Associated Papers
TDP-43 mutants with different aggregation properties exhibit distinct toxicity, axonal transport, and secretion for disease progression in a mouse ALS/FTLD model.
Mori H et al.
Neurobiology of Disease, 2025
Downregulation of NEAT1 due to loss of TDP-43 function exacerbates motor neuron degeneration in amyotrophic lateral sclerosis.
Kawakami Y et al.
Brain Communications, 2025
Short Repeat Ribonucleic Acid Reduces Cytotoxicity by Preventing the Aggregation of TDP-43 and Its 25 KDa Carboxy-Terminal Fragment.
Fujimoto A et al.
Jacs Au, 2024
TDP-43 differentially propagates to induce antero- and retrograde degeneration in the corticospinal circuits in mouse focal ALS models.
Tsuboguchi S et al.
Acta Neuropathologica, 2023
In vivo analysis of aggregation propensity of low levels of mislocalized TDP-43 on cytopathological and behavioral phenotype of ALS/FTLD.
Wada H et al.
Neuroscience Research, 2023
Loss of TDP-43 function underlies hippocampal and cortical synaptic deficits in TDP-43 proteinopathies.
Ni J et al.
Molecular Psychiatry, 2023
Conformational change of RNA-helicase DHX30 by ALS/FTD-linked FUS induces mitochondrial dysfunction and cytosolic aggregates.
Hikiami R et al.
Scientific Reports, 2022
36163369 (PubMed )
Supplement: 41598_2022_20405_MOESM1_ESM.pdf
TAR DNA-binding protein 43 oligomers in physiology and pathology.
Lye YS et al.
Iubmb Life, 2022
TDP-43 pathology: From noxious assembly to therapeutic removal.
Keating SS et al.
Progress in Neurobiology, 2022
Direct targeting of TDP-43, from small molecules to biologics: the therapeutic landscape.
Francois-Moutal L et al.
Rsc Chemical Biology, 2021
Elimination of TDP-43 inclusions linked to amyotrophic lateral sclerosis by a misfolding-specific intrabody with dual proteolytic signals.
Tamaki Y et al.
Scientific Reports, 2018
Chronic oxidative stress promotes GADD34-mediated phosphorylation of the TAR DNA-binding protein TDP-43, a modification linked to neurodegeneration.
Goh CW et al.
The Journal of Biological Chemistry, 2018
Structural insights into the multi-determinant aggregation of TDP-43 in motor neuron-like cells.
Bozzo F et al.
Neurobiology of Disease, 2016
CUL2-mediated clearance of misfolded TDP-43 is paradoxically affected by VHL in oligodendrocytes in ALS.
Uchida T et al.
Scientific Reports, 2016
26751167 (PubMed )
Supplement: srep19118-s1.pdf
Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking.
Cohen TJ et al.
The Embo Journal, 2012
Select a paper to view details