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Learn MoreTAR DNA binding protein 43 (TDP-43) is a nucleic acid binding protein involved in RNA-related metabolism. Aggregated TDP-43 has been identified as a hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD), and more widely in several neurodegenerative diseases: TDP-43 proteinopathies.
Learn MoreMoreover, TDP-43 is an aggregation-prone protein and, given the role of toxic protein aggregates in neurodegeneration, a toxic gain-of-function mechanism is another rational hypothesis. Importantly, ALS related mutations modulate the propensity of TDP-43 to aggregate in cell culture.
Learn MoreIn some neurodegenerative diseases, a protein called TDP-43 forms aggregates in the brain, resulting in neuronal cell death. The structure of these aggregates and their properties have been
Learn Moreof TDP-43 in an aggregation and sequestration model cell line HEK293 Flp-in Flag-TDP-43-12x-Q/N F4L. Our results show that differential expression of proteins in TDP-12xQ/N-F4L cells correlated with proteomic results of TDP-43 knockdown in SH-SY5Y, revealing a common set of proteins whose expression is influenced via TDP-43 aggregation or
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Learn MoreThe formation of TDP-43 inclusions within micronuclei induced by metabolic stress is a novel mechanism of protein aggregate formation which may
Learn MoreIntraneuronal aggregation of TDP-43 is seen in 97% of all amyotrophic lateral sclerosis cases and occurs by a poorly understood mechanism.
Learn MoreThe HTRF signal was recorded after an overnight incubation. As expected, the overexpression of WT or mutated TDP-43 alone increase the aggregated ratio compared to non-transfected cells.
Learn MoreFor example, co-expression of αS and TDP-43 enhances neurodegeneration and loss of dopaminergic neurons in C.elegans and transgenic mice (41, 42). Similarly, incubation of exogenous αS fibrils in SH-SY5Y cells enhances TDP-43 phosphorylation and aggregation .
Learn MoreThe major aggregating protein in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), the RNA-binding protein TDP-43,
Learn MoreOur study addressed the impact of selected ALS-associated genes on TDP-43 aggregation behavior in wild-type and aggregation prone TDP-43 in vitro cell
Learn More2019. 5. 1. · Transactive response DNA-binding protein-43 (TDP-43) is an RNA/DNA binding protein that forms phosphorylated and ubiquitinated aggregates in the cytoplasm of motor
Learn MoreInterestingly, although TDP-43 is a nuclear protein, aggregates often occur in the cytoplasm. It has also been shown that full-length TDP-43 aggregates are more common in the spinal cord, whereas CTF aggregates are common in cortex [10]. The role of TDP-43 aggregation, ubiquitination, and phosphorylation in ALS and FTLD-U is unknown.
Learn More2019. 3. 8. · TAR DNA-binding protein 43 (TDP-43) is a nucleic acid–binding protein, and its aggregation represents the defining pathology in amyotrophic lateral sclerosis (ALS) and related proteinopathies. Recent studies implicate cytoplasmic stress granules (SGs) as hubs that may facilitate TDP-43 aggregation. Here, using cellular fractionation, biochemical analyses, and
Learn MoreFIGURE 1 Aggregation of TDP-43 and TDP-43 fragments in vitro. A, a diagram of the domain structure of TDP-43 indicating both RNA recognition motifs (RRM1 and RRM2) and the glycine-rich C-terminal domain. B, TDP-43 or the indicated TDP-43 fragment (1-275 or 188-414) (3 μm) were incubated at 25 °C with agitation for 0-120 min.
Learn MoreThe C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism TAR DNA binding protein 43 KD (TDP-43) is an essential gene that regulates gene transcription, mRNA splicing and stability.
Learn MoreTDP-43 is a nuclear RNA-binding protein that forms neuronal cytoplasmic inclusions in two major neurodegenerative diseases, ALS and FTLD.
Learn More2011. 11. 1. · TDP-43 aggregation and neuropathology have been observed in a spectrum of distinct neurodegenerative disorders collectively known as the TDP-43 proteinopathies, suggesting a central role for TDP-43 in neurodegenerative disease pathogenesis 2, 3. Indeed, the identification of more than 35 missense mutations in the TARDBP gene has further
Learn MoreCytoplasmic aggregation of hyperphosphorylated TDP-43 (depicted by blue P) is a hallmark of TDP-43 proteinopathies and may result in cellular stress,
Learn MoreTDP-43 can form cytoplasmic aggregates that deleteriously affect neuronal health, including cellular toxicity, signaling cascade interference, and sequestration of additional TDP-43, thus rendering it inactive. Such aggregates are present in 97% and 50% of ALS and FTLD patients, respectively (de Boer et al., ; Jo et al., ).
Learn MoreTAR DNA binding protein (TDP-43) has been found to be a major component of inclusion bodies in motor neurons of ALS patients. Inclusion bodies are protein aggregates considered a pathological hallmark of neurodegeneration. Our group and eight independent research groups screened TDP-43 for mutations.
Learn MoreInitial studies of cytoplasmic TDP-43 aggregates focused on the assumption that they represented inclusion bodies, i.e. abnormal accumulations of misfolded ubiquitinated TDP-43 that could not be properly degraded by the cell.
Learn More2022. 9. 1. · Request PDF | Finding a chaperone for TDP-43 | Aggregation of the RNA-binding protein TDP-43 is commonly observed in neurodegenerative disorders. A new study reveals that this process may be
Learn MoreSG assembly can trigger TDP-43 aggregation . We and others have shown that poly(GR) promotes the aggregation of recombinant TDP-43, colocalizes with TDP-43 in SGs in cultured cells, and coaggregates with TDP-43 in postmortem tissue from patients with c9ALS/FTD (11, 14, 27). Together, these findings suggest that poly(GR) contributes to c9ALS/FTD
Learn Moreaccordingly, in the present study, we report that not only exogenous but also endogenous rns can trigger tdp-43 aggregation via s-nitrosylation and consequent disulfide bond formation; in models of ftd and als, we identify endogenous sno-tdp-43 formation as a critical effector of pathological signaling, leading to its aggregation, altered
Learn MoreTDP-43 seems to be intrinsically aggregation prone, and various mutations in TDP-43 can accelerate aggregate formation. Such intrinsic potential
Learn More2012. 6. 26. · Moreover, TDP-43 is an aggregation-prone protein and, given the role of toxic protein aggregates in neurodegeneration, a toxic gain-of-function mechanism is another
Learn MoreTransactive response DNA binding protein 43 (TDP-43) is a DNA/RNA binding TDP-43 aggregation but rather to both loss and gain-of-function processes
Learn More2022. 9. 6. · Dysfunction and aggregation of the RNA-binding protein, TDP-43, is the unifying hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Mechanisms and relative contributions of concurrent TDP-43 nuclear depletion, cytoplasmic accumulation, and post-translational modification to neurodegeneration remain unresolved.
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