[Identification of beta-aggregate sites in protein chain].
Studying amyloid diseases (amyloidoses) has been especially actual and has attracted the attention of researchers all over the world in connection with the appearance of epidemic prion diseases such as Bovine Spongiform Encephalopathie in cattle and Creutzfeldt-Jakob in human. Amyloidoses are caused by transition of a "healthy" protein molecule or peptide from a native conformation to a very stable pathologic form: molecules in a pathologic conformation aggregate, that results in the amyloid fibrils which can grow infinitely. Investigation of molecular mechanisms of these diseases and the ability to find protein regions responsible for the appearance of the given diseases is a fundamental problem. Theoretical and experimental studies of amyloid fibril formation are considered in this review.
Galzitskaia
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D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D007562:Creutzfeldt-Jakob Syndrome / Q000209:etiology* / Q000378:metabolism; D016643:Encephalopathy, Bovine Spongiform / Q000209:etiology* / Q000378:metabolism; D006801:Humans; D017433:Protein Structure, Secondary
D000682:Amyloid; D016229:Amyloid beta-Peptides