Bibliography
- ABRAHAM CR: Amyloid 13 peptide: a century of discoveries. Int. j Chh. Invest. (2000) 7:7–9.
- GLENNER GG, WONG CW: Alzheimer's disease and Down's syndrome: sharing a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. (1984) 122:1131–1135.
- SELKOE DJ: Amyloid I3-protein and the genetics of Alzheimer's disease. j Biol. Chem. (1996) 271:18295–18298.
- ••Comprehensive description of the amyloidhypothesis and data supporting it.
- THORSETT ED, LATIMER LH: Therapeutic approaches to Alzheimer's disease. Curr. Opin. Chem. Biol. (2000) 4:377–382.
- ••Potential treatments for AD.
- JHEE S, SHIOVITZ T, CRAWFORD AW, CUTLER NR: I3-Amyloid therapies in Alzheimer's disease. Expert Opin. Investig. Drugs (2001) 10(4):593–605.
- ••Basic general survey of the AD treatmentapproaches related to amyloid peptide.
- SAIDO TC: Degradation of amyloid-I3 peptide: a key to Alzheimer pathogenesis, prevention and therapy. Neurosci. News (2000) 3:52–62.
- SEO J, KIM S, KIM H et al.: Effects of nicotine on APP secretion and A13- or CT(105)-induced toxicity. Biol. Psychiatry (2001) 49:240–247.
- SELKOE DJ: Translating cell biology into therapeutic advances in Alzheimer's disease. Nature (1999) 399(6738 Suppl.):A23–31.
- LAHIRI DK, GE YW, FARLOW MR: Effect of a memory-enhancing drug, AIT-082, on the level of synaptophysin. Ann. N Y Acad. Li. (2000) 903:387–393.
- OPAZO C, RUIZ FH, INESTROSA NC: Amyloid-13-peptide reduces copper (II) to copper (I) independent of its aggregation state. Biol. Res. (2000) 33:125–131.
- HOWLETT DR, SIMMONS DL, DINGWALL C, CHRISTIE G: In search of an enzyme: the I3-secretase of Alzheimer's disease is an aspartic proteinase. Trends Neurosci. (2000) 23:565–570.
- FARZAN M, SCHNITZLER CE, VASILIEVA N, LEUNG D, CHOE H: BACE2, a I3-secretase homolog, cleaves at the 13 site and within the amyloid-I3 region of the amyloid-I3 precursor protein. Proc. Nati Acad. Sci. USA (2000) 97:9712–9717.
- GHOSH AK, SHIN D, DOWNS D et al.: Design of potent inhibitors for human brain memapsin 2 (I3-secretase). j Am. Chem. Soc. (2000) 122:3522–3523.
- HONG L, KOELSCH G, LIN X etal. Structure of the protease domain of memapsin 2 (I3-secretase) complexed with inhibitor. Science (2000) 290:150–153.
- GHOSH AK, BILCER G, HARWOOD C et al.: Structure-based design: potent inhibitors for human brain memapsin 2 (p-secretase). J Med. Chem. (2001) 44:2865–2868.
- OLSON RE, THOMPSON LA: Secretase inhibitors as therapeutics for Alzheimer's disease. In: Ann. Reports Med. Chem. (2000) 35(Chap. 4):31–40.
- •General survey of secretases inhibitors as potential treatment for AD.
- DE STROOPER B, SAFTIG P, CRAESSAERTS K et al.: Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature (1998) 391:387–390.
- WOLFE MS, XIA W, OSTASZEWSKI BL, DIEHL TS, KIMBERLY WT, SELKOE DJ: Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and y-secretase activity. Nature (1999) 398:513–517.
- CITRON M, WESTAWAY D, XIA W et al.: Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid I3-protein in both transfected cells and transgenic mice. Nat. Med. (1997) 3:67–72
- YU G, NISHIMURA M, ARAWAKA S et al.: Nicastrin modulates presenilin-mediated notch/g1p-1 signal transduction and I3APP processing. Nature (2000) 407:48–54.
- SCHENK D: A partner for presenilin. Nature (2000) 407:34–35.
