Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid
Reexamination Certificate
2006-02-14
2006-02-14
Riley, Jezia (Department: 1634)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving nucleic acid
C435S320100, C435S252800, C435S174000, C435S183000, C382S129000, C382S133000, C382S153000, C382S173000, C382S286000, C382S291000, C702S019000, C702S022000, C536S022100
Reexamination Certificate
active
06998231
ABSTRACT:
The present invention relates to a method for typing a sample of a prion or spongiform encephalopathy disease, a kit suitable for use in such a typing method, a method for identifying infection in an animal and/or tissue of bovine spongiform encephalopathy (BSE), a method for assessing and/or predicting the susceptibility of an animal to BSE, a kit for use in such an assessment and/or prediction method, a method for the treatment of a prion disease, and compounds suitable for such a method.
REFERENCES:
patent: 4892814 (1990-01-01), Harrington
patent: 5846533 (1998-12-01), Prusiner
patent: 6008435 (1999-12-01), Prusiner
patent: 2 258 867 (1993-02-01), None
patent: WO 95/31466 (1995-11-01), None
patent: WO 96/17249 (1996-06-01), None
patent: WO 97/04814 (1997-02-01), None
patent: WO 97/46572 (1997-12-01), None
Race et al., “Proteinase K-resistant prion protein dtection in animal tissues and in vitro”, Bovine Spongiform Encephalopathy The BSE Dilemma, 6tg, Williamsburg, Va., Feb. 26-Mar. 1, 1995 (1996), pp. 317-324.
Race et al., “Diagnostic implications of detection of proteinase K-resistant protein in spleen, lymph nodes, and brain of sheep”,,American Journal of Vet Res.,vol. 53, No. 6, pp. 883-889, 1992.
Baker, et al., “Aminoacid polymorphism in human prion protein and age at death in inherited prion disease,” Lancet, vol. 337, pp. 1286 (1991).
Bessen, et al., “Biochemical and Physical Properties of the Prion Protein from Two Strains of the Transmissible Mink Encephalopathy Agent,” J. Virol., 66(12):2096-2101 (1992).
Bessen, et al., “Distinct PrP Properties Suggest the Molecular Basis of Strain Variation in Transmissible Mink Encephalopathy,” J. Virol., 68(12):7859-7868 (1994).
Bessen, et al., “Non-genetic propagation of strain-specific properties of scrapie prion protein,” Nature, vol. 375, pp. 698-700 (1995).
Brown, et al., “Friendly fire” in medicine: hormones, homografts, and Creutzfeldt-Jakob disease, Lancet, vol. 340, pp. 24-27 (1992).
Brown et al., “Iatrogenic Creutzfeldt-Jakob disease: An example of the interplay between ancient genes and modern medicine” Neurology, vol. 44., pp. 291-293 (1994).
Bruce, et al., “Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier,” Phil. Trans. R. Soc. Lond. B, pp. 405-411 (1994).
Bueler, et al., “Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein,” Nature, vol. 356, pp. 577-582 (1992).
Carlson, et al., “Linkage of Prion Protein and Scrapie Incubation Time Genes,” Cell, vol. 46, pp. 503-511 (1986).
Caughey, et al., “The Scrapie-associated Form of PrP Is Made From a Cell Surface Precursor That is Both Protease- and Phospholipase-sensitive,” J. BioL. Chem., 266(27):18217-18223 (1991).
Collinge, et al., “Genetic predisposition to Iatrogenic Creutzfeldt-Jakob disease,” Lancet, vol. 337., pp. 1441-1442 (1991).
Collinge, et al., “Unaltered susceptibility to BSE in transgenic mice expressing human prion protein,” Nature, vol. 378, pp. 779-783 (1995).
Collinge, et al., “Prion protein gene analysis in new variant cases of Creutzfeldt-Jakob disease,” Lancet, vol. 348, pp. 56 (1996).
Collinge, et al., “Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD,” Nature, vol. 383, pp. 685-690 (1996).
Fraser, et al., “The lymphoreticular system in the pathogenesis of scrapie,” inPrion Diseases in Humans and Animals,Eds. Prusiner, Collinge, Powell, and Anderton, pp. 308-317 (1992).
Heckler, et al., “Replication of distinct scrapie prion isolates is region specific in brains of transgenic mice and hamsters” Genes & Development, vol. 6, pp. 1213-1228 (1992).
