PubMed:1301189 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":150},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":151,"end":258},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":259,"end":444},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":445,"end":569},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":570,"end":807},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":808,"end":1042},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1043,"end":1184},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1185,"end":1389},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1390,"end":1535},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1536,"end":1746},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":150},"obj":"Sentence"},{"id":"T2","span":{"begin":151,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":444},"obj":"Sentence"},{"id":"T4","span":{"begin":445,"end":569},"obj":"Sentence"},{"id":"T5","span":{"begin":570,"end":807},"obj":"Sentence"},{"id":"T6","span":{"begin":808,"end":1042},"obj":"Sentence"},{"id":"T7","span":{"begin":1043,"end":1184},"obj":"Sentence"},{"id":"T8","span":{"begin":1185,"end":1389},"obj":"Sentence"},{"id":"T9","span":{"begin":1390,"end":1535},"obj":"Sentence"},{"id":"T10","span":{"begin":1536,"end":1746},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"PubCasesORDO","denotations":[{"id":"AB1","span":{"begin":181,"end":198},"obj":"ORDO:845"},{"id":"TI1","span":{"begin":102,"end":119},"obj":"ORDO:845"},{"id":"AB2","span":{"begin":1638,"end":1655},"obj":"ORDO:845"}],"namespaces":[{"prefix":"ORDO","uri":"http://www.orpha.net/ORDO/Orphanet_"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBIDiseaseCorpus","denotations":[{"id":"T1","span":{"begin":102,"end":119},"obj":"SpecificDisease:D013661"},{"id":"T2","span":{"begin":181,"end":198},"obj":"SpecificDisease:D013661"},{"id":"T3","span":{"begin":200,"end":203},"obj":"SpecificDisease:D013661"},{"id":"T4","span":{"begin":1638,"end":1655},"obj":"Modifier:D013661"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBI-Disease-Train","denotations":[{"id":"T2315","span":{"begin":102,"end":119},"obj":"SpecificDisease"},{"id":"T2316","span":{"begin":181,"end":198},"obj":"SpecificDisease"},{"id":"T2317","span":{"begin":200,"end":203},"obj":"SpecificDisease"},{"id":"T2318","span":{"begin":1638,"end":1655},"obj":"Modifier"}],"attributes":[{"id":"A2315","pred":"database_id","subj":"T2315","obj":"D013661"},{"id":"A2316","pred":"database_id","subj":"T2316","obj":"D013661"},{"id":"A2317","pred":"database_id","subj":"T2317","obj":"D013661"},{"id":"A2318","pred":"database_id","subj":"T2318","obj":"D013661"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBI-Disease-Corpus-All","denotations":[{"id":"T2315","span":{"begin":102,"end":119},"obj":"SpecificDisease"},{"id":"T2316","span":{"begin":181,"end":198},"obj":"SpecificDisease"},{"id":"T2317","span":{"begin":200,"end":203},"obj":"SpecificDisease"},{"id":"T2318","span":{"begin":1638,"end":1655},"obj":"Modifier"}],"attributes":[{"id":"A2315","pred":"database_id","subj":"T2315","obj":"D013661"},{"id":"A2316","pred":"database_id","subj":"T2316","obj":"D013661"},{"id":"A2317","pred":"database_id","subj":"T2317","obj":"D013661"},{"id":"A2318","pred":"database_id","subj":"T2318","obj":"D013661"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBI-Disease-Corpus-2stage-All","denotations":[{"id":"T1","span":{"begin":87,"end":119},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":172,"end":198},"obj":"SpecificDisease"},{"id":"T3","span":{"begin":200,"end":203},"obj":"SpecificDisease"},{"id":"T4","span":{"begin":1626,"end":1655},"obj":"SpecificDisease"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBI-Disease-Corpus-rezarta-All","denotations":[{"id":"T1","span":{"begin":87,"end":119},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":172,"end":198},"obj":"SpecificDisease"},{"id":"T3","span":{"begin":200,"end":203},"obj":"SpecificDisease"},{"id":"T4","span":{"begin":1626,"end":1655},"obj":"SpecificDisease"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBI-Disease-Corpus-4oGuideline-All","denotations":[{"id":"T1","span":{"begin":87,"end":119},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":172,"end":204},"obj":"SpecificDisease"},{"id":"T3","span":{"begin":1626,"end":1655},"obj":"SpecificDisease"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}

{"project":"NCBI-Disease-Corpus-Simple-All","denotations":[{"id":"T1","span":{"begin":102,"end":119},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":181,"end":198},"obj":"SpecificDisease"},{"id":"T3","span":{"begin":1626,"end":1637},"obj":"Modifier"},{"id":"T4","span":{"begin":1638,"end":1655},"obj":"SpecificDisease"}],"text":"A glycine250--\u003e aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.\nThe mutation causing juvenile Tay-Sachs disease (TSD) in two sibs of Lebanese-Maronite origin is described. An mRNA-containing extract of cultured fibroblasts obtained from one of the probands was used as a template to amplify the coding sequence of the hexosaminidase A (Hex A) alpha-subunit. Sequencing of amplified cDNA fragments revealed a single alteration, guanine to adenine at nt 749 creating a G250D mutation. The mutation introduces a new recognition site for the restriction enzyme Eco RV, permitting identification of heterozygotes for this allele following PCR amplification and Eco RV digestion of exon 7 sequences from genomic DNA templates. In order to test the effect of this substitution, an in vitro mutagenized cDNA construct was introduced into a mammalian expression vector and transfected into monkey Cos-1 cells separately or along with a beta-cDNA expression vector. When the mutant alpha-cDNA was the only gene introduced into COS cells no enzymatic activity above endogenous COS cell activity was detected. Cotransfection of normal alpha-cDNA and beta-cDNA followed by immunoprecipitation of human Hex A resulted in 20-fold increase in the ratio between positive and negative (mock transfection) control values. This allowed the detection of some residual activity (12% of the positive control) when the mutant alpha-cDNA replaced its wild-type counterpart. The predicted protein environment in which the mutation occurs is compared to that of the adult-onset Tay-Sachs disease mutation caused by a Gly269--\u003eSer substitution in exon 7.(ABSTRACT TRUNCATED AT 250 WORDS)"}