Publications by authors named "Jean-Baptiste Moog"
Article Synopsis
- Mammalian prions are infectious proteins formed from misfolded variants of the normal prion protein (PrP), exhibiting different conformations that can self-propagate and cause various prion diseases.
- Research demonstrates that fibrillar assemblies from recombinant PrP (rPrP) derived from various species (hamster, mouse, human, and bovine) show distinct pathogenic behaviors and strain properties when tested in transgenic mice.
- The findings indicate that rPrP assemblies can be used to study the transmission of prions and their strain diversity, as they can mimic the adaptation processes of genuine prions despite lacking certain crucial amino acid regions for infectivity.
Eukaryotic cells contain membrane-bound and membrane-less organelles that are often in contact with each other. How the interface properties of membrane-less organelles regulate their interactions with membranes remains challenging to assess. Here, we employ graphene-based sensors to investigate the electrostatic properties of synapsin 1, a major synaptic phosphoprotein, either in a single phase or after undergoing phase separation to form synapsin condensates.
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