Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid.

By K. Conway, and J. W. Harper, P. Lansbury. Biochemistry, 2000

785 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/5207f183db6a860df0e4828952f0f318fb0e4757

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Citations in the corpus

Toll-like receptor 4 is required for α-synuclein dependent activation of microglia and astroglia (2013, background): “It is known that AS is able to self-assemble under certain conditions (Cole et al., 2002), including incubation at 37 C (Conway et al., 2000).”
DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation (2004, methodology): “…and sporadic forms of PD, as mutations associated with autosomal dominant familial primary Parkinsonism alter the propensity of aSyn to aggregate (Conway et al. 2000a), and as aSyn fibrils are a major constituent of the Lewy body intracytoplasmic inclusions that typify PD pathology (Spillantini…”
Structures of α-Synuclein Filaments from Multiple System Atrophy (2020, background): “Upon assembly, recombinantly expressed α-synuclein undergoes conformational changes and takes on a cross-β structure characteristic of amyloid (39,40).”
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide (2007, background): “Moreover, in vitro PF formation is accelerated by α-synuclein mutations that cause early onset PD; the A30P α-synuclein mutation promotes the formation of spherical PFs but actually slows the conversion to insoluble amyloid fibril”
Unfolding the role of protein misfolding in neurodegenerative diseases (2003, background): “Low-resolution structural studies have shown, in all cases, a large secondary structural difference between the monomeric native protein and the aggregated materia”
Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance (2002, background): “Although the observation of a strong amide I band near 1630 cm 1 and a weaker band near 1690 cm 1 in infrared spectra of amyloid fibrils has been interpreted as evidence for antiparallel -sheets in amyloid fibrils (Hilbich et al., 1991; Fraser et al., 1992; Conway et al., 2000), recent measurements ”
Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. (2006, background): “This same spectrum of aggregation intermediates and morphologies have been observed for many types of amyloids, such as -synuclein [ 14 ], islet amyloid [30] and non-disease associated “neoamyloids” [11].”
In vivo demonstration that α-synuclein oligomers are toxic (2011, background): “These oligomers interact with lipids, disrupt membranes (7, 8), and cause cell death in vitro (10, 11) and in nonmammalian models, such as Caenorhabditis elegans and Drosophila melanogaster (12).”