PubMed:15604092
Annnotations
Glycan-Motif
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 1025-1034 | https://glytoucan.org/Structures/Glycans/G65889KE | denotes | galactose |
| T2 | 1025-1034 | https://glytoucan.org/Structures/Glycans/G68158BT | denotes | galactose |
| T3 | 1072-1091 | https://glytoucan.org/Structures/Glycans/G00055MO | denotes | N-acetyllactosamine |
| T4 | 1193-1200 | https://glytoucan.org/Structures/Glycans/G70323CJ | denotes | mannose |
GlyCosmos6-Glycan-Motif-Image
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 1025-1034 | Glycan_Motif | denotes | galactose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT|https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE |
| T3 | 1072-1091 | Glycan_Motif | denotes | N-acetyllactosamine | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO |
| T4 | 1193-1200 | Glycan_Motif | denotes | mannose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| TextSentencer_T1 | 0-146 | Sentence | denotes | Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure. |
| TextSentencer_T2 | 147-300 | Sentence | denotes | The mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. |
| TextSentencer_T3 | 301-434 | Sentence | denotes | The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. |
| TextSentencer_T4 | 435-612 | Sentence | denotes | Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. |
| TextSentencer_T5 | 613-930 | Sentence | denotes | In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. |
| TextSentencer_T6 | 931-1044 | Sentence | denotes | The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. |
| TextSentencer_T7 | 1045-1147 | Sentence | denotes | Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. |
| TextSentencer_T8 | 1148-1246 | Sentence | denotes | A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. |
| TextSentencer_T9 | 1247-1313 | Sentence | denotes | MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. |
| TextSentencer_T10 | 1314-1611 | Sentence | denotes | By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. |
| TextSentencer_T11 | 1612-1859 | Sentence | denotes | Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides. |
| T1 | 0-146 | Sentence | denotes | Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure. |
| T2 | 147-300 | Sentence | denotes | The mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. |
| T3 | 301-434 | Sentence | denotes | The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. |
| T4 | 435-612 | Sentence | denotes | Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. |
| T5 | 613-930 | Sentence | denotes | In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. |
| T6 | 931-1044 | Sentence | denotes | The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. |
| T7 | 1045-1147 | Sentence | denotes | Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. |
| T8 | 1148-1246 | Sentence | denotes | A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. |
| T9 | 1247-1313 | Sentence | denotes | MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. |
| T10 | 1314-1611 | Sentence | denotes | By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. |
| T11 | 1612-1859 | Sentence | denotes | Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides. |
| T1 | 0-146 | Sentence | denotes | Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure. |
| T2 | 147-300 | Sentence | denotes | The mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. |
| T3 | 301-434 | Sentence | denotes | The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. |
| T4 | 435-612 | Sentence | denotes | Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. |
| T5 | 613-930 | Sentence | denotes | In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. |
| T6 | 931-1044 | Sentence | denotes | The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. |
| T7 | 1045-1147 | Sentence | denotes | Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. |
| T8 | 1148-1246 | Sentence | denotes | A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. |
| T9 | 1247-1313 | Sentence | denotes | MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. |
| T10 | 1314-1611 | Sentence | denotes | By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. |
| T11 | 1612-1859 | Sentence | denotes | Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides. |
GlyCosmos6-Glycan-Motif-Structure
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 1025-1034 | https://glytoucan.org/Structures/Glycans/G65889KE | denotes | galactose |
| T2 | 1025-1034 | https://glytoucan.org/Structures/Glycans/G68158BT | denotes | galactose |
