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LitCovid-OGER-BB

Id Subject Object Predicate Lexical cue
T1 13-19 MOP:0002162 denotes N- and
T2 20-36 MOP:0003162 denotes O- glycosylation
T3 75-86 NCBITaxon:11118 denotes coronavirus
T4 87-97 SP_7 denotes SARS-CoV-2
T5 134-145 NCBITaxon:11118 denotes coronavirus
T6 165-175 SP_7 denotes SARS-CoV-2
T7 276-287 NCBITaxon:11118 denotes coronavirus
T8 325-330 NCBITaxon:10239 denotes viral
T9 353-361 GO:0016020 denotes membrane
T10 353-368 GO:0061025 denotes membrane fusion
T11 445-449 GO:0006955 denotes host
T12 450-456 UBERON:0002405 denotes immune
T13 450-465 GO:0006955 denotes immune response
T14 571-586 MOP:0002162 denotes N-glycosylation
T15 674-683 GO:0010467 denotes expressed
T16 687-692 SP_6 denotes human
T17 687-692 NCBITaxon:9606 denotes human
T18 781-796 MOP:0002162 denotes N-glycosylation
T19 861-876 MOP:0003162 denotes O-glycosylation
T20 915-921 SO:0000417 denotes domain
T21 969-984 MOP:0003162 denotes O-glycosylation
T22 1028-1032 PR:000014459 denotes SARS
T23 1028-1038 SP_7 denotes SARS-CoV-2
T24 1107-1122 MOP:0003162 denotes O-glycosylation
T25 1145-1152 MOP:0002162 denotes glycans
T26 1145-1152 CHEBI:59521 denotes glycans
T27 1145-1152 CHEBI:59521 denotes glycans
T28 1197-1203 MOP:0002162 denotes N- and
T29 1204-1220 MOP:0003162 denotes O- glycosylation
T30 1280-1292 MOP:0002162 denotes glycopeptide
T31 1280-1292 CHEBI:24396 denotes glycopeptide
T32 1280-1292 CHEBI:24396 denotes glycopeptide
T33 1431-1437 CHEBI:17089 denotes glycan
T34 1431-1437 CHEBI:17089 denotes glycan
T35 1497-1502 NCBITaxon:10239 denotes viral

sentences

Id Subject Object Predicate Lexical cue
T1 0-98 Sentence denotes Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2.
T2 99-271 Sentence denotes The current emergence of the novel coronavirus pandemic caused by SARS-CoV-2 demands the development of new therapeutic strategies to prevent rapid progress of mortalities.
T3 272-466 Sentence denotes The coronavirus spike (S) protein, which facilitates viral attachment, entry and membrane fusion is heavily glycosylated and plays a critical role in the elicitation of the host immune response.
T4 467-593 Sentence denotes The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites.
T5 594-741 Sentence denotes Herein, we report the glycosylation mapping on spike protein subunits S1 and S2 expressed on human cells through high resolution mass spectrometry.
T6 742-956 Sentence denotes We have characterized the quantitative N-glycosylation profile on spike protein and interestingly, observed unexpected O-glycosylation modifications on the receptor binding domain (RBD) of spike protein subunit S1.
T7 957-1180 Sentence denotes Even though O-glycosylation has been predicted on the spike protein of SARS-CoV-2, this is the first report of experimental data for both the site of O-glycosylation and identity of the O-glycans attached on the subunit S1.
T8 1181-1407 Sentence denotes Our data on the N- and O- glycosylation is strengthened by extensive manual interpretation of each glycopeptide spectra in addition to using bioinformatics tools to confirm the complexity of glycosylation in the spike protein.
T9 1408-1614 Sentence denotes The elucidation of the glycan repertoire on the spike protein provides insights into the viral binding studies and more importantly, propels research towards the development of a suitable vaccine candidate.
T1 0-98 Sentence denotes Deducing the N- and O- glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2.
T2 99-271 Sentence denotes The current emergence of the novel coronavirus pandemic caused by SARS-CoV-2 demands the development of new therapeutic strategies to prevent rapid progress of mortalities.
T3 272-466 Sentence denotes The coronavirus spike (S) protein, which facilitates viral attachment, entry and membrane fusion is heavily glycosylated and plays a critical role in the elicitation of the host immune response.
T4 467-593 Sentence denotes The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites.
T5 594-741 Sentence denotes Herein, we report the glycosylation mapping on spike protein subunits S1 and S2 expressed on human cells through high resolution mass spectrometry.
T6 742-956 Sentence denotes We have characterized the quantitative N-glycosylation profile on spike protein and interestingly, observed unexpected O-glycosylation modifications on the receptor binding domain (RBD) of spike protein subunit S1.
T7 957-1180 Sentence denotes Even though O-glycosylation has been predicted on the spike protein of SARS-CoV-2, this is the first report of experimental data for both the site of O-glycosylation and identity of the O-glycans attached on the subunit S1.
T8 1181-1407 Sentence denotes Our data on the N- and O- glycosylation is strengthened by extensive manual interpretation of each glycopeptide spectra in addition to using bioinformatics tools to confirm the complexity of glycosylation in the spike protein.
T9 1408-1614 Sentence denotes The elucidation of the glycan repertoire on the spike protein provides insights into the viral binding studies and more importantly, propels research towards the development of a suitable vaccine candidate.

mondo_disease

Id Subject Object Predicate Lexical cue mondo_id
T1 87-97 Disease denotes SARS-CoV-2 http://purl.obolibrary.org/obo/MONDO_0100096
T2 165-175 Disease denotes SARS-CoV-2 http://purl.obolibrary.org/obo/MONDO_0100096
T3 1028-1038 Disease denotes SARS-CoV-2 http://purl.obolibrary.org/obo/MONDO_0100096

HP-phenotype

Id Subject Object Predicate Lexical cue hp_id
T1 923-926 Phenotype denotes RBD HP:5200291

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 87-95 OrganismTaxon denotes SARS-CoV 694009
T2 165-173 OrganismTaxon denotes SARS-CoV 694009
T3 687-692 OrganismTaxon denotes human 9606
T4 1028-1036 OrganismTaxon denotes SARS-CoV 694009

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 353-361 Body_part denotes membrane http://purl.obolibrary.org/obo/GO_0016020|http://purl.obolibrary.org/obo/UBERON_0000094|http://purl.obolibrary.org/obo/UBERON_0000158