PubMed:11159919 JSONTXT

{"project":"GlyCosmos6-UBERON","denotations":[{"id":"T1","span":{"begin":41,"end":47},"obj":"Body_part"},{"id":"T2","span":{"begin":227,"end":232},"obj":"Body_part"},{"id":"T3","span":{"begin":331,"end":336},"obj":"Body_part"},{"id":"T4","span":{"begin":453,"end":464},"obj":"Body_part"},{"id":"T5","span":{"begin":466,"end":479},"obj":"Body_part"},{"id":"T6","span":{"begin":498,"end":508},"obj":"Body_part"},{"id":"T7","span":{"begin":561,"end":569},"obj":"Body_part"},{"id":"T10","span":{"begin":660,"end":665},"obj":"Body_part"},{"id":"T11","span":{"begin":778,"end":784},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL_0000312"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL_0000738"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A8","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A9","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":621,"end":628},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":41,"end":47},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T2","span":{"begin":778,"end":784},"obj":"http://purl.bioontology.org/ontology/STY/T024"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":621,"end":628},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":103,"end":247},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":248,"end":358},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":359,"end":509},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":510,"end":721},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":722,"end":795},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"T2","span":{"begin":103,"end":247},"obj":"Sentence"},{"id":"T3","span":{"begin":248,"end":358},"obj":"Sentence"},{"id":"T4","span":{"begin":359,"end":509},"obj":"Sentence"},{"id":"T5","span":{"begin":510,"end":721},"obj":"Sentence"},{"id":"T6","span":{"begin":722,"end":795},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":102},"obj":"Sentence"},{"id":"T2","span":{"begin":103,"end":247},"obj":"Sentence"},{"id":"T3","span":{"begin":248,"end":358},"obj":"Sentence"},{"id":"T4","span":{"begin":359,"end":509},"obj":"Sentence"},{"id":"T5","span":{"begin":510,"end":721},"obj":"Sentence"},{"id":"T6","span":{"begin":722,"end":795},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":621,"end":628},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":61,"end":98},"obj":"Disease"},{"id":"T2","span":{"begin":131,"end":168},"obj":"Disease"},{"id":"T3","span":{"begin":170,"end":173},"obj":"Disease"},{"id":"T4","span":{"begin":342,"end":348},"obj":"Disease"},{"id":"T5","span":{"begin":705,"end":711},"obj":"Disease"},{"id":"T6","span":{"begin":768,"end":774},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0015286"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0015286"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0015286"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0008907"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0008907"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0008907"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GlyCosmos6-CLO","denotations":[{"id":"T1","span":{"begin":453,"end":464},"obj":"http://purl.obolibrary.org/obo/CL_0000057"},{"id":"T2","span":{"begin":466,"end":479},"obj":"http://purl.obolibrary.org/obo/CL_0000312"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

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in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":29,"end":37},"obj":"FMAID:165447"},{"id":"_T2","span":{"begin":29,"end":37},"obj":"FMAID:67257"},{"id":"_T3","span":{"begin":41,"end":47},"obj":"FMAID:256050"},{"id":"_T4","span":{"begin":227,"end":232},"obj":"FMAID:167330"},{"id":"_T5","span":{"begin":233,"end":246},"obj":"FMAID:167256"},{"id":"_T6","span":{"begin":233,"end":246},"obj":"FMAID:62925"},{"id":"_T7","span":{"begin":331,"end":336},"obj":"FMAID:167330"},{"id":"_T8","span":{"begin":453,"end":464},"obj":"FMAID:162340"},{"id":"_T9","span":{"begin":453,"end":464},"obj":"FMAID:63877"},{"id":"_T10","span":{"begin":466,"end":479},"obj":"FMAID:170966"},{"id":"_T11","span":{"begin":481,"end":492},"obj":"FMAID:62122"},{"id":"_T12","span":{"begin":481,"end":492},"obj":"FMAID:166407"},{"id":"_T13","span":{"begin":498,"end":508},"obj":"FMAID:167148"},{"id":"_T14","span":{"begin":498,"end":508},"obj":"FMAID:62852"},{"id":"_T15","span":{"begin":590,"end":602},"obj":"FMAID:167256"},{"id":"_T16","span":{"begin":590,"end":602},"obj":"FMAID:62925"},{"id":"_T17","span":{"begin":621,"end":628},"obj":"FMAID:82743"},{"id":"_T18","span":{"begin":621,"end":628},"obj":"FMAID:196732"},{"id":"_T19","span":{"begin":660,"end":665},"obj":"FMAID:167330"},{"id":"_T20","span":{"begin":666,"end":680},"obj":"FMAID:62871"},{"id":"_T21","span":{"begin":666,"end":680},"obj":"FMAID:167177"},{"id":"_T22","span":{"begin":666,"end":682},"obj":"FMAID:167187"},{"id":"_T23","span":{"begin":666,"end":682},"obj":"FMAID:167178"},{"id":"_T24","span":{"begin":666,"end":682},"obj":"FMAID:62875"},{"id":"_T25","span":{"begin":666,"end":682},"obj":"FMAID:167181"},{"id":"_T26","span":{"begin":666,"end":682},"obj":"FMAID:167183"},{"id":"_T27","span":{"begin":666,"end":682},"obj":"FMAID:62874"},{"id":"_T28","span":{"begin":666,"end":682},"obj":"FMAID:62872"},{"id":"_T29","span":{"begin":666,"end":682},"obj":"FMAID:62873"},{"id":"_T30","span":{"begin":666,"end":682},"obj":"FMAID:62876"},{"id":"_T31","span":{"begin":666,"end":682},"obj":"FMAID:167185"},{"id":"_T32","span":{"begin":778,"end":784},"obj":"FMAID:256050"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":641,"end":647},"obj":"http://www.uniprot.org/uniprot/P11166"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":641,"end":647},"obj":"http://www.uniprot.org/uniprot/P17809"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":41,"end":47},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T2","span":{"begin":778,"end":784},"obj":"http://purl.bioontology.org/ontology/STY/T024"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":10,"end":37},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T2","span":{"begin":12,"end":25},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T3","span":{"begin":85,"end":98},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T4","span":{"begin":155,"end":168},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T5","span":{"begin":12,"end":37},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T6","span":{"begin":621,"end":640},"obj":"http://purl.obolibrary.org/obo/GO_0015758"},{"id":"T7","span":{"begin":629,"end":640},"obj":"http://purl.obolibrary.org/obo/GO_0006810"},{"id":"T8","span":{"begin":697,"end":701},"obj":"http://purl.obolibrary.org/obo/GO_0004617"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":666,"end":680},"obj":"http://purl.obolibrary.org/obo/GO_0003823"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":561,"end":569},"obj":"http://purl.obolibrary.org/obo/GO_0016020"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":41,"end":47},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T2","span":{"begin":778,"end":784},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"T3","span":{"begin":227,"end":232},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"T4","span":{"begin":331,"end":336},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"T5","span":{"begin":660,"end":665},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"bionlp-st-epi-2011-training","denotations":[{"id":"T1","span":{"begin":274,"end":292},"obj":"Protein"},{"id":"T2","span":{"begin":419,"end":437},"obj":"Protein"},{"id":"T3","span":{"begin":641,"end":647},"obj":"Protein"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":29,"end":37},"obj":"http://edamontology.org/topic_0078"},{"id":"T2","span":{"begin":743,"end":753},"obj":"http://edamontology.org/topic_0625"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":29,"end":37},"obj":"http://edamontology.org/data_1467"},{"id":"T2","span":{"begin":29,"end":37},"obj":"http://edamontology.org/format_1208"},{"id":"T3","span":{"begin":303,"end":311},"obj":"http://edamontology.org/operation_2423"},{"id":"T4","span":{"begin":391,"end":397},"obj":"http://edamontology.org/operation_2423"},{"id":"T5","span":{"begin":545,"end":555},"obj":"http://edamontology.org/operation_2423"},{"id":"T6","span":{"begin":743,"end":753},"obj":"http://edamontology.org/data_3275"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":227,"end":232},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":331,"end":336},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"PD-UBERON-AE-B_T3","span":{"begin":660,"end":665},"obj":"http://purl.obolibrary.org/obo/UBERON_0001977"},{"id":"PD-UBERON-AE-B_T4","span":{"begin":41,"end":47},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"PD-UBERON-AE-B_T5","span":{"begin":778,"end":784},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is tissue-dependent."}