Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The ethics case for longevity science.

Ageing research reviews·2026

Same author

Expression of progerin enhances disease-related endpoints in a tau seeding reporter cell system.

GeroScience·2025

Same author

Microbial Composition, Disease Trajectory and Genetic Background in a Slow Onset Model of Frontotemporal Lobar Degeneration.

Biomolecules·2025

Same author

The non-cytotoxic small molecule NPB does not inhibit BAD phosphorylation and forms colloidal aggregates.

Communications medicine·2025

Same author

Prion Protein Endoproteolysis: Cleavage Sites, Mechanisms and Connections to Prion Disease.

Journal of neurochemistry·2025

Same author

In Vitro and In Vivo Evidence towards Fibronectin's Protective Effects against Prion Infection.

International journal of molecular sciences·2023

Search research articles

Related Experiment Video

Updated: Sep 26, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Prion-like strain effects in tauopathies.

Zhuang Zhuang Han^1,2,3, Sang-Gyun Kang^1,2, Luis Arce^1,2,3

¹Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, AB, T6G 2M8, Canada.

Cell and Tissue Research

|April 23, 2022

Summary

Different tau protein conformers, or "strains," may explain the diverse forms of tauopathies, a group of neurodegenerative diseases. Understanding these tau strains is crucial for developing effective dementia treatments.

Keywords:

Conformer Prion Strain Tau Tauopathy

More Related Videos

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

Related Experiment Videos

Last Updated: Sep 26, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry

Published on: December 8, 2015

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster

Published on: March 12, 2018

Area of Science:

Neuroscience
Biochemistry
Pathology

Background:

Tau protein is vital for normal physiology but its misfolding causes neurodegenerative tauopathies.
Tauopathies exhibit diverse clinical and pathological features, suggesting underlying heterogeneity.
The tau strain hypothesis proposes distinct tau conformers explain this diversity.

Purpose of the Study:

To summarize recent advancements in understanding tau conformers.
To explore the implications of pathological tau heterogeneity for drug development.

Main Methods:

In vivo experimental paradigms.
In vitro experimental paradigms.

Main Results:

Tau strains exhibit distinct clinical features, neuropathological profiles, and biochemical signatures.
Prior research on prion protein strains offers insights into protein-only pathogen diversity.

Conclusions:

Distinct tau conformers (strains) are likely responsible for the heterogeneity observed in tauopathies.
Understanding tau heterogeneity is critical for advancing therapeutic strategies for dementia and related disorders.