PubMed:16595633 JSONTXT

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":190,"end":212},"obj":"HP_0000707"},{"id":"T2","span":{"begin":400,"end":409},"obj":"HP_0001300"},{"id":"T3","span":{"begin":1156,"end":1167},"obj":"HP_0100315"},{"id":"T4","span":{"begin":1185,"end":1194},"obj":"HP_0001300"},{"id":"T5","span":{"begin":1217,"end":1226},"obj":"HP_0100315"},{"id":"T6","span":{"begin":1332,"end":1341},"obj":"HP_0100315"}],"text":"Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients.\nalpha-Synucleinopathies are a group of neurological disorders characterized by the presence of intracellular inclusion bodies containing alpha-synuclein. We previously demonstrated that synphilin-1 interacts with alpha-synuclein, implying a role in Parkinson's disease. We now report the identification and characterization of synphilin-1A, an isoform of synphilin-1, which has enhanced aggregatory properties and causes neurotoxicity. The two transcripts encoding synphilin-1A and synphilin-1 originate from the SNCAIP gene but differ in both their exon organization and initial reading frames used for translation. Synphilin-1A binds to alpha-synuclein and induces the formation of intracellular aggregates in human embryonic kidney 293 cells, primary neuronal cultures, and human dopaminergic cells. Overexpression of synphilin-1A in neurons results in striking cellular toxicity that is attenuated by the formation of synphilin-1A inclusions, which recruit alpha-synuclein. Synphilin-1A is present in Lewy bodies of patients with Parkinson's disease and Diffuse Lewy Body disease, and is observed in detergent-insoluble fractions of brain protein samples obtained from Diffuse Lewy Body disease patients. These findings suggest that synphilin-1A may contribute to neuronal degeneration in alpha-synucleinopathies and also provide important insights into the role of inclusion bodies in neurodegenerative disorders."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"16595633-7#0#9#gene9627","span":{"begin":1129,"end":1138},"obj":"gene9627"},{"id":"16595633-7#56#75#diseaseC0030567","span":{"begin":1185,"end":1204},"obj":"diseaseC0030567"},{"id":"16595633-7#80#105#diseaseC0752347","span":{"begin":1209,"end":1234},"obj":"diseaseC0752347"},{"id":"16595633-8#28#37#gene9627","span":{"begin":1388,"end":1397},"obj":"gene9627"},{"id":"16595633-8#181#208#diseaseC0524851","span":{"begin":1541,"end":1568},"obj":"diseaseC0524851"}],"relations":[{"id":"0#9#gene962756#75#diseaseC0030567","pred":"associated_with","subj":"16595633-7#0#9#gene9627","obj":"16595633-7#56#75#diseaseC0030567"},{"id":"0#9#gene962780#105#diseaseC0752347","pred":"associated_with","subj":"16595633-7#0#9#gene9627","obj":"16595633-7#80#105#diseaseC0752347"},{"id":"28#37#gene9627181#208#diseaseC0524851","pred":"associated_with","subj":"16595633-8#28#37#gene9627","obj":"16595633-8#181#208#diseaseC0524851"}],"text":"Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients.\nalpha-Synucleinopathies are a group of neurological disorders characterized by the presence of intracellular inclusion bodies containing alpha-synuclein. We previously demonstrated that synphilin-1 interacts with alpha-synuclein, implying a role in Parkinson's disease. We now report the identification and characterization of synphilin-1A, an isoform of synphilin-1, which has enhanced aggregatory properties and causes neurotoxicity. The two transcripts encoding synphilin-1A and synphilin-1 originate from the SNCAIP gene but differ in both their exon organization and initial reading frames used for translation. Synphilin-1A binds to alpha-synuclein and induces the formation of intracellular aggregates in human embryonic kidney 293 cells, primary neuronal cultures, and human dopaminergic cells. Overexpression of synphilin-1A in neurons results in striking cellular toxicity that is attenuated by the formation of synphilin-1A inclusions, which recruit alpha-synuclein. Synphilin-1A is present in Lewy bodies of patients with Parkinson's disease and Diffuse Lewy Body disease, and is observed in detergent-insoluble fractions of brain protein samples obtained from Diffuse Lewy Body disease patients. These findings suggest that synphilin-1A may contribute to neuronal degeneration in alpha-synucleinopathies and also provide important insights into the role of inclusion bodies in neurodegenerative disorders."}

