15
Views
4
CrossRef citations to date
0
Altmetric
Review

Therapeutic possibilities in CJD: patents 1996 - 1999

Pages 49-57 | Published online: 25 Feb 2005

Bibliography

  • WILL RG, IRONSIDE JW, ZEIDLER M et al.: A new variant of Creutzfeldt-Jakob disease in the UK. Lancet (1996) 347:921–925.
  • ••The original description of vCJD.
  • KNIGHT R: The relationship between new variant Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Vox Sang (1999) 76:203–208.
  • •A review of the evidence that BSE in diet is the cause of vCJD.
  • PRUSINER SB: An introduction to prion biology and diseases. In: Prion Biology and Diseases. Prusiner SB (Ed.), Cold Spring Harbour Laboratory Press, New York (1999):1–66.
  • •A good introduction to prion disease and the prion concept.
  • WILL RG, ALPERS MP, DORMONT D, SCHONBERGER LB, TATEISHI J: Infectious and sporadic prion diseases. In: Prion Biology and Diseases. Prusiner SB (Ed.), Cold Spring Harbour Laboratory Press, New York (1999):465–507.
  • ••A thorough, up-to-date review of acquired and sporadichuman prion disease.
  • GAMBETTI P, PETERSEN RB, PARCHI P et al.: Inherited prion diseases. In: Prion Biology and Diseases. Prusiner SB (Ed.), Cold Spring Harbour Laboratory Press, New York (1999):509–583.
  • •A comprehensive review of genetic aspects of human prion disease.
  • BROWN P, PREECE MA, WILL RG: 'Friendly fire' in medicine: hormones, homografts, and Creutzfeldt-Jakob disease. Lancet (1992) 340:24–27.
  • IRONSIDE JW, BELL JE: Pathology of prion diseases. In: Prion Diseases. Collinge J, Palmer MS (Eds.) Oxford Univer-sity Press, Oxford (1997):57–88.
  • PALMER S, COLLINGE J: Prion diseases: an introduction. In: Prion Diseases. Collinge J, Palmer MS (Eds.) Oxford University Press, Oxford (1997):1–17.
  • BeELER H, AGUZZI A, SAILER A et al.: Mice devoid of PrP are resistant to scrapie. Cell (1993) 73:1339–1347.
  • •An important result indicating the pivotal role of PrP in prion disease.
  • WESTAWAY D, DEARMOND SJ, CAYETANO-CANLAS J et al.: Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type proteins. Cell (1994) 76(0:117–129.
  • BeELER H, FISCHER M, LANG Y et al: Normal develop-ment and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature (1992) 356:577–582 .
  • MANSON JC, CLARKE AR, HOOPER ML, AITCHISON L, MCCONNELL I, HOPE J: 129/ola mice carrying a null mutation in PrP that abolishes mrna production are developmentally normal. Mol. Biol. (1994) 8:121–127.
  • COLLING SB, COLLINGE J, JEFFERYS JG: Hippocampal slices from prion protein null mice: disrupted Ca(2F)activated K± currents. Neurosci. Lett. (1996) 209(1)49–52.
  • TOBLER I, GAUSS SE, DEBOER T et al.: Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature (1996) 380(6575):639–642.
  • COLLINGE J, WHITTINGTON MA, SIDLE KCL et al: Prion protein is necessary for normal synaptic function. Nature (1994) 370:295–297.
  • HERMS JW, KRETZSCHMAR HA, TITZ S, KLLER BU: Patch-clamp analysis of synaptic transmission to cerebellar Purkinje cells of prion protein knockout mice. Eur. Neurosci. (1995) 7:2508–2512.
  • LLEDO P-M, TREMBLAY P, DEARMOND SJ, PRUSINER SB, NICOLL RA: Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmis-sion in the hippocampus. Proc. Natl. Acad. Sci. (1996) 93:2403–2407.
  • TREMBLAY P, MEINER Z, GALOU M et al: Doxycyclinecontrol of prion protein transgene expression modulates prion disease in mice. Proc. Natl. Acad. Sci. USA (1998) 13:12580–12585.
  • SAKAGUCHI S, KATAMINE S, NISHIDA N et al: Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature (1996) 380:528–531.
  • MOORE R: Gene targeting studies at the mouse prion protein locus. PhD Thesis, University of Edinburgh, Edinburgh (1997).
  • MOORE R C, LEE I Y, SILVERMAN G L et al. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J. Mol. Biol. (1999) 292:797–817.
  • ••An important review of PrPM mice models and a discussionof the possible role of Dpl protein in prion disease.
