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

Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations.

The Journal of biological chemistry - 3 Jun 2016

Meyer Virginia, Holden Michael R, Weismiller Hilary A, Eaton Gareth R, Eaton Sandra S, Margittai Martin

Abstract excerpt

Tau fibrils are pathological aggregates that can transfer between neurons and then recruit soluble Tau monomers by template-assisted conversion. The propagation of different fibril polymorphs is thought to be a contributing factor to phenotypic diversity in Alzheimer disease and other Tauopathies. We found that a homogeneous population of Tau fibrils composed of the truncated version K18 (residues 244-372)...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Electron Spin Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Microscopy, Electron

Share to Protein Aggregation, Pathological

Share to Protein Conformation

Share to tau Proteins

Share to Tauopathies

Source

Open in PubMed Open full text

Identifiers

PMID: 27080260
DOI: 10.1074/jbc.M116.715557
PMCID: PMC4933275

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Fracture and Growth Are Competing Forces Determining the Fate of Conformers in Tau Fibril Populations.PMID 27080260Read ↗

Passaging Human Tauopathy Patient Samples in Cells Generates Heterogeneous Fibrils with a Subpopulation Adopting Disease FoldsSemantic proximity Read ↗

Single mutations in tau modulate the populations of fibril conformers through seed selection.Semantic proximity Read ↗

Tau AD fragment aggregates proliferate through autocatalytic secondary nucleationSemantic proximity Read ↗

Structure-specific Mini-Prion Model for Alzheimer’s Disease Tau FibrilsSemantic proximity Read ↗

Reconstitution of the Alzheimer’s Disease Tau Core Structure from Recombinant Tau 297–391 Yields Variable Quaternary Structures as Seen by Negative Stain and Cryo-EMSemantic proximity Read ↗

Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and KineticsSemantic proximity Read ↗

Zinc Differentially Modulates Tau Aggregation, Fibril Morphology, and Prion-like Seeding in a Construct-Dependent MannerSemantic proximity Read ↗

Fibril fragmentation generates diversity in seed populationSemantic proximity Read ↗

Measurement of Tau Filament Fragmentation Provides Insights into Prion-like SpreadingSemantic proximity Read ↗

Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer’s diseaseSemantic proximity Read ↗

Direct evidence for self-propagation of different amyloid-β fibril conformations.Semantic proximity Read ↗

Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth.Semantic proximity Read ↗

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