Metal-protein attenuating compounds and Alzheimer’s disease

Bibliography

• McLEAN CA, CHERNY RA, FRASER FW et al.: Soluble pools of AP amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol (1999) 46:860–866
   PubMed Web of Science ®Google Scholar
• WANG J, DICKSON DW, TROJANOWSKI JQ, LEE VM: The levels of soluble versus insoluble brain AP distinguish Alzheimer's disease from normal and pathological aging. Exp. Neurol (1999) 158:328–337.
   PubMed Web of Science ®Google Scholar
• LUE LF: Soluble amyloid 13 peptide concentrations as a predictor of synaptic change in Alzheimer's disease. Am. J. Pathol (1999) 55:853–862.
   Google Scholar
• ATTWOOD CS, OBRENOVICH ME, LIU T et al.: Amyloid-P: a chameleon walking in two worlds: a review of the trophic and toxic properties of amyloid-P. Brad) Res. Rev (2003) 43:1–16.
   PubMed Web of Science ®Google Scholar
• •This article provides a well-referenced argument for the physiological role of amyloid-3.
   Google Scholar
• VIGO-PELFREY C, LEE D, KEIM P, LIEBERBURG I, SCHENK DB et al: Characterization of 3-amyloid peptide from human cerebrospinal fluid. Neurochem. (1993) 61(5):1965–1968.
   PubMed Web of Science ®Google Scholar
• SMITH MA, NUNOMURA A, ZHU X, TAKEDA A, PERRY G: Metabolic, metallic, and mitotic sources of oxidative stress in Alzheimer's disease. Antioxid. Redox Signal. (2000) 2:413–420.
   PubMed Web of Science ®Google Scholar
• CASTELLANI R, HIRAI K, ALIEV G et al.: Role of mitochondrial dysfunction in Alzheimer's disease. Neurosci. Res. (2002) 70:357–360.
   Web of Science ®Google Scholar
• •Recent review of the role mitochondrial dysfunction plays in the aetiology of oxidative stress in Alzheimer's disease.
   Google Scholar
• MONSONEGO A, WEINER HL: Immunotherapeutic approaches to Alzheimer's disease. Science (2003) 302:834–838.
   PubMed Web of Science ®Google Scholar
• NICOLL JA, WILKINSON D, HOLMES C, STEART P, MARKHAM H, WELLER RO: Neuropathology of human Alzheimer's disease after immunization with amyloid-3 peptide: a case report. Nat. Med. (2003) 9:448–452.
   PubMed Web of Science ®Google Scholar
• KOSTYSZYN B, COWBURN RF, SEIGER A, KJAELDGAARD A, SUNDSTROM E: Distribution of presenilin 1 and 2 and their relation to Notch receptors and ligands in human embryonic/foetal central nervous system. Brad) Res. Dev. Brad) Res. (2004) 151(1-2):75–86.
   PubMedGoogle Scholar
• CURTAIN CC, ALI F, VOLITAKIS I et al:Alzheimer's disease amyloid binds Cu and Zn to generate an allosterically-ordered membrane-penetrating structure containing SOD-like subunits. Biol. Chem. (2001) 276:20466–20473.
   Web of Science ®Google Scholar
• ATTWOOD CS, SCARPA RL, HUANG Y et al: Characterisation of copper interactions with Alzheimer's Ap peptides - identifiaction of an attomolar affinity copper binding site on A31-42. Neurochem. (2000) 5:1219–1233.
   Google Scholar
• ATTWOOD CS, HUANG Y, KHATRI A et al.: Copper catalysed oxidation of Alzheimer AP. Cell. MM. Biol. (2000) 46:777–783.
   PubMed Web of Science ®Google Scholar
• LEVY E, CARMAN MD: Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type. Science (1990) 248(4959):1124–1126.
   PubMed Web of Science ®Google Scholar
• FREDERICKSON CJ, BUSH Al: Synaptically released zinc: physiological functions and pathological effects. Biometals (2001) 14:353–366.
