An Amyloid-like Pathological Conformation of TDP-43 is Stabilized by Hypercooperative Hydrogen Bonds

An Amyloid-like Pathological Conformation of TDP-43 is Stabilized by Hypercooperative Hydrogen Bonds

TDP-43 is an essential RNA-binding protein forming aggregates in almost all cases of sporadic ALS and many cases of FTLD and other neurodegenerative diseases. TDP-43 consists of a folded N-terminal domain with a singular structure, two RRM RNA-binding domains, and a long disordered C-terminal regio...

Full description

Bibliographic Details
Main Authors: Miguel Mompeán, Marco Baralle, Emanuele Buratti, Douglas Vinson Laurents
Format: Article
Language:English
Published: Frontiers Media S.A. 2016-11-01
Series:Frontiers in Molecular Neuroscience
Subjects:
Frontotemporal Lobar Degeneration
Protein misfolding and Disease
Amyotrophic lateral sclerosis (ALS)
hnRNPs
Pathological Amyloids
transitive response DNA-bonding Protein 43kDa (TDP-43)
Online Access:http://journal.frontiersin.org/Journal/10.3389/fnmol.2016.00125/full

Internet

http://journal.frontiersin.org/Journal/10.3389/fnmol.2016.00125/full

Similar Items