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Human Monoclonal TARDBP Primary Antibody für 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 für 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 für 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 für 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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Monoclonal TARDBP Primary Antibody für 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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Polyclonal TARDBP Primary Antibody für 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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Human Polyclonal TARDBP Primary Antibody für 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 für ICC, ELISA - ABIN1003253
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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We propose that TDP-43 has a novel role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts.
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.
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.
This report here an age-related increase and formation of ubiquitinated TDP-43 cytoplasmic inclusions after stroke.
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.
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.
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.
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.
the progression of frontotemporal lobar degeneration-TAR DNA-binding 43 protein reflects the templated cell-to-cell transneuronal spread of pathological TDP-43.
TDP-43 deposition leads to targeted RNA instability in amyotrophic lateral sclerosis and frontotemporal dementia
CHCHD10 mutations have a role in cytoplasmic TDP-43 accumulation and synaptic integrity
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.
The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in 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.
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
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
These data provide structural detail for the established mechanistic role of the well-folded TDP-43 NTD in splicing and link this function to liquid-liquid phase separation.
TDP43 alters most splicing events with splicing factor SRSF3 in triple-negative breast cancer.
Of the whole cohort of patients with Motor Neuron Disease and Frontotemporal Dementia, 1 patient harboured a mutation in the TAR DNA-binding protein (TARDBP) gene.
Study demonstrated TDP-43/pTDP-43 deposition in skin nerves in ALS patients. Although the mechanisms underlying TDP-43 in ALS are currently unknown, its detection is of interest, and the deposition may occur not only in ALS but also during the aging process which is based on observations of the present study.
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.
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.
The mutated TDP-43 has a significant pathological effect at the dendritic spine that is associated with attenuated neural transmission.
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.
TDP-43 overexpression decreases amyloid-Beta plaque deposition while increasing abnormal tau aggregation.
pTDP-43 granules were cleared and the number of pTDP-43-positive neurons returned to baseline after traumatic injury
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
this study shows that HSF1 overexpression protects against TDP-43 pathology by upregulation of chaperones, especially HSP70, rather than enhancing autophagy
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.
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.
Study reports the altered expression and/or mislocalization of the TAR-DNA binding protein 43 (TDP-43) in both niemann-pick disease type C mouse and in a human neuronal model of the disease. Results extend the importance of the role of TDP-43 in neurodegenerative disease and further highlight the need to prioritize the targeting of this protein to develop novel therapeutic strategies.
superoxide dismutase function of SOD1 might not be required to preserve DNA integrity in motor neurons, at least when the function of TDP-43 is unaltered
The findings of this study support a role for nuclear depletion of TDP-43 in the pathogenesis of AD and provide strong rationale for developing novel therapeutics to alleviate the depletion of TDP-43 and functional antemortem biomarkers associated with its nuclear loss.
These results suggested that nuclear localization signal -tagged TDP25 (a carboxyl-terminal fragment of TDP-43) can change its structure to use ordered oligomeric but nontoxic state. Moreover, the structure of ordered oligomers as well as nuclear sequestration may be important in mediating cytotoxicity in ALS pathology.
Mutatgion M337V in TDP-43 impaired the Nrf2/ARE pathway by reducing the expression of MafK and JDP2 proteins.
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