PubMed:8226878 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":32,"end":43},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":285,"end":296},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":32,"end":43},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"},{"id":"T2","span":{"begin":285,"end":296},"obj":"https://glytoucan.org/Structures/Glycans/G43702JT"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":180},"obj":"Sentence"},{"id":"T2","span":{"begin":181,"end":434},"obj":"Sentence"},{"id":"T3","span":{"begin":435,"end":630},"obj":"Sentence"},{"id":"T4","span":{"begin":631,"end":762},"obj":"Sentence"},{"id":"T5","span":{"begin":763,"end":989},"obj":"Sentence"},{"id":"T6","span":{"begin":990,"end":1324},"obj":"Sentence"},{"id":"T7","span":{"begin":1325,"end":1607},"obj":"Sentence"},{"id":"T8","span":{"begin":1608,"end":1723},"obj":"Sentence"},{"id":"T9","span":{"begin":1724,"end":1822},"obj":"Sentence"},{"id":"T10","span":{"begin":1823,"end":1982},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":180},"obj":"Sentence"},{"id":"T2","span":{"begin":181,"end":434},"obj":"Sentence"},{"id":"T3","span":{"begin":435,"end":630},"obj":"Sentence"},{"id":"T4","span":{"begin":631,"end":762},"obj":"Sentence"},{"id":"T5","span":{"begin":763,"end":989},"obj":"Sentence"},{"id":"T6","span":{"begin":990,"end":1324},"obj":"Sentence"},{"id":"T7","span":{"begin":1325,"end":1607},"obj":"Sentence"},{"id":"T8","span":{"begin":1608,"end":1723},"obj":"Sentence"},{"id":"T9","span":{"begin":1724,"end":1822},"obj":"Sentence"},{"id":"T10","span":{"begin":1823,"end":1982},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"http://purl.obolibrary.org/obo/MAT_0000189"},{"id":"T2","span":{"begin":327,"end":336},"obj":"http://purl.obolibrary.org/obo/MAT_0000189"},{"id":"T3","span":{"begin":610,"end":616},"obj":"http://purl.obolibrary.org/obo/MAT_0000226"},{"id":"T4","span":{"begin":1635,"end":1640},"obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":32,"end":43},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"T2","span":{"begin":285,"end":296},"obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":53,"end":75},"obj":"gene:176"},{"id":"T1","span":{"begin":152,"end":168},"obj":"disease:C0008449"},{"id":"T2","span":{"begin":118,"end":126},"obj":"gene:176"},{"id":"T3","span":{"begin":152,"end":168},"obj":"disease:C0008449"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"8226878-0#53#75#gene176","span":{"begin":53,"end":75},"obj":"gene176"},{"id":"8226878-0#118#126#gene176","span":{"begin":118,"end":126},"obj":"gene176"},{"id":"8226878-0#152#168#diseaseC0008449","span":{"begin":152,"end":168},"obj":"diseaseC0008449"},{"id":"8226878-4#115#123#gene176","span":{"begin":878,"end":886},"obj":"gene176"},{"id":"8226878-4#100#114#diseaseC0008479","span":{"begin":863,"end":877},"obj":"diseaseC0008479"}],"relations":[{"id":"53#75#gene176152#168#diseaseC0008449","pred":"associated_with","subj":"8226878-0#53#75#gene176","obj":"8226878-0#152#168#diseaseC0008449"},{"id":"118#126#gene176152#168#diseaseC0008449","pred":"associated_with","subj":"8226878-0#118#126#gene176","obj":"8226878-0#152#168#diseaseC0008449"},{"id":"115#123#gene176100#114#diseaseC0008479","pred":"associated_with","subj":"8226878-4#115#123#gene176","obj":"8226878-4#100#114#diseaseC0008479"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":32,"end":43},"obj":"Glycan"},{"id":"T2","span":{"begin":285,"end":296},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Body_part"},{"id":"T2","span":{"begin":327,"end":336},"obj":"Body_part"},{"id":"T3","span":{"begin":610,"end":616},"obj":"Body_part"},{"id":"T4","span":{"begin":1635,"end":1640},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000189"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000189"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000226"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":863,"end":877},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0006765"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":152,"end":168},"obj":"Disease"},{"id":"T3","span":{"begin":863,"end":877},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005516"},{"id":"A2","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0020779"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0008977"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":32,"end":43},"obj":"Glycan"},{"id":"T2","span":{"begin":285,"end":296},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G43702JT"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