ProMIS Neurosciences announced the publication of two papers highlighting the role of toxic misfolded superoxide dismutase-1 aggregates in the pathogenesis of ALS. One paper published in Acta Neuropathologica is titled, “Seeding activity of human superoxide dismutase 1 aggregates in familial and sporadic amyotrophic lateral sclerosis postmortem neural tissues by real-time quaking-induced conversion,” and the other publication in the online journal Open Biology is titled, “Amyloidogenic regions in beta-strands II and III modulate the aggregation and toxicity of SOD1 in living cells.” The newly published research in Acta Neuropathologica reports on the seminal finding that aggregated SOD1 seeds are present in ALS neural tissues, not only in patients with SOD1 mutations, but also in patients with the most common sporadic form of the disease, which supports the relevance of misfolded SOD1 as a therapeutic target and as a potential biomarker of disease.
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