The prionoses and other conformational disorders

References

• Wisniewski T, Ghiso J, Frangione B. Biology of AD amyloid in Alzheimer's disease. Neurobiol Dis 1997; 4: 313–328
   PubMedGoogle Scholar
• Welch W J, Gambetti P. Chaperoning brain diseases. Nature 1998; 392: 23–24
   Google Scholar
• Carrell R W, Lomas D A. Conformational disease. Lancet 1997; 350: 134–138
   PubMed Web of Science ®Google Scholar
• Prusiner S B, Scott M R, DeArmond S J, Cohen F E. Prion protein biology. Cell 1998; 93: 337–348
   PubMed Web of Science ®Google Scholar
• Honvich A L, Weismann J S. Deadly conformations-protein misfolding in prion diseases. Cell 1997; 89: 499–510
   Google Scholar
• Wisniewski T, Frangione B. Molecular biology of brain aging and neurodegenerative disorders. Acta Neurobiol Exp 1996; 56: 267–279
   Google Scholar
• Gordon W S. Advances in veterinary research. Vet Rec 1946; 58: 518–525
   Google Scholar
• Gajdusek D C, Zigas V. Degenerative disease of the central nervous system in New Guinea: the epidemic occurrence of “kuru” in the native population. N Eng J Med 1957; 257: 974–978
   PubMedGoogle Scholar
• Gajdusek D C, Zigas V. Clinical, pathological and epidemiological study of an acute progressive degenerative disease of the central nervous system among natives of the eastern highlands of New Guinea. Am J Med 1959; 26: 442–469
   PubMedGoogle Scholar
• Hadlow W J. Scrapie and kuru. Lancet 1959; 11: 289–290
   Google Scholar
• Gajdusek D C, Gibbs C J, Jr., Alpers M. Experimental transmission of a kuru-like syndrome to chimpanzees. Nature 1966; 209: 794–796
   PubMed Web of Science ®Google Scholar
• Gerstmann J., Straussler E, Scheinker I. Uber eine eigenartige hereditar-familiare erkrankung des zentralnervensystems sugleich ein beitrag zur frage des vorzeitigen lokalen alterns. Z Neurol 1936; 154: 736–762
   Google Scholar
• Ghetti B, Tagliavini F, Giaccone G, Bugiani O, Frangione B, Farlow M R, Dlouhy S R. Familial Gerstmann-Straussler-Scheinker disease with neurofibrillary tangles. Mol Neurobiol 1994; 8: 41–48
   PubMed Web of Science ®Google Scholar
• Ghetti B, Piccardo P, Spillantini M G, Ichimiya Y, Porro M, Perini F, Kitamoto T, Tateishi J, Seiler C, Frangione B, Bugiani O, Giaccone G, Prelli F, Goedert M, Dlouhy S R, Tagliavini F. Vascular variant of prion protein cerebral amyloidosis with t -positive neurofibrillary tangles: The phenotype of the stop codon 145 mutation in PRVP. Proc Natl Acad Sci USA 1996; 93: 744–748
   PubMed Web of Science ®Google Scholar
• Jakob A. Uber eigenaritge erkrankungen des zentral-nervensystems mit bemerkenswertern anatomischen befunde (spastische pseudosklerose-encephalomyelopathie mit disseminierten degenerationsherden). Z Gesamte Neurol Psychiatre 1921; 64: 147–228
   Google Scholar
• Medori R, Trischler H J, LeBlanc A, Villare F, Manetto V, Chen H Y, Xue R, Leal S, Montagna P, Cortelli P, Tinuper P, Avoni P, Mochi M, Baruzzi A, Hauw J J, Ott J, Lugaresi E, Autilio-Gambetti L, Gambetti P. Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene. N Eng J Med 1992; 326: 444–449
   PubMed Web of Science ®Google Scholar
• Goldfarb L G, Petersen M B, Tabaton M, Brown P, LeBlanc A C, Montagna P, Cortelli P, Julien J, Vital C, Pendelbury W W, Haltia M, Wills P R, Hauw J J, McKeever P E, Monari L, Schrank B, Swergold G D, Autilio-Gambetti L, Gajdusek D C, Lugaresi E, Gambetti P. Fatal familial insomnia and familial Creutzfeldt-Jacob disease: disease phenotype determined by a DNA polymorphism. Science 1992; 258: 806–808
   PubMed Web of Science ®Google Scholar
• Collinge J. Human prion diseases and bovine spongiform encephalopathy (BSE). Hum Mol Genet 1997; 6: 1699–1705
   PubMedGoogle Scholar
