While β-synuclein doesn't form fibrils at physiological pH 7.4, environmental changes can induce its aggregation, but the structural determinants governing this transition are poorly understood. This knowledge gap limits our understanding of conditions that might compromise β-synuclein's protective function in disease states. Gap type: unexplained_observation Source paper: Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein. (2018, Journal of molecular biology, PMID:29782835)
Landscape Summary: How do environmental perturbations overcome β-synuclein's inherent resistance to fibrilization? is a 0.79 priority gap in neurodegeneration. It has 0 linked hypotheses with average composite score 0.000. Status: open.
Colonna, Sevlever, et al. (TREM2 biology)
How do environmental perturbations overcome β-synuclein's inherent resistance to fibrilization? — INVOKE-2 (completed)
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