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References from Persistent export bias of TDP-43 under native autoregulation links insoluble accumulation to nuclear dysfunction. Local targets link to admitted publications; unresolved targets remain external evidence.
Accurate structure prediction of biomolecular interactions with AlphaFold 3
10.1038/s41586-024-07487-w · 2024 · External reference
Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
10.1038/s41467-017-00062-0 · 2017 · External reference
TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
10.1016/j.bbrc.2006.10.093 · 2006 · External reference
Structure of pathological TDP-43 filaments from ALS with FTLD
10.1038/s41586-021-04199-3 · 2022 · External reference
Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection
10.1101/gad.194829.112 · 2012 · External reference
TDP-43 regulates its mRNA levels through a negative feedback loop
10.1038/emboj.2010.310 · 2011 · External reference
Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
10.1523/jneurosci.4988-09.2010 · 2010 · External reference
TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
10.1038/s41593-017-0047-3 · 2018 · External reference
Concentration-dependent cytoplasmic phase separation of TDP-43 drives aggregation and proteinopathy
10.1111/febs.70429 · 2026 · External reference
Cytoplasmic TDP-43 de-mixing independent of stress granules drives inhibition of nuclear import, loss of nuclear TDP-43, and cell death
10.1016/j.neuron.2019.02.038 · 2019 · External reference
Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
10.1002/ana.21425 · 2008 · External reference
TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
10.1074/jbc.m109.010264 · 2009 · External reference
Quantifying subpercent nuclear TDP-43 loss in cells and ALS cortex using junction-specific cryptic exon RT-qPCR
10.1002/1873-3468.70198 · 2026 · External reference
Increased cytoplasmic TARDBP mRNA in affected spinal motor neurons in ALS caused by abnormal autoregulation of TDP-43
10.1093/nar/gkw499 · 2016 · External reference
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
10.1038/nrn3121 · 2012 · External reference
Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis
10.1016/j.neuron.2013.07.033 · 2013 · External reference
A quantitative cell-based reporter links TDP-43 aggregation and dysfunction to define pathogenic mechanisms
10.1371/journal.pbio.3003662 · 2026 · External reference
Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration
10.1038/s41593-018-0293-z · 2019 · External reference
Maturation process of TDP-43-positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis with and without dementia
10.1007/s00401-008-0396-9 · 2008 · External reference
Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
10.1126/science.1134108 · 2006 · External reference
UCSF ChimeraX: structure visualization for researchers, educators, and developers
10.1002/pro.3943 · 2021 · External reference
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
10.1038/nn.2779 · 2011 · External reference
Nuclear trafficking in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
10.1093/brain/aww197 · 2017 · External reference
Alteration of POLDIP3 splicing associated with loss of function of TDP-43 in tissues affected with ALS
10.1371/journal.pone.0043120 · 2012 · External reference
TDP-43 dimerizes in human cells in culture
10.1007/s10571-009-9489-9 · 2010 · External reference
Robustness and vulnerability of the autoregulatory system that maintains nuclear TDP-43 levels: a trade-off hypothesis for ALS pathology based on in silico data
10.3389/fnins.2018.00028 · 2018 · External reference
Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
10.1038/nn.2778 · 2011 · External reference
Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
10.1038/s41583-021-00431-1 · 2021 · External reference
Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43
10.1007/s00401-015-1460-x · 2015 · External reference
Identification of a signal for rapid export of proteins from the nucleus
10.1016/0092-8674(95)90435-2 · 1995 · External reference
Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
10.1074/jbc.m800342200 · 2008 · External reference
Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA
10.1126/science.aad2033 · 2016 · External reference
Stress granule assembly disrupts nucleocytoplasmic transport
10.1016/j.cell.2018.03.025 · 2018 · External reference
The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation
10.1093/hmg/ddt166 · 2013 · External reference