  • BROWN DR, QIN K, HERMS JW et al: The cellular prion protein binds copper in vivo. Nature (1997) 390:684–687.
  • BROWN DR, WONG B-S, HAFIZ F, CLIVE C, HASWELL SJ, JONES IM: Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. (1999) 344:1–5.
  • ••Evidence for a direct role of PrP in cellular resistance to oxidative stress.
  • BROWN DR, SCHMIDT B, KRETZSCHMAR HA: Effects of copper on survival of prion protein knockout neurons and glia. j Neurochem. (1998) 70:1686–1693.
  • PAULY PC, HARRIS DA: Copper stimulates endocytosis of the prion protein. J. Biol. Chem. (1998) 273:33107–33110.
  • MCKENZIE D, BARTZ J, MIRWALD J, OLADER D, MARSH R,AIKEN J: Reversibility of scrapie inactivation is enhanced by copper. J. Biol. Chem. (1998) 273:25545–25547.
  • BROWN DR, BESINGER A: Prion protein expression andsuperoxide dismutase activity. Biochem. J. (1998) 334:423–429.
  • BROWN DR, MOHN CM: Astrocytic glutamate uptake and prion protein expression. Glia (1999) 25:282–292.
  • BROWN DR, SCHMIDT B, KRETZSCHMAR HA: Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature (1996) 380:345–347.
  • BROWN DR: Prion protein-overexpressing cells show altered response to a neurotoxic prion protein peptide. J. Neurosci. Res. (1998) 54:331–340.
  • BROWN DR: Prion Protein peptide neurotoxicity can be mediated by astrocytes. J. Neurochem. (1999) 73:1105–1113.
  • KUNZ B, SANDMEIER E, CHRISTEN P: Neurotoxicity of prion peptide 106-126 not confirmed. FEBS Lett. (1999) 458:65–68.
  • STEWART GE, STOCKMAN PK: New variant Creutzfeldt- Jakob disease and the risk of blood transfusion. Proc. R. Coll. Physicians Edinb. (1999) 29:232–235.
  • BRANDNER S, ISENMANN S, RAEBER A et al.: Normal host prion protein necessary for scrapie-induced neurotoxicty. Nature (1996) 379:339–343.
  • PROUT KA, LARNER AJ: Emerging therapeutic possibili-ties in prion diseases: patents 1993-1998. Exp. Opin. Ther. Patents (1998) 8(9) :1099–1108.
  • •A previous review of therapeutic patents in the prion disease area.
  • WILL RG, KIMBERLIN RH: Creuztfeldt-Jakob disease and the risk from blood or blood products. Vox Sang (1998) 75:178–180.
  • ••A comprehensive review of the potential risk of CJD fromblood and blood products. WILL RG, KIMBERLIN RH: Creuztfeldt-Jakob disease and the risk from blood or blood products. Vox Sang (1998) 75:178-180. A comprehensive review of the potential risk of CJD from blood and blood products.
  • KORTH C, STIERLI B, STREIT P et al.: Prion(PrPs)-specific epitope defined by a monoclonal antibody. Nature (1997) 390:74–77.
  • SANDERS WL, DUNN TL: Creutzfeldt-Jakob diseasetreated with amantadine. A report of two cases. J. Neurol Neurosurg. Psych. (1973) 36:581–584.
  • POCCHIARI M, SALVATORE M, LADOGANA A et al.: Experimental drug treatment of scrapie: a pathoge-netic basis for rationale therapeutics. Euro. J. Epidemiol. (1991) 7:556–561.
  • •A review of the theoretical background to possible treatment strategies in prion disease.
  • MCKENZIE D, KACZKOWSKI J, MARSH R, AIKEN J: Amphotericin B delays both Scrapie agent replication and PrP-res accumulation early in infection. J. Virol. (1994) 68:7534–7536.
  • MASULLO C, MACCHI G, Xi YG, POCCHIARI M: Failure toameliorate Creutzfeldt-Jakob disease with amphotericin B therapy. J. Infect. Dis. (1992) 165:784–785.
  • MANUELIDIS L, FRITCH W, ZAITSEV I: Dapsone to delaysymptoms in Creutzfeldt-Jakob disease. Lancet (1998) 352:456.
  • GADJOU KT, DEMAIMAY R, LASMÉZAS CI, SEMAN M, DESLYS J-P, DORMONT D: Differential effects of a new amphotericin B derivative, MS-8209, on mouse BSE and scrapie: implications for the mechanism of action of polyene antibiotics. Res. Vim]: (1996) 147:213–218.
  • XI YG, INGROSSO L, LAGONDA A, MASULLO C, POCCHIARI M: Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumu-lation. Nature (1992) 356:598–601.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.