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
From TDP-43/RNA complex formation to disease-linked TDP-43 aggregation through a structural and cellular approach.
Feng Y et al.
Nature Communications, 2026
TDP-43 skein-like inclusions are formed by BAG3- and HSP70-guided co-aggregation with actin-binding proteins.
Lu S et al.
Nature Cell Biology, 2025
Critical impact of lysine 136 in TDP-43 phase separation, compartmentalization, and aggregation in living vertebrates.
Maurel C et al.
Iscience, 2025
ALS-associated TDP-43 aggregates drive innate and adaptive immune cell activation.
Evangelista BA et al.
Iscience, 2025
Challenges of modelling TDP-43 pathology in mice.
Armas JMB et al.
Mammalian Genome : Official Journal of the International Mammalian Genome Society, 2025
C9orf72 poly-PR forms anisotropic condensates causative of nuclear TDP-43 pathology.
Hodgson RE et al.
Iscience, 2024
Single Acetylation-mimetic Mutation in TDP-43 Nuclear Localization Signal Disrupts Importin α1/β Signaling.
Ko YH et al.
Journal of Molecular Biology, 2024
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
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
TDP-43 pathology links innate and adaptive immunity in amyotrophic lateral sclerosis.
Evangelista BA et al.
Biorxiv : the Preprint Server for Biology, 2024
RNA-binding deficient TDP-43 drives cognitive decline in a mouse model of TDP-43 proteinopathy.
Necarsulmer JC et al.
Elife, 2023
Tandem detergent-extraction and immunoprecipitation of proteinopathy: Scalable enrichment of ALS-associated TDP-43 aggregates.
Evangelista BA et al.
Iscience, 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
Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43.
Garcia Morato J et al.
Nature Communications, 2022
HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells.
Yu H et al.
Science (new York, N.y.), 2021
HDAC1 inhibition ameliorates TDP-43-induced cell death in vitro and in vivo.
Sanna S et al.
Cell Death & Disease, 2020
Aggregation of the nucleic acid-binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation.
Chen Y et al.
The Journal of Biological Chemistry, 2019
Structural Insights Into TDP-43 and Effects of Post-translational Modifications.
François-Moutal L et al.
Frontiers in Molecular Neuroscience, 2019
Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program.
Wang P et al.
Nature Communications, 2017
An acetylation switch controls TDP-43 function and aggregation propensity.
Cohen TJ et al.
Nature Communications, 2015