PubMed:16361247 / 0-742 JSON TXT

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sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":144},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":145,"end":612},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":144},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":144},"obj":"Sentence"},{"id":"T2","span":{"begin":145,"end":612},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

GlycoBiology-GDGDB

{"project":"GlycoBiology-GDGDB","denotations":[{"id":"_T1","span":{"begin":280,"end":284},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00012"},{"id":"_T2","span":{"begin":280,"end":284},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00013"},{"id":"_T3","span":{"begin":280,"end":284},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00014"},{"id":"_T4","span":{"begin":280,"end":284},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00015"},{"id":"_T5","span":{"begin":280,"end":284},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00016"},{"id":"_T6","span":{"begin":280,"end":284},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00017"},{"id":"_T7","span":{"begin":371,"end":375},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00012"},{"id":"_T8","span":{"begin":371,"end":375},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00013"},{"id":"_T9","span":{"begin":371,"end":375},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00014"},{"id":"_T10","span":{"begin":371,"end":375},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00015"},{"id":"_T11","span":{"begin":371,"end":375},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00016"},{"id":"_T12","span":{"begin":371,"end":375},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00017"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":242,"end":261},"obj":"http://www.uniprot.org/uniprot/Q99519"},{"id":"T2","span":{"begin":280,"end":284},"obj":"http://www.uniprot.org/uniprot/Q99519"},{"id":"T3","span":{"begin":371,"end":375},"obj":"http://www.uniprot.org/uniprot/Q99519"},{"id":"T8","span":{"begin":290,"end":318},"obj":"http://www.uniprot.org/uniprot/P10619"},{"id":"T9","span":{"begin":332,"end":336},"obj":"http://www.uniprot.org/uniprot/P10619"},{"id":"T11","span":{"begin":600,"end":611},"obj":"http://www.uniprot.org/uniprot/P10619"},{"id":"T12","span":{"begin":577,"end":595},"obj":"http://www.uniprot.org/uniprot/P16278"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":242,"end":261},"obj":"http://www.uniprot.org/uniprot/O35657"},{"id":"T2","span":{"begin":290,"end":318},"obj":"http://www.uniprot.org/uniprot/P16675"},{"id":"T3","span":{"begin":332,"end":336},"obj":"http://www.uniprot.org/uniprot/P16675"},{"id":"T5","span":{"begin":600,"end":611},"obj":"http://www.uniprot.org/uniprot/P16675"},{"id":"T6","span":{"begin":577,"end":595},"obj":"http://www.uniprot.org/uniprot/P23780"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":577,"end":581},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T2","span":{"begin":577,"end":581},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":192,"end":199},"obj":"http://purl.obolibrary.org/obo/GO_0051235"},{"id":"T2","span":{"begin":192,"end":199},"obj":"http://purl.obolibrary.org/obo/GO_0035732"},{"id":"T3","span":{"begin":441,"end":452},"obj":"http://purl.obolibrary.org/obo/GO_0032502"},{"id":"T4","span":{"begin":648,"end":671},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T6","span":{"begin":650,"end":662},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T8","span":{"begin":650,"end":671},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T10","span":{"begin":704,"end":713},"obj":"http://purl.obolibrary.org/obo/GO_0046960"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":182,"end":191},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T2","span":{"begin":242,"end":251},"obj":"http://purl.obolibrary.org/obo/GO_0005764"},{"id":"T3","span":{"begin":290,"end":299},"obj":"http://purl.obolibrary.org/obo/GO_0005764"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":182,"end":191},"obj":"http://edamontology.org/topic_0616"},{"id":"T2","span":{"begin":200,"end":208},"obj":"http://edamontology.org/topic_0634"},{"id":"T3","span":{"begin":223,"end":230},"obj":"http://edamontology.org/topic_3053"},{"id":"T4","span":{"begin":242,"end":251},"obj":"http://edamontology.org/topic_0616"},{"id":"T5","span":{"begin":290,"end":299},"obj":"http://edamontology.org/topic_0616"},{"id":"T6","span":{"begin":311,"end":318},"obj":"http://edamontology.org/topic_0078"},{"id":"T7","span":{"begin":663,"end":671},"obj":"http://edamontology.org/topic_0078"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":100,"end":106},"obj":"http://edamontology.org/operation_3435"},{"id":"T2","span":{"begin":300,"end":318},"obj":"http://edamontology.org/format_1219"},{"id":"T3","span":{"begin":311,"end":318},"obj":"http://edamontology.org/format_1208"},{"id":"T4","span":{"begin":311,"end":318},"obj":"http://edamontology.org/data_1467"},{"id":"T5","span":{"begin":616,"end":628},"obj":"http://edamontology.org/operation_2246"},{"id":"T6","span":{"begin":663,"end":671},"obj":"http://edamontology.org/data_1467"},{"id":"T7","span":{"begin":663,"end":671},"obj":"http://edamontology.org/format_1208"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

DisGeNET5_gene_disease

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":514,"end":520},"obj":"http://purl.obolibrary.org/obo/MAT_0000488"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

DisGeNET

mondo_disease

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":64,"end":74},"obj":"Disease"},{"id":"T2","span":{"begin":79,"end":96},"obj":"Disease"},{"id":"T3","span":{"begin":145,"end":155},"obj":"Disease"},{"id":"T4","span":{"begin":160,"end":177},"obj":"Disease"},{"id":"T5","span":{"begin":182,"end":208},"obj":"Disease"},{"id":"T6","span":{"begin":371,"end":386},"obj":"Disease"},{"id":"T7","span":{"begin":561,"end":595},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0017734"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0009737"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0017734"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0009737"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0002561"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0009738"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MONDO_0018149"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

Lectin-Jamboree-Sentence

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":144},"obj":"Sentence"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":47,"end":58},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000057"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":47,"end":58},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000057"}],"text":"Elimination of abnormal sialylglycoproteins in fibroblasts with sialidosis and galactosialidosis by normal gene transfer and enzyme replacement.\nSialidosis and galactosialidosis are lysosomal storage diseases caused by the genetic defects of lysosomal sialidase (neuraminidase-1; NEU1) and lysosomal protective protein/cathepsin A (PPCA), respectively, associated with a NEU1 deficiency, excessive accumulation of sialylglycoconjugates, and development of progressive neurosomatic manifestations; in addition, the latter disorder is accompanied by simultaneous deficiencies of beta-galactosidase and cathepsin A. We demonstrated that a few soluble N-glycosylated proteins carrying sialyloligosaccharides sensitive to glycopeptidase F (GPF) ca"}

PubMed:16361247 / 0-742 JSONTXT

Annnotations TAB JSON ListView MergeView

PubMed:16361247 / 0-742 JSON TXT