The role of metallobiology and amyloid-β peptides in Alzheimer's disease

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619 · see citing works

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431 · see citing works

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · cited 1× · see citing works

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works

Plasma Homocysteine as a Risk Factor for Dementia and Alzheimer's Disease

Seshadri, S., Beiser, A., Selhub, J., Jacques, P. F., Rosenberg, I. H., D'Agostino, R. B., Wilson, P. W. F., & Wolf, P. A. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa011613 · Cited by 3,237 · see citing works

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120 · see citing works

Aβ Oligomers – a decade of discovery

Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938 · see citing works

Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database

Bertram, L., McQueen, M. B., Mullin, K., Blacker, D., & Tanzi, R. E. (2007) · Nature Genetics · doi:10.1038/ng1934 · Cited by 1,857 · see citing works

The neurobiology of zinc in health and disease

Frederickson, C. J., Koh, J., & Bush, A. I. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1671 · Cited by 1,841 · see citing works

The toxicology of mercury—current exposures and clinical manifestations

Clarkson, T. W., Magos, L., & Myers, G. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmra022471 · Cited by 1,766 · see citing works

Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693 · see citing works

Purification and cloning of amyloid precursor protein β-secretase from human brain

Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612 · see citing works

Rapid induction of Alzheimer A beta amyloid formation by zinc

Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522 · see citing works

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447 · see citing works

Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity

Yan, R., Bienkowski, M. J., Shuck, M. E., Miao, H., Tory, M. C., Pauley, A. M., Brashler, J. R., Stratman, N. C., Mathews, W. R., Buhl, A. E., et al. (1999) · Nature · doi:10.1038/990107 · Cited by 1,438 · see citing works

Trace elements in human physiology and pathology: zinc and metallothioneins

Tapiero, H., & Tew, K. D. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(03)00081-7 · Cited by 1,297 · see citing works

Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease

Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239 · see citing works

Regulating the fate of mRNA: the control of cellular iron metabolism

Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210 · see citing works

The ADAM metalloproteinases

Edwards, D. R., Handsley, M. M., & Pennington, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,165 · see citing works

Neurotoxic Effects and Biomarkers of Lead Exposure: A Review

Sanders, T., Liu, Y., Buchner, V., & Tchounwou, P. B. (2009) · Reviews on Environmental Health · doi:10.1515/reveh.2009.24.1.15 · Cited by 1,084 · see citing works

Neurobiology of Zinc and Zinc-Containing Neurons

Frederickson, C. J. (1989) · International review of neurobiology · doi:10.1016/s0074-7742(08)60279-2 · Cited by 1,070 · see citing works

Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease

Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · see citing works

Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels.

Masters, C. L., Multhaup, G., Simms, G., Pottgiesser, J., Martins, R. N., & Beyreuther, K. T. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04000.x · Cited by 1,043 · see citing works

Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦

Demuro, A., Mina, E. W., Kayed, R., Milton, S. C. F., Parker, I., & Glabe, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500997200 · Cited by 1,038 · see citing works

Trace elements in human physiology and pathology. Copper

Tapiero, H., Townsend, D. M., & Tew, K. D. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(03)00012-x · Cited by 1,030 · see citing works

Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009 · see citing works

Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation

Luo, Y., Bolon, B., Kahn, