Two neuronal models of TDP-43 proteinopathy display reduced axonal translation, increased oxidative stress, and defective exocytosis (original) (raw)

Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations

Edward Chaum, Nael H Alami

Neuron, 2014

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ALS-Linked Mutations Enlarge TDP-43-Enriched Neuronal RNA Granules in the Dendritic Arbor

A. Ebata

Journal of Neuroscience, 2014

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Cytoplasmic Expression of the ALS/FTD-Related Protein TDP-43 Decreases Global Translation Both in vitro and in vivo

Matias Blaustein

Frontiers in Cellular Neuroscience, 2020

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Altered TDP-43 Structure and Function: Key Insights into Aberrant RNA, Mitochondrial, and Cellular and Systemic Metabolism in Amyotrophic Lateral Sclerosis

Leanne Jiang

Metabolites

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Loss of Tdp-43 disrupts the axonal transcriptome of motoneurons accompanied by impaired axonal translation and mitochondria function

michael sendtner

Acta Neuropathologica Communications, 2020

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Antisense RNA foci in the motor neurons of C9ORF72-ALS patients are associated with TDP-43 proteinopathy

Matthew Stopford, Robin Highley, Johnathan Cooper-Knock, Janine Kirby

Acta Neuropathologica, 2015

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Increased cytoplasmicTARDBPmRNA in affected spinal motor neurons in ALS caused by abnormal autoregulation of TDP-43

Osamu Onodera

Nucleic Acids Research, 2016

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Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs

Magdalini Polymenidou

Nature Neuroscience, 2012

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Loss of nuclear TDP‐43 in amyotrophic lateral sclerosis (ALS) causes altered expression of splicing machinery and widespread dysregulation of RNA splicing in motor neurones

Pamela Shaw

Neuropathology and Applied Neurobiology, 2014

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TDP-43 enhances translation of specific mRNAs linked to neurodegenerative disease

Giorgio Gonnella

Nucleic Acids Research, 2018

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Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses

jiayu zhang

Nature communications, 2016

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RNA targets of TDP-43 identified by UV-CLIP are deregulated in ALS

Lorne Zinman, David Sheps

Molecular and cellular neurosciences, 2011

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Low molecular weight species of TDP-43 generated by abnormal splicing form inclusions in amyotrophic lateral sclerosis and result in motor neuron death

Lorne Zinman

Acta neuropathologica, 2015

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Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis

Leonardo Aliaga

Proceedings of the National Academy of Sciences, 2014

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Alteration of POLDIP3 splicing associated with loss of function of TDP-43 in tissues affected with ALS

Osamu Onodera

PloS one, 2012

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{"__content__"=>"Robustness and Vulnerability of the Autoregulatory System That Maintains Nuclear TDP-43 Levels: A Trade-off Hypothesis for ALS Pathology Based on Data.", "i"=>{"__content__"=>"in Silico"}}

Osamu Onodera

Frontiers in neuroscience, 2018

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A Computational Approach to Investigate TDP-43 RNA-Recognition Motif 2 C-Terminal Fragments Aggregation in Amyotrophic Lateral Sclerosis

Elsa Zacco

Biomolecules, 2021

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TDP-43: gumming up neurons through protein-protein and protein-RNA interactions

Emanuele Buratti

2012

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Identification of RNA bound to the TDP-43 ribonucleoprotein complex in the adult mouse brain

Ajay Panwar

Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, 2012

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Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders

Christine Van Broeckhoven

Human Molecular Genetics, 2013

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Multi-phaseted problems of TDP-43 in selective neuronal vulnerability in ALS

Kazuhide Asakawa

Cellular and Molecular Life Sciences

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Global Analysis of TDP-43 Interacting Proteins Reveals Strong Association with RNA Splicing and Translation Machinery

Raghu Chitta

Journal of Proteome Research, 2010

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TDP-43 and FUS RNA-binding Proteins Bind Distinct Sets of Cytoplasmic Messenger RNAs and Differently Regulate Their Post-transcriptional Fate in Motoneuron-like Cells

Emanuele Buratti

Journal of Biological Chemistry, 2012

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RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43

Bryan Hurtle

Neuron, 2019

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MTHFSD and DDX58 are novel RNA-binding proteins abnormally regulated in amyotrophic lateral sclerosis

Lorne Zinman, Jean-Pierre Julien

Brain : a journal of neurology, 2015

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Cell environment shapes TDP-43 function with implications in neuronal and muscle disease

Emanuele Buratti

Communications Biology

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TDP-43 proteinopathies: a new wave of neurodegenerative diseases

Parvathi Menon

Journal of Neurology, Neurosurgery & Psychiatry

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The role of TDP-43 in the pathogenesis of ALS and FTLD

Emanuele Buratti

2013

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Advances in Neurobiology 20 RNA Metabolism in Neurodegenerative Diseases

Antia Alvarez Pazo

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TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

Magdalini Polymenidou

Human Molecular Genetics, 2010

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Cell environment shapes TDP-43 function: implications in neuronal and muscle disease

Emanuele Buratti

2021

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