{"begin":123,"end":135},"obj":"Disease"}],"attributes":[{"id":"A193","pred":"tao:has_database_id","subj":"193","obj":"Gene:7018"},{"id":"A194","pred":"tao:has_database_id","subj":"194","obj":"Gene:1356"},{"id":"A195","pred":"tao:has_database_id","subj":"195","obj":"Gene:280846"},{"id":"A196","pred":"tao:has_database_id","subj":"196","obj":"Gene:3240"},{"id":"A197","pred":"tao:has_database_id","subj":"197","obj":"Gene:3263"},{"id":"A198","pred":"tao:has_database_id","subj":"198","obj":"Gene:1356"},{"id":"A199","pred":"tao:has_database_id","subj":"199","obj":"Tax:139"},{"id":"A200","pred":"tao:has_database_id","subj":"200","obj":"MESH:D007501"},{"id":"A201","pred":"tao:has_database_id","subj":"201","obj":"MESH:D007501"},{"id":"A204","pred":"tao:has_database_id","subj":"204","obj":"MESH:D017665"},{"id":"A205","pred":"tao:has_database_id","subj":"205","obj":"MESH:D007501"},{"id":"A206","pred":"tao:has_database_id","subj":"206","obj":"MESH:D007501"},{"id":"A207","pred":"tao:has_database_id","subj":"207","obj":"MESH:D018455"}],"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":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T50","span":{"begin":127,"end":135},"obj":"Body_part"},{"id":"T51","span":{"begin":162,"end":172},"obj":"Body_part"},{"id":"T52","span":{"begin":180,"end":192},"obj":"Body_part"},{"id":"T53","span":{"begin":258,"end":270},"obj":"Body_part"},{"id":"T54","span":{"begin":280,"end":290},"obj":"Body_part"},{"id":"T55","span":{"begin":339,"end":349},"obj":"Body_part"},{"id":"T56","span":{"begin":424,"end":429},"obj":"Body_part"},{"id":"T57","span":{"begin":566,"end":574},"obj":"Body_part"}],"attributes":[{"id":"A50","pred":"fma_id","subj":"T50","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A51","pred":"fma_id","subj":"T51","obj":"http://purl.org/sig/ont/fma/fma62293"},{"id":"A52","pred":"fma_id","subj":"T52","obj":"http://purl.org/sig/ont/fma/fma62845"},{"id":"A53","pred":"fma_id","subj":"T53","obj":"http://purl.org/sig/ont/fma/fma62845"},{"id":"A54","pred":"fma_id","subj":"T54","obj":"http://purl.org/sig/ont/fma/fma62293"},{"id":"A55","pred":"fma_id","subj":"T55","obj":"http://purl.org/sig/ont/fma/fma62293"},{"id":"A56","pred":"fma_id","subj":"T56","obj":"http://purl.org/sig/ont/fma/fma63083"},{"id":"A57","pred":"fma_id","subj":"T57","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T16","span":{"begin":424,"end":429},"obj":"Body_part"}],"attributes":[{"id":"A16","pred":"uberon_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T17","span":{"begin":919,"end":927},"obj":"Disease"}],"attributes":[{"id":"A17","pred":"mondo_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/MONDO_0019632"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T74","span":{"begin":92,"end":93},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T75","span":{"begin":180,"end":192},"obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"T76","span":{"begin":258,"end":270},"obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"T77","span":{"begin":365,"end":376},"obj":"http://purl.obolibrary.org/obo/PR_000008725"},{"id":"T78","span":{"begin":442,"end":455},"obj":"http://purl.obolibrary.org/obo/PR_000005794"},{"id":"T79","span":{"begin":492,"end":505},"obj":"http://purl.obolibrary.org/obo/PR_000005794"},{"id":"T80","span":{"begin":517,"end":518},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T81","span":{"begin":593,"end":594},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T82","span":{"begin":631,"end":644},"obj":"http://purl.obolibrary.org/obo/PR_000005794"},{"id":"T83","span":{"begin":774,"end":782},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_2"},{"id":"T84","span":{"begin":834,"end":842},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_2"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T76","span":{"begin":24,"end":28},"obj":"Chemical"},{"id":"T77","span":{"begin":107,"end":118},"obj":"Chemical"},{"id":"T78","span":{"begin":127,"end":135},"obj":"Chemical