Associated Papers
Defining RNA oligonucleotides that reverse deleterious phase transitions of RNA-binding proteins with prion-like domains.
Guo L et al.
Molecular Cell, 2026
J-domain proteins cooperate with Hsp70 to drive multiphase separation of RNA-binding-deficient TDP-43.
Yeo KH et al.
The Journal of Biological Chemistry, 2025
RNA helicase maheshvara interacts with TDP-43 and exacerbates neurodegeneration in Drosophila model of amyotrophic lateral sclerosis.
Pandey P et al.
Neurobiology of Disease, 2025
Critical impact of lysine 136 in TDP-43 phase separation, compartmentalization, and aggregation in living vertebrates.
Maurel C et al.
Iscience, 2025
SUMO2/3 conjugation of TDP-43 protects against aggregation.
Verde EM et al.
Science Advances, 2025
Decoding Missense Variants by Incorporating Phase Separation via Machine Learning.
Feng M et al.
Nature Communications, 2024
RNA-binding properties orchestrate TDP-43 homeostasis through condensate formation in vivo.
Scherer NM et al.
Nucleic Acids Research, 2024
Establishing mRNA and microRNA interactions driving disease heterogeneity in amyotrophic lateral sclerosis patient survival.
Waller R et al.
Brain Communications, 2024
TDP-43 Epigenetic Facets and Their Neurodegenerative Implications.
Gimenez J et al.
International Journal of Molecular Sciences, 2023
Defining RNA oligonucleotides that reverse deleterious phase transitions of RNA-binding proteins with prion-like domains.
Guo L et al.
Biorxiv : the Preprint Server for Biology, 2023
Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43.
Keating SS et al.
Cellular and Molecular Life Sciences : Cmls, 2023
Nuclear RNA binding regulates TDP-43 nuclear localization and passive nuclear export.
Duan L et al.
Cell Reports, 2022
TDP-43 pathology: From noxious assembly to therapeutic removal.
Keating SS et al.
Progress in Neurobiology, 2022
RNA-assisted sequestration of RNA-binding proteins by cytoplasmic inclusions of the C-terminal 35-kDa fragment of TDP-43.
Jiang LL et al.
Journal of Cell Science, 2022
Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43.
Garcia Morato J et al.
Nature Communications, 2022
Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons.
Vishal SS et al.
Frontiers in Cell and Developmental Biology, 2022
TDP-43 stabilizes G3BP1 mRNA: relevance to amyotrophic lateral sclerosis/frontotemporal dementia.
Sidibé H et al.
Brain : a Journal of Neurology, 2021
Exploring the molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43 using molecular dynamics simulation and free energy calculation.
Sun H et al.
Journal of Computational Chemistry, 2021
TDP-43 aggregation induced by oxidative stress causes global mitochondrial imbalance in ALS.
Zuo X et al.
Nature Structural & Molecular Biology, 2021
TDP-43 α-helical structure tunes liquid-liquid phase separation and function.
Conicella AE et al.
Proceedings of the National Academy of Sciences of the United States of America, 2020
Splicing repression is a major function of TDP-43 in motor neurons.
Donde A et al.
Acta Neuropathologica, 2019
C9-ALS/FTD-linked proline-arginine dipeptide repeat protein associates with paraspeckle components and increases paraspeckle formation.
Suzuki H et al.
Cell Death & Disease, 2019
Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation.
French RL et al.
The Journal of Biological Chemistry, 2019
An Intramolecular Salt Bridge Linking TDP43 RNA Binding, Protein Stability, and TDP43-Dependent Neurodegeneration.
Flores BN et al.
Cell Reports, 2019
TDP-43 misexpression causes defects in dendritic growth.
Herzog JJ et al.
Scientific Reports, 2017
Genetic mutations in RNA-binding proteins and their roles in ALS.
Kapeli K et al.
Human Genetics, 2017
Regulatory Role of RNA Chaperone TDP-43 for RNA Misfolding and Repeat-Associated Translation in SCA31.
Ishiguro T et al.
Neuron, 2017
Heat Shock-induced Phosphorylation of TAR DNA-binding Protein 43 (TDP-43) by MAPK/ERK Kinase Regulates TDP-43 Function.
Li W et al.
The Journal of Biological Chemistry, 2017
TBPH/TDP-43 modulates translation of Drosophila futsch mRNA through an UG-rich sequence within its 5'UTR.
Romano M et al.
Brain Research, 2016
From animal models to human disease: a genetic approach for personalized medicine in ALS.
Picher-Martel V et al.
Acta Neuropathologica Communications, 2016
Nuclear TDP-43 causes neuronal toxicity by escaping from the inhibitory regulation by hnRNPs.
Suzuki H et al.
Human Molecular Genetics, 2015
TDP-43 suppresses CGG repeat-induced neurotoxicity through interactions with HnRNP A2/B1.
He F et al.
Human Molecular Genetics, 2014
Binding of TDP-43 to the 3'UTR of its cognate mRNA enhances its solubility.
Sun Y et al.
Biochemistry, 2014
The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids.
Kuo PH et al.
Nucleic Acids Research, 2014
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43.
Lukavsky PJ et al.
Nature Structural & Molecular Biology, 2013
Spliceosome integrity is defective in the motor neuron diseases ALS and SMA.
Tsuiji H et al.
Embo Molecular Medicine, 2013
Inhibition of TDP-43 aggregation by nucleic acid binding.
Huang YC et al.
Plos One, 2013
Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region.
Budini M et al.
The Journal of Biological Chemistry, 2012
TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR.
Fiesel FC et al.
Nucleic Acids Research, 2012
Alteration of POLDIP3 splicing associated with loss of function of TDP-43 in tissues affected with ALS.
Shiga A et al.
Plos One, 2012
TDP-43 is a transcriptional repressor: the testis-specific mouse acrv1 gene is a TDP-43 target in vivo.
Lalmansingh AS et al.
The Journal of Biological Chemistry, 2011
TDP-43 regulates Drosophila neuromuscular junctions growth by modulating Futsch/MAP1B levels and synaptic microtubules organization.
Godena VK et al.
Plos One, 2011
TDP-43-mediated neuron loss in vivo requires RNA-binding activity.
Voigt A et al.
Plos One, 2010
Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo.
D'Ambrogio A et al.
Nucleic Acids Research, 2009
Structural determinants of the cellular localization and shuttling of TDP-43.
Ayala YM et al.
Journal of Cell Science, 2008