anti-TAR DNA Binding Protein (TARDBP) 抗体产品概述

Human TAR DNA Binding Protein (TARDBP) interaction partners

1. we suggest that TDP-43 and WDR79 have separate roles in determining Cajal bodies (CBs) localization of subsets of C/D and H/ACA scaRNAs.

2. These combined results strongly suggest that liquid-liquid phase separation may play a major role in pathological TDP-43 aggregation, contributing to pathogenesis in neurodegenerative diseases.

3. we found that inhibition of transcription causes accelerated nuclear egress of TDP-43, suggesting that newly synthesized RNA retains TDP-43 in the nucleus, limiting its egress into the cytoplasm. Our findings implicate reduced nuclear retention as a possible factor contributing to mislocalization of TDP-43 in ALS/FTD.

4. TARDBP is required for maintaining the expression of ATG4B.

5. Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis

6. computational study describes the structural details to unravel the mutant effects at the atomistic resolution and has implications for understanding the TDP-43's physiological and pathological role

7. In patient specific TDP43 mutations, there was aging-related neurodegeneration in induced pluripotent stem cells from motor neurons.

8. our data reveal that TDP-43 can function as an mRNA-specific translational enhancer. Moreover, since CAMTA1 and DENND4A are linked to neurodegeneration, they suggest that this function could contribute to disease.

9. structures suggest how TDP-43 adopts both reversible and irreversible beta-sheet aggregates and the role of mutation in the possible transition of reversible to irreversible pathogenic aggregation

10. activated microglia may make unique contributions to cortical thinning and TDP-43 inclusion formation

11. TDP-43 regulates poly(A) tail length of endogenous Progranulin (GRN) mRNA.

12. Lymphoblasts from Amyotrophic lateral sclerosis patients recapitulate the hallmarks of TDP-43 processing in affected motoneurons, such as increased phosphorylation, truncation, and mislocalization of TDP-43.

13. The N-terminal region of the protein is critical for rapid TDP-43 granulo-filamentous aggregation. Progressive N-terminal truncation of TDP-43 can decelerate aggregation kinetics and promote formation of thread-like filaments.

14. Using the low-complexity disordered domain of the archetypical stress granule-protein TDP-43 as a model system, we show that TMAO enhances RNP liquid condensation yet inhibits protein fibrillation. Our results demonstrate effective decoupling of physiologic condensation from pathologic aggregation.

15. The TDP-43-regulated miRNAs may play multifaceted roles in the pathogenesis of cancer.

16. analysis of polymorphs formed by a segment of human TAR DNA-binding protein 43 (TDP-43) as a model for the polymorphic capabilities of pathological amyloid aggregation

17. In non-amnestic AD, This study find little evidence that clinical or anatomical features of the disease are related to TDP-43.

18. These results indicate that the interneuron degeneration occurs upon aging, and TDP-43 accelerates age-dependent neuronal degeneration, which may be related to the impaired memory of TDP-43 transgenic mice, expressing human TDP-43.

19. amyotrophic lateral sclerosis patients with documented TDP-43 pathology showed neuronal hnRNP A1B cytoplasmic accumulation, indicating that TDP-43 mislocalization may contribute to neuronal vulnerability and loss via altered HNRNPA1 pre-mRNA splicing and function.

20. that mutations in TARDBP in ALS patients of Iran are rare and occur at similar frequencies to European populations

Mouse (Murine) TAR DNA Binding Protein (TARDBP) interaction partners

1. ata show that TDP43A315T directly affects sensory neurons. In culture, sensory neurons expressing TDP43A315T grow and elaborate neuritic branches at a slower rate compared to control neurons. Additionally, sensory neurons expressing TDP43A315T are more sensitive to vincristine which affects the expression of two stress response genes, ATF3 and PERK.

2. We demonstrate that cross-regulation between TDP-43 and Neat1 is essential for their efficient regulation of a broad network of genes and, therefore, of pluripotency and differentiation.

3. TDP-43 induces p53-mediated cell death of cortical progenitors and immature neurons

4. Results demonstrate the importance of TDP-43 in stress granules (SG) assembly and disassembly in neurons and astrocytes. Specifcally, reducing the levels of TDP-43 resulted in an acceleration of SG disassembly in astrocytes and cortical neurons.

