The pathobiology of TDP-43 C-terminal fragments in ALS and FTLD

BA Berning, AK Walker - Frontiers in neuroscience, 2019 - frontiersin.org
During neurodegenerative disease, the multifunctional RNA-binding protein TDP-43
undergoes a vast array of post-translational modifications, including phosphorylation …

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 …

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 …

Stress induces dynamic, cytotoxicity-antagonizing TDP-43 nuclear bodies via paraspeckle LncRNA NEAT1-mediated liquid-liquid phase separation

C Wang, Y Duan, G Duan, Q Wang, K Zhang, X Deng… - Molecular cell, 2020 - cell.com
Despite the prominent role of TDP-43 in neurodegeneration, its physiological and
pathological functions are not fully understood. Here, we report an unexpected role of TDP …

A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids

J Kang, L Lim, Y Lu, J Song - PLoS biology, 2019 - journals.plos.org
526-residue Fused in sarcoma (FUS) undergoes liquid–liquid phase separation (LLPS) for
its functions, which can further transit into pathological aggregation. ATP and nucleic acids …

[HTML][HTML] Molecular mechanisms of phase separation and amyloidosis of ALS/FTD-linked FUS and TDP-43

J Song - Aging and Disease, 2024 - pmc.ncbi.nlm.nih.gov
FUS and TDP-43, two RNA-binding proteins from the heterogeneous nuclear
ribonucleoprotein family, have gained significant attention in the field of neurodegenerative …

Adenosine triphosphate energy‐independently controls protein homeostasis with unique structure and diverse mechanisms

J Song - Protein Science, 2021 - Wiley Online Library
Proteins function in the crowded cellular environments with high salt concentrations, thus
facing tremendous challenges of misfolding/aggregation which represents a pathological …

ATP enhances at low concentrations but dissolves at high concentrations liquid-liquid phase separation (LLPS) of ALS/FTD-causing FUS

J Kang, L Lim, J Song - Biochemical and biophysical research …, 2018 - Elsevier
ATP is the universal energy currency but mysteriously its cellular concentration is much
higher than that needed for providing energy. Recently ATP was decoded to act as a …

ATP binds and inhibits the neurodegeneration-associated fibrillization of the FUS RRM domain

J Kang, L Lim, J Song - Communications biology, 2019 - nature.com
Adenosine triphosphate (ATP) provides energy for cellular processes but has recently been
found to act also as a hydrotrope to maintain protein homeostasis. ATP bivalently binds the …

Small Molecule Targeting TDP-43's RNA Recognition Motifs Reduces Locomotor Defects in a Drosophila Model of Amyotrophic Lateral Sclerosis (ALS)

L François-Moutal, R Felemban, DD Scott… - ACS chemical …, 2019 - ACS Publications
RNA dysregulation likely contributes to disease pathogenesis of amyotrophic lateral
sclerosis (ALS) and other neurodegenerative diseases. A pathological form of the …