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lüll The molecular pathology of CJD: old and new variants Jackson GS; Collinge JMol Pathol 2001[Dec]; 54 (6): 393-9The study of prion disease has become an area of intense interest since experimental evidence emerged for the transmission of phenotypic variation without the involvement of a nucleic acid component. Additional impetus has come from the widespread concern that exposure to bovine spongiform encephalopathy contaminated material poses a distinct and, conceivably, a severe threat to public health in the UK and other countries. The occurrence of new variant Creutzfeldt-Jakob disease has dramatically highlighted the need for a precise understanding of the molecular basis of prion propagation. The molecular basis of prion strain diversity, previously a major challenge to the "protein only" model, can now be reconciled with propagation of infectious protein topologies. The conformational change known to be central to prion propagation, from a predominantly alpha-helical fold to one predominantly comprising beta-structure, can now be reproduced in vitro, and the ability of beta-PrP to form fibrillar aggregates provides a plausible molecular mechanism for prion propagation. Concomitantly, advances in the fundamental biology of prion disease have done much to reinforce the protein only hypothesis of prion replication.|Animals[MESH]|Brain Chemistry[MESH]|Cell Death[MESH]|Creutzfeldt-Jakob Syndrome/classification/*genetics/pathology[MESH]|Dendritic Cells, Follicular/metabolism[MESH]|Humans[MESH]|Mice[MESH]|Mice, Transgenic[MESH]|Models, Animal[MESH]|Models, Genetic[MESH]|Neurons/metabolism/pathology[MESH]|PrPC Proteins/genetics/metabolism[MESH]|PrPSc Proteins/genetics/metabolism[MESH]|Prions/*genetics/metabolism[MESH]|Protein Conformation[MESH] |