- ••Hypothesis of the cleavage of APP byy-secretase.
- HADLAND BK, MANLEY NR, SU D et al.: y-secretase inhibitors repress thymocyte development. Proc. Nati Acad. Li. USA (2001) 98:7487–7491.
- •Potential side effects of ysecretase inhibition.
- KOZLOWSKI MR, SPANOYANNIS A, MANLY SP, FIDEL SA, NEVE RL: The neurotoxic carboxy-terminal fragment of the Alzheimer amyloid precursor binds specifically to a neuronal cell surface molecule: pH dependence of the neurotoxicity and the binding. j Neurosci. (1992) 12:1679–1687.
- HIGAKI JN, CHAKRAVARTY S, BRYANT CM et al.: A combinatorial approach to the identification of dipeptide aldehyde inhibitors of 13-amyloid production. j Med. Chem. (1999) 42:3889–3898.
- ••Application of combinatorial techniques tomedicinal chemistry.
- WOLFE MS, CITRON M DIEHL TS et al.: A substrate-based difluoroketone selectively inhibits Alzheimer's y-secretase activity. I Med. Chem. (1998) 41:6–9.
- SHEARMAN MS, BEHER D, CLARKE EE et al.: L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid I3-protein precursor y-secretase activity. Biochemistry (2000) 39:8698–8704.
- •Interactions enzyme/inhibitor.
- DOVEY HF, JOHN V, ANDERSON JP et al.: Functional y-secretase inhibitors reduce 13-amyloid peptide levels in brain. Neurochem. (2001) 76:173–181.
- •First demonstrated reduction of brain Ap in vivo.
- LANSBURY PT: Evolution of amyloid: what normal protein folding may tell us about flbrillogenesis and disease. Proc. Nati Acad. Sci. USA (1999) 96:3342–3344
- ALLAIN H, BENTUE-FERRER D, ZEKRI O, SCHUCK S, LEBRETON S, REYMANN JM: Experimental and clinical methods in the development of anti-Alzheimer drugs. Fundam. Gun. Pharmacol. (1998) 12:13–29.
- GEULA C, WU CK, SAROFF D, LORENZO A, YUAN M, YANKNER BA: Aging renders the brain vulnerable to amyloid I3-protein neurotoxicity. Nat. Med. (1998) 4:827–831.
- HARPER JD, LANSBURY PT: Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Ann. Rev. Biochem. (1997) 66:385–407.
- TALAGA P: P-Amyloid aggregation inhibitors for the treatment of Alzheimer's disease: dream or reality? Mini Rev. Med. Chem. (2001) 1:175–186.
- ••Updated review on amyloid aggregation.
- LORENZO A, YANKNER BA: P-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo Red. Proc. Nati Acad. Sci. USA (1994) 91:12243–12247.
- LEVINE H: Thioflavine T interaction with synthetic Alzheimer's disease P-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. (1993) 2:404–410.
- TVVYMAN LJ, ALLSOP D: A short synthesis of the P-amyloid (AP) aggregation inhibitor 3-p-toluoyl 2 [4' (3 diethyl-aminopropoxy)-phenyll-benzofuran. Tetrahedron Lett. (1999) 40:9383–9384.
- SOTO C: Protein misfolding and disease: protein refolding and therapy. FEBS Lett. (2001) 498:204–207.
- SOTO C, SABORIO GP, PERMANNE B: Inhibiting the conversion of soluble amyloid-P peptide into abnormally folded amyloidogenic intermediates: relevance for Alzheimer's disease therapy. Acta. Neurol. Scary/. Suppl. (2000) 176:90–95.
- FINDEIS MA: Approaches to discovery and characterization of inhibitors of amyloid 3-peptide polymerization. Biochim. Biophys. Acta (2000) 1502:76–84.
- FINDEIS MA, MUSSO GM, ARICO-MUENDEL CC et al.: Modified-peptide inhibitors of amyloid 3-peptide polymerization. Biochemistry (1999) 38:6791–800.
- GHANTA J, SHEN CL, KIESSLING LL,MURPHY RM: A strategy for designing inhibitors of P-amyloid toxicity. _J. Biol. Chem. (1996) 271:29525–29528.
