PubMed:10764834 JSON TXT

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sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":89},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":90,"end":281},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":282,"end":366},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":367,"end":456},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":457,"end":710},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":711,"end":920},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":921,"end":1015},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1016,"end":1255},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1256,"end":1456},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1457,"end":1582},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":89},"obj":"Sentence"},{"id":"T2","span":{"begin":90,"end":281},"obj":"Sentence"},{"id":"T3","span":{"begin":282,"end":366},"obj":"Sentence"},{"id":"T4","span":{"begin":367,"end":456},"obj":"Sentence"},{"id":"T5","span":{"begin":457,"end":710},"obj":"Sentence"},{"id":"T6","span":{"begin":711,"end":920},"obj":"Sentence"},{"id":"T7","span":{"begin":921,"end":1015},"obj":"Sentence"},{"id":"T8","span":{"begin":1016,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1456},"obj":"Sentence"},{"id":"T10","span":{"begin":1457,"end":1582},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":89},"obj":"Sentence"},{"id":"T2","span":{"begin":90,"end":281},"obj":"Sentence"},{"id":"T3","span":{"begin":282,"end":366},"obj":"Sentence"},{"id":"T4","span":{"begin":367,"end":456},"obj":"Sentence"},{"id":"T5","span":{"begin":457,"end":710},"obj":"Sentence"},{"id":"T6","span":{"begin":711,"end":920},"obj":"Sentence"},{"id":"T7","span":{"begin":921,"end":1015},"obj":"Sentence"},{"id":"T8","span":{"begin":1016,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1456},"obj":"Sentence"},{"id":"T10","span":{"begin":1457,"end":1582},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":335,"end":338},"obj":"http://www.uniprot.org/uniprot/P01730"},{"id":"T2","span":{"begin":1366,"end":1397},"obj":"http://www.uniprot.org/uniprot/Q5STK9"},{"id":"T3","span":{"begin":1366,"end":1389},"obj":"http://www.uniprot.org/uniprot/P78560"},{"id":"T4","span":{"begin":1366,"end":1397},"obj":"http://www.uniprot.org/uniprot/Q8WWZ3"},{"id":"T5","span":{"begin":1366,"end":1397},"obj":"http://www.uniprot.org/uniprot/Q13158"},{"id":"T6","span":{"begin":1420,"end":1438},"obj":"http://www.uniprot.org/uniprot/P01138"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":335,"end":338},"obj":"http://www.uniprot.org/uniprot/P06332"},{"id":"T2","span":{"begin":1362,"end":1365},"obj":"http://www.uniprot.org/uniprot/P25446"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":17,"end":29},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T2","span":{"begin":30,"end":40},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3564"},{"id":"T3","span":{"begin":41,"end":52},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/185167"},{"id":"T4","span":{"begin":41,"end":52},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/188318"},{"id":"T5","span":{"begin":139,"end":151},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T6","span":{"begin":156,"end":166},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3564"},{"id":"T7","span":{"begin":167,"end":178},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/185167"},{"id":"T8","span":{"begin":167,"end":178},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/188318"},{"id":"T9","span":{"begin":320,"end":325},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T10","span":{"begin":371,"end":383},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T11","span":{"begin":535,"end":542},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3846"},{"id":"T12","span":{"begin":535,"end":542},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1462605"},{"id":"T13","span":{"begin":1032,"end":1041},"obj":"http://purl.bioontology.org/ontology/STY/T192"},{"id":"T14","span":{"begin":1115,"end":1120},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/62990"},{"id":"T15","span":{"begin":1434,"end":1438},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T16","span":{"begin":1434,"end":1438},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T17","span":{"begin":1576,"end":1581},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":1073,"end":1082},"obj":"http://purl.obolibrary.org/obo/GO_0007586"},{"id":"T2","span":{"begin":1151,"end":1157},"obj":"http://purl.obolibrary.org/obo/GO_0060361"},{"id":"T3","span":{"begin":1377,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0016265"},{"id":"T4","span":{"begin":1420,"end":1426},"obj":"http://purl.obolibrary.org/obo/GO_0040007"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":1420,"end":1438},"obj":"http://purl.obolibrary.org/obo/GO_0005160"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":320,"end":325},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":1576,"end":1581},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":356,"end":365},"obj":"http://edamontology.org/topic_0625"},{"id":"T2","span":{"begin":701,"end":709},"obj":"http://edamontology.org/topic_2839"},{"id":"T3","span":{"begin":842,"end":852},"obj":"http://edamontology.org/topic_0154"},{"id":"T4","span":{"begin":927,"end":935},"obj":"http://edamontology.org/topic_0749"},{"id":"T5","span":{"begin":936,"end":946},"obj":"http://edamontology.org/topic_0154"},{"id":"T6","span":{"begin":1043,"end":1051},"obj":"http://edamontology.org/topic_0154"},{"id":"T7","span":{"begin":1246,"end":1254},"obj":"http://edamontology.org/topic_3489"},{"id":"T8","span":{"begin":1286,"end":1294},"obj":"http://edamontology.org/topic_0154"},{"id":"T9","span":{"begin":1338,"end":1343},"obj":"http://edamontology.org/topic_2815"},{"id":"T10","span":{"begin":1349,"end":1356},"obj":"http://edamontology.org/topic_0078"},{"id":"T11","span":{"begin":1383,"end":1397},"obj":"http://edamontology.org/topic_0736"},{"id":"T12","span":{"begin":1383,"end":1397},"obj":"http://edamontology.org/topic_3539"},{"id":"T13","span":{"begin":1390,"end":1397},"obj":"http://edamontology.org/topic_0078"},{"id":"T14","span":{"begin":1537,"end":1547},"obj":"http://edamontology.org/topic_0625"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":274,"end":280},"obj":"http://edamontology.org/data_2082"},{"id":"T2","span":{"begin":356,"end":365},"obj":"http://edamontology.org/data_3275"},{"id":"T3","span":{"begin":642,"end":650},"obj":"http://edamontology.org/data_1756"},{"id":"T4","span":{"begin":947,"end":955},"obj":"http://edamontology.org/data_1756"},{"id":"T5","span":{"begin":1043,"end":1051},"obj":"http://edamontology.org/data_2906"},{"id":"T6","span":{"begin":1099,"end":1105},"obj":"http://edamontology.org/data_2082"},{"id":"T7","span":{"begin":1246,"end":1254},"obj":"http://edamontology.org/data_0581"},{"id":"T8","span":{"begin":1286,"end":1294},"obj":"http://edamontology.org/data_2906"},{"id":"T9","span":{"begin":1349,"end":1356},"obj":"http://edamontology.org/format_1208"},{"id":"T10","span":{"begin":1349,"end":1356},"obj":"http://edamontology.org/data_1467"},{"id":"T11","span":{"begin":1383,"end":1397},"obj":"http://edamontology.org/data_1468"},{"id":"T12","span":{"begin":1390,"end":1397},"obj":"http://edamontology.org/format_1208"},{"id":"T13","span":{"begin":1390,"end":1397},"obj":"http://edamontology.org/data_1467"},{"id":"T14","span":{"begin":1537,"end":1547},"obj":"http://edamontology.org/data_3275"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlyTouCan-IUPAC