• Collinge J, Sidle K CL, Meads J, Ironside J, Hill A F. Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature 1996; 383: 685–690
   PubMed Web of Science ®Google Scholar
• Bateman D, Hilton D, Love S, Zeidler M, Beck J, Collinge J. Sporadic Creutzfeldt-Jakob disease in a 18-year old in the UK. Lancet 1995; 346: 1155–1156
   Google Scholar
• Britton T C, Al-Sarraj S, Shaw C, Campbell T, Collinge J. Sporadic Creutzfeldt-Jakob disease in a 16-year old in the UK. Lancet 1995; 346: 1155
   PubMedGoogle Scholar
• Collee J G, Bradley R. BSE: a decade on. Lancet 1997; 349: 636–641
   PubMed Web of Science ®Google Scholar
• Will R G, Ironside J, Zeidler M, Cousens S N, Estibeiro K, Alperovitch A, Poser S, Pocchiari M, Hofman A, Smith P G. A new variant of Creutzfeldt-Jacob disease in the UK. Lancet 1997; 347: 921–925
   Google Scholar
• Griffith J S. Self-replication and scrapie. Nature 1967; 215: 1043–1044
   PubMed Web of Science ®Google Scholar
• Prusiner S B. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216: 136–144
   PubMed Web of Science ®Google Scholar
• Weissmann C. Molecular biology of transmissible spongiform encephalopathies. FEES Lett 1996; 389: 3–11
   PubMed Web of Science ®Google Scholar
• Alper T, Cramp W A, Haig D A, Clarke M C. Does the agent of scrapie replicate without nucleic acid?. Nature 1967; 214: 764–766
   PubMed Web of Science ®Google Scholar
• Latarjet R, Muel B, Haig D A, Clarke M C, Alper T. Inactivation of the scrapie agent by near monchromatic ultraviolet light. Nature 1970; 227: 1341–1443
   PubMedGoogle Scholar
• Merz P A, Sornerville R, Wisniewski H M, Iqbal K. Abnormal fibrils from scrapie-infected brain. Acta Neuropathol 1981; 54: 63–74
   PubMed Web of Science ®Google Scholar
• Pan K M, Baldwin M, Njuyen J, Gassett M, Serban A, Groth D, Mehlhorn I, Prusiner S B. Conversion of alpha-helices into β-sheets features in the formation of scrapie prion poteins. Proc Natl Acad Sci (USA) 1993; 90: 10962–10966
   PubMed Web of Science ®Google Scholar
• Caughey B, Raymond G J, Kocisko D A, Lansbury P T, Jr. Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies. J Virol 1997; 71: 4107–4110
   PubMed Web of Science ®Google Scholar
• Safar J, Roller P P, Gajdusek D C, Gibbs C J, Jr. Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlates with infectivity. Protein Sci 1993; 2: 2206–2216
   PubMed Web of Science ®Google Scholar
• Collinge J, Sidle K CL, Meads J, Ironside J, Hill A F. Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature 1996; 383: 685–690
   PubMed Web of Science ®Google Scholar
• Liao Y CJ, Lebo R V, Clawson G A, Smuckler E A. Human prion protein cDNA: molecular cloning, chromosomal mapping and biological implications. Science 1986; 233: 364–367
   PubMed Web of Science ®Google Scholar
• Oesch B, Westaway D, Walchli M, McKinley M P, Kent S BH, Aebersold R, Barry R A, Tempst P, Teplow D B, Hood L, Prusiner S B, Weissman C. A cellular gene encodes scrapie PrP 27–30 protein. Cell 1985; 40: 735–746
   PubMed Web of Science ®Google Scholar
• Kretzschmar H, Prusiner S B, Stowring L E, DeArmond S J. Scrapie prion protein are synthesized in neurons. Am J Pathol 1986; 122: 1–5
   PubMed Web of Science ®Google Scholar
• Chesebro B, Race R, Wehrly K, Nishio J, Bloom M, Lechner D, Bergstrom S, Robbins K, Mayer L, Keith J M. Identification of scrapie prion protein-specific mRNA in scrapie infected and uninfected brain. Nature 1985; 315: 331–333
   PubMed Web of Science ®Google Scholar
• Taraboulos A, Raeber A, Borchelt D R, Serban D, Prusiner S B. Synthesis and trafficking of prion proteins in cultured cells. Mol Biol Cell 1992; 3: 851–863
   PubMed Web of Science ®Google Scholar
• Shyng S L, Huber M T, Harris D A. A prion protein cycles between the cell surface and endocytic compartment in cultured neuroblastoma cells. J Biol Chem 1993; 268: 15922–15928
