Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43

M Polymenidou, C Lagier-Tourenne, KR Hutt… - Nature …, 2011 - nature.com
We used cross-linking and immunoprecipitation coupled with high-throughput sequencing to
identify binding sites in 6,304 genes as the brain RNA targets for TDP-43, an RNA binding …

Characterizing the RNA targets and position-dependent splicing regulation by TDP-43

JR Tollervey, T Curk, B Rogelj, M Briese… - Nature …, 2011 - nature.com
TDP-43 is a predominantly nuclear RNA-binding protein that forms inclusion bodies in
frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). The …

TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD

JP Ling, O Pletnikova, JC Troncoso, PC Wong - Science, 2015 - science.org
Cytoplasmic aggregation of TDP-43, accompanied by its nuclear clearance, is a key
common pathological hallmark of amyotrophic lateral sclerosis and frontotemporal dementia …

Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection

SE Avendaño-Vázquez, A Dhir, S Bembich… - Genes & …, 2012 - genesdev.cshlp.org
TDP-43 is a critical RNA-binding factor associated with pre-mRNA splicing in mammals. Its
expression is tightly autoregulated, with loss of this regulation implicated in human …

Rapamycin rescues TDP-43 mislocalization and the associated low molecular mass neurofilament instability

A Caccamo, S Majumder, JJ Deng, Y Bai… - Journal of Biological …, 2009 - ASBMB
TDP-43 is a nuclear protein involved in exon skipping and alternative splicing. Recently,
TDP-43 has been identified as the pathological signature protein in frontotemporal lobar …

[HTML][HTML] RNA binding antagonizes neurotoxic phase transitions of TDP-43

JR Mann, AM Gleixner, JC Mauna, E Gomes… - Neuron, 2019 - cell.com
TDP-43 proteinopathy is a pathological hallmark of amyotrophic lateral sclerosis and
frontotemporal dementia where cytoplasmic TDP-43 inclusions are observed within …

[HTML][HTML] High-resolution RNA maps suggest common principles of splicing and polyadenylation regulation by TDP-43

G Rot, Z Wang, I Huppertz, M Modic, T Lenče… - Cell reports, 2017 - cell.com
Many RNA-binding proteins (RBPs) regulate both alternative exons and poly (A) site
selection. To understand their regulatory principles, we developed expressRNA, a web …

TDP-43 represses cryptic exon inclusion in the FTD–ALS gene UNC13A

XR Ma, M Prudencio, Y Koike, SC Vatsavayai, G Kim… - Nature, 2022 - nature.com
A hallmark pathological feature of the neurodegenerative diseases amyotrophic lateral
sclerosis (ALS) and frontotemporal dementia (FTD) is the depletion of RNA-binding protein …

RNA binding mediates neurotoxicity in the transgenic Drosophila model of TDP-43 proteinopathy

R Ihara, K Matsukawa, Y Nagata… - Human molecular …, 2013 - academic.oup.com
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder characterized by
progressive and selective loss of motor neurons. The discovery of mutations in the gene …

TDP-43-Mediated Neuron Loss In Vivo Requires RNA-Binding Activity

A Voigt, D Herholz, FC Fiesel, K Kaur, D Müller… - PloS one, 2010 - journals.plos.org
Alteration and/or mutations of the ribonucleoprotein TDP-43 have been firmly linked to
human neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and …