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• W2090889243 abstract "Future Medicinal ChemistryVol. 4, No. 13 EditorialTargeting the cellular prion protein to treat neurodegenerationEmiliano Biasini & David A HarrisEmiliano BiasiniDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USASearch for more papers by this author & David A Harris* Author for correspondenceDepartment of Biochemistry, Boston University School of Medicine, Boston, MA, USA. Search for more papers by this authorEmail the corresponding author at daharris@bu.eduPublished Online:28 Aug 2012https://doi.org/10.4155/fmc.12.114AboutSectionsView ArticleView Full TextPDF/EPUB ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareShare onFacebookTwitterLinkedInRedditEmail View articleKeywords: Alzheimer’s diseasedrugsneurodegenerationpriontherapyReferences1 Prusiner SB. Prions. Proc. Natl Acad. Sci. USA95,13363–13383 (1998).Crossref, Medline, CAS, Google Scholar2 Trevitt CR, Collinge J. A systematic review of prion therapeutics in experimental models. Brain129(Pt 9),2241–2265 (2006).Crossref, Medline, Google Scholar3 Sim VL. Prion disease: chemotherapeutic strategies. Infect. Disord. Drug Targets12(2),144–160 (2012).Crossref, Medline, CAS, Google Scholar4 Collinge J, Gorham M, Hudson F et al. Safety and efficacy of quinacrine in human prion disease (PRION-1 study): a patient-preference trial. Lancet Neurol.8(4),334–344 (2009).Crossref, Medline, CAS, Google Scholar5 Sandberg MK, Al-Doujaily H, Sharps B, Clarke AR, Collinge J. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature470(7335),540–542 (2011).Crossref, Medline, CAS, Google Scholar6 Harris DA, True HL. New insights into prion structure and toxicity. Neuron50(3),353–357 (2006).Crossref, Medline, CAS, Google Scholar7 Brandner S, Isenmann S, Raeber A et al. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature379,339–343 (1996).Crossref, Medline, CAS, Google Scholar8 Mallucci G, Dickinson A, Linehan J, Klohn PC, Brandner S, Collinge J. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science302(5646),871–874 (2003).Crossref, Medline, CAS, Google Scholar9 White MD, Farmer M, Mirabile I, Brandner S, Collinge J, Mallucci GR. Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease. Proc. Natl Acad. Sci. USA105(29),10238–10243 (2008).Crossref, Medline, CAS, Google Scholar10 Biasini E, Turnbaugh JA, Unterberger U, Harris DA. Prion protein at the crossroads of physiology and disease. Trends Neurosci.35(2),92–103 (2012).Crossref, Medline, CAS, Google Scholar11 Poncet-Montange G, St Martin SJ, Bogatova OV, Prusiner SB, Shoichet BK, Ghaemmaghami S. A survey of antiprion compounds reveals the prevalence of non-PrP molecular targets. J. Biol. Chem.286(31),27718–27728 (2011).Crossref, Medline, CAS, Google Scholar12 Kuwata K, Nishida N, Matsumoto T et al. Hot spots in prion protein for pathogenic conversion. Proc. Natl Acad. Sci. USA104(29),11921–11926 (2007).Crossref, Medline, CAS, Google Scholar13 Nicoll AJ, Trevitt CR, Tattum MH et al. Pharmacological chaperone for the structured domain of human prion protein. Proc. Natl Acad. Sci. USA107(41),17610–17615 (2010).Crossref, Medline, CAS, Google Scholar14 Zhang YW, Thompson R, Zhang H, Xu H. APP processing in Alzheimer’s disease. Mol. Brain4,3 (2011).Crossref, Medline, CAS, Google Scholar15 Walsh DM, Selkoe DJ. A beta oligomers – a decade of discovery. J. Neurochem.101(5),1172–1184 (2007).Crossref, Medline, CAS, Google Scholar16 Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature457(7233),1128–1132 (2009).Crossref, Medline, CAS, Google Scholar17 Gimbel DA, Nygaard HB, Coffey EE et al. Memory impairment in transgenic Alzheimer mice requires cellular prion protein. J. Neurosci.30(18),6367–6374 (2010).Crossref, Medline, CAS, Google Scholar18 Freir DB, Nicoll AJ, Klyubin I et al. Interaction between prion protein and toxic amyloid beta assemblies can be therapeutically targeted at multiple sites. Nat. Commun.2,336 (2011).Crossref, Medline, Google Scholar19 Balducci C, Beeg M, Stravalaci M et al. Synthetic amyloid-beta oligomers impair long-term memory independently of cellular prion protein. Proc. Natl Acad. Sci. USA107(5),2295–2300 (2010).Crossref, Medline, CAS, Google Scholar20 Resenberger UK, Harmeier A, Woerner AC et al. The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication. EMBO J.30(10),2057–2070 (2011).Crossref, Medline, CAS, Google ScholarFiguresReferencesRelatedDetailsCited ByPharmacological Agents Targeting the Cellular Prion Protein7 March 2018 | Pathogens, Vol. 7, No. 1Diverse functions of the prion protein – Does proteolytic processing hold the key?Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol. 1864, No. 11Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongationJournal of Biological Chemistry, Vol. 292, No. 41An antipsychotic drug exerts anti-prion effects by altering the localization of the cellular prion protein7 August 2017 | PLOS ONE, Vol. 12, No. 8A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein15 March 2016 | Scientific Reports, Vol. 6, No. 1Decoding the function of the N-terminal tail of the cellular prion protein to inspire novel therapeutic avenues for neurodegenerative diseasesVirus Research, Vol. 207Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration13 March 2013 | FEBS Journal, Vol. 280, No. 18Neurodegenerative diseases: challenges and opportunitiesGregory D Cuny28 August 2012 | Future Medicinal Chemistry, Vol. 4, No. 13 Vol. 4, No. 13 Follow us on social media for the latest updates Metrics Downloaded 461 times History Published online 28 August 2012 Published in print September 2012 Information© Future Science LtdKeywordsAlzheimer’s diseasedrugsneurodegenerationpriontherapyFinancial & competing interests disclosureThe authors have no relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript. This includes employment, consultancies, honoraria, stock ownership or options, expert testimony, grants or patents received or pending, or royalties.No writing assistance was utilized in the production of this manuscript.PDF download" @default.
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