protein misfolding – mycolab.ai

Long term worsening of amyloid pathology, cerebral function, and cognition after a single inoculation of beta-amyloid seeds with Osaka mutation

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Researchers found that a single exposure to mutated amyloid-beta proteins (Aβ Osaka) in the brains of genetically modified mice caused lasting damage over four months. The mutated proteins triggered more severe memory loss, brain connectivity problems, and synapse damage compared to normal amyloid-beta. This suggests that even one encounter with mutated amyloid proteins can set off a chain reaction of disease progression that persists long after initial exposure.

Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function

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Prion diseases are deadly brain conditions caused by misfolded proteins. This study used computer simulations and fruit fly experiments to understand how tiny changes in prion protein structure affect its ability to cause disease. Researchers found that proteins with flexible loops are more toxic, while those with more rigid structures cause less damage, suggesting new ways to develop treatments by stabilizing the protein’s structure.

Research Keyword: protein misfolding

Long term worsening of amyloid pathology, cerebral function, and cognition after a single inoculation of beta-amyloid seeds with Osaka mutation

Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function