PubMed:22128166 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":64,"end":67},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":107,"end":112},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":438,"end":443},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":461,"end":476},"obj":"Glycan_Motif"},{"id":"T8","span":{"begin":556,"end":565},"obj":"Glycan_Motif"},{"id":"T10","span":{"begin":669,"end":678},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G48558GR"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G46613JI"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82109MW"},{"id":"A8","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A9","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"},{"id":"A10","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G68158BT"},{"id":"A11","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G65889KE"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":461,"end":476},"obj":"GlycoEpitope"}],"attributes":[{"id":"A1","pred":"glyco_epitope_db_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0085"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":64,"end":67},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T2","span":{"begin":64,"end":67},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T3","span":{"begin":107,"end":112},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T4","span":{"begin":107,"end":112},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T5","span":{"begin":438,"end":443},"obj":"https://glytoucan.org/Structures/Glycans/G46613JI"},{"id":"T6","span":{"begin":438,"end":443},"obj":"https://glytoucan.org/Structures/Glycans/G48558GR"},{"id":"T7","span":{"begin":461,"end":476},"obj":"https://glytoucan.org/Structures/Glycans/G82109MW"},{"id":"T8","span":{"begin":556,"end":565},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T9","span":{"begin":556,"end":565},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"},{"id":"T10","span":{"begin":669,"end":678},"obj":"https://glytoucan.org/Structures/Glycans/G65889KE"},{"id":"T11","span":{"begin":669,"end":678},"obj":"https://glytoucan.org/Structures/Glycans/G68158BT"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":106},"obj":"Sentence"},{"id":"T2","span":{"begin":107,"end":291},"obj":"Sentence"},{"id":"T3","span":{"begin":292,"end":575},"obj":"Sentence"},{"id":"T4","span":{"begin":576,"end":727},"obj":"Sentence"},{"id":"T5","span":{"begin":728,"end":823},"obj":"Sentence"},{"id":"T6","span":{"begin":824,"end":989},"obj":"Sentence"},{"id":"T7","span":{"begin":990,"end":1049},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":27,"end":42},"obj":"gene:2720"},{"id":"T1","span":{"begin":64,"end":82},"obj":"disease:C0085131"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":146,"end":165},"obj":"HP_0000007"},{"id":"T2","span":{"begin":241,"end":249},"obj":"HP_0003510"},{"id":"T3","span":{"begin":254,"end":276},"obj":"HP_0000924"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"Allie","denotations":[{"id":"SS1_22128166_2_0","span":{"begin":358,"end":375},"obj":"expanded"},{"id":"SS2_22128166_2_0","span":{"begin":377,"end":382},"obj":"abbr"}],"relations":[{"id":"AE1_22128166_2_0","pred":"abbreviatedTo","subj":"SS1_22128166_2_0","obj":"SS2_22128166_2_0"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"22128166-0#27#42#gene2720","span":{"begin":27,"end":42},"obj":"gene2720"},{"id":"22128166-0#64#82#diseaseC0085131","span":{"begin":64,"end":82},"obj":"diseaseC0085131"}],"relations":[{"id":"27#42#gene272064#82#diseaseC0085131","pred":"associated_with","subj":"22128166-0#27#42#gene2720","obj":"22128166-0#64#82#diseaseC0085131"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":64,"end":67},"obj":"Glycan"},{"id":"T2","span":{"begin":107,"end":112},"obj":"Glycan"},{"id":"T3","span":{"begin":438,"end":443},"obj":"Glycan"},{"id":"T4","span":{"begin":461,"end":476},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A5","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A6","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G48558GR"},{"id":"A7","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G48558GR"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G82109MW"},{"id":"A8","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G82109MW"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":241,"end":249},"obj":"Phenotype"},{"id":"T2","span":{"begin":254,"end":276},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003510"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0000924"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":64,"end":82},"obj":"Disease"},{"id":"T2","span":{"begin":107,"end":127},"obj":"Disease"},{"id":"T3","span":{"begin":166,"end":192},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0018149"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0018149"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0002561"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":461,"end":476},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G82109MW"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G82109MW"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":461,"end":476},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0085"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":241,"end":249},"obj":"Phenotype"},{"id":"T2","span":{"begin":254,"end":276},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003510"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0000924"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":64,"end":82},"obj":"Disease"},{"id":"T2","span":{"begin":107,"end":127},"obj":"Disease"},{"id":"T3","span":{"begin":166,"end":192},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0018149"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"MONDO:0018149"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"MONDO:0002561"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":21,"end":26},"obj":"Organism"},{"id":"T2","span":{"begin":619,"end":624},"obj":"Organism"},{"id":"T3","span":{"begin":728,"end":733},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":106},"obj":"Sentence"},{"id":"T2","span":{"begin":107,"end":291},"obj":"Sentence"},{"id":"T3","span":{"begin":292,"end":575},"obj":"Sentence"},{"id":"T4","span":{"begin":576,"end":727},"obj":"Sentence"},{"id":"T5","span":{"begin":728,"end":823},"obj":"Sentence"},{"id":"T6","span":{"begin":824,"end":989},"obj":"Sentence"},{"id":"T7","span":{"begin":990,"end":1049},"obj":"Sentence"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":461,"end":476},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0085"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":146,"end":155},"obj":"Body_part"},{"id":"T2","span":{"begin":166,"end":175},"obj":"Body_part"},{"id":"T3","span":{"begin":341,"end":350},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:74406"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:63836"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:63836"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":21,"end":26},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":619,"end":624},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":728,"end":733},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases.\nG(M1) gangliosidosis and Morquio B are autosomal recessive lysosomal storage diseases associated with a neurodegenerative disorder or dwarfism and skeletal abnormalities, respectively. These diseases are caused by deficiencies in the lysosomal enzyme β-d-galactosidase (β-Gal), which lead to accumulations of the β-Gal substrates, G(M1) ganglioside, and keratan sulfate. β-Gal is an exoglycosidase that catalyzes the hydrolysis of terminal β-linked galactose residues. This study shows the crystal structures of human β-Gal in complex with its catalytic product galactose or with its inhibitor 1-deoxygalactonojirimycin. Human β-Gal is composed of a catalytic TIM barrel domain followed by β-domain 1 and β-domain 2. To gain structural insight into the molecular defects of β-Gal in the above diseases, the disease-causing mutations were mapped onto the three-dimensional structure. Finally, the possible causes of the diseases are discussed."}