PubMed:26762173 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":413,"end":420},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":425,"end":434},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T3","span":{"begin":425,"end":434},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T4","span":{"begin":498,"end":506},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T5","span":{"begin":540,"end":550},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T6","span":{"begin":540,"end":550},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":413,"end":420},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":425,"end":434},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":498,"end":506},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":540,"end":550},"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/G68158BT"},{"id":"A3","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"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/G68158BT"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":413,"end":420},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":425,"end":434},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T3","span":{"begin":425,"end":434},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T4","span":{"begin":498,"end":506},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T5","span":{"begin":540,"end":550},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T6","span":{"begin":540,"end":550},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":65,"end":282},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":283,"end":435},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":436,"end":629},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":630,"end":883},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"T2","span":{"begin":65,"end":282},"obj":"Sentence"},{"id":"T3","span":{"begin":283,"end":435},"obj":"Sentence"},{"id":"T4","span":{"begin":436,"end":629},"obj":"Sentence"},{"id":"T5","span":{"begin":630,"end":883},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"T2","span":{"begin":65,"end":282},"obj":"Sentence"},{"id":"T3","span":{"begin":283,"end":435},"obj":"Sentence"},{"id":"T4","span":{"begin":436,"end":629},"obj":"Sentence"},{"id":"T5","span":{"begin":630,"end":883},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":86,"end":97},"obj":"FMAID:50603"},{"id":"_T2","span":{"begin":86,"end":97},"obj":"FMAID:146309"},{"id":"_T3","span":{"begin":219,"end":226},"obj":"FMAID:165447"},{"id":"_T4","span":{"begin":219,"end":226},"obj":"FMAID:67257"},{"id":"_T5","span":{"begin":239,"end":244},"obj":"FMAID:169002"},{"id":"_T6","span":{"begin":239,"end":244},"obj":"FMAID:68646"},{"id":"_T7","span":{"begin":272,"end":281},"obj":"FMAID:196737"},{"id":"_T8","span":{"begin":272,"end":281},"obj":"FMAID:82748"},{"id":"_T9","span":{"begin":351,"end":359},"obj":"FMAID:226027"},{"id":"_T10","span":{"begin":351,"end":359},"obj":"FMAID:226028"},{"id":"_T11","span":{"begin":413,"end":420},"obj":"FMAID:196796"},{"id":"_T12","span":{"begin":413,"end":420},"obj":"FMAID:82801"},{"id":"_T13","span":{"begin":425,"end":434},"obj":"FMAID:82794"},{"id":"_T14","span":{"begin":425,"end":434},"obj":"FMAID:196789"},{"id":"_T15","span":{"begin":498,"end":506},"obj":"FMAID:196796"},{"id":"_T16","span":{"begin":498,"end":506},"obj":"FMAID:82801"},{"id":"_T17","span":{"begin":540,"end":550},"obj":"FMAID:82794"},{"id":"_T18","span":{"begin":540,"end":550},"obj":"FMAID:196789"},{"id":"_T19","span":{"begin":584,"end":591},"obj":"FMAID:67257"},{"id":"_T20","span":{"begin":584,"end":591},"obj":"FMAID:165447"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":594,"end":615},"obj":"http://www.uniprot.org/uniprot/P23336"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":46,"end":56},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/5140"},{"id":"T2","span":{"begin":46,"end":63},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/5141"},{"id":"T3","span":{"begin":57,"end":63},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/688987"},{"id":"T4","span":{"begin":129,"end":139},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/5140"},{"id":"T5","span":{"begin":129,"end":146},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/5141"},{"id":"T6","span":{"begin":140,"end":146},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/688987"},{"id":"T7","span":{"begin":239,"end":244},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T8","span":{"begin":622,"end":628},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/688987"},{"id":"T9","span":{"begin":690,"end":696},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/688987"},{"id":"T10","span":{"begin":801,"end":819},"obj":"http://purl.bioontology.org/ontology/STY/T043"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":21,"end":40},"obj":"http://purl.obolibrary.org/obo/GO_0016162"},{"id":"T2","span":{"begin":147,"end":166},"obj":"http://purl.obolibrary.org/obo/GO_0016162"},{"id":"T3","span":{"begin":219,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0009306"},{"id":"T4","span":{"begin":227,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0046903"},{"id":"T5","span":{"begin":227,"end":244},"obj":"http://purl.obolibrary.org/obo/GO_0032940"},{"id":"T6","span":{"begin":293,"end":305},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T7","span":{"begin":784,"end":797},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T8","span":{"begin":828,"end":839},"obj":"http://purl.obolibrary.org/obo/GO_0032502"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":239,"end":244},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":272,"end":281},"obj":"http://rdf.glycoinfo.org/glycan/G00025MO"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":46,"end":63},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":129,"end":146},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":622,"end":628},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":690,"end":696},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"5141"},{"id":"A2","pred":"db_id","subj":"T2","obj":"5141"},{"id":"A3","pred":"db_id","subj":"T3","obj":"2510790"},{"id":"A4","pred":"db_id","subj":"T3","obj":"688987"},{"id":"A5","pred":"db_id","subj":"T5","obj":"2510790"},{"id":"A6","pred":"db_id","subj":"T5","obj":"688987"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":219,"end":244},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000154"}],"text":"O-Glycan Analysis of Cellobiohydrolase I from Neurospora crassa.\nWe describe here the composition of the O-linked glycans on the Neurospora crassa cellobiohydrolase I (CBHI), which accounts for approximately 40% of the protein secreted by cells growing in the presence of cellulose. CBHI is O-glycosylated with six types of linear, and three types of branched, O-glycans containing approximately equal amounts of mannose and galactose. In addition to the classic fungal O-glycans with reducing end mannoses, we also identified reducing end galactoses which suggest the existence of a protein-O-galactosyltransferase in N. crassa. Because of the excellent genetic resources available for N. crassa, the knowledge of the CBHI O-glycans may enable the future evaluation of the role of O-glycosylation on cellulase function and the development of directed O-glycan/cellulase engineering."}