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GlyCosmos600-Glycan-Motif-Structure

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":26,"end":33},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":145,"end":152},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":257,"end":264},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":281,"end":288},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T5","span":{"begin":518,"end":525},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T6","span":{"begin":624,"end":631},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T7","span":{"begin":694,"end":701},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T8","span":{"begin":749,"end":756},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T9","span":{"begin":807,"end":814},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":26,"end":33},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":145,"end":152},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":257,"end":264},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":281,"end":288},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":518,"end":525},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":624,"end":631},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":694,"end":701},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":749,"end":756},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":807,"end":814},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":26,"end":33},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":145,"end":152},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":257,"end":264},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":281,"end":288},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T5","span":{"begin":518,"end":525},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T6","span":{"begin":624,"end":631},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T7","span":{"begin":694,"end":701},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T8","span":{"begin":749,"end":756},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T9","span":{"begin":807,"end":814},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

GlyCosmos600-FMA

glycosmos-test-glycan-structure

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":26,"end":33},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":145,"end":152},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":257,"end":264},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":281,"end":288},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T5","span":{"begin":518,"end":525},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T6","span":{"begin":624,"end":631},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T7","span":{"begin":694,"end":701},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T8","span":{"begin":749,"end":756},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T9","span":{"begin":807,"end":814},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

glycosmos-test-structure-v1

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":26,"end":33},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":145,"end":152},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":257,"end":264},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":281,"end":288},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T5","span":{"begin":518,"end":525},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T6","span":{"begin":624,"end":631},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T7","span":{"begin":694,"end":701},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T8","span":{"begin":749,"end":756},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T9","span":{"begin":807,"end":814},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

GlyCosmos600-GlycoProteins

{"project":"GlyCosmos600-GlycoProteins","denotations":[{"id":"PD-GlycoProteins-B_T1","span":{"begin":26,"end":49},"obj":"http://purl.uniprot.org/uniprot/P39039"},{"id":"PD-GlycoProteins-B_T2","span":{"begin":694,"end":717},"obj":"http://purl.uniprot.org/uniprot/P39039"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":72,"end":94},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":201,"end":223},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:228735"},{"id":"A2","pred":"db_id","subj":"T2","obj":"NCBItxid:228735"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":96,"end":390},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":391,"end":834},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":835,"end":934},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":935,"end":1049},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1050,"end":1212},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1213,"end":1489},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1490,"end":1642},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1643,"end":1723},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":95},"obj":"Sentence"},{"id":"T2","span":{"begin":96,"end":390},"obj":"Sentence"},{"id":"T3","span":{"begin":391,"end":834},"obj":"Sentence"},{"id":"T4","span":{"begin":835,"end":934},"obj":"Sentence"},{"id":"T5","span":{"begin":935,"end":1049},"obj":"Sentence"},{"id":"T6","span":{"begin":1050,"end":1212},"obj":"Sentence"},{"id":"T7","span":{"begin":1213,"end":1489},"obj":"Sentence"},{"id":"T8","span":{"begin":1490,"end":1642},"obj":"Sentence"},{"id":"T9","span":{"begin":1643,"end":1723},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Isolation of a methylated mannose-binding protein from terrestrial worm Enchytraeus japonensis.\nTo elucidate a biological role of the methylated mannose residues found in N-glycans of terrestrial worm Enchytraeus japonensis, we first synthesized 3-O-methyl mannose- and 4-O-methyl mannose-derivatives and immobilized them to Sepharose 4B beads in order to isolate the sugar-binding protein. When whole protein extracts from the worms was applied to a series of the columns immobilized with the modified and unmodified mannose-derivatives, respectively, a protein with a molecular weight of 25,000 was isolated by 4-O-methyl mannose-immobilized column chromatography, and termed as a methylated mannose-binding protein (mMBP). mMBP bound weakly to a mannose-immobilized column and moderately to a 3-O-methyl mannose-immobilized column. The N-terminal amino acid sequences of mMBP and its endoprotease-digested peptides were determined. Using the degenerate first primers synthesized based on the primary sequence, a genomic DNA fragment was isolated. Then, the second primers were synthesized based on the genomic DNA fragment, and with use of them two cDNA fragments were obtained by the 3'- and 5'-RACE methods. Finally, the third primers were synthesized based on the sequences of the two cDNA fragments and one genomic DNA fragment, and with use of them a full-length cDNA of mMBP was isolated and shown to comprise a putative 633 bp open reading frame encoding 210 amino acid residues. BLAST analysis revealed that mMBP has identities by 26 ~ 55% to several proteins including the regeneration-upregulated protein 3 from the same species. Whether mMBP is involved in the regeneration of the worm is under investigation."}

pubmed-enju-pas