":32,"end":43},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":285,"end":296},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":863,"end":877},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0006765"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-CL","denotations":[{"id":"T1","span":{"begin":1594,"end":1606},"obj":"Cell"},{"id":"T2","span":{"begin":1970,"end":1981},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000138"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000138"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Body_part"},{"id":"T3","span":{"begin":327,"end":336},"obj":"Body_part"},{"id":"T5","span":{"begin":492,"end":501},"obj":"Body_part"},{"id":"T6","span":{"begin":610,"end":616},"obj":"Body_part"},{"id":"T7","span":{"begin":1594,"end":1606},"obj":"Body_part"},{"id":"T8","span":{"begin":1635,"end":1640},"obj":"Body_part"},{"id":"T9","span":{"begin":1970,"end":1981},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002418"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007844"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002418"},{"id":"A4","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0007844"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000922"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000138"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL_0000138"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":152,"end":168},"obj":"Disease"},{"id":"T2","span":{"begin":863,"end":877},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0020779"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"MONDO:0008977"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":849,"end":854},"obj":"Organism"},{"id":"T2","span":{"begin":859,"end":862},"obj":"Organism"},{"id":"T4","span":{"begin":965,"end":974},"obj":"Organism"},{"id":"T5","span":{"begin":1095,"end":1100},"obj":"Organism"},{"id":"T6","span":{"begin":1104,"end":1107},"obj":"Organism"},{"id":"T8","span":{"begin":1151,"end":1158},"obj":"Organism"},{"id":"T9","span":{"begin":1219,"end":1226},"obj":"Organism"},{"id":"T10","span":{"begin":1309,"end":1318},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10114"},{"id":"A3","pred":"db_id","subj":"T2","obj":"10116"},{"id":"A4","pred":"db_id","subj":"T4","obj":"40674"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"},{"id":"A6","pred":"db_id","subj":"T6","obj":"10114"},{"id":"A7","pred":"db_id","subj":"T6","obj":"10116"},{"id":"A8","pred":"db_id","subj":"T8","obj":"3846"},{"id":"A9","pred":"db_id","subj":"T9","obj":"3846"},{"id":"A10","pred":"db_id","subj":"T10","obj":"40674"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":32,"end":43},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":285,"end":296},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0081"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0081"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":180},"obj":"Sentence"},{"id":"T2","span":{"begin":181,"end":434},"obj":"Sentence"},{"id":"T3","span":{"begin":435,"end":630},"obj":"Sentence"},{"id":"T4","span":{"begin":631,"end":762},"obj":"Sentence"},{"id":"T5","span":{"begin":763,"end":989},"obj":"Sentence"},{"id":"T6","span":{"begin":990,"end":1324},"obj":"Sentence"},{"id":"T7","span":{"begin":1325,"end":1607},"obj":"Sentence"},{"id":"T8","span":{"begin":1608,"end":1723},"obj":"Sentence"},{"id":"T9","span":{"begin":1724,"end":1822},"obj":"Sentence"},{"id":"T10","span":{"begin":1823,"end":1982},"obj":"Sentence"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":180},"obj":"Sentence"},{"id":"T2","span":{"begin":181,"end":434},"obj":"Sentence"},{"id":"T3","span":{"begin":435,"end":630},"obj":"Sentence"},{"id":"T4","span":{"begin":631,"end":762},"obj":"Sentence"},{"id":"T5","span":{"begin":763,"end":989},"obj":"Sentence"},{"id":"T6","span":{"begin":990,"end":1324},"obj":"Sentence"},{"id":"T7","span":{"begin":1325,"end":1607},"obj":"Sentence"},{"id":"T8","span":{"begin":1608,"end":1723},"obj":"Sentence"},{"id":"T9","span":{"begin":1724,"end":1822},"obj":"Sentence"},{"id":"T10","span":{"begin":1823,"end":1982},"obj":"Sentence"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Body_part"},{"id":"T2","span":{"begin":327,"end":336},"obj":"Body_part"},{"id":"T3","span":{"begin":610,"end":616},"obj":"Body_part"},{"id":"T4","span":{"begin":1594,"end":1606},"obj":"Body_part"},{"id":"T5","span":{"begin":1635,"end":1640},"obj":"Body_part"},{"id":"T6","span":{"begin":1970,"end":1981},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