   PubMed Web of Science ®Google Scholar
• Harris D A, Huber M T, Vankijken P, Shyng S L, Chait B T, Wang R. Processing of a cellular prion protein: identification of N-terminal and C-terminal cleavage sites. Biochem 1993; 32: 1009–1016
   PubMedGoogle Scholar
• Kitamoto T, Iizuka T, Tateishi J. An amber mutation of prion protein in Gerstmann-Straussler syndrome with mutant PrP plaques. Biochem Biophys Res Commun 1993; 192: 525–531
   PubMed Web of Science ®Google Scholar
• Dlouhy S, Hsiao K, Farlow M, Foroud T, Conneally P M, Johnson P, Prusiner S B, Hodes M E, Ghetti B. Linkage of the Indiana kindred of Gertmann-Straussler Scheinker disease to the prion protein gene. Nat Genet 1992; 1: 64–67
   PubMed Web of Science ®Google Scholar
• Hsiao K K, Dlouhy S, Farlow M, Cass C, DaCosta M, Conneally P M, Hodes M E, Ghetti B, Prusiner S B. Mutant prion proteins in Gerstmann-Straussler-Scheinker disease with neurofibrillary tangles. Nature Genet 1992; 1: 68–71
   PubMed Web of Science ®Google Scholar
• Bueler H, Fischer M, Lang Y, Bluethmann H, Lipp H P, DeArmond S J, Prusiner S B, Aguet M, Weismann J S. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992; 356: 577–582
   PubMed Web of Science ®Google Scholar
• Manson J C, Clarke A R, Hooper M L, Aitchison L, McConnell I, Hope J. 129/01a mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 1994; 8: 121–127
   PubMed Web of Science ®Google Scholar
• Tobler I, Gaus S E, Deboer T, Achermann P, Fischer M, Rulicke T, Moser M, Oesch B, McBride P A, Manson J C. Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 1996; 380: 639–642
   PubMed Web of Science ®Google Scholar
• Collinge J, Whittington M A, Sidle K C, Smith C J, Palmer M S, Clarke A R, Jefferys J GR. Prion protein is necessary for normal synaptic function. Nature 1994; 370: 295–297
   PubMed Web of Science ®Google Scholar
• Liedo P M, Tremblay P, DeArmond S J, Prusiner S B, Nicoll R A. Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc Natl Acad Sci (USA) 1996; 93: 2403–2407
   Google Scholar
• Sakaguchi S, Katamine S, Nishida N, Moriuchi R, Shigematsu K., Sugimoto T, Nakatani A, Kataoka Y, Houtani T, Shirabe S. Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 1996; 380: 528–531
   PubMed Web of Science ®Google Scholar
• Bueler H, Aguzzi A, Sailer A, Greiner R A, Autenried P, Aguet M, Weissmann C. Mice devoid of PrP are resistant to scrapie. Cell 1993; 73: 1339–1347
   PubMed Web of Science ®Google Scholar
• Prusiner S B, Groth D, Serban A, Koehler R, Foster D, Torchia M, Burton D, Yang S L, DeArmond S J. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc Natl Acad Sci (USA) 1993; 90: 10608–10612
   PubMed Web of Science ®Google Scholar
• Telling G C, Haga T, Torchia M, Tremblay P, DeArmond S J, Prusiner S B. Interactions between wild-type and mutant prion proteins modulate neurodegeneration transgenic mice. Genes Dev 1996; 10: 1736–1750
   PubMed Web of Science ®Google Scholar
• Hsiao K, Groth D, Scott M, Yang S L, Serban H, Rapp D, Foster D, Torchia M, DeArmond S J, Prusiner S B. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc Natl Acad Sci (USA) 1994; 91: 9126–9130
   PubMed Web of Science ®Google Scholar
• Liberski P P. Prions, β-sheets and transmissible dementias: is there still something missing?. Acta Neuropathol 1995; 90: 113–125
   Google Scholar
• Bessen R A, Marsh R F. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 1992; 66: 2096–2101
   PubMed Web of Science ®Google Scholar
• Bessen R A, Marsh R F. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 1994; 68: 7859–7868
   PubMed Web of Science ®Google Scholar
