ADDITIONAL INFORMATION

• Prion Diseases
• Thermostability of mouse-passaged BSE and scrapie is independent of host PrP genotype: implications for the nature of the causal agents
• Transmission of prion diseases by blood transfusion
• Early and advanced chronic wasting disease of mule deer
• Clinical features of variant Creutzfeldt-Jakob disease
• Mutant prion protein acquires resistance to protease in mouse neuroblastoma cells
• Prions in skeletal muscle
• Migrating intestinal dendritic cells transport PrPSc from the gut
• Distribution of the prion protein in sheep terminally affected with BSE following experimental oral transmission
• PrPCWD in deer with chronic wasting disease
• Neuroinvasion by a Creutzfeldt-Jakob disease agent in the absence of B cells and follicular dendritic cells
• Scrapie prion protein accumulation abrogated by exposure to a prion protein antibody
• Cellular prion protein status in sheep: tissue-specific biochemical signatures
• Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein
• A role for intermolecular disulfide bonds in prion diseases?
• Prion protein: Evolution caught en route
• Complement facilitates earl prion pathogenesis
• Conformational diversity in a yeast prion
• Mapping the early steps in the pH-induced conformational conversion of the prion protein
• BSE information site: England
• European Concern Over BSE Transmission
• Heat stability of prion rods and recombinant prion protein
• Prion infection impairs the cellular response to oxidative stress
• Early accumulation of PrPSc in gut-associated lymphoid and nervous tissues
• New recruits for French Prion research
• Were some CJD victims infected by vaccines?
• Inquiry blames missed warnings for scale of Britain's BSE crisis
• Tracking the Human Fallout From 'Mad Cow Disease
• Signal Transduction Through Prion Protein
• Experts Downplay New vCJD Fears
• Species-barrier-independent prion replication in apparently resistant species
• Identification of upregulated genes in scrapie-infected brain tissue
• Genetic influence on the structural variations of the abnormal prion protein
• Evidence for the Prion Hypothesis
• Encephalopathies: Scrapie in Britain during the BSE years
• NMR structure of the bovine prion protein
• NMR structures of three single-residue variants of the human prion protein
• Alzheimer's amyloids and amyloidogenic prion fragments
• Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid
• Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
• Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans
• Mad cow disease in the United States
• Creutzfeld-Jakob Disease
• Characterization of the murine BSE infectious agent
• Molecular analysis of Irish sheep scrapie cases
• Treatment of the scrapie agent infection
• Ultrasensitive detection of pathological prion protein aggregates
• Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells
• Writing Scrapie's Coda, Codon by Codon?
• Susceptibility of sheep for scrapie
• Prions: A Lone Killer or a Vital Accomplice?
• NMR solution structure of the human prion protein
• Brain injury and prion disease
• Oral infection of BSE prion
• Pathogenesis of the oral route of infection of mice with scrapie and bovinespongiform encephalopathy agents
• Elimination of prions by branched polyamines and implications for therapeutics
• Transmission of the 263K scrapie strain by the dental route
• Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells
• Scrapie Pathogenesis in Subclinically Infected B-Cell-Deficient Mice
• BSE in goats
• Genetics of prions
• B-cell role in prion neuroinvasion
• Review of Spongiform Encephalopathies
• Effect of prions on a neuronal cell line
• Prion protein immunoassay
• Tracking down the prion protein
• Mechanism of prion protein conversion
• Unresolved issues as to the nature of prions
• Transmissible Spongiform Encephalopathies; Anne M. Haywood, The New England Journal of Medicine, 1997, Volume 337, No. 25, pages 1821-1828.
• Prion disease vaccine
• Prion protein epitope/transmission of BSE in transgenic mice
• Cellular prion protein receptor
• Laminin receptor precursor/prion protein
• Protein chaperones/prion protein conversion
• Deadly Conformations-Protein Misfolding in Prion Disease
• No "niche selection" for prion protein
• Immunodetection of prion protein
• SCID/BSE
• Propagation of prion strains