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":224,"end":231},"obj":"id"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":625,"end":631},"obj":"Glycan"},{"id":"T2","span":{"begin":636,"end":641},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlyCosmos15-CL

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":78,"end":88},"obj":"Cell"},{"id":"T2","span":{"begin":112,"end":122},"obj":"Cell"},{"id":"T3","span":{"begin":293,"end":303},"obj":"Cell"},{"id":"T4","span":{"begin":763,"end":772},"obj":"Cell"},{"id":"T5","span":{"begin":1490,"end":1499},"obj":"Cell"},{"id":"T6","span":{"begin":1568,"end":1581},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000898"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":625,"end":631},"obj":"Glycan"},{"id":"T2","span":{"begin":636,"end":641},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G39738WL"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G39738WL"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":78,"end":88},"obj":"Body_part"},{"id":"T2","span":{"begin":112,"end":122},"obj":"Body_part"},{"id":"T3","span":{"begin":293,"end":303},"obj":"Body_part"},{"id":"T4","span":{"begin":763,"end":772},"obj":"Body_part"},{"id":"T5","span":{"begin":1490,"end":1499},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000893"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlyCosmos15-Taxon

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":30,"end":52},"obj":"Organism"},{"id":"T2","span":{"begin":156,"end":178},"obj":"Organism"},{"id":"T3","span":{"begin":535,"end":542},"obj":"Organism"},{"id":"T4","span":{"begin":1338,"end":1343},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"2613835"},{"id":"A2","pred":"db_id","subj":"T2","obj":"2613835"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3846"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":89},"obj":"Sentence"},{"id":"T2","span":{"begin":90,"end":281},"obj":"Sentence"},{"id":"T3","span":{"begin":282,"end":366},"obj":"Sentence"},{"id":"T4","span":{"begin":367,"end":456},"obj":"Sentence"},{"id":"T5","span":{"begin":457,"end":710},"obj":"Sentence"},{"id":"T6","span":{"begin":711,"end":920},"obj":"Sentence"},{"id":"T7","span":{"begin":921,"end":1015},"obj":"Sentence"},{"id":"T8","span":{"begin":1016,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1456},"obj":"Sentence"},{"id":"T10","span":{"begin":1457,"end":1582},"obj":"Sentence"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

