> top > docs > PMC:7228307 > spans > 33839-35482 > annotations

PMC:7228307 / 33839-35482 JSONTXT

Annnotations TAB JSON ListView MergeView

LitCovid_Glycan-Motif-Structure

Id Subject Object Predicate Lexical cue
T1 1349-1355 https://glytoucan.org/Structures/Glycans/G82576YO denotes fucose

LitCovid-PubTator

Id Subject Object Predicate Lexical cue tao:has_database_id
579 31-35 Gene denotes FcγR Gene:2213
583 183-188 Gene denotes FcγRI Gene:2214
584 131-135 Gene denotes FcγR Gene:2213
585 82-86 Gene denotes FcγR Gene:2213
588 311-315 Gene denotes FcγR Gene:2213
589 352-357 Species denotes human Tax:9606
602 617-622 Gene denotes FcγRI Gene:2214
603 634-641 Gene denotes FcγRIII Gene:2214
604 1289-1297 Gene denotes FcγRIIIa Gene:2214
605 624-630 Gene denotes FcγRII Gene:2214
606 1165-1169 Gene denotes FcγR Gene:2213
607 761-765 Gene denotes FcγR Gene:2213
608 588-593 Species denotes human Tax:9606
609 959-974 Chemical denotes N‐linked glycan
610 978-988 Chemical denotes asparagine MESH:D001216
611 994-998 Chemical denotes N297
612 1349-1355 Chemical denotes fucose MESH:D005643
613 1373-1388 Chemical denotes oligosaccharide MESH:D009844
617 1467-1471 Gene denotes FcγR Gene:2213
618 1638-1642 Gene denotes FcγR Gene:2213
619 1515-1519 Gene denotes FcγR Gene:2213

LitCovid-PD-FMA-UBERON

Id Subject Object Predicate Lexical cue fma_id
T328 23-26 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T329 245-248 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T330 288-291 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T331 499-502 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T332 1068-1071 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T333 1268-1271 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T334 1349-1355 Body_part denotes fucose http://purl.org/sig/ont/fma/fma82790
T335 1373-1388 Body_part denotes oligosaccharide http://purl.org/sig/ont/fma/fma82742

LitCovid-PD-CLO

Id Subject Object Predicate Lexical cue
T653 31-33 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T654 82-84 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T655 131-133 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T656 136-139 http://purl.obolibrary.org/obo/CLO_0051582 denotes has
T657 183-185 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T658 189-192 http://purl.obolibrary.org/obo/CLO_0051582 denotes has
T659 193-194 http://purl.obolibrary.org/obo/CLO_0001020 denotes a
T660 311-313 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T661 352-357 http://purl.obolibrary.org/obo/NCBITaxon_9606 denotes human
T662 548-550 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T663 551-553 http://purl.obolibrary.org/obo/CLO_0008882 denotes Rs
T664 588-593 http://purl.obolibrary.org/obo/NCBITaxon_9606 denotes human
T665 599-601 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T666 617-619 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T667 624-626 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T668 634-636 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T669 761-763 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T670 1072-1074 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T671 1165-1167 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T672 1289-1291 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T673 1370-1372 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T674 1448-1450 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T675 1467-1469 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T676 1504-1506 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T677 1515-1517 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc
T678 1638-1640 http://purl.obolibrary.org/obo/CLO_0052676 denotes Fc

LitCovid-PD-CHEBI

Id Subject Object Predicate Lexical cue chebi_id
T184 186-188 Chemical denotes RI http://purl.obolibrary.org/obo/CHEBI_73814|http://purl.obolibrary.org/obo/CHEBI_8753
T186 620-622 Chemical denotes RI http://purl.obolibrary.org/obo/CHEBI_73814|http://purl.obolibrary.org/obo/CHEBI_8753
T188 933-935 Chemical denotes FG http://purl.obolibrary.org/obo/CHEBI_73635
T189 978-988 Chemical denotes asparagine http://purl.obolibrary.org/obo/CHEBI_22653
T190 1349-1355 Chemical denotes fucose http://purl.obolibrary.org/obo/CHEBI_33984
T191 1373-1388 Chemical denotes oligosaccharide http://purl.obolibrary.org/obo/CHEBI_50699

LitCovid-sample-MedDRA

Id Subject Object Predicate Lexical cue meddra_id
T17 371-376 http://purl.bioontology.org/ontology/MEDDRA/10022891 denotes X‐ray http://purl.bioontology.org/ontology/MEDDRA/10048064

LitCovid-sample-PD-IDO

Id Subject Object Predicate Lexical cue
T196 429-437 http://purl.obolibrary.org/obo/BFO_0000034 denotes function

LitCovid-sample-CHEBI

Id Subject Object Predicate Lexical cue chebi_id
T37 978-988 Chemical denotes asparagine http://purl.obolibrary.org/obo/CHEBI_22653
T38 1349-1355 Chemical denotes fucose http://purl.obolibrary.org/obo/CHEBI_33984
T39 1373-1388 Chemical denotes oligosaccharide http://purl.obolibrary.org/obo/CHEBI_50699