• Parchi P, Castellani R, Capellari S, Ghetti B, Young K, Chen S G, Farlow M, Dickson D W, Sima A AF, Trojanowski J Q, Petersen R B, Gambetti P. Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jacob disease. Ann Neurol 1996; 39: 767–778
   PubMed Web of Science ®Google Scholar
• Parchi P, Capellari S, Chen S G, Petersen R B, Gambetti P, Kopp N., Brown P, Kitamoto T, Tateishi J, Giese A, Kretzschmar H. Typing prion isoforms. Nature 1997; 386: 232–233
   PubMed Web of Science ®Google Scholar
• Lasmezas C I, Deslys J P, Demaimay R, Adjou K T, Lamoury F, Dormont D, Robain O, Omside J, Hauw J J. BSE transmission to macaques. Nature 1996; 381: 743–744
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Frangione B. Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci Lett 1992; 135: 235–238
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Lalowski M, Golabek A A, Vogel T, Frangione B. Is Alzheimer's disease an apolipoprotein E amyloidosis?. Lancet 1995; 345: 956–958
   PubMed Web of Science ®Google Scholar
• Soto C, Golabek A A, Wisniewski T, Castaiio E M. Alzheimer's soluble P-amyloid is conformationally modified by apolipoproteins in vitro. Neuroreport 1996; 7: 721–725
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Golabek A A, Matsubara E, Ghiso J, Frangione B. Apolipoprotein E: binding to soluble Alzheimer's beta-amyloid. Biochem Biophys Res Commun 1993; 192: 359–365
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Castatio E M, Golabek A A, Vogel T, Frangione B. Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am J Pathol 1994; 145: 1030–1035
   PubMed Web of Science ®Google Scholar
• Corder E H, Saunders A M, Strittmatter W J, Schmechel D E, Gaskell P C, Small G W, Roses A D, Haines J L, Pericak-Vance M A. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 1993; 261: 921–923
   PubMed Web of Science ®Google Scholar
• Strittmatter W J, Saunders A M, Schmechel D, Pericak-Vance M, Enghild J, Salvesen G S, Roses A D. Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc Natl Acad Sci (USA) 1993; 90: 1977–1981
   PubMed Web of Science ®Google Scholar
• Bales K R, Verina T, Dodel R C, Du Y S, Altsti L., el Bender M, Hyslop P, Johnstone E M, Little S P, Cummins D J, Piccardo P, Ghetti B, Paul S M. Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition. Nature Gen 1997; 17: 263–264
   PubMed Web of Science ®Google Scholar
• Tatzelt J, Maeda N, Pekny M, Yang S L, Betsholtz C, Eliasson C, Cayetano J, Camerino A P, DeArmond S J, Prusiner S B. Scrapie in mice deficient in apolipoprotein E or glial fibrillary acidic protein. Neurol 1996; 47: 449–453
   Google Scholar
• Telling G C, Scott M, Hsiao K K, Foster D, Yang S C, Torchia M, Sidla K CL, Collinge J, DeArmond S J, Prusiner S B. Transmission to Creutzfeldt-Jacob disease from human to transgenic mice expressing chimeric human-mouse prion protein. Proc Natl Acad Sci (USA) 1994; 91: 9936–9940
   PubMed Web of Science ®Google Scholar
• Telling G C, Scott M, Mastrianni J., Gabizon R, Torchia M, Cohen F E, DeArmond S J, Prusiner S B. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995; 83: 79–90
   PubMed Web of Science ®Google Scholar
• Caughey B, Race R E. Potent inhibition of scrapie associated PrP accumulation by Congo Red. J Neurochem 1992; 59: 768–771
   PubMed Web of Science ®Google Scholar
• Tagliavini F, McArthur R A, Canciani B, Giaccone G, Porro M., Bugiani M, Lievens P M, Bugiani O, Peri 'Dall E., Ara P, Rocchi M, Poli G, Forloni G, Bandiera T, Varasi M, Suarato A, Cassutti P, Cervini M A, Lansen J, Salmona M, Post C. Effectiveness of anthracycline against experimental prion disease in Syrian hamsters. Science 1997; 276: 1119–1122
   PubMed Web of Science ®Google Scholar
• Kim C A, Berg J M. Thermodynamic beta-sheet properties measured using a zinc-finger host peptide. Nature 1993; 362: 267–270
