https://www.selleckchem.com/products/az32.html
https://www.selleckchem.com/products/az32.html
Diagnosis of cell prion proteins throughout exosomes produced by ovine lcd. Our results suggest that these events alter the transient α-synuclein intramolecular contacts, inducing a greater solvent exposure of its hydrophobic, aggregation-prone NAC domain, in full agreement with a recent experimental study on Ca2+ binding. Moreover, metal-binding residues directly participate in the long-range contacts that shield this domain and regulate α-synuclein aggregation. These results provide a
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