How understanding the dynamics of yeast prions can shed light on neurodegenerative diseases

How understanding the dynamics of yeast prions can shed light on neurodegenerative diseases
Based on the HS-AFM observations, we propose that the freely moving tails of the monomers of the yeast prion protein Sup35 are incorporated into the fibril ends, and then the structural conversions to cross-β structures gradually occur. Credit: Tokyo Tech

Prions are a class of misfolded proteins that form aggregates called amyloid fibrils. These aggregates are the main culprit behind severe mammalian neurodegenerative diseases like Alzheimer’s. What makes them so deadly is that they are capable of transmitting their erroneous conformation to otherwise healthy proteins, causing an imbalance in cellular function. Currently, there are no effective treatments for fatal prion diseases, mainly because studying mammalian prions is challenging. Thus, scientists have turned to studying prions in less complex organisms like yeast,…

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