Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 29, Issue 4, Pages 162-165Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2004.02.008
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A detailed mechanistic or structural understanding of the misfolding events that render the normal cellular prion protein, PrPC, amyloidogenic and infectious has been elusive. Many groups have observed that, under certain conditions, PrPC has a tendency to form beta-strand-rich fibers. A recently published protocol for in vitro conversion of PrPC shows that the formation of intermolecular disulfide bonds between monomers of recombinant PrP might play a role in the folding and fibrilization of this protein in vitro.
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