5. A novel long non-coding RNA Myolinc-TDP-43 interaction is essential for the binding of TDP-43 to the promoter regions of muscle marker genes.

6. Cytoplasmic mislocalization of TDP-43 is associated with enteroviral infection related Amyotrophic lateral sclerosis.

7. The effect on dendritic morphology is dependent on the RNA-binding ability of TDP-43. Thus, this model system will be useful in identifying pathways downstream of TDP-43 that mediate dendritic arborization, which may provide potential new avenues for therapeutic intervention in myotrophic Lateral Sclerosis (ALS) and Frontotemporal Dementia (FTD).

8. TDP-43 is an essential protein for normal skeletal muscle formation that unexpectedly forms cytoplasmic, amyloid-like oligomeric assemblies, which we call myo-granules, during regeneration of skeletal muscle in mice and humans; myo-granules bind to mRNAs that encode sarcomeric proteins and are cleared as myofibres mature

9. This study identifies TDP-43 misregulation as a pathogenic mechanism that may underpin ALS-FTD and exploits phenotypic heterogeneity to yield candidate suppressors of neurodegenerative disease

10. Study shows that TDP-43 interacts with mitochondrial proteins critical for mitophagy and mitochondrial dynamics. This suggest that TDP-43 processing may contribute to metabolism and mitochondrial function.

11. These results indicate that the local complement activation and increased expression of C5aR1 may contribute to motor neuron death and neuromuscular junction denervation in the TDP-43(Q331K) mouse ALS model.

12. This study demonstrated here that muscle-dominant TDP-43 transgenic mice had lower body weights and increased serum levels of myogenic enzymes

13. Our findings provide a novel pathogenic mechanism and highlight how TDP-43 gain of function and loss of function affect RNA processing differently, suggesting they may act at different disease stages.

14. Demonstrate that TDP-43 is indispensable for oligodendrocyte survival and myelination, and loss of TDP-43 in oligodendrocytes exerts no apparent toxicity on motor neurons.

15. morphologic alterations that were associated with the TDP-43(Q331K) mutation, such as aberrant innervation patterns and the distribution of synaptic vesicle-related proteins, which is indicative of a failing neuromuscular junction (NMJ) undergoing synaptic remodeling. These findings support a growing acceptance that dysregulation of the NMJ function is a key early event in the pathology of amyotrophic lateral sclerosis.

16. Findings highlight that the phosphatase regulator, GADD34, also functions as a kinase scaffold in response to chronic oxidative stress and recruits CK1 and oxidized TDP-43 to facilitate its phosphorylation, as seen in TDP-43 proteinopathies.

17. FUS and TAF15 exhibit similar global RNA interaction profiles in vivo, but affect a strikingly small subset of common genes. Unexpectedly, TAF15 influences a small fraction of amyotrophic lateral sclerosis events compared with TDP-43 and FUS in the mouse CNS.

18. Increased excitatory synaptic inputs and dendritic spine densities is associated with TDP-43(Q331K) mutation resulting in amyotrophic lateral sclerosis.

19. Given the close association of stress granules and TDP-43, we wondered whether internalisation of SOD1 aggregates stimulated TDP-43 cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 to the cytoplasm where it was still accumulated after 48 h.

20. The mutated TDP-43 has a significant pathological effect at the dendritic spine that is associated with attenuated neural transmission.

Zebrafish TAR DNA Binding Protein (TARDBP) interaction partners

1. tardbp hom/hom mutants displayed gross morphological defects, early lethality, reduced locomotor function, aberrant quantal transmission, and perturbed synapse architecture at the NMJ. tardbp(+/-); tardbpl(-/-), but not hom/hom mutants, were sensitive to chronic treatments of BAY K 8644, an L-type calcium channel agonist. This result highlights the importance of partial vs. complete loss of allelic functions of TDP-43.

2. Data indicate a method for site-directed single nucleotide editing in two disease-related genes, DNA binding protein tardbp and RNA binding protein fus.

3. Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.

4. TARDBP and FUS act in a pathogenic pathway that is independent of SOD1.