NR APMY
AU Wadsworth,J.D.F.; Hill,A.F.; Beck,J.A.; Collinge,J.
TI Molecular and clinical classification of human prion disease
QU British Medical Bulletin 2003; 66: 241-54
PT journal article; review; review, tutorial
AB While rare in humans, the prion diseases have become an area of intense clinical and scientific interest. The recognition that variant Creutzfeldt-Jakob disease is caused by the same prion strain as bovine spongiform encephalopathy in cattle has dramatically highlighted the need for a precise understanding of the molecular biology of human prion diseases. Detailed clinical, pathological and molecular data from a large number of human prion disease cases have shown that distinct abnormal isoforms of prion protein are associated with prion protein gene polymorphism and neuropathological phenotypes. A molecular classification of human prion diseases seems achievable through characterisation of structural differences of the infectious agent itself.
ZR 64
MH Adult; Aged; Amyloid/analysis; Blotting, Western; Brain Chemistry; Cerebellar Ataxia/etiology; Creutzfeldt-Jakob Syndrome/diagnosis/genetics; Dementia/etiology; Genetic Diseases, Inborn; Genetic Predisposition to Disease; Human; Iatrogenic Disease; Middle Aged; Myoclonus/etiology; *Polymorphism (Genetics); PrPsc Proteins/analysis/*genetics; Prion Diseases/*classification/diagnosis/*genetics; Protein Precursors/analysis; Surgical Instruments; Tissue Distribution; Tonsil/chemistry
AD MRC Prion Unit and Department of Neurodegenerative Disease, Institute of Neurology, University College, London, UK
SP englisch
PO England