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

Human TAR DNA Binding Protein (TARDBP) interaction partners

1. SGs form distinct cytoplasmic structures that can indirectly enhance TDP-43 aggregation

2. 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

3. Ubiquitinylation at Lys-84 promotes nuclear import, while ubiquitinylation at Lys-95 or Lys-408 impairs phosphorylation of TDP-43 at Ser(409,410).

4. Using single-molecule fluorescence and ensemble biophysical techniques, and a wide range of pH and temperature conditions, this study shows that TDP-43(N-Terminal Domain ) is thermodynamically stable, well-folded and undergoes reversible oligomerization.

5. We propose that TDP-43 has a novel role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts.

6. Study found that TDP-43 N-terminal domain forms a dimer or tetramer under normal conditions and inhibits TDP-43 aggregation. Disruption of dimerization can result in loss of TDP-43 splicing activity. These data provide insights into the physiological function of TDP-43 and its related proteinopathies.

7. The results imply that ERp57 has a protective role against pathological events induced by mutant SOD1 and they link ERp57 to the misfolding of TDP-43 in amyotrophic lateral sclerosis.

8. This report here an age-related increase and formation of ubiquitinated TDP-43 cytoplasmic inclusions after stroke.

9. Study reports end-stage hippocampal sclerosis-aging to be characterized by quantifiable measures of neuron loss location, extent and severity in association with presence of dentate TDP-43 inclusions.

10. Overexpression of FUS or TDP-43 causes inhibition of the ubiquitin proteasome system (UPS) and toxicity, both of which are mitigated by overexpression of the Hsp40 chaperone.

11. the present analysis highlighting the structural and functional aspects of wild and mutant tdp43 will form the basis to gain insight into the proteinopathy of tdp43 and the related structure-based drug discovery. Thus, tdp43 can be used as target to develop novel therapeutic approaches or drug designing.

12. The C-terminal domain of TDP-43 contains approximately 50 disease-related mutations, with no clear physicochemical link between them. This study proposes that they may disrupt liquid-liquid phase separation indirectly by interfering with the key aromatic residues identified here.

13. the progression of frontotemporal lobar degeneration-TAR DNA-binding 43 protein reflects the templated cell-to-cell transneuronal spread of pathological TDP-43.

14. TDP-43 deposition leads to targeted RNA instability in amyotrophic lateral sclerosis and frontotemporal dementia

15. CHCHD10 mutations have a role in cytoplasmic TDP-43 accumulation and synaptic integrity

16. Study confirms the high expression of hTDP-43 in the CNS, increased microgliosis and motor deficits, exhibiting further prominent ALS/FTLD pathologies, such as cytoplasmic and insoluble TDP-43 in TAR6/6 mice. This model represents not only pathological TDP-43 expression but also disease-relevant posttranslational changes.

17. The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis.

18. 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.

19. We identified impaired RNA metabolism, secondary to TDP-43 loss of function, as a possible pathological mechanism of HSPB8 toxicity, leading to muscle and nerve degeneration

20. the introduction of SOD1(G93A) and TDP43(A315T), established Amyotrophic lateral sclerosis (ALS)-related mutations, changed the subcellular expression and localization of RNAs within the neurons, showing a spatial specificity to either the soma or the axon. Altogether, we provide here the first combined inclusive profile of mRNA and miRNA expression in two ALS models at the subcellular level

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

1. 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

2. 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

3. 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.

4. 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.

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

6. 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.

7. 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.

8. 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.

9. 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.

10. 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.

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

12. 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.

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

14. Studied expression and localization of TAR DNA-binding protein 43 (TDP-43) in mouse seminiferous epithelium. Found TDP-43 is expressed by both germ cells and Sertoli cells and appears to have a role in specific stages of spermatogenesis.

15. TDP-43 overexpression decreases amyloid-Beta plaque deposition while increasing abnormal tau aggregation.

16. pTDP-43 granules were cleared and the number of pTDP-43-positive neurons returned to baseline after traumatic injury

17. results suggest that regulation of the U6 snRNA expression level by TDP-43 is a key factor in the increase in cell death upon TDP-43 loss-of-function

18. this study shows that HSF1 overexpression protects against TDP-43 pathology by upregulation of chaperones, especially HSP70, rather than enhancing autophagy

19. Acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein.

20. These studies showed that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dynamic oligomers antagonizing pathologic aggregation.

Zebrafish TAR DNA Binding Protein (TARDBP) interaction partners

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

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

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