"},{"id":"T79","span":{"begin":144,"end":148},"obj":"Chemical"},{"id":"T80","span":{"begin":162,"end":172},"obj":"Chemical"},{"id":"T81","span":{"begin":206,"end":210},"obj":"Chemical"},{"id":"T82","span":{"begin":280,"end":290},"obj":"Chemical"},{"id":"T83","span":{"begin":294,"end":298},"obj":"Chemical"},{"id":"T84","span":{"begin":339,"end":349},"obj":"Chemical"},{"id":"T85","span":{"begin":382,"end":386},"obj":"Chemical"},{"id":"T86","span":{"begin":477,"end":479},"obj":"Chemical"},{"id":"T87","span":{"begin":538,"end":549},"obj":"Chemical"},{"id":"T88","span":{"begin":545,"end":549},"obj":"Chemical"},{"id":"T89","span":{"begin":566,"end":574},"obj":"Chemical"},{"id":"T90","span":{"begin":614,"end":625},"obj":"Chemical"},{"id":"T91","span":{"begin":621,"end":625},"obj":"Chemical"},{"id":"T92","span":{"begin":709,"end":717},"obj":"Chemical"},{"id":"T94","span":{"begin":718,"end":726},"obj":"Chemical"},{"id":"T95","span":{"begin":755,"end":759},"obj":"Chemical"},{"id":"T96","span":{"begin":784,"end":786},"obj":"Chemical"},{"id":"T97","span":{"begin":875,"end":879},"obj":"Chemical"},{"id":"T98","span":{"begin":986,"end":988},"obj":"Chemical"},{"id":"T99","span":{"begin":1002,"end":1011},"obj":"Chemical"}],"attributes":[{"id":"A76","pred":"chebi_id","subj":"T76","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A77","pred":"chebi_id","subj":"T77","obj":"http://purl.obolibrary.org/obo/CHEBI_4056"},{"id":"A78","pred":"chebi_id","subj":"T78","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A79","pred":"chebi_id","subj":"T79","obj":"http://purl.obolibrary.org/obo/CHEBI_30413"},{"id":"A80","pred":"chebi_id","subj":"T80","obj":"http://purl.obolibrary.org/obo/CHEBI_35143"},{"id":"A81","pred":"chebi_id","subj":"T81","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A82","pred":"chebi_id","subj":"T82","obj":"http://purl.obolibrary.org/obo/CHEBI_35143"},{"id":"A83","pred":"chebi_id","subj":"T83","obj":"http://purl.obolibrary.org/obo/CHEBI_30413"},{"id":"A84","pred":"chebi_id","subj":"T84","obj":"http://purl.obolibrary.org/obo/CHEBI_35143"},{"id":"A85","pred":"chebi_id","subj":"T85","obj":"http://purl.obolibrary.org/obo/CHEBI_30413"},{"id":"A86","pred":"chebi_id","subj":"T86","obj":"http://purl.obolibrary.org/obo/CHEBI_73585"},{"id":"A87","pred":"chebi_id","subj":"T87","obj":"http://purl.obolibrary.org/obo/CHEBI_29034"},{"id":"A88","pred":"chebi_id","subj":"T88","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A89","pred":"chebi_id","subj":"T89","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A90","pred":"chebi_id","subj":"T90","obj":"http://purl.obolibrary.org/obo/CHEBI_29034"},{"id":"A91","pred":"chebi_id","subj":"T91","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A92","pred":"chebi_id","subj":"T92","obj":"http://purl.obolibrary.org/obo/CHEBI_29191"},{"id":"A93","pred":"chebi_id","subj":"T92","obj":"http://purl.obolibrary.org/obo/CHEBI_43176"},{"id":"A94","pred":"chebi_id","subj":"T94","obj":"http://purl.obolibrary.org/obo/CHEBI_26519"},{"id":"A95","pred":"chebi_id","subj":"T95","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A96","pred":"chebi_id","subj":"T96","obj":"http://purl.obolibrary.org/obo/CHEBI_73585"},{"id":"A97","pred":"chebi_id","subj":"T97","obj":"http://purl.obolibrary.org/obo/CHEBI_18248"},{"id":"A98","pred":"chebi_id","subj":"T98","obj":"http://purl.obolibrary.org/obo/CHEBI_73585"},{"id":"A99","pred":"chebi_id","subj":"T99","obj":"http://purl.obolibrary.org/obo/CHEBI_59163"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T6","span":{"begin":40,"end":69},"obj":"http://purl.obolibrary.org/obo/GO_0051651"},{"id":"T7","span":{"begin":107,"end":118},"obj":"http://purl.obolibrary.org/obo/GO_0045158"},{"id":"T8","span":{"begin":107,"end":118},"obj":"http://purl.obolibrary.org/obo/GO_0045157"},{"id":"T9","span":{"begin":107,"end":118},"obj":"http://purl.obolibrary.org/obo/GO_0045156"},{"id":"T10","span":{"begin":107,"end":118},"obj":"http://purl.obolibrary.org/obo/GO_0008121"},{"id":"T11","span":{"begin":678,"end":687},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T12","span":{"begin":862,"end":874},"obj":"http://purl.obolibrary.org/obo/GO_0051235"},{"id":"T13","span":{"begin":964,"end":970},"obj":"http://purl.obolibrary.org/obo/GO_0040007"},{"id":"T14","span":{"begin":975,"end":984},"obj":"http://purl.obolibrary.org/obo/GO_0016032"},{"id":"T15","span":{"begin":975,"end":984},"obj":"http://purl.obolibrary.org/obo/GO_0009405"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"LitCovid-sentences","denotations":[{"id":"T49","span":{"begin":0,"end":193},"obj":"Sentence"},{"id":"T50","span":{"begin":194,"end":252},"obj":"Sentence"},{"id":"T51","span":{"begin":253,"end":405},"obj":"Sentence"},{"id":"T52","span":{"begin":406,"end":592},"obj":"Sentence"},{"id":"T53","span":{"begin":593,"end":783},"obj":"Sentence"},{"id":"T54","span":{"begin":784,"end":985},"obj":"Sentence"},{"id":"T55","span":{"begin":986,"end":1100},"obj":"Sentence"},{"id":"T56","span":{"begin":1101,"end":1137},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"MyTest","denotations":[{"id":"32574271-19133145-34514583","span":{"begin":244,"end":246},"obj":"19133145"},{"id":"32574271-24549403-34514584","span":{"begin":248,"end":250},"obj":"24549403"},{"id":"32574271-20711357-34514585","span":{"begin":401,"end":403},"obj":"20711357"},{"id":"32574271-22040722-34514586","span":{"begin":588,"end":590},"obj":"22040722"},{"id":"32574271-29575574-34514587","span":{"begin":728,"end":730},"obj":"29575574"},{"id":"32574271-10834845-34514588","span":{"begin":941,"end":943},"obj":"10834845"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"TEST0","denotations":[{"id":"32574271-50-56-2882175","span":{"begin":244,"end":246},"obj":"[\"19133145\"]"},{"id":"32574271-54-60-2882176","span":{"begin":248,"end":250},"obj":"[\"24549403\"]"},{"id":"32574271-148-154-2882177","span":{"begin":401,"end":403},"obj":"[\"20711357\"]"},{"id":"32574271-182-188-2882178","span":{"begin":588,"end":590},"obj":"[\"22040722\"]"},{"id":"32574271-135-141-2882179","span":{"begin":728,"end":730},"obj":"[\"29575574\"]"},{"id":"32574271-157-163-2882180","span":{"begin":941,"end":943},"obj":"[\"10834845\"]"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}

{"project":"2_test","denotations":[{"id":"32574271-19133145-34514583","span":{"begin":244,"end":246},"obj":"19133145"},{"id":"32574271-24549403-34514584","span":{"begin":248,"end":250},"obj":"24549403"},{"id":"32574271-20711357-34514585","span":{"begin":401,"end":403},"obj":"20711357"},{"id":"32574271-22040722-34514586","span":{"begin":588,"end":590},"obj":"22040722"},{"id":"32574271-29575574-34514587","span":{"begin":728,"end":730},"obj":"29575574"},{"id":"32574271-10834845-34514588","span":{"begin":941,"end":943},"obj":"10834845"}],"text":"In healthy individuals, iron is largely intracellular and sequestered within ferritin or as a co-factor of cytochromes and FeS proteins, and as haem complexed to hemoglobin within erythrocytes. Circulating iron is rapidly bound by transferrin (28, 29). When erythrocytes lyse and hemoglobin or haem is released into the circulation, their hemoglobin is captured by haptoglobin, and haem by hemopexin (30). Here, circulating serum ferroxidase ceruloplasmin is of importance, as LF can bind to ceruloplasmin, such that a direct transfer of ferric iron between the two proteins is possible (31). A direct transfer of ferric iron from ceruloplasmin to lactoferrin prevents both the formation of potentially toxic hydroxyl radicals (32) and the utilization of iron by pathogenic bacteria. LF is therefore an important player in preventing bacteria from acquiring and sequestering iron, which [with the possible exception of Borrelia burgdorferi (33)]; they require for growth and virulence. LF also acts as biomarker, as it is commonly upregulated when the host is suffering from various kinds of disease. See Table 1 for selected references."}