Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Fibrillogenic Nuclei Composed of P301L Mutant Tau Induce Elongation of P301L Tau but Not Wild-type Tau

26 May 2007

Abstract excerpt

Frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), an autosomal, dominantly inherited neurodegenerative disorder caused by tau gene mutations, is neuropathologically characterized by intraneuronal filamentous inclusions of hyperphosphorylated tau protein. Biochemical and immunocytochemical analyses have shown that only mutant tau is deposited in patients harboring P301L missense mutation,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alzheimer's disease research and treatments
Share to Cancer-related gene regulation
Share to Nuclear Receptors and Signaling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 17526496
DOI: 10.1074/jbc.m611876200

Provenance

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fibrillogenic Nuclei Composed of P301L Mutant Tau Induce Elongation of P301L Tau but Not Wild-type TauPMID 17526496Read ↗

Conformation Determines the Seeding Potencies of Native and Recombinant Tau AggregatesSemantic proximity Read ↗

Frontotemporal dementia with Parkinsonism linked to chromosome-17 mutations enhance tau oligomer formation.Semantic proximity Read ↗

Tau Fibril Formation in Cultured Cells Compatible with a Mouse Model of TauopathySemantic proximity Read ↗

Distinct microscopic mechanisms for the accelerated aggregation of pathogenic Tau mutants revealed by kinetic analysis.Semantic proximity Read ↗

Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathiesSemantic proximity Read ↗

Familial frontotemporal dementia and parkinsonism with a novel N296H mutation in exon 10 of the tau gene and a widespread tau accumulation in the glial cells.Semantic proximity Read ↗

Tau filament formation in transgenic mice expressing P301L tau.Semantic proximity Read ↗

Mutated tau binds less avidly to microtubules than wildtype tau in living cells.Semantic proximity Read ↗

alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease.Semantic proximity Read ↗

Mutant MAPT Induces rDNA Transcriptional Hyperactivation and Nucleolar Stress in Cellular ModelsSemantic proximity Read ↗

Cryo‐EM structures of tau filaments from SH‐SY5Y cells seeded with brain extracts from cases of Alzheimer's disease and corticobasal degenerationSemantic proximity Read ↗

Tau antibody 77G7 targeting microtubule binding domain suppresses proteopathic tau to seed tau aggregationSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.