Kascsak, et al., “Mouse Polyclonal and Monoclonal Antibody to Scrapie-Associated Fibril Proteins,” J. Virol. 61(12):3688-3693 (1987).
Kimberlin, et al., “Incubation Periods in Six Models of Intraperitoneally Injected Scrapie Depend Mainly on the Dynamics of Agent Replication within the Nervous System and Not the Lymphoreticular System” J. Gen. Virol., vol. 69, pp. 2953-2960 (1988).
Kimberlin, “The role of the spleen in the neuroinvasion of scrapie in mice,” Virus Res., vol. 12, pp. 201-211 (1989).
Kocisko, et al., “Cell-free formation of protease-resistant prion protein,” Nature, vol. 370, pp. 471-474 (1994).
Laemmli, “Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4,” Nature, vol. 227, pp. 680-685 (1970).
Lasmezas, et al., “BSE transmittion to macaques” Nature, (1996), vol. 381, pp. 743-744.
Marsh et al., “Comparison of Scrapie and Transmissible Mink Encephalopathy in Hamsters. II. Clinical Signs, Pathology, and Pathogenesis,” J. of Infectious Diseases, 131(2), pp. 104-110 (1975).
Masood, “Britain draws up ‘superleague’ plan for leading research universities,” p. G, Nature, vol. 382, pp. 381 (1996).
Palmer, et al., “Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease,” Nature, vol. 352, pp. 340-342 (1991).
Palmer, et al., “Sequence Variation in Intron of Prion Protein Gene, Curcial for Complete Diagnostic Strategies,” Human Mutation, vol. 7, pp. 280-281 (1996).
Pan, et al., “Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins,” Proc. Nat. Acad. Sci. USA, vol. 90, pp. 10962-10966 (1993).
Piccardo, et al., “An Antiserum to Residues 95-108 of Human PrP Detects PrPres in a Variety of Human and Animal Prion Diseases,” J. Neuro. Exp. Neurol., vol. 56, pp. 589 (1997) (abstract only).
Pirola, et al., “Inhibition of scrapie-associated PrP accumulation. Probing the role of glycoaminoglycans in amyloidogenesis”, Molecular Neurobiology, 8:113-120 (1994).
Prusiner, et al., “Transgenic Studies Implicate Interactions between Homologous PrP Isoforms in Scrapie Prion Replication,” Cell, vol. 63, pp. 673-686 (1990).
Prusiner, S.B., “Molecular Biology of Prion Diseases,” Science, vol. 252, No. 5012, pp. 1515-1522 (1991).
Schreuder, et al., “Preclinical test for prion disease,” Nature, vol. 381, pp. 563 (1996).
Serban, et al., “Rapid detection of Creutzfeldt-Jakob disease and scrapie prion proteins,” Neurology, vol. 40, pp. 110-117 (1990).
Telling, et al., “Transmission of Creutzfeldt-Jakob disease from humans to transgenic mice expressing chimeric human-mouse prion protein” Proc Natl Acad Sci, vol. 91, pp. 9936-9940 (1994).
Telling, et al., “Prion Propagation in Mice Expressing Human and Chimeric PrP Transgenes Implicates the Interaction of Cellular PrP with Another Protein,” Cell, vol. 83, pp. 79-90 (1995).
Towbin, et al., “Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications,” Proc. Natl. Acad. Sci., 76(9):4350-4354 (1979).
Weissmann, “The prion's progress,” Nature, vol. 349, pp. 569-571 (1991).
Weller, “Iatrogenic transmission of Creutzfeldt-Jakob disease,” Psychol. Med., pp. 1-4 (1989).
Wells, et al., “The Neuropathology and Epidemiology of Bovine Spongiform Encephalopathy,” Brain Pathol., vol. 5, pp. 91-103 (1995).
Whittington, et al., “Rescue of Neurophysiological Phenotype seen in Prp null mice by transgene encoding human prion protein,” Nat. Gene., vol. 9, pp. 197-201 (1995).
Will, et al., “A new variant of Creutzfeldt-Jakob disease in the UK,” Lancet, vol. 347, pp. 921-925 (1996).
Windl, et al., “Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: a systematic analysis of predisposing mutations and allelic variation in the PRNP gene” Hum. Genet., vol. 98,
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Riley Jezia
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