title: Tracking protein aggregate interactions.
abstract: Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis ( 1, 2) . At each fibril end, β-sheets provide a template for recruiting and converting monomers ( 3) . Various amyloid fibrils often occur in the same individual, yet whether distinct protein aggregates aid or inhibit the assembly of heterologous proteins is unclear. In prion disease, different amyloid-like prion aggregate structures, or strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences ( 4-7) . Here we focus on the interactions reported to occur when two pre-existing amyloids or two distinct prion strains occur together in the central nervous system.
authors: Department of Pathology, University of California San Diego, La Jolla, CA, USA. red b-sheets aligne
authors: Christina J
authors: CJ
authors: Sigurdson
authors: Jason C
authors: JC
authors: Bartz
authors: K Peter R
authors: KP
authors: Nilsson
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