The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.
Several neurodegenerative diseases are triggered by proteins containing a polyglutamine (polyQ) stretch expanded beyond a critical threshold. Among these, ataxin-3 (AT3) is the causative agent of spinocerebellar ataxia type-3. We expressed three authentic AT3 variants in Escherichia coli: one normal...
Saved in:
Main Authors: | Gaetano Invernizzi, Francesco A Aprile, Antonino Natalello, Andrea Ghisleni, Amanda Penco, Annalisa Relini, Silvia M Doglia, Paolo Tortora, Maria E Regonesi |
---|---|
Format: | article |
Language: | EN |
Published: |
Public Library of Science (PLoS)
2012
|
Subjects: | |
Online Access: | https://doaj.org/article/51f96e25ab6c46fa83b96860acab1cb9 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Polyglutamine expansion accelerates the dynamics of ataxin-1 and does not result in aggregate formation.
by: Hilde A Krol, et al.
Published: (2008) -
A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.
by: Alessandra Apicella, et al.
Published: (2013) -
Na+/H+ exchangers induce autophagy in neurons and inhibit polyglutamine-induced aggregate formation.
by: Kazuya Togashi, et al.
Published: (2013) -
CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins
by: Ashley A. Zurawel, et al.
Published: (2016) -
Curcumin prevents formation of polyglutamine aggregates by inhibiting Vps36, a component of the ESCRT-II complex.
by: Meenakshi Verma, et al.
Published: (2012)