. Distinct α-synuclein strains differentially promote tau inclusions in neurons. Cell. 2013 Jul 3;154(1):103-17. PubMed.

Recommends

Please login to recommend the paper.

Comments

Make a Comment

To make a comment you must login or register.

Comments on this content

  1. This work demonstrates the existence of assembled α-synuclein strains, based on the cross-seeding (or not) of tau aggregation. This is important for understanding some human neurodegenerative diseases, where α-synuclein inclusions are present in different cell types and different parts of the nervous system, sometimes in conjunction with tau inclusions. Aggregates of tau give rise to distinct human tauopathies and recent experiments have shown that strains of assembled four-repeat tau appear to exist (Clavaguera et al., 2013). Strains of assembled α-synuclein and tau provide a further link with prion diseases, where different aggregate conformations of the prion protein give rise to distinct disease phenotypes and neuropathologies.

    References:

    . Brain homogenates from human tauopathies induce tau inclusions in mouse brain. Proc Natl Acad Sci U S A. 2013 Jun 4;110(23):9535-40. PubMed.

This paper appears in the following:

News

  1. An Extra Strain on the Brain—α-Synuclein Seeds Tau Aggregation