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Article

Are neuronal intranuclear inclusions the common neuropathology of triplet-repeat disorders with polyglutamine-repeat expansions?

1 Jan 1998

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Identifiers

PMID: 9439509
DOI: 10.1016/s0140-6736(97)08360-8

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Are neuronal intranuclear inclusions the common neuropathology of triplet-repeat disorders with polyglutamine-repeat expansions?PMID 9439509Read ↗

Intranuclear Neuronal Inclusions: A Common Pathogenic Mechanism for Glutamine-Repeat Neurodegenerative Diseases?Semantic proximity Read ↗

Neuronal intranuclear inclusion disease: Polyglycine protein is the culpritSemantic proximity Read ↗

Trinucleotide repeats and neurodegenerative disease.Semantic proximity Read ↗

Intranuclear Inclusions of Expanded Polyglutamine Protein in Spinocerebellar Ataxia Type 3Semantic proximity Read ↗

Non-expanded polyglutamine proteins in intranuclear inclusions of hereditary ataxias – triple-labeling immunofluorescence studySemantic proximity Read ↗

Progressive formation of inclusions in the striatum and hippocampus of mice transgenic for the human Huntington's disease mutation.Semantic proximity Read ↗

Distribution of dipeptide repeat proteins in cellular models and C9orf72 mutation cases suggests link to transcriptional silencingSemantic proximity Read ↗

Dipeptide repeat protein inclusions are rare in the spinal cord and almost absent from motor neurons in C9ORF72 mutant amyotrophic lateral sclerosis and are unlikely to cause their degenerationSemantic proximity Read ↗

p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS.Semantic proximity Read ↗

A 30-unit hexanucleotide repeat expansion in C9orf72 induces pathological lesions with dipeptide-repeat proteins and RNA foci, but not TDP-43 inclusions and clinical diseaseSemantic proximity Read ↗

Nucleo–cytoplasmic transport defects and protein aggregates in neurodegenerationSemantic proximity Read ↗

Neuronal intranuclear inclusion disease is genetically heterogeneous.Semantic proximity Read ↗

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