PubMed:3265398 JSONTXT

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":6,"end":52},"obj":"gene:3251"},{"id":"T1","span":{"begin":131,"end":151},"obj":"disease:C0023374"},{"id":"T2","span":{"begin":6,"end":52},"obj":"gene:3251"},{"id":"T3","span":{"begin":153,"end":164},"obj":"disease:C0023374"},{"id":"T4","span":{"begin":210,"end":256},"obj":"gene:3251"},{"id":"T5","span":{"begin":300,"end":320},"obj":"disease:C0023374"},{"id":"T6","span":{"begin":258,"end":262},"obj":"gene:3251"},{"id":"T7","span":{"begin":300,"end":320},"obj":"disease:C0023374"}],"relations":[{"id":"R4","pred":"associated_with","subj":"T6","obj":"T7"},{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"},{"id":"R3","pred":"associated_with","subj":"T4","obj":"T5"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland).\nWe have determined the molecular basis for hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency in a patient, J.H., with Lesch-Nyhan syndrome. Radioimmunoassay of lysates of erythrocytes or cultured B-lymphoblasts showed that this patient had no detectable HPRT enzyme activity or HPRT protein. HPRT-specific mRNA levels were normal by Northern analysis. We created a cDNA library from mRNA isolated from cultured lymphoblasts derived from this patient. Nucleotide sequencing of full-length HPRT cDNA clones revealed a single nucleotide (nt) substitution: a T-to-A transversion at nt 389. We have designated this variant HPRTMidland. The predicted amino acid (aa) substitution in HPRTMidland is a valine to aspartic acid at aa 130. This substitution is within 2 aa of the amino acid substitution in a previously defined HPRT variant, HPRTAnn Arbor. Both mutations are within a highly conserved sequence in the putative 5-phosphoribosyl-1-pyrophosphate-binding domain. The amino acid substitution in HPRTMidland causes a significant perturbation in the predicted secondary structure of this region. The HPRTMidland mutation affects a different domain of HPRT than the HPRTFlint mutation located at 167 nt away."}

{"project":"DisGeNET5_variant_disease","denotations":[{"id":"3265398-7#63#96#geners137852483","span":{"begin":876,"end":909},"obj":"geners137852483"},{"id":"3265398-7#46#57#diseaseC0023374","span":{"begin":859,"end":870},"obj":"diseaseC0023374"}],"relations":[{"id":"63#96#geners13785248346#57#diseaseC0023374","pred":"associated_with","subj":"3265398-7#63#96#geners137852483","obj":"3265398-7#46#57#diseaseC0023374"}],"text":"Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland).\nWe have determined the molecular basis for hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency in a patient, J.H., with Lesch-Nyhan syndrome. Radioimmunoassay of lysates of erythrocytes or cultured B-lymphoblasts showed that this patient had no detectable HPRT enzyme activity or HPRT protein. HPRT-specific mRNA levels were normal by Northern analysis. We created a cDNA library from mRNA isolated from cultured lymphoblasts derived from this patient. Nucleotide sequencing of full-length HPRT cDNA clones revealed a single nucleotide (nt) substitution: a T-to-A transversion at nt 389. We have designated this variant HPRTMidland. The predicted amino acid (aa) substitution in HPRTMidland is a valine to aspartic acid at aa 130. This substitution is within 2 aa of the amino acid substitution in a previously defined HPRT variant, HPRTAnn Arbor. Both mutations are within a highly conserved sequence in the putative 5-phosphoribosyl-1-pyrophosphate-binding domain. The amino acid substitution in HPRTMidland causes a significant perturbation in the predicted secondary structure of this region. The HPRTMidland mutation affects a different domain of HPRT than the HPRTFlint mutation located at 167 nt away."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"3265398-0#6#52#gene3251","span":{"begin":6,"end":52},"obj":"gene3251"},{"id":"3265398-0#131#151#diseaseC0023374","span":{"begin":131,"end":151},"obj":"diseaseC0023374"},{"id":"3265398-0#153#164#diseaseC0023374","span":{"begin":153,"end":164},"obj":"diseaseC0023374"}],"relations":[{"id":"6#52#gene3251131#151#diseaseC0023374","pred":"associated_with","subj":"3265398-0#6#52#gene3251","obj":"3265398-0#131#151#diseaseC0023374"},{"id":"6#52#gene3251153#164#diseaseC0023374","pred":"associated_with","subj":"3265398-0#6#52#gene3251","obj":"3265398-0#153#164#diseaseC0023374"}],"text":"Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland).\nWe have determined the molecular basis for hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency in a patient, J.H., with Lesch-Nyhan syndrome. Radioimmunoassay of lysates of erythrocytes or cultured B-lymphoblasts showed that this patient had no detectable HPRT enzyme activity or HPRT protein. HPRT-specific mRNA levels were normal by Northern analysis. We created a cDNA library from mRNA isolated from cultured lymphoblasts derived from this patient. Nucleotide sequencing of full-length HPRT cDNA clones revealed a single nucleotide (nt) substitution: a T-to-A transversion at nt 389. We have designated this variant HPRTMidland. The predicted amino acid (aa) substitution in HPRTMidland is a valine to aspartic acid at aa 130. This substitution is within 2 aa of the amino acid substitution in a previously defined HPRT variant, HPRTAnn Arbor. Both mutations are within a highly conserved sequence in the putative 5-phosphoribosyl-1-pyrophosphate-binding domain. The amino acid substitution in HPRTMidland causes a significant perturbation in the predicted secondary structure of this region. The HPRTMidland mutation affects a different domain of HPRT than the HPRTFlint mutation located at 167 nt away."}