Lectin-Jamboree

{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":53,"end":59},"obj":"lectin"},{"id":"T2","span":{"begin":179,"end":185},"obj":"lectin"},{"id":"T3","span":{"begin":232,"end":238},"obj":"lectin"},{"id":"T4","span":{"begin":389,"end":395},"obj":"lectin"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

Lectin-Jamboree-Sentence

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":89},"obj":"Sentence"},{"id":"T2","span":{"begin":90,"end":281},"obj":"Sentence"},{"id":"T3","span":{"begin":282,"end":366},"obj":"Sentence"},{"id":"T4","span":{"begin":367,"end":456},"obj":"Sentence"},{"id":"T5","span":{"begin":457,"end":710},"obj":"Sentence"},{"id":"T6","span":{"begin":711,"end":920},"obj":"Sentence"},{"id":"T7","span":{"begin":921,"end":1015},"obj":"Sentence"},{"id":"T8","span":{"begin":1016,"end":1255},"obj":"Sentence"},{"id":"T9","span":{"begin":1256,"end":1456},"obj":"Sentence"},{"id":"T10","span":{"begin":1457,"end":1582},"obj":"Sentence"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

GlyCosmos15-FMA

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":78,"end":88},"obj":"Body_part"},{"id":"T2","span":{"begin":112,"end":122},"obj":"Body_part"},{"id":"T3","span":{"begin":293,"end":303},"obj":"Body_part"},{"id":"T4","span":{"begin":763,"end":772},"obj":"Body_part"},{"id":"T5","span":{"begin":1490,"end":1499},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:72202"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:72202"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:72202"},{"id":"A4","pred":"db_id","subj":"T4","obj":"FMA:72202"},{"id":"A5","pred":"db_id","subj":"T5","obj":"FMA:72202"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":30,"end":52},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":156,"end":178},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":535,"end":542},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1338,"end":1343},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"2613835"},{"id":"A2","pred":"db_id","subj":"T2","obj":"2613835"},{"id":"A3","pred":"db_id","subj":"T3","obj":"3846"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":78,"end":88},"obj":"Body_part"},{"id":"T2","span":{"begin":112,"end":122},"obj":"Body_part"},{"id":"T3","span":{"begin":293,"end":303},"obj":"Body_part"},{"id":"T4","span":{"begin":763,"end":772},"obj":"Body_part"},{"id":"T5","span":{"begin":1490,"end":1499},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000893"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000893"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":78,"end":88},"obj":"Cell"},{"id":"T2","span":{"begin":112,"end":122},"obj":"Cell"},{"id":"T3","span":{"begin":293,"end":303},"obj":"Cell"},{"id":"T4","span":{"begin":763,"end":772},"obj":"Cell"},{"id":"T5","span":{"begin":1490,"end":1499},"obj":"Cell"},{"id":"T6","span":{"begin":1568,"end":1581},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0000893"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0000898"}],"text":"Isolation of the receptor for Amaranthus leucocarpus lectin from murine naive thymocytes.\nFrom murine medullary thymocytes we purified the receptor for the Amaranthus leucocarpus lectin (ALL) using a complex with the biotin-labeled lectin and avidin-agarose as the affinity matrix. Most ALL(+)thymocytes (83%) are naive cells with the CD4(+)CD8(-)CD45RB(+)phenotype. The receptor for this lectin is a 70 kDa glycoprotein that contains 20% of sugar by mass. It is constituted mainly by aspartic and glutamic acids, serine, proline, and glycine; its glycosidic portion contains mainly O-glycosidically linked glycans with Gal, GalNAc and NeuAc residues as well as one N-glycosidically linked glycan per molecule. Ionic strength chromatography revealed that the ALL-thymocyte receptor (ALLTr) is made up by three isoforms, which possess similar amino acid composition but show slight differences in their sugar composition. The N-terminal amino acid residues are blocked both in the receptor and its purified isoforms. Analyses of the receptor's peptides, obtained by trypsin digestion with MALDI-TOF (matrix assisted laser desorption ionization-time of flight), were compared with the relative values obtained from the NCBInr (Swiss-Prot 10/01/99) database. Our results indicate that the peptides of ALLTr show low homology (\u003c17%) with the human KIIA protein, the Fas-associated death domain protein, and the transforming growth factor-beta type II receptor. Our results suggest that the ALL thymocyte receptor could be considered a novel phenotypic marker specific for naive T cells."}