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The Leuven Protein Aggregation Meeting

Date September 21 - September 23
Website https://www.vibconferences.be/events/the-leuven-protein-aggregation-meeting
Organizers VIB Conferences
Venue Groot Begijnhof
Location
Faculty Club; Groot Begijnhof 14
Leuven, 3000 Belgium

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Frederic Rousseau, Joost Schymkowitz, and the Switch Lab are bringing together inspiring speakers from around the world to talk about some of the most exciting research in protein aggregation field during a small and focussed meeting in Leuven. With less than 150 participants in an informal setting, there will be ample opportunity for discussion and interaction among all participants. Poster sessions and blitzes are included in the program to allow contributions from as many attendees as possible.

The interests of the invited speakers encompass a wide range of topics:

  • the structure and function of amyloidogenic proteins and the mechanism of the formation of amyloid structures, both in the case of functional amyloids as well as in the context of disease, as well as the biophysical and biochemical aspects of protein folding and misfolding in general
  • the molecular basis of toxicity of amyloids in prion disease and neurodegenerative disorders associated with protein misfolding, the molecular architecture of neurons in health and how it changes in protein aggregation diseases, and ageing, as well as the protective role of polyphosphates against amyloid cytotoxicity
  • how the proteostasis network (including the extracellular proteostasis) keeps proteins functional, as well as how it can break down, leading to toxic protein aggregation in neurodegenerative disease, cancer, or ageing
  • the role of protein fibrils in microbiology, the repurposing anti-amyloid compounds as antimicrobial agents, and using metal-containing synthetic amyloids as catalysts
  • the interaction of the microbial and the human ‘amylomes’ in health and disease
  • using biophysical methods to investigate amyloid polymorphism, including differences between patient-derived and synthetic amyloid fibres using cryo-electron microscopy and X-ray micro-crystallography and the properties of misfolding proteins at the nanoscale.