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University of Cambridge > Talks.cam > Physical Chemistry Research Interest Group > Chaperone-mediated neuroprotection against protein aggregation
Chaperone-mediated neuroprotection against protein aggregationAdd to your list(s) Download to your calendar using vCal
If you have a question about this talk, please contact David Madden. In this seminar, I will discuss the relevance of intra- and extracellular proteostasis in countering disease-associated protein misfolding and aggregation, particularly in neurodegenerative diseases characterized by protein deposition. I will present recent findings that link the multifunctional Ca-binding S100 family proteins to neuroprotective functions as both intra- and extracellular chaperones. The focus will be on S100B , highlighting its structural properties and mechanisms underlying its holdase activity that mitigates the aggregation, phase separation, neurotoxicity, and cell-to-cell spreading of amyloidogenic proteins, notably tau and amyloid β. I will discuss the diverse activities and changes in the levels of S100 proteins across the neurodegeneration continuum and propose their protective role as an early response mechanism to intra- and extracellular proteostasis dysfunction. This talk is part of the Physical Chemistry Research Interest Group series. This talk is included in these lists:
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