- PALLITTO MM, GHANTA J, HEINZELMAN P, KIESSLING LL, MURPHY RM: Recognition sequence design for peptidyl modulators of 13-amyloid aggregation and toxicity. Biochemistry (1999) 38:3570–3578.
- SOLOMON B, KOPPEL R, FRANKEL, D, HANAN-AHARON E: Disaggregation of Alzheimer P-amyloid by site-directed mAb. Proc. Natl. Acad. Li. USA (1997) 94:4109–4112.
- GAMES D, ADAMS D, ALESSANDRINI R et al.: Alzheimer-type neuropathology in transgenic mice overexpressing V717F 13-amyloid precursor protein. Nature (1995) 373:523–527.
- •Transgenic mice (ADAPP) developed by Athena Neurosciences.
- HSIAO K, CHAPMAN P, NILSEN S et al.: Correlative memory deficits, AP elevation and amyloid plaques in transgenic mice. Science (1996) 274:99–102.
- •Transgenic mice (Hsiao Tg 2576) developed by researchers at the University of Minnesota.
- STURCHLER-PIERRAT C, ABRAMOWSKI D, DUKE M etal.: Two amyloid precursor protein transgenic mouse models with Alzheimer's disease-like pathology. Proc. Nati Acad. Li. USA (1997) 94:13287–13292.
- •Transgenic mice (APP23) developed by Novartis Pharma.
- CHISHTI MA, YANG DS, JANUS C et al.: Early-onset amyloid deposition and cognitive deficits in transgenic mice expressing a double mutant form of amyloid precursor protein 695. _J. Biol. Chem. (2001) 276:21562–21570.
- ••Double mutant transgenic mice(TgCRND8) developed by researchers at the University of Toronto. A potent tool for biological tests.
- SOLOMON B, FRENKEL D: Vaccination for the prevention and treatment of Alzheimer's disease. Drugs Today (2000) 36:655–663.
- ••Detailed description of the immunisationprocess.
- SCHENK DB, BARBOUR R, DUNN W et al.: Immunization with amyloid-P attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature (1999) 400:173–177.
- ••Basic work on the immune approach. Thefirst report of a treatment that reduces AD progression in a transgenic animal model.
- SCHENK DB, SEUBERT P, LIEBERBURG I, WALLACE J: Peptide immunization. A possible new treatment for Alzheimer's disease. Arch. Neurol. (2000) 57:934–936.
- BARD F, CANNON C, BARBOUR R etal.: Peripherally administered antibodies against amyloid 3-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer's disease. Nat. Med. (2000) 6:916–919.
- ••Assertion that antibodies against AP couldcross the blood-brain barrier to act directly in the CNS.
- DEMATTOS RB, BALES KR, CUMMINS DJ, DODART JC, PAUL SM, HOLTZMAN DM: Peripheral anti-A13 antibody alters CNS and plasma AP clearance and decreases brain AP burden in a mouse model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA (2001) 98:8850–8855.
- ••Reduction of AP deposition in brain maybe due to a change in the AP equilibrium between the CNS and plasma, by clearing AP from plasma.
- JANUS C, PEARSON J, MCLAURIN JA etal.: AP peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature (2000) 408:979–982.
- •Confirmation of the efficacy of immunisation with AP in a second animal model.
- SIGURDSSON EM, SCHOLTZOVA H, MEHTA PD, FRANGIONE B, WISNIEWSKI T: Immunisation with nontoxidnonflbrillar amyloid-3 homologous peptide reduces Alzheimer's disease-associated pathology in transgenic mice. Am. J Pathol. (2001) 159:439–447.
- ••A new and possibly safer form of ADvaccine.
- KLEIN WL, KRAFFT GA, FINCH CE: Targeting small AP oligomers: the solution to an Alzheimer's disease conundrum? Trends Neurosci. (2001) 24:219–224.
- •This work explains the idea that fibrils and AP deposits are not the only and perhaps even the most relevant toxic form of AP: protofibrils and small oligomers may also play an important role in the neurotoxic process.
Websites
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