In 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
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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 MoreTaken together, aggregation of TDP-43 is most probably the root cause of ALS/FTLD either through a gain of toxic function (GOF) on its own or through a loss of function (LOF) with sequestration and
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 MoreHaving established that TDP-43 is inherently aggregation-prone, we next asked if ALS-linked TDP-43 mutations affect aggregation in vivo. We have developed a
Learn MoreA Possible Path to Preventing TDP-43 Aggregation. TDP-43 is known to increase with age, and also forms aggregates observed in ALS and frontemporal dementia, among other conditions. The increased amount of TDP-43 alone, even without aggregates, appears to diminish the cellular housekeeping process of autophagy, with detrimental long term
Learn MoreThe major aggregating protein in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), the RNA-binding protein TDP-43,
Learn MoreTDP-43 aggregation inhibitors for the treatment of ALS. Award Information. Agency: Department of field This proposal provides an innovative new therapeutic approach to the disease that is based on reversing the aggregation of TDP which is a protein that is both genetically linked to familial ALS and is the predominant protein species
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
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Learn MoreIn , Liu and collaborators developed peptides targeting TDP-43-CTD to decrease TDP-43 aggregation and reduce subsequent toxicity in cells.
Learn More2021. 12. 31. · Background. TDP-43 is a highly conserved protein localized to the nucleus. Under pathological conditions, it forms fibrillar aggregates, characteristic of Amyotrophic Lateral Sclerosis (ALS) progression. The exact mechanism of TDP-43 aggregation and formation into a pathological state has yet to be elucidated, but is an important therapeutic target to consider.
Learn MoreThe TDP-43 assays are SIMOA® assay kits for the measurement of the TAR DNA binding protein of 43 kDa in serum and human plasma.
Learn More2018. 4. 13. · Phosphorylated TDP-43 (pTDP-43) aggregates in the axial skeletal muscle of patients with sporadic and familial amyotrophic lateral sclerosis Acta Neuropathol Commun.
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 MoreAs discussed in Section 1, the significance of TDP-43 aggregation in disease is still a very debated subject.
Learn More2021. 3. 10. · Aggregation and cell-to-cell spread of TDP-43 are thought to underlie many cases of frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). Additionally, the aging process and environmental toxins stimulate excessive generation of reactive oxygen and nitrogen species (ROS/RNS), thus contributing to the pathological processes of these
Learn MoreCytoplasmic TDP-43 aggregates in neurons are a hallmark pathology of ALS. Under various stress conditions, TDP-43 localizes sequentially to two
Learn MoreTDP-43 acetylation-mimic mutations or acute treatment with arsenite led to the formation of cytoplasmic aggregates that co-localized with HDAC6. Scale bar, 25 μm. ( e) Protein levels of the
Learn MoreIn ALS and FTLD-U, aggregated, ubiquitinated, and N-terminally truncated TDP-43 can be isolated from brain tissue rich in neuronal and glial cytoplasmic inclusions. The loss of TDP-43 function resulting from inappropriate cleavage, translocation from the nucleus, or its sequestration into inclusions could play important roles in neurodegeneration.
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