Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

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Aromatic and aliphatic residues of the disordered region of TDP-43 are on a fast track for self-assembly

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Combining molecular dynamics simulations with small-angle X-ray and neutron scattering data to study multi-domain proteins in solution

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Stress Induces Dynamic, Cytotoxicity-Antagonizing TDP-43 Nuclear Bodies via Paraspeckle LncRNA NEAT1-Mediated Liquid-Liquid Phase Separation

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Simulation of FUS Protein Condensates with an Adapted Coarse-Grained Model

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Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death

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Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation

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Chronic optogenetic induction of stress granules is cytotoxic and reveals the evolution of ALS-FTD pathology

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Phase separation-deficient TDP43 remains functional in splicing

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Site-Specific Hyperphosphorylation Inhibits, Rather than Promotes, Tau Fibrillization, Seeding Capacity, and Its Microtubule Binding

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Hierarchical Ensembles of Intrinsically Disordered Proteins at Atomic Resolution in Molecular Dynamics Simulations

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In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment

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A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing

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TDP-43 post-translational modifications in health and disease

(2018) Emanuele Buratti   EXPERT OPINION ON THERAPEUTIC TARGETS

TAR DNA-binding protein 43 (TDP-43) liquid–liquid phase separation is mediated by just a few aromatic residues

(2018) Hao-Ru Li et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Pathological phosphorylation of tau and TDP-43 by TTBK1 and TTBK2 drives neurodegeneration

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Developing a molecular dynamics force field for both folded and disordered protein states

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Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1

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Sequence determinants of protein phase behavior from a coarse-grained model

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Friend or foe — post-translational modifications as regulators of phase separation and RNP granule dynamics

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Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

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Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications

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Phosphorylation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Truncated Casein Kinase 1δ Triggers Mislocalization and Accumulation of TDP-43

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ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain

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Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains

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Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

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A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

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Water Dispersion Interactions Strongly Influence Simulated Structural Properties of Disordered Protein States

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Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice

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TDP-43 is a key player in the clinical features associated with Alzheimer’s disease

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Ribosomal Protein s15 Phosphorylation Mediates LRRK2 Neurodegeneration in Parkinson’s Disease

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Protein Kinase CK-1 Inhibitors As New Potential Drugs for Amyotrophic Lateral Sclerosis

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The Tau Tubulin Kinases TTBK1/2 Promote Accumulation of Pathological TDP-43

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CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration

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TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo

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Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection

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Characterizing the RNA targets and position-dependent splicing regulation by TDP-43

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TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR

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Hyperphosphorylation as a Defense Mechanism to Reduce TDP-43 Aggregation

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TDP-43 regulates its mRNA levels through a negative feedback loop

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Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1

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Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies

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Identification of casein kinase-1 phosphorylation sites on TDP-43

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Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin

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Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS

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The MARTINI Coarse-Grained Force Field: Extension to Proteins

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