   PubMed Web of Science ®Google Scholar
• LEE JY, COLE TB, PALMITER RD, SUH SW, KOH JY: Contribution by synaptic zinc to the gender disparate plaque formation in human Swedish mutant APP transgenic mice Proc. Nati Acad. Sci. USA (2002) 99:7705–7710.
   PubMed Web of Science ®Google Scholar
• CUAJUNGCO MP, GOLDSTEIN LE, NUNOMURA A et al.: Evidence that the 3-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of AP by zinc. j Biol. Chem. (2000) 275:19439–19442.
   PubMed Web of Science ®Google Scholar
• BUSH Al, PETTINGELL WH Jr, PARADIS MD, TANZI RE: Modulation of AB adhesiveness and secretase site cleavage by zinc. Biol. Chem. (1994) 269:12152–12158.
   Web of Science ®Google Scholar
• BUSH Al, PETTINGELL WH, MULTHAUP G et al.: Rapid induction of Alzheimer's A 13 amyloid formation by zinc. Science (1994) 265:1464–1467.
   PubMed Web of Science ®Google Scholar
• BUSH Al: The metallobiology of Alzheimer's disease. Trends Neurosci. (2003) 26(4):207–214.
   PubMed Web of Science ®Google Scholar
• ••Recent review article covering the topic ofmetal ion interactions with key proteins in the aetiology of Alzheimer's disease.
   Google Scholar
• CHERNEY RA, LEGG JT, McLEAN CAet al.: Aqueous dissolution of Alzheimer's disease Ab amyloid deposits by biometal depletion. J. Biol. Chem. (1999) 274:23223–23228.
   Google Scholar
• HUANG X, ATWOOD CS, HARTSHORN MA et al: The AP peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry (1999) 38:7609–7616.
   PubMed Web of Science ®Google Scholar
• HUANG X, CUAJUNGCO MP, AT WOOD CS et al: Cu(II) potentiation of Alzheimer's Ap neurotoxicity: correlation with cell-free hydrogen peroxide production and metal reduction. Biol. Chem. (1999) 274:37111–37116.
   Web of Science ®Google Scholar
• OPAZO C, HUANG X, CHERNY RA et al.: Metalloenzyme-like activity of Alzheimer's disease 3-amyloid: Cu-dependent catalytic conversion of dopamine, cholesterol and biological reducing agents to neurotoxic H202. / Biol. Chem. (2002) 277:40302–40308.
   PubMed Web of Science ®Google Scholar
• CHERNEY RA, ATTWOOD CS, XILINAS ME et al.: Treatment with a copper-zinc chelator markedly and rapidly inhibits 3-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron (2001) 30:665–676.
   PubMed Web of Science ®Google Scholar
• •Strong animal evidence for the efficacy of dioquinol in hitting the metal-amyloid-3 target.
   Google Scholar
• RE GLAND B, LEHMANN W, ABEDINI I et al.: Treatment of Alzheimer's disease with clioquinol. Dement. Ceriatr. Cogn. Disord. (2001) 12:408–414.
   PubMed Web of Science ®Google Scholar
• RITCHIE CW, BUSH Al, MacKINNON A et al.: Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Ap amyloid deposition and toxicity in Alzheimer's disease: biochemical and clinical responses in a pilot Phase II clinical trial. Arch. Neurology (2003) 60(12):1685–1691.
   PubMed Web of Science ®Google Scholar
• ••First conclusive evidence of the efficacy ofdioquinol in improving cognition and affecting amyloid-3 in a clinical population.
   Google Scholar
• TABIRA T: Clioquinol's return: cautions from Japan. Science (2001) 292:2251–2252.
   PubMed Web of Science ®Google Scholar
• SOBUE I, ANDO K, IIDA M, TAKAYANAGI T, YAMAMURA Y, MATSUOKA Y: Myeloneuropathy with abdominal disorders in Japan. Neurology (1971) 21:168.
   PubMed Web of Science ®Google Scholar
• BAUMGARTNER G, GAWEL MJ, KAESER HE et al.: Neurotoxicity of halogenated hydroquinolones: clinical analysis of cases reported outside Japan. Neurol Neurosurg. Psychiatry (1979) 42:1073–1083.
