Amyloid fibrillogenesis: themes and variations.

By J. Rochet, P. Lansbury. Current Opinion in Structural Biology, 2000

1,015 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/7786b6c99905716231a3ba29b05cdd311af3aff5

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Citations in the corpus

Atomic structures of amyloid cross-β spines reveal varied steric zippers (2007, background): “(4) The finding of distinct crystalline polymorphs of the same zipper-forming segments offers a molecular-level hypothesis for amyloid polymorphism and prion strains, which awaits verification or disproof.”
Therapeutic approaches to protein-misfolding diseases (2003, background): “The major representatives of these disorders are the amyloidoses, in which protein aggregation in the extracellular space is associated with the appearance of a toxic functio”
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “Spherical oligomers, or worm-like structures, often referred to as 'protofibrils', have been proposed as crucial assembly intermediates in the aggregation pathway [ 2 ].”
Conformational constraints for amyloid fibrillation: the importance of being unfolded. (2004, background): “of a partially unfolded conformation or intermediate [1– 6,48–51].”
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides (2007, positive): “The size of the sliding window ([5,7,9], and [11] residues) was trained against a database of 57 amyloidogenic proteins, in which the location of "hot spots" was experimentally known.”
Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. (2011, background): “Many small peptides and proteins are able to create fibrils in vitro with amyloid-like properties (86, 310).”
Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. (2002, background): “Although a toxic role for protofibrils has been suggested in several neurodegenerative diseases, the mechanism of its toxicity has not been elucidated.(14,26) – 28 Our own studies have demonstrated that protofibrillar a-synuclein exhibits tight binding to phosphatidylglycerol (PG) vesicles via a b-s”