A filamentous inclusion body within anterior horn neurones in motor neurone disease defined by immunocytochemical localisation of ubiquitin
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The prion-like nature of amyotrophic lateral sclerosis
2020, Progress in Molecular Biology and Translational ScienceCitation Excerpt :Histopathological examination of fALS and sALS patient tissue has not fully elucidated the structure that SOD1, TDP-43, or FUS adopt when they are observed in a pathological state. TDP-43 has been reported to adopt a filamentous amyloid-like structure that can bind thioflavin-S in some cases.65,115,116 To our knowledge, there is no evidence for FUS forming amyloid fibrils in ALS patient tissue, however, evidence from FUS-associated FTLD has shown that FUS-reactive antibodies label filamentous structures within inclusions,117 although further confirmation is required as well as a more exhaustive examination in ALS patient tissue.
In vitro prion-like behaviour of TDP-43 in ALS
2016, Neurobiology of DiseaseNeuropathology of Amyotrophic Lateral Sclerosis and Its Variants
2015, Neurologic ClinicsIdentification of a rod domain-truncated isoform of nestin, Nes-Sδ<inf>107-254</inf>, in rat dorsal root ganglia
2013, Neuroscience LettersCitation Excerpt :This is consistent with our statistical analysis which demonstrated that when exogenously expressed in HEK293T cells, Nes-SΔ107–254 had a greater tendency to form aggregates than Nes-S (Fig. S6). It is known that presence of abnormal IF aggregates in neurons is a pathological feature of neurodegenerative diseases [11,12,16,22,28]. Similarly, we observed that the expression level of Nes-SΔ107–254 is low in DRG neurons of adult rats (Fig. 1A and C).
Gene Therapies in Motor Neuron Diseases ALS and SMA
2022, Fortschritte der Neurologie Psychiatrie