| T3 | 1072-1091 | https://glytoucan.org/Structures/Glycans/G00055MO | denotes | N-acetyllactosamine |
| T4 | 1193-1200 | https://glytoucan.org/Structures/Glycans/G70323CJ | denotes | mannose |
uniprot-human
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 68-71 | http://www.uniprot.org/uniprot/Q05996 | denotes | ZPA |
| T2 | 282-285 | http://www.uniprot.org/uniprot/Q05996 | denotes | ZPA |
| T3 | 528-531 | http://www.uniprot.org/uniprot/Q05996 | denotes | ZPA |
| T4 | 673-676 | http://www.uniprot.org/uniprot/Q05996 | denotes | ZPA |
| T5 | 1441-1444 | http://www.uniprot.org/uniprot/Q05996 | denotes | ZPA |
| T6 | 85-87 | http://www.uniprot.org/uniprot/Q99707 | denotes | MS |
| T7 | 872-874 | http://www.uniprot.org/uniprot/Q99707 | denotes | MS |
| T8 | 1247-1249 | http://www.uniprot.org/uniprot/Q99707 | denotes | MS |
| T9 | 1250-1252 | http://www.uniprot.org/uniprot/Q99707 | denotes | MS |
| T10 | 1608-1610 | http://www.uniprot.org/uniprot/Q99707 | denotes | MS |
| T11 | 1771-1773 | http://www.uniprot.org/uniprot/Q99707 | denotes | MS |
| T12 | 287-290 | http://www.uniprot.org/uniprot/Q12836 | denotes | ZPB |
| T13 | 389-392 | http://www.uniprot.org/uniprot/Q12836 | denotes | ZPB |
| T14 | 296-299 | http://www.uniprot.org/uniprot/P21754 | denotes | ZPC |
| T15 | 393-396 | http://www.uniprot.org/uniprot/P21754 | denotes | ZPC |
| T16 | 771-789 | http://www.uniprot.org/uniprot/P16278 | denotes | beta-galactosidase |
| T17 | 1366-1384 | http://www.uniprot.org/uniprot/P16278 | denotes | beta-galactosidase |
uniprot-mouse
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 85-87 | http://www.uniprot.org/uniprot/A6H5Y3 | denotes | MS |
| T2 | 872-874 | http://www.uniprot.org/uniprot/A6H5Y3 | denotes | MS |
| T3 | 1247-1249 | http://www.uniprot.org/uniprot/A6H5Y3 | denotes | MS |
| T4 | 1250-1252 | http://www.uniprot.org/uniprot/A6H5Y3 | denotes | MS |
| T5 | 1608-1610 | http://www.uniprot.org/uniprot/A6H5Y3 | denotes | MS |
| T6 | 1771-1773 | http://www.uniprot.org/uniprot/A6H5Y3 | denotes | MS |
| T7 | 771-789 | http://www.uniprot.org/uniprot/P23780 | denotes | beta-galactosidase |
| T8 | 1366-1384 | http://www.uniprot.org/uniprot/P23780 | denotes | beta-galactosidase |
| T9 | 1542-1545 | http://www.uniprot.org/uniprot/Q61024 | denotes | Asn |
| T10 | 1699-1702 | http://www.uniprot.org/uniprot/Q61024 | denotes | Asn |
GlycoBiology-NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 643-662 | http://purl.bioontology.org/ontology/NCBITAXON/8004 | denotes | electrophoretically |
| T2 | 771-775 | http://purl.bioontology.org/ontology/NCBITAXON/158455 | denotes | beta |
| T3 | 771-775 | http://purl.bioontology.org/ontology/NCBITAXON/3554 | denotes | beta |
| T4 | 1366-1370 | http://purl.bioontology.org/ontology/NCBITAXON/158455 | denotes | beta |
| T5 | 1366-1370 | http://purl.bioontology.org/ontology/NCBITAXON/3554 | denotes | beta |
GO-BP
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 360-373 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylation |
| T2 | 477-490 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylation |
| T3 | 1519-1532 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylation |
| T4 | 1642-1654 | http://purl.obolibrary.org/obo/GO_0070085 | denotes | glycosylated |
| T5 | 1136-1146 | http://purl.obolibrary.org/obo/GO_0097503 | denotes | sialylated |
| T6 | 1162-1168 | http://purl.obolibrary.org/obo/GO_0023052 | denotes | signal |
| T7 | 1344-1353 | http://purl.obolibrary.org/obo/GO_0007586 | denotes | digestion |
| T8 | 1428-1437 | http://purl.obolibrary.org/obo/GO_0007586 | denotes | digestion |
GO-MF
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 121-145 | http://purl.obolibrary.org/obo/GO_0035804 | denotes | zona pellucida structure |
GO-CC
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 196-209 | http://purl.obolibrary.org/obo/GO_0005576 | denotes | extracellular |
| T2 | 196-216 | http://purl.obolibrary.org/obo/GO_0031012 | denotes | extracellular matrix |
UBERON-AE
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 40-54 | http://purl.obolibrary.org/obo/UBERON_0000086 | denotes | zona pellucida |
| T2 | 121-135 | http://purl.obolibrary.org/obo/UBERON_0000086 | denotes | zona pellucida |
| T3 | 222-236 | http://purl.obolibrary.org/obo/UBERON_0000086 | denotes | zona pellucida |
GlycoBiology-Motifs
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 454-462 | http://rdf.glycoinfo.org/glycan/G00027MO | denotes | N-glycan |
| T2 | 1304-1312 | http://rdf.glycoinfo.org/glycan/G00027MO | denotes | N-glycan |
