Modelling C9ORF72 hexanucleotide repeat expansion in amyotrophic lateral sclerosis and frontotemporal dementia.
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The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulationBioinformatics Data Mining Approach Suggests Coexpression of AGTPBP1 with an ALS-linked Gene C9orf72.Molecular network analysis suggests a logical hypothesis for the pathological role of c9orf72 in amyotrophic lateral sclerosis/frontotemporal dementia.C9orf72 hypermethylation protects against repeat expansion-associated pathology in ALS/FTD.Structural basis of nucleic-acid recognition and double-strand unwinding by the essential neuronal protein Pur-alphaC9orf72 and RAB7L1 regulate vesicle trafficking in amyotrophic lateral sclerosis and frontotemporal dementia.Endocytic membrane trafficking and neurodegenerative disease.Isoform-specific antibodies reveal distinct subcellular localizations of C9orf72 in amyotrophic lateral sclerosis.Characterization of the dipeptide repeat protein in the molecular pathogenesis of c9FTD/ALS.A feedback loop between dipeptide-repeat protein, TDP-43 and karyopherin-α mediates C9orf72-related neurodegeneration
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Modelling C9ORF72 hexanucleotide repeat expansion in amyotrophic lateral sclerosis and frontotemporal dementia.
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article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artículo científico
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name
Modelling C9ORF72 hexanucleoti ...... s and frontotemporal dementia.
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type
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Modelling C9ORF72 hexanucleoti ...... s and frontotemporal dementia.
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prefLabel
Modelling C9ORF72 hexanucleoti ...... s and frontotemporal dementia.
@en
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Modelling C9ORF72 hexanucleoti ...... is and frontotemporal dementia
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Alan Stepto
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10.1007/S00401-013-1235-1
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2013-12-24T00:00:00Z
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1023364081