   Google Scholar
• CLIFFORD-ROSE F, GAWEL M: Clioquinol neurotoxicity: An overview. Acta Neurol Scand. (1984) 70:137–145.
   Web of Science ®Google Scholar
• •Review article of the evidence associating clioquinol with SMON.
   Google Scholar
• MEADE TW: Subacute myelo-optic neuropathy and clioquinol. Br. j Prey. Soc. Med. (1975) 29:157–169.
   PubMedGoogle Scholar
• •Review article of evidence associating clioquinol with SMON.
   Google Scholar
• NAKAE K, YAMAMOTO S, SHIGEMATSU I, KONO R: Relation between subacute myelo-optic neuropathy (SMON) and Clioquinol: nation-wide survey. Lancet (1973) 1:171–173.
   PubMed Web of Science ®Google Scholar
• IGATA A et al.: No English translation of title. Igaku no Ayurni (1971) 77: 572.
   Google Scholar
• YOSHITAKE Y, IGATA A: SMON cases following abdominal surgery. Igaku no Ayurni (1970) 74:598.
   Google Scholar
• KURATSUNE T et al.: Epidemiological survey on the relationship between SMON and chinoform. Presented at the meeting of SMON Research Committee (1971).
   Google Scholar
• AOKI K et al: Relationship between chinoform administration and SMON incidence observed in some medical institutes. Presented at the meeting of SMON Research Committee (1971).
   Google Scholar
• TSUBAKI T, HONMA Y, HOSHI M: Neurological syndrome associated with Clioquinol. Lancet (1971) 1:696.
   PubMed Web of Science ®Google Scholar
• HINO S: Clioquinol and SMON Chiro Chiryo (1972) 54.
   Google Scholar
• TAKASU T, TOYOKURA Y, NAKAE K, KATSHIRA K, SUGIYAMA S: Suspected cases of SMON in Japan in 1938. Nihon Rinsho (1973) 31:204.
   Google Scholar
• LEOPOLD IH: Zinc deficiency and visualimpairment. Am. I Ophthahnol (1978) 85:871–875.
   PubMed Web of Science ®Google Scholar
• SCHAUMBURG H et al: The CNS distal axonopathy in dogs intoxicated with Clioquinol. I Neuropath. Exp. Near. (1978). 37:686a.
   Web of Science ®Google Scholar
• KRINKE G, PERICIN C, THOMANN P, HESS R: Toxic encephalopathy with hippocampal lesions. Zentralblatt fur Vetinannedizin A (1978) 25:277–296.
   PubMedGoogle Scholar
• YASSIN MS, EKBLOM J, XILINAS M, GOTTFRIES CG, ORELAND L: Changes in uptake of vitamin B(12) and trace metals in brains of mice treated with clioquinol. Neurol Sci. (2000) 173:40–44.
   Web of Science ®Google Scholar
• BUSH Al, MASTERS CL: Clioquinas return. Science (2001) 292:2251–2252.
   PubMedGoogle Scholar
• MARTIN FL: Alpha-synuclein and the pathogenesis of Parkinson's disease. Protein Pept. Lett. (2004) 11(3):229–37.
   PubMed Web of Science ®Google Scholar
• DURR A: Friedreich's ataxia: treatment within reach. Lancet Neurol (2002) 1(6)370–374.
   Google Scholar
• RICHARDSON DR: Novel chelators for central nervous system disorders that involve alterations in the metabolism of iron and other metals. Ann. NY Acad. Sci. (2004); 1012:326–341.
   PubMed Web of Science ®Google Scholar
• ••Thorough review of the pathologicalinteractions between metal ions and a range of neurological conditions that may be affected by chelation therapy in the future.
   Google Scholar
• KAUR D: Genetic or pharmacological ironchelation prevents MPTP-induced neurotoxicity in vivo: a novel therapy for Parkinson's disease. Neuron, (2003) 37(6)899–909.
   Google Scholar