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  1. The generation of a pathogenic molecule through protein misfolding cycling amplification (PMCA) in the presence of phospholipid is reminiscent of the "globulomer" complex formed from Aβ and specific lipids (Barghorn et al., 2005). There may also be some relationship to the role of gangliosides in creation of a toxic Aβ moiety (Kakio et al., 2002; Yamamoto et al., 2007). Perhaps lipid-protein interactions play a general and critical role in the development of peptide misfolding disorders.


    . Globular amyloid beta-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease. J Neurochem. 2005 Nov;95(3):834-47. PubMed.

    . Interactions of amyloid beta-protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry. 2002 Jun 11;41(23):7385-90. PubMed.

    . A ganglioside-induced toxic soluble Abeta assembly. Its enhanced formation from Abeta bearing the Arctic mutation. J Biol Chem. 2007 Jan 26;282(4):2646-55. PubMed.

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  1. Shape-shifting Prions: Infectious Recombinant and Myelin-Minding Normal