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Human TARDBP Protein expressed in HEK-293 Cells - ABIN2733240
Yang, Lin, Robertson, Wang: Dual vulnerability of TDP-43 to calpain and caspase-3 proteolysis after neurotoxic conditions and traumatic brain injury. in Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2014
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Expression of PFN1 (zeige PFN1 Proteine) mutants induces accumulation of TDP-43, and promotes conversion of normal TDP-43 into an abnormal form. These results provide new insight into the mechanisms of TDP-43 proteinopathies and other diseases associated with amyloid-like protein deposition.
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.
This study demonstrated that increased rates of TDP-43-associated hippocampal atrophy might occur at least 10 years before death in patient with Alzheimer disease.
Authors observed impaired levels of glutathione (downstream Nrf2 (zeige GABPA Proteine) antioxidant) in TDP-43M337V patient fibroblasts and astrocyte cultures from TDP-43Q331K mice, indicative of elevated oxidative stress and failure of some upregulated antioxidant genes to be translated into protein.
removing the human orthologs of Hrb27c (DAZAP1 (zeige DAZAP1 Proteine)) in human neuronal cell lines can correct several pre-mRNA splicing events altered by TDP-43 depletion
TDP-43 suppressed tau expression by promoting its mRNA instability through the UG repeats of its 3-UTR. The C-terminal region of TDP-43 was required for this function.The level of TDP-43, which is decreased in AD brains, was found to correlate negatively with the tau level in human brain.
Amyotrophic lateral sclerosis mutations disrupt phase separation mediated by alpha-helical structure in the TDP-43 low-complexity C-terminal domain.
we demonstrated cytoplasmic TDP-43 aggregate formation in neuronal and glial cells following adenoviral transduction of WT and CTF (zeige NFIA Proteine) TDP-43 under MG-132 treatment. These TDP-43 aggregates were phosphorylated and ubiquitinated and consisted of electron-dense granules.
emphasize the importance of distinguishing cerebral age-related TDP-43 with sclerosis from late-onset frontotemporal lobar degeneration with TDP-43 pathology and from advanced Alzheimer disease with TDP-43 pathology
Mutant and wild type human TDP-43 replacing the endogenous Drosophila gene reveals phosphorylation and ubiquitination in mutant lines in the absence of viability or lifespan defects.
superoxide dismutase (zeige SOD1 Proteine) function of SOD1 (zeige SOD1 Proteine) 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 (zeige NFE2L2 Proteine)/ARE pathway by reducing the expression of MafK and JDP2 (zeige JDP2 Proteine) proteins.
The suppression of TDP-43 mitochondrial localization abolishes WT and mutant TDP-43-induced mitochondrial dysfunction and neuronal loss, and improves phenotypes of transgenic mutant TDP-43 mice.
we found a significant overlap in genes that undergo both RBM17 (zeige RBM17 Proteine)- and TDP-43-dependent cryptic splicing repression, many of which are associated with survival. We propose that repression of cryptic splicing by RBPs is critical for neuronal health and survival
These results establish that SMN overexpression in motor neurons slows disease onset and outcome by ameliorating pathological signs in this model of mutant TDP-43-mediated amyotrophic lateral sclerosis (ALS).
These findings suggest that TDP-43 promotes tau exon 10 inclusion and 4R-tau expression and that disease-related changes of TDP-43, truncations and mutations, affect its function in tau exon 10 splicing, possibly because of TDP-43 mislocalization to the cytoplasm.
this study suggests hemizygous TDP-43(M337V) mice as a useful animal model to study TDP-43 toxicity and further consolidates mitochondrial TDP-43 as a novel therapeutic target for TDP-43-linked neurodegenerative diseases.
Data indicate a method for site-directed single nucleotide editing in two disease-related genes, DNA binding protein (zeige CNBP Proteine) tardbp and RNA binding protein fus (zeige FUS Proteine).
Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.
TARDBP and FUS (zeige FUS Proteine) act in a pathogenic pathway that is independent of SOD1 (zeige SOD1 Proteine).
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