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Human Monoclonal TARDBP Primary Antibody for IF, IHC (p) - ABIN565080
Arai, Hasegawa, Akiyama, Ikeda, Nonaka, Mori, Mann, Tsuchiya, Yoshida, Hashizume, Oda: TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. in Biochemical and biophysical research communications 2006
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Chicken Polyclonal TARDBP Primary Antibody for ICC, IF - ABIN188986
Neumann, Sampathu, Kwong, Truax, Micsenyi, Chou, Bruce, Schuck, Grossman, Clark, McCluskey, Miller, Masliah, Mackenzie, Feldman, Feiden, Kretzschmar, Trojanowski, Lee: Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. in Science (New York, N.Y.) 2006
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Human Polyclonal TARDBP Primary Antibody for ELISA, WB - ABIN565079
Johnson, McCaffery, Lindquist, Gitler: A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. in Proceedings of the National Academy of Sciences of the United States of America 2008
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Polyclonal TARDBP Primary Antibody for WB - ABIN540268
De Marco, Lomartire, Mandili, Lupino, Buccinnà, Ramondetti, Moglia, Novelli, Piccinini, Mostert, Rinaudo, Chiò, Calvo: Reduced cellular Ca(2+) availability enhances TDP-43 cleavage by apoptotic caspases. in Biochimica et biophysica acta 2014
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Polyclonal TARDBP Primary Antibody for ELISA, WB - ABIN539699
Zhang, Xu, Dickey, Buratti, Baralle, Bailey, Pickering-Brown, Dickson, Petrucelli: Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2007
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Monoclonal TARDBP Primary Antibody for IHC (p), ELISA - ABIN533778
Ou, Wu, Harrich, García-Martínez, Gaynor: Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. in Journal of virology 1995
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Human Polyclonal TARDBP Primary Antibody for ICC, IF - ABIN4358265
Sharma, Burré, Südhof: CSPα promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity. in Nature cell biology 2010
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Human Polyclonal TARDBP Primary Antibody for IF, WB - ABIN541623
Buratti, Dörk, Zuccato, Pagani, Romano, Baralle: Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. in The EMBO journal 2001
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The work has not only uncovered a previously unknown role of LonP1 in regulating mitochondrial TDP-43 levels, but also advanced understanding of the pathogenic mechanisms leading to TDP-43 proteinopathy.
The formation of poly-GA protein inclusions in C9ORF72 leads to intracellular aggregation of TDP-43 in cultured neuronal cells.Poly-GA protein aggregation directly promotes pathogenic changes of TDP-43 without the formation of nuclear RNA foci containing GGGGCC repeat expansion or loss-of-function of the C9ORF72 protein.
Hippocampal subfield pathological shape is related to TDP-43
Findings identify a neuronal cell death mechanism that can be initiated by transient-stress-induced cytosolic de-mixing of TDP-43.
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.
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.
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.
TARDBP is required for maintaining the expression of ATG4B.
Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis
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
In patient specific TDP43 mutations, there was aging-related neurodegeneration in induced pluripotent stem cells from motor neurons.
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.
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
activated microglia may make unique contributions to cortical thinning and TDP-43 inclusion formation
TDP-43 regulates poly(A) tail length of endogenous Progranulin (GRN) mRNA.
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.
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.
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.
The TDP-43-regulated miRNAs may play multifaceted roles in the pathogenesis of cancer.
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
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.
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.
TDP-43 induces p53-mediated cell death of cortical progenitors and immature neurons
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.
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.
Cytoplasmic mislocalization of TDP-43 is associated with enteroviral infection related Amyotrophic lateral sclerosis.
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).
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
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
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.
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.
This study demonstrated here that muscle-dominant TDP-43 transgenic mice had lower body weights and increased serum levels of myogenic enzymes
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.
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.
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.
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.
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.
Increased excitatory synaptic inputs and dendritic spine densities is associated with TDP-43(Q331K) mutation resulting in amyotrophic lateral sclerosis.
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.
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.
Data indicate a method for site-directed single nucleotide editing in two disease-related genes, DNA binding protein tardbp and RNA binding protein fus.
Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.
TARDBP and FUS act in a pathogenic pathway that is independent of SOD1.
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, this protein regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20.
TAR DNA binding protein
, TAR DNA-binding protein 43
, Tardbp protein
, TAR DNA-binding protein-43