| T3 | 1188-1200 | http://rdf.glycoinfo.org/glycan/G00028MO | denotes | high-mannose |
performance-test
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| PD-UBERON-AE-B_T1 | 40-54 | http://purl.obolibrary.org/obo/UBERON_0000086 | denotes | zona pellucida |
| PD-UBERON-AE-B_T2 | 121-135 | http://purl.obolibrary.org/obo/UBERON_0000086 | denotes | zona pellucida |
| PD-UBERON-AE-B_T3 | 222-236 | http://purl.obolibrary.org/obo/UBERON_0000086 | denotes | zona pellucida |
Lectin-Jamboree
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 1450-1456 | lectin | denotes | lectin |
Lectin-Jamboree-Sentence
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-146 | Sentence | denotes | Analysis of N-linked glycans of porcine zona pellucida glycoprotein ZPA by MALDI-TOF MS: a contribution to understanding zona pellucida structure. |
| T2 | 147-300 | Sentence | denotes | The mammalian oocyte is encased by a transparent extracellular matrix, the zona pellucida (ZP), which consists of three glycoproteins, ZPA, ZPB, and ZPC. |
| T3 | 301-434 | Sentence | denotes | The glycan structures of the porcine ZP and the complete N-glycosylation pattern of the ZPB/ZPC oligomer has been recently described. |
| T4 | 435-612 | Sentence | denotes | Here we report the N-glycan pattern and N-glycosylation sites of the porcine ZP glycoprotein ZPA of an immature oocyte population as determined by a mass spectrometric approach. |
| T5 | 613-930 | Sentence | denotes | In-gel deglycosylation of the electrophoretically separated ZPA protein and comparison of the pattern obtained from the native, the desialylated and the endo-beta-galactosidase-treated glycoprotein allowed the assignment of the glycan structures by MALDI-TOF MS by considering the reported oligosaccharide structures. |
| T6 | 931-1044 | Sentence | denotes | The major N-glycans are neutral biantennary complex structures containing one or two terminal galactose residues. |
| T7 | 1045-1147 | Sentence | denotes | Complex N-glycans carrying N-acetyllactosamine repeats are minor components and are mostly sialylated. |
| T8 | 1148-1246 | Sentence | denotes | A significant signal corresponding to a high-mannose type chain appeared in the three glycan maps. |
| T9 | 1247-1313 | Sentence | denotes | MS/MS analysis confirmed its identity as a pentamannosyl N-glycan. |
| T10 | 1314-1611 | Sentence | denotes | By the combination of tryptic digestion of the endo-beta-galactosidase-treated ZP glycoprotein mixture and in-gel digestion of ZPA with lectin affinity chromatography and reverse-phase HPLC, five of six N-glycosylation sites at Asn(84/93), Asn268, Asn316, Asn323, and Asn530 were identified by MS. |
| T11 | 1612-1859 | Sentence | denotes | Only one site was found to be glycosylated in the N-terminal tryptic glycopeptide with Asn(84/93.) N-glycosidase F treatment of the isolated glycopeptides and MS analysis resulted in the identification of the corresponding deglycosylated peptides. |
Anatomy-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 40-54 | Body_part | denotes | zona pellucida | http://purl.obolibrary.org/obo/GO_0035805|http://purl.obolibrary.org/obo/UBERON_0000086|http://purl.obolibrary.org/obo/UBERON_0003125 |
| T4 | 121-135 | Body_part | denotes | zona pellucida | http://purl.obolibrary.org/obo/GO_0035805|http://purl.obolibrary.org/obo/UBERON_0000086|http://purl.obolibrary.org/obo/UBERON_0003125 |
| T7 | 161-167 | Body_part | denotes | oocyte | http://purl.obolibrary.org/obo/CL_0000023 |
| T8 | 196-216 | Body_part | denotes | extracellular matrix | http://purl.obolibrary.org/obo/GO_0031012 |
| T9 | 222-236 | Body_part | denotes | zona pellucida | http://purl.obolibrary.org/obo/GO_0035805|http://purl.obolibrary.org/obo/UBERON_0000086|http://purl.obolibrary.org/obo/UBERON_0003125 |
| T12 | 238-240 | Body_part | denotes | ZP | http://purl.obolibrary.org/obo/GO_0035805 |
| T13 | 338-340 | Body_part | denotes | ZP | http://purl.obolibrary.org/obo/GO_0035805 |
| T14 | 512-514 | Body_part | denotes | ZP | http://purl.obolibrary.org/obo/GO_0035805 |
| T15 | 547-553 | Body_part | denotes | oocyte | http://purl.obolibrary.org/obo/CL_0000023 |
| T16 | 1393-1395 | Body_part | denotes | ZP | http://purl.obolibrary.org/obo/GO_0035805 |
CL-cell
| Id | Subject | Object | Predicate | Lexical cue | cl_id |
|---|---|---|---|---|---|
| T1 | 161-167 | Cell | denotes | oocyte | http://purl.obolibrary.org/obo/CL:0000023 |
| T2 | 547-553 | Cell | denotes | oocyte | http://purl.obolibrary.org/obo/CL:0000023 |