[HTML][HTML] Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis

J Root, P Merino, A Nuckols, M Johnson… - Neurobiology of disease, 2021 - Elsevier
Frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) are fatal
neurodegenerative disorders that are thought to exist on a clinical and pathological …

Ultrastructural and biochemical classification of pathogenic tau, α-synuclein and TDP-43

A Tarutani, T Adachi, H Akatsu, Y Hashizume… - Acta …, 2022 - Springer
Intracellular accumulation of abnormal proteins with conformational changes is the defining
neuropathological feature of neurodegenerative diseases. The pathogenic proteins that …

Targeting an RNA-binding protein network in acute myeloid leukemia

E Wang, SX Lu, A Pastore, X Chen, J Imig, SCW Lee… - Cancer cell, 2019 - cell.com
RNA-binding proteins (RBPs) are essential modulators of transcription and translation
frequently dysregulated in cancer. We systematically interrogated RBP dependencies in …

[HTML][HTML] RBM33 is a unique m6A RNA-binding protein that regulates ALKBH5 demethylase activity and substrate selectivity

F Yu, AC Zhu, S Liu, B Gao, Y Wang, N Khudaverdyan… - Molecular Cell, 2023 - cell.com
Regulation of RNA substrate selectivity of m 6 A demethylase ALKBH5 remains elusive.
Here, we identify RNA-binding motif protein 33 (RBM33) as a previously unrecognized m 6 …

PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis

DS Kim, S Challa, A Jones, WL Kraus - Genes & Development, 2020 - genesdev.cshlp.org
ADP-ribosylation (ADPRylation) is a posttranslational modification of proteins discovered
nearly six decades ago, but many important questions remain regarding its molecular …

Loss of dynamic RNA interaction and aberrant phase separation induced by two distinct types of ALS/FTD-linked FUS mutations

AG Niaki, J Sarkar, X Cai, K Rhine, V Vidaurre, B Guy… - Molecular cell, 2020 - cell.com
FUS is a nuclear RNA-binding protein, and its cytoplasmic aggregation is a pathogenic
signature of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). It …

[HTML][HTML] RNA-binding proteins in amyotrophic lateral sclerosis

M Zhao, JR Kim, R van Bruggen, J Park - Molecules and cells, 2018 - Elsevier
Significant research efforts are ongoing to elucidate the complex molecular mechanisms
underlying amyotrophic lateral sclerosis (ALS), which may in turn pinpoint potential …

Intron retention and nuclear loss of SFPQ are molecular hallmarks of ALS

R Luisier, GE Tyzack, CE Hall, JS Mitchell… - Nature …, 2018 - nature.com
Mutations causing amyotrophic lateral sclerosis (ALS) strongly implicate ubiquitously
expressed regulators of RNA processing. To understand the molecular impact of ALS …

Genetic convergence brings clarity to the enigmatic red line in ALS

C Cook, L Petrucelli - Neuron, 2019 - cell.com
Amyotrophic lateral sclerosis (ALS) is an aggressive neurodegenerative disorder that
orchestrates an attack on the motor nervous system that is unrelenting. Recent discoveries …

Cytoplasmic functions of TDP-43 and FUS and their role in ALS

N Birsa, MP Bentham, P Fratta - Seminars in cell & developmental biology, 2020 - Elsevier
TAR DNA-binding protein of 43 kDa (TDP-43) and fused in sarcoma (FUS) are RNA binding
proteins (RBPs) primarily located in the nucleus, and involved in numerous aspects of RNA …