{"project":"LocText","denotations":[{"id":"T1","span":{"begin":0,"end":12},"obj":"uniprot:Q9Y6H5"},{"id":"T2","span":{"begin":46,"end":57},"obj":"uniprot:Q9Y6H5"},{"id":"T3","span":{"begin":288,"end":303},"obj":"uniprot:P37840"},{"id":"T4","span":{"begin":337,"end":348},"obj":"uniprot:Q9Y6H5"},{"id":"T5","span":{"begin":364,"end":379},"obj":"uniprot:P37840"},{"id":"T6","span":{"begin":478,"end":490},"obj":"uniprot:Q9Y6H5"},{"id":"T7","span":{"begin":506,"end":517},"obj":"uniprot:Q9Y6H5"},{"id":"T8","span":{"begin":616,"end":628},"obj":"uniprot:Q9Y6H5"},{"id":"T9","span":{"begin":633,"end":644},"obj":"uniprot:Q9Y6H5"},{"id":"T10","span":{"begin":664,"end":670},"obj":"uniprot:Q9Y6H5"},{"id":"T11","span":{"begin":768,"end":780},"obj":"uniprot:Q9Y6H5"},{"id":"T12","span":{"begin":790,"end":805},"obj":"uniprot:P37840"},{"id":"T13","span":{"begin":863,"end":868},"obj":"taxonomy:9606"},{"id":"T14","span":{"begin":928,"end":933},"obj":"taxonomy:9606"},{"id":"T15","span":{"begin":972,"end":984},"obj":"uniprot:Q9Y6H5"},{"id":"T16","span":{"begin":1073,"end":1085},"obj":"uniprot:Q9Y6H5"},{"id":"T17","span":{"begin":1112,"end":1127},"obj":"uniprot:P37840"},{"id":"T18","span":{"begin":1129,"end":1141},"obj":"uniprot:Q9Y6H5"},{"id":"T19","span":{"begin":1388,"end":1400},"obj":"uniprot:Q9Y6H5"}],"namespaces":[{"prefix":"uniprot","uri":"http://identifiers.org/uniprot/"},{"prefix":"taxonomy","uri":"http://identifiers.org/taxonomy/"},{"prefix":"go","uri":"http://identifiers.org/go/"}],"text":"Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients.\nalpha-Synucleinopathies are a group of neurological disorders characterized by the presence of intracellular inclusion bodies containing alpha-synuclein. We previously demonstrated that synphilin-1 interacts with alpha-synuclein, implying a role in Parkinson's disease. We now report the identification and characterization of synphilin-1A, an isoform of synphilin-1, which has enhanced aggregatory properties and causes neurotoxicity. The two transcripts encoding synphilin-1A and synphilin-1 originate from the SNCAIP gene but differ in both their exon organization and initial reading frames used for translation. Synphilin-1A binds to alpha-synuclein and induces the formation of intracellular aggregates in human embryonic kidney 293 cells, primary neuronal cultures, and human dopaminergic cells. Overexpression of synphilin-1A in neurons results in striking cellular toxicity that is attenuated by the formation of synphilin-1A inclusions, which recruit alpha-synuclein. Synphilin-1A is present in Lewy bodies of patients with Parkinson's disease and Diffuse Lewy Body disease, and is observed in detergent-insoluble fractions of brain protein samples obtained from Diffuse Lewy Body disease patients. These findings suggest that synphilin-1A may contribute to neuronal degeneration in alpha-synucleinopathies and also provide important insights into the role of inclusion bodies in neurodegenerative disorders."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":1129,"end":1138},"obj":"gene:9627"},{"id":"T1","span":{"begin":1209,"end":1234},"obj":"disease:C0752347"},{"id":"T2","span":{"begin":1388,"end":1397},"obj":"gene:9627"},{"id":"T3","span":{"begin":1541,"end":1568},"obj":"disease:C0524851"}],"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":"Synphilin-1A: an aggregation-prone isoform of synphilin-1 that causes neuronal death and is present in aggregates from alpha-synucleinopathy patients.\nalpha-Synucleinopathies are a group of neurological disorders characterized by the presence of intracellular inclusion bodies containing alpha-synuclein. We previously demonstrated that synphilin-1 interacts with alpha-synuclein, implying a role in Parkinson's disease. We now report the identification and characterization of synphilin-1A, an isoform of synphilin-1, which has enhanced aggregatory properties and causes neurotoxicity. The two transcripts encoding synphilin-1A and synphilin-1 originate from the SNCAIP gene but differ in both their exon organization and initial reading frames used for translation. Synphilin-1A binds to alpha-synuclein and induces the formation of intracellular aggregates in human embryonic kidney 293 cells, primary neuronal cultures, and human dopaminergic cells. Overexpression of synphilin-1A in neurons results in striking cellular toxicity that is attenuated by the formation of synphilin-1A inclusions, which recruit alpha-synuclein. Synphilin-1A is present in Lewy bodies of patients with Parkinson's disease and Diffuse Lewy Body disease, and is observed in detergent-insoluble fractions of brain protein samples obtained from Diffuse Lewy Body disease patients. These findings suggest that synphilin-1A may contribute to neuronal degeneration in alpha-synucleinopathies and also provide important insights into the role of inclusion bodies in neurodegenerative disorders."}