Development of multifunctional molecules as potential therapeutic candidates for Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis in the …

MG Savelieff, G Nam, J Kang, HJ Lee, M Lee… - Chemical …, 2018 - ACS Publications
Neurodegenerative diseases pose a substantial socioeconomic burden on society.
Unfortunately, the aging world population and lack of effective cures foreshadow a negative …

Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation

P Tziortzouda, L Van Den Bosch, F Hirth - Nature Reviews …, 2021 - nature.com
Cytoplasmic aggregation of TAR DNA-binding protein 43 (TDP43; also known as TARDBP
or TDP-43) is a key pathological feature of several neurodegenerative diseases, including …

[HTML][HTML] ALS mutations disrupt phase separation mediated by α-helical structure in the TDP-43 low-complexity C-terminal domain

AE Conicella, GH Zerze, J Mittal, NL Fawzi - Structure, 2016 - cell.com
RNA-binding protein TDP-43 mediates essential RNA processing but forms cytoplasmic
neuronal inclusions via its C-terminal domain (CTD) in amyotrophic lateral sclerosis (ALS). It …

[HTML][HTML] The role of liquid–liquid phase separation in aggregation of the TDP-43 low-complexity domain

WM Babinchak, R Haider, BK Dumm, P Sarkar… - Journal of Biological …, 2019 - ASBMB
Pathological aggregation of the transactive response DNA-binding protein of 43 kDa (TDP-
43) is associated with several neurodegenerative disorders, including ALS, frontotemporal …

Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins

A Ratti, E Buratti - Journal of neurochemistry, 2016 - Wiley Online Library
The multiple roles played by RNA binding proteins in neurodegeneration have become
apparent following the discovery of TAR DNA binding protein 43 kDa (TDP‐43) and fused in …

[HTML][HTML] TAR DNA-binding protein 43 (TDP-43) liquid–liquid phase separation is mediated by just a few aromatic residues

HR Li, WC Chiang, PC Chou, WJ Wang… - Journal of Biological …, 2018 - ASBMB
Eukaryotic cells contain distinct organelles, but not all of these compartments are enclosed
by membranes. Some intrinsically disordered proteins mediate membraneless organelle …

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation

EL Guenther, Q Cao, H Trinh, J Lu… - Nature structural & …, 2018 - nature.com
The normally soluble TAR DNA-binding protein 43 (TDP-43) is found aggregated both in
reversible stress granules and in irreversible pathogenic amyloid. In TDP-43, the low …

[HTML][HTML] Prion-like propagation of protein misfolding and aggregation in amyotrophic lateral sclerosis

L McAlary, SS Plotkin, JJ Yerbury… - Frontiers in molecular …, 2019 - frontiersin.org
The discovery that prion protein can misfold into a pathological conformation that encodes
structural information capable of both propagation and inducing severe neuropathology has …

[HTML][HTML] Structural insights into TDP-43 and effects of post-translational modifications

L François-Moutal, S Perez-Miller, DD Scott… - Frontiers in molecular …, 2019 - frontiersin.org
Transactive response DNA binding protein (TDP-43) is a key player in neurodegenerative
diseases. In this review, we have gathered and presented structural information on the …

[HTML][HTML] ALS-causing mutations significantly perturb the self-assembly and interaction with nucleic acid of the intrinsically disordered prion-like domain of TDP-43

L Lim, Y Wei, Y Lu, J Song - PLoS biology, 2016 - journals.plos.org
TAR-DNA-binding protein-43 (TDP-43) C-terminus encodes a prion-like domain widely
presented in RNA-binding proteins, which functions to form dynamic oligomers and also …