:71500"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:71500"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:296970"},{"id":"A4","pred":"db_id","subj":"T4","obj":"FMA:66782"},{"id":"A5","pred":"db_id","subj":"T5","obj":"FMA:7197"},{"id":"A6","pred":"db_id","subj":"T6","obj":"FMA:66782"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Body_part"},{"id":"T2","span":{"begin":327,"end":336},"obj":"Body_part"},{"id":"T3","span":{"begin":610,"end":616},"obj":"Body_part"},{"id":"T4","span":{"begin":1635,"end":1640},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000189"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000189"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000226"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000097"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":849,"end":854},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":859,"end":862},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1095,"end":1100},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1104,"end":1107},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1151,"end":1158},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1219,"end":1226},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10114"},{"id":"A3","pred":"db_id","subj":"T2","obj":"10116"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"10114"},{"id":"A6","pred":"db_id","subj":"T5","obj":"10116"},{"id":"A7","pred":"db_id","subj":"T7","obj":"3846"},{"id":"A8","pred":"db_id","subj":"T8","obj":"3846"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":22,"end":31},"obj":"Body_part"},{"id":"T3","span":{"begin":327,"end":336},"obj":"Body_part"},{"id":"T5","span":{"begin":492,"end":501},"obj":"Body_part"},{"id":"T6","span":{"begin":610,"end":616},"obj":"Body_part"},{"id":"T7","span":{"begin":1594,"end":1606},"obj":"Body_part"},{"id":"T8","span":{"begin":1635,"end":1640},"obj":"Body_part"},{"id":"T9","span":{"begin":1970,"end":1981},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002418"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007844"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002418"},{"id":"A4","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0007844"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_2000106"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000922"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CL_0000138"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0002107"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CL_0000138"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":1594,"end":1606},"obj":"Cell"},{"id":"T2","span":{"begin":1970,"end":1981},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000138"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000138"}],"text":"cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.\nWe previously reported the cloning and sequencing of a 1.5-kilobase cDNA which encoded a portion of the chondroitin sulfate domain from the chick cartilage proteoglycan core protein and the localization of a species-specific monoclonal antibody epitope. Using polymerase chain reaction amplification and primer extension, cDNA clones which code for the entire proteoglycan core protein have now been obtained from a 10-day chick embryo cDNA library. The composite sequence is 6464 nucleotides long, coding for a protein of 2109 amino acid residues with a calculated M(r) = 223,500. The overall arrangement of globular and carbohydrate-attachment domains is similar to human and rat chondrosarcoma aggrecan, but there are significant differences in detailed homology between chick and mammalian core proteins. Most significantly a highly repetitive region (19 repeat units of 20 residues each), not found in either human or rat, enlarges one of the characteristic serine-glycine containing regions (designated CS-2) while the other serine-glycine containing domain (designated CS-1) is approximately one-fourth the length of the mammalian CS-1. Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation at position 4553 (G to T transversion) that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes. Genomic DNA from nanomelic liver was also digested with restriction enzyme BsaBI to verify the G to T transversion. This single mutation leads to a shortened core protein precursor with a calculated M(r) = 158,300. The resulting phenotype, nanomelia, arises because the truncated core protein is neither processed to a mature proteoglycan, nor secreted from the chondrocyte."}