Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

By M. Bucciantini, E. Giannoni, Fabrizio Chiti, F. Baroni, L. Formigli, J. Zurdo, Niccolò Taddei, G. Ramponi, Christopher M. Dobson, M. Stefani. Nature, 2002

2,483 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/5bc42343328b81622d3bd9b8eb990287ed6e2e8e

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Citations in the corpus

A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea (2002, background): “This observation is potentially of great importance to understand the evolved properties of native proteins, including their folding behavior, and the mechanism in which misfolding and aggregation are normally avoided in correctly functioning living systems (Dobson 2001; Bucciantini et al. 2002).”
Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue (2010, background): “Protein aggregation is classically considered to occur through random association of like proteins [42].”
Different Species of α-Synuclein Oligomers Induce Calcium Influx and Seeding (2007, background): “…than mature fibrils of -syn, are the pathogenic species (Conway et al., 2000; Goldberg and Lansbury, 2000; Masliah et al., 2000; Auluck et al., 2002; Bucciantini et al., 2002, 2004; Gosavi et al., 2002; Kayed et al., 2003, 2004; Park and Lansbury, 2003; Bodner et al., 2006; ElAgnaf et al., 2006).”
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, methodology): “To investigate whether EGCG-generated oligomers are toxic for mammalian cells, we carried out standardized 3- (4,5-dimethylthiazol-2yl)-2,5-diphenyltetrazolium bromide (MTT) reduction assays with PC12 cells [ 37 ].”
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, neutral): “Aggregated species obtained from this protein have been found to be cytotoxic when added to cell cultures [44].”
Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies (2002, neutral): “, aggresomes) (Kopito, 2000), and other large protein accretions may be late-stage features of a disease process in which the most important effectors of neuronal dysfunction are soluble assemblies that act early and irreversibly (Bucciantini et al., 2002).”
The amyloid state and its association with protein misfolding diseases (2014, background): “Paired betasheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy.”
Sox2 deficiency causes neurodegeneration and impaired neurogenesis in the adult mouse brain (2004, background): “Protein inclusions in neurodegenerative diseases are caused by the aggregation of potentially toxic misfolded proteins, and may represent an ‘attempt’ to clear the cell of harmful proteins through, for example, ubiquitination (Bucciantini et al., 2002; Taylor et al., 2002; Zoghbi and Botas, 2002).”
Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism (2006, background): “We imply that, as previously shown ( 21 ), using the right experimental conditions, almost any protein sequence can form amyloid fibrils and the presence of aromatic residues can enhance the fibrillation process.”