Associated Papers
From Evasion to Collapse: The Kinetic Cascade of TDP-43 and the Failure of Proteostasis.
Jamerlan A et al.
International Journal of Molecular Sciences, 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
A human forebrain organoid model phenocopies dysregulated RNA and protein homeostasis in ALS/FTD-associated TDP-43 proteinopathies.
Zhang Q et al.
Biorxiv : the Preprint Server for Biology, 2025
On the potential roles of TDP-43 in the formation of membraneless organelles and their transformation into toxic aggregates.
Sergeeva OS et al.
Biochemical and Biophysical Research Communications, 2025
TRAF6 regulates ubiquitination-independent TDP-43 condensation and related neurodegeneration.
Guo S et al.
Molecular Psychiatry, 2025
De novo design of protein binders to stabilize monomeric TDP-43 and inhibit its pathological aggregation.
Sun G et al.
Proceedings of the National Academy of Sciences of the United States of America, 2025
Familial ALS/FTD-associated RNA-binding deficient TDP-43 mutants cause neuronal and synaptic transcript dysregulation in vitro.
Magarotto M et al.
Human Molecular Genetics, 2025
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
Scouring the human Hsp70 network uncovers diverse chaperone safeguards buffering TDP-43 toxicity.
Barbieri EM et al.
Biorxiv : the Preprint Server for Biology, 2025
Molecular mechanisms and consequences of TDP-43 phosphorylation in neurodegeneration.
Kellett EA et al.
Molecular Neurodegeneration, 2025
Pathogenic TDP-43 in amyotrophic lateral sclerosis.
Chong ZZ et al.
Drug Discovery Today, 2025
Amyotrophic lateral sclerosis caused by TARDBP mutations: from genetics to TDP-43 proteinopathy.
Balendra R et al.
The Lancet. Neurology, 2025
The Regulation of TDP-43 Structure and Phase Transitions: A Review.
Liu Y et al.
The Protein Journal, 2025
Decoding Missense Variants by Incorporating Phase Separation via Machine Learning.
Feng M et al.
Nature Communications, 2024
Halogen doped graphene quantum dots modulate TDP-43 phase separation and aggregation in the nucleus.
Zhang H et al.
Nature Communications, 2024
Understanding age-related pathologic changes in TDP-43 functions and the consequence on RNA splicing and signalling in health and disease.
Cheng F et al.
Ageing Research Reviews, 2024
The implications of physiological biomolecular condensates in amyotrophic lateral sclerosis.
Fakim H et al.
Seminars in Cell & Developmental Biology, 2024
IκB kinase phosphorylates cytoplasmic TDP-43 and promotes its proteasome degradation.
Iguchi Y et al.
The Journal of Cell Biology, 2024
A complex network of interdomain interactions underlies the conformational ensemble of monomeric TDP-43 and modulates its phase behavior.
Mohanty P et al.
Protein Science : a Publication of the Protein Society, 2024
Slow disease progression and characteristic TDP-43 inclusions in a patient with familial amyotrophic lateral sclerosis carrying a TARDBP G357S variant.
Sainouchi M et al.
Neuropathology and Applied Neurobiology, 2024
Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.
Khalil B et al.
Molecular Neurodegeneration, 2024
Aberrant axon initial segment plasticity and intrinsic excitability of ALS hiPSC motor neurons.
Harley P et al.
Cell Reports, 2023
RNA-binding deficient TDP-43 drives cognitive decline in a mouse model of TDP-43 proteinopathy.
Necarsulmer JC et al.
Elife, 2023
Genetic variability in sporadic amyotrophic lateral sclerosis.
Van Daele SH et al.
Brain : a Journal of Neurology, 2023
Shapeshifter TDP-43: Molecular mechanism of structural polymorphism, aggregation, phase separation and their modulators.
Doke AA et al.
Biophysical Chemistry, 2023
TAR DNA-binding protein 43 oligomers in physiology and pathology.
Lye YS et al.
Iubmb Life, 2022
Genotype-phenotype association of TARDBP mutations in Chinese patients with amyotrophic lateral sclerosis: a single-center study and systematic review of published literature.
Li J et al.
Journal of Neurology, 2022
Altered TDP-43 Structure and Function: Key Insights into Aberrant RNA, Mitochondrial, and Cellular and Systemic Metabolism in Amyotrophic Lateral Sclerosis.
Jiang L et al.
Metabolites, 2022
Dynamics of binding interactions of TDP-43 and RNA: An equally weighted multiscale elastic network model study.
Deng X et al.
Proteins, 2022
Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions.
Versluys L et al.
Frontiers in Neuroscience, 2022
Specific RNA interactions promote TDP-43 multivalent phase separation and maintain liquid properties.
Grese ZR et al.
Embo Reports, 2021
The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation.
Rengifo-Gonzalez JC et al.
Elife, 2021
RNA modulates physiological and neuropathological protein phase transitions.
Mann JR et al.
Neuron, 2021
Insights into the aggregation mechanism of RNA recognition motif domains in TDP-43: a theoretical exploration.
Liu W et al.
Royal Society Open Science, 2021
Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD.
Wood A et al.
International Journal of Molecular Sciences, 2021
HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells.
Yu H et al.
Science (new York, N.y.), 2021
Frontotemporal dementia-linked P112H mutation of TDP-43 induces protein structural change and impairs its RNA binding function.
Agrawal S et al.
Protein Science : a Publication of the Protein Society, 2021
RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy.
Chen HJ et al.
Brain : a Journal of Neurology, 2019