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

Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates

19 Nov 2014

Abstract excerpt

Intracellular Tau inclusions are a pathological hallmark of several neurodegenerative diseases, collectively known as the tauopathies. They include Alzheimer disease, tangle-only dementia, Pick disease, argyrophilic grain disease, chronic traumatic encephalopathy, progressive supranuclear palsy, and corticobasal degeneration. Tau pathology appears to spread through intercellular propagation, requiring the...

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 Neurological diseases and metabolism
Share to Prion Diseases and Protein Misfolding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25406315
DOI: 10.1074/jbc.m114.589309

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformation Determines the Seeding Potencies of Native and Recombinant Tau AggregatesPMID 25406315Read ↗

Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathiesSemantic proximity Read ↗

Tau Seeding Mouse Models with Patient Brain-Derived AggregatesSemantic proximity Read ↗

Sensitive detection and propagation of brain-derived tau assemblies in HEK293 based wild-type tau seeding assaysSemantic proximity Read ↗

In vitro amplification of pathogenic tau conserves disease-specific bioactive characteristicsSemantic proximity Read ↗

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

Seed-competent tau monomer initiates pathology in PS19 tauopathy miceSemantic proximity Read ↗

Structure-based inhibitors halt prion-like seeding by Alzheimer’s disease–and tauopathy–derived brain tissue samplesSemantic proximity Read ↗

Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice.Semantic proximity Read ↗

Tau seeding without tauopathySemantic proximity Read ↗

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

Cellular and pathological heterogeneity of primary tauopathies.Semantic proximity Read ↗

GFP-Mutant Human Tau Transgenic Mice Develop Tauopathy Following CNS Injections of Alzheimer's Brain-Derived Pathological Tau or Synthetic Mutant Human Tau Fibrils.Semantic proximity Read ↗

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