   PubMed Web of Science ®Google Scholar
• Wouters M A, Curmi P MG. An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen bonded residue pairs. Protein Sci 1994; 2: 43
   Google Scholar
• Wetzel R. Mutations and off-pathway aggregation of proteins. Trends Biotechnol 1994; 12: 193–198
   PubMed Web of Science ®Google Scholar
• Soto C, Kindy M, Baumann S. M, Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent β-sheet conformation. Biochem Biophys Res Commun 1996; 226: 672–680
   PubMed Web of Science ®Google Scholar
• Soto C, Sigurdsson E, Morelli M., Kumar L. A., Castatio E M, Frangione B. β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: potential Alzheimer's therapy. Nat Med 1998; 4: 822–826
   PubMed Web of Science ®Google Scholar
• Bukau B, Horwich A L. The Hsp70 and Hsp60 chaperone machine. Cell 1998; 92: 351–366
   PubMed Web of Science ®Google Scholar
• Anfinsen C B. Principles that govern the folding of protein chains. Science 1973; 181: 223–230
   PubMed Web of Science ®Google Scholar
• Lindquist S. Mad cows meet Psi-chotic yeast: the expansion of the prion hypothesis. Cell 1997; 89: 495–498
   PubMed Web of Science ®Google Scholar
• Coustou V, Deleu C, Saupe S, Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci (USA) 1997; 94: 9773–9778
   PubMed Web of Science ®Google Scholar
• Levy E, Carman M D, Fernandez-Madrid I, Lieberburg I, Power M D, vanDuinen S G, Bots G TAM, Luyendijk W, Frangione B. Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science 1990; 248: 1124–1126
   PubMed Web of Science ®Google Scholar
• Wisniewski T, Ghiso J, Frangione B. Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation. Biochem Biophys Res Commun 1991; 179: 1247–1254
   PubMed Web of Science ®Google Scholar
• Clements A, Walsh D M, Williams C H, Allsop D. Effects of the mutation Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid β/A4 peptide. Neurosci Lett 1993; 161: 17–20
   PubMed Web of Science ®Google Scholar
• Castaño E M, Prelli F, Wisniewski T, Golabek A A, Kumar R A, Soto C, Frangione B. Fibrillogenesis in Alzheimer's disease of amyloid beta peptides and apolipoprotein E. Biochem J 1995; 306: 599–604
   PubMed Web of Science ®Google Scholar
• Prelli F, Levy E, Van Duinen S G, Bots G T, Luyendijk W, Frangione B. Expression of a normal and variant Alzheimer's beta-protein in amyloid of hereditary cerebral hemorrhage, Dutch type: DNA and protein diagnostic assays. Biochem Biophys Res Commun 1990; 170: 301–307
   Google Scholar
• Collinge J, Palmer M S, Dryden A J. Genetic predisposition to iatrogenic Creutzfeldt-Jacob disease. Lancet 1991; 337: 1441–1442
   PubMed Web of Science ®Google Scholar
• Miyazono M, Kitamoto T, Doh-Ura K, Iwaki T, Tateishi J. Creutzfeldt-Jacob disease with codon 129 polymorphism (valine): a compartive study of patients with codon 129 point mutation or without mutations. Acta Neuropathol 1992; 84: 349–354
   Google Scholar
• Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wuthrich K. NMR structure of the mouse prion protein domain PrP(121–231). Nature 1996; 382: 180–182
   PubMed Web of Science ®Google Scholar
• Billeter M, Riek R, Wider G, Hornemann S, Glockshuber R, Wiithrich K. Prion protein NMR structure and species barrier for prion diseases. Proc Natl Acad Sci USA 1997; 94: 7281–7285
   PubMed Web of Science ®Google Scholar
• Riek R, Hornemann S, Wider G, Glockshuber R, Wuthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23–231). FEBS Lett 1997; 413: 282–288
   PubMed Web of Science ®Google Scholar
• Goldfarb L, Brown P, McCombie W R, Goldgaber D, Swergold G D, Wills P R, Cervenakova L, Baron H, Gibbs C J, Jr., Gajdusek D C. Transmissible familial Creutzfeldt-Jacob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene. Proc Natl Acad Sci (USA) 1991; 88: 10926–10930
