| P50 | author | Witold Surewicz | Q88985521 |
| P2093 | author name string | Jin-Kyu Choi | |
| | Krystyna Surewicz | |
| | Benjamin K Dumm | |
| | Raza Haider | |
| | Prottusha Sarkar | |
| | W Michael Babinchak | |
| P2860 | cites work | Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs | Q24317451 |
| | The TDP-43 N-terminal domain structure at high resolution | Q27703592 |
| | Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis | Q28131672 |
| | Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue | Q28475724 |
| | Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization | Q28588090 |
| | TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis | Q29615597 |
| | Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin. | Q30368889 |
| | The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism | Q33786698 |
| | The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43. | Q47681989 |
| | Reversible induction of TDP-43 granules in cortical neurons after traumatic injury | Q47754563 |
| | Delineation of the core aggregation sequences of TDP-43 C-terminal fragment | Q47990018 |
| | Updated TDP-43 in Alzheimer's disease staging scheme | Q48949710 |
| | A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing | Q50037033 |
| | Traumatic injury induces Stress Granule Formation and enhances Motor Dysfunctions in ALS/FTD Models | Q50047147 |
| | Liquids, Fibers, and Gels: The Many Phases of Neurodegeneration. | Q51613027 |
| | TDP-43 NTD can be induced while CTD is significantly enhanced by ssDNA to undergo liquid-liquid phase separation. | Q52349971 |
| | TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues. | Q52365240 |
| | A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. | Q53368534 |
| | Tau protein liquid-liquid phase separation can initiate tau aggregation. | Q53395943 |
| | Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation | Q57909514 |
| | The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration | Q58779202 |
| | A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation. | Q64958474 |
| | Spreading of amyotrophic lateral sclerosis lesions--multifocal hits and local propagation? | Q85740599 |
| | The amyloidogenicity of a C-terminal region of TDP-43 implicated in Amyotrophic Lateral Sclerosis can be affected by anions, acetylation and homodimerization | Q88641884 |
| | Poly(ADP-ribose) Engages the TDP-43 Nuclear-Localization Sequence to Regulate Granulo-Filamentous Aggregation | Q90425583 |
| | Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization | Q90903690 |
| | Aggregation of the nucleic acid-binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation | Q90989134 |
| | Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation | Q33854229 |
| | TDP-43 proteinopathy and motor neuron disease in chronic traumatic encephalopathy. | Q34131994 |
| | TDP-43 is a key player in the clinical features associated with Alzheimer's disease | Q34232167 |
| | The epidemiology of ALS: a conspiracy of genes, environment and time | Q34377698 |
| | An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution. | Q34575728 |
| | ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. | Q35886826 |
| | Spread of pathology in amyotrophic lateral sclerosis: assessment of phosphorylated TDP-43 along axonal pathways | Q35896504 |
| | Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation | Q35994644 |
| | Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins | Q36172705 |
| | Mechanisms of prion protein assembly into amyloid | Q36497270 |
| | TDP-43 skeins show properties of amyloid in a subset of ALS cases | Q36508239 |
| | Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis | Q36734898 |
| | Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation | Q36748388 |
| | TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis | Q36965517 |
| | Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion | Q37000560 |
| | TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity | Q37339064 |
| | Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy | Q37349941 |
| | ALS-linked mutations enlarge TDP-43-enriched neuronal RNA granules in the dendritic arbor | Q37650180 |
| | Amyotrophic lateral sclerosis--a model of corticofugal axonal spread | Q38161789 |
| | Review: Prion-like mechanisms of transactive response DNA binding protein of 43 kDa (TDP-43) in amyotrophic lateral sclerosis (ALS). | Q38285314 |
| | "Structural characterization of the minimal segment of TDP-43 competent for aggregation". | Q38450952 |
| | The Role of TDP-43 in Alzheimer's Disease | Q38529627 |
| | Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils | Q38793335 |
| | Phase Separation: Linking Cellular Compartmentalization to Disease. | Q38799797 |
| | "New Old Pathologies": AD, PART, and Cerebral Age-Related TDP-43 With Sclerosis (CARTS). | Q38841003 |
| | The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity | Q38915658 |
| | Phase to Phase with TDP-43. | Q39098675 |
| | Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. | Q39839659 |
| | Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. | Q40075711 |
| | Soluble Prion Protein Binds Isolated Low Molecular Weight Amyloid-β Oligomers Causing Cytotoxicity Inhibition | Q40432963 |
| | Macromolecular crowding: biochemical, biophysical, and physiological consequences | Q40488946 |
| | ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain. | Q41036092 |
| | Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid. | Q41341998 |
| | Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins | Q41550219 |
| | The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation | Q41839526 |
| | Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis | Q43200632 |
| | Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism | Q43607506 |
| | Thioflavin T as a molecular rotor: fluorescent properties of thioflavin T in solvents with different viscosity | Q44679366 |
| | Delineating the membrane-disrupting and seeding properties of the TDP-43 amyloidogenic core. | Q44723108 |
| | Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides. | Q46554622 |
| P433 | issue | 16 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 6306-6317 | |
| P577 | publication date | 2019-02-27 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | The role of liquid-liquid phase separation in aggregation of the TDP-43 low-complexity domain | |
| P478 | volume | 294 | |