LitCovid-sample-Pubtator

Id Subject Object Predicate Lexical cue pubann:denotes
579 31-35 Gene denotes FcγR Gene:2213
583 183-188 Gene denotes FcγRI Gene:2214
584 131-135 Gene denotes FcγR Gene:2213
585 82-86 Gene denotes FcγR Gene:2213
588 311-315 Gene denotes FcγR Gene:2213
589 352-357 Species denotes human Tax:9606
602 617-622 Gene denotes FcγRI Gene:2214
603 634-641 Gene denotes FcγRIII Gene:2214
604 1289-1297 Gene denotes FcγRIIIa Gene:2214
605 624-630 Gene denotes FcγRII Gene:2214
606 1165-1169 Gene denotes FcγR Gene:2213
607 761-765 Gene denotes FcγR Gene:2213
608 588-593 Species denotes human Tax:9606
609 959-974 Chemical denotes N‐linked glycan
610 978-988 Chemical denotes asparagine MESH:D001216
611 994-998 Chemical denotes N297
612 1349-1355 Chemical denotes fucose MESH:D005643
613 1373-1388 Chemical denotes oligosaccharide MESH:D009844
617 1467-1471 Gene denotes FcγR Gene:2213
618 1638-1642 Gene denotes FcγR Gene:2213
619 1515-1519 Gene denotes FcγR Gene:2213

LitCovid-sample-PD-NCBITaxon

Id Subject Object Predicate Lexical cue ncbi_taxonomy_id
T39 352-357 Species denotes human NCBItxid:9606
T40 588-593 Species denotes human NCBItxid:9606

LitCovid-sample-sentences

Id Subject Object Predicate Lexical cue
T193 0-48 Sentence denotes The molecular basis of IgG and FcγR interactions
T194 49-112 Sentence denotes The extracellular regions of the FcγR are structurally similar.
T195 113-259 Sentence denotes Each low‐affinity FcγR has two ectodomains, whereas the high‐affinity FcγRI has a third domain but this is not directly involved in IgG binding.62
T196 260-554 Sentence denotes The interaction between the IgG subclasses and the FcγR is most comprehensively defined for human IgG1 by both X‐ray crystallographic7, 62, 63 and mutagenesis structure/function analyses.64, 65, 66 These studies defined key regions of the IgG sequence required for interaction with their FcγRs.
T197 555-721 Sentence denotes Crystallographic analyses of the human IgG1‐Fc complexed with FcγRI, FcγRII or FcγRIII show that these interactions are similar in topology, and asymmetric in nature.
T198 722-803 Sentence denotes The second extracellular domain of the FcγR inserts between the two heavy chains.
T199 804-954 Sentence denotes Here it makes contacts with the lower hinge of both H chains and with residues of the adjacent BC loop of one CH2 domain and the FG loop of the other.
T200 955-1136 Sentence denotes The N‐linked glycan at asparagine 297 (N297) of the heavy chain is essential for the structural integrity of the IgG‐Fc by affecting the spacing and conformation of the CH2 domains.
T201 1137-1391 Sentence denotes Indeed, its removal ablates FcγR binding.67 Of particular relevance to therapeutic mAb development is that the normal low‐affinity IgG interaction with FcγRIIIa is profoundly increased by the removal of the core fucose from the N297 Fc oligosaccharide.68
T202 1392-1643 Sentence denotes No crystallographic data are available for IgG2 or IgG4 Fc in complex with FcγR, but mutagenesis studies of the Fc and the FcγR revealed general similarity, but with critical differences, in the interaction of these subclasses with their cognate FcγR.

LitCovid-sample-PD-FMA

Id Subject Object Predicate Lexical cue fma_id
T327 23-26 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T328 245-248 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T329 288-291 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T330 499-502 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T331 1068-1071 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T332 1268-1271 Body_part denotes IgG http://purl.org/sig/ont/fma/fma62872
T333 1349-1355 Body_part denotes fucose http://purl.org/sig/ont/fma/fma82790
T334 1373-1388 Body_part denotes oligosaccharide http://purl.org/sig/ont/fma/fma82742

LitCovid-sentences

Id Subject Object Predicate Lexical cue
T193 0-48 Sentence denotes The molecular basis of IgG and FcγR interactions
T194 49-112 Sentence denotes The extracellular regions of the FcγR are structurally similar.
T195 113-259 Sentence denotes Each low‐affinity FcγR has two ectodomains, whereas the high‐affinity FcγRI has a third domain but this is not directly involved in IgG binding.62
T196 260-554 Sentence denotes The interaction between the IgG subclasses and the FcγR is most comprehensively defined for human IgG1 by both X‐ray crystallographic7, 62, 63 and mutagenesis structure/function analyses.64, 65, 66 These studies defined key regions of the IgG sequence required for interaction with their FcγRs.
T197 555-721 Sentence denotes Crystallographic analyses of the human IgG1‐Fc complexed with FcγRI, FcγRII or FcγRIII show that these interactions are similar in topology, and asymmetric in nature.
T198 722-803 Sentence denotes The second extracellular domain of the FcγR inserts between the two heavy chains.
T199 804-954 Sentence denotes Here it makes contacts with the lower hinge of both H chains and with residues of the adjacent BC loop of one CH2 domain and the FG loop of the other.
T200 955-1136 Sentence denotes The N‐linked glycan at asparagine 297 (N297) of the heavy chain is essential for the structural integrity of the IgG‐Fc by affecting the spacing and conformation of the CH2 domains.
T201 1137-1391 Sentence denotes Indeed, its removal ablates FcγR binding.67 Of particular relevance to therapeutic mAb development is that the normal low‐affinity IgG interaction with FcγRIIIa is profoundly increased by the removal of the core fucose from the N297 Fc oligosaccharide.68
T202 1392-1643 Sentence denotes No crystallographic data are available for IgG2 or IgG4 Fc in complex with FcγR, but mutagenesis studies of the Fc and the FcγR revealed general similarity, but with critical differences, in the interaction of these subclasses with their cognate FcγR.