   PubMed Web of Science ®Google Scholar
• Owen F, Poulter M, Lofthouse R, Collinge J, Crow T J, Risby D, Baker H F, Ridley R M, Hsiao K, Prusiner S B. Insertion in prion protein gene in familial Creutzfeldt-Jacob disease. Lancet 1989; 1: 51–52
   PubMed Web of Science ®Google Scholar
• Owen F, Poulter M, Shah T, Collinge J, Lofthouse R, Baker H F, Ridley R M, McVey J, Crow T J. An in-frame insertion in the prion protein gene in familial Creutzfeldt-Jacob disease. Mol Brain Res 1990; 7: 273–276
   PubMedGoogle Scholar
• Hsiao K, Baker H F, Crow T J, Poulter M, Owen F, Terwilliger J D, Westaway D, Ott J, Prusiner S B. Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 1989; 338: 342–345
   PubMed Web of Science ®Google Scholar
• Goldfarb L G, Brown P, Goldgaber D, Asher D M, Rubenstein R, Brown W T, Piccardo P, Kascsak R J, Boellaard J W, Gajdusek D C. Creutzfeldt-Jakob disease and kuru patients lack a mutation consistently found in the Gerstmann-Straussler-Scheinker syndrome. Ekp Neurol 1990; 108: 247–250
   Google Scholar
• Goldgaber D, Goldfarb L G, Brown P, Asher D M, Brown W T, Lin S, Teener J W, Feinstone S M, Rubenstein R, Kascsak R J, et al. Mutations in familial Creutzfeldt-Jakob disease and Gerstmann-Straussler-Scheinker's syndrome. Exp Neurol 1989; 106: 204–206
   PubMed Web of Science ®Google Scholar
• Kitamoto T, Ohta M, Doh-Ura K, Hitoshi S, Terao Y, Tateishi J. Novel missense variants of prion protein in Creutzfeldt-Jacob disease or Gerstmann-Straussler syndrome. Biochem Biophys Res Commun 1993; 191: 709–714
   PubMed Web of Science ®Google Scholar
• Hsiao K, Doh-Ura K, Kitamoto T, Tateishi J, Prusiner S B. A prion protein amino acid substitution in ataxic Gerstmann-Straussler syndrome. Ann Neurol 1989; 26: 137
   Google Scholar
• Nochlin D, Sumi M, Bird T, Snow A D, Leventhal C M, Beyreuther K, Masters C L. Familial dementia with PrP-positive amyloid plaques: a variant of Gerstmann-Straussler syndrome. Neurol 1989; 39: 910–918
   PubMed Web of Science ®Google Scholar
• Goldfarb L, Brown P, Haltia M, Cathala F, McCombie W R, Kovanen J, Cervenakova L, Goldin L, Nieto A, Godec M S, Asher D M, Gajdusek D C. Creutzfeldt-Jacob disease cosegregates with the codon 178Asn PRNP mutation in families of European origin. Ann Neurol 1992; 31: 274–281
   PubMed Web of Science ®Google Scholar
• Gabizon R, Meiner Z, Cass C, Kahana I, Avrahami D, Abramsky O, Scarlato G, Prusiner S B, Hsiao K. Prion protein gene mutation in Libyan Jews with Creutzfeldt-Jabob disease. Neurol 1991; 41: 160
   Google Scholar
• Goldfarb L, Haltia M, Brown P, Nieto A, Kovanen J, McCombie W R, Trapp S, Gajdusek D C. New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jacob kindred. Lancet 1991; 337: 425
   PubMed Web of Science ®Google Scholar
• Goldfarb L, Mitrova E, Brown P, Toh B H, Gajdusek D C. Mutation in codon 200 of scrapie amyloid gene in two clusters of Creuzfeldt-Jacob disease in Slovakia. Lancet 1990; 336: 514–515
   PubMed Web of Science ®Google Scholar
• Hsiao K, Meiner Z, Kahana E, Cass C, Kahana I, Avrahami D, Scarlato G, Abramsky O, Prusiner S B, Gabizon R. Mutation of the prion protein in Libyan Jews with Creutzfeldt-Jacob disease. N Eng J Med 1991; 324: 1091–1097
   PubMed Web of Science ®Google Scholar
• Ripoll L, Laplanche J L, Salzmann M, Jouvet A, Planques B, Dussaucy M, Chatelain J, Beaudry P, Launay J M. A new point mutation in the prion protein gene at codon 210 in Creutzfeldt-Jacob disease. Neurol 1993; 43: 1934–1938
   PubMedGoogle Scholar
• Kascsak R J, Rubenstein R, Merz P A, Tonna-DeMasi M, Fersko R, Carp R I, Wisniewski H M, Diringer H. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol 1987; 61: 3688–3693
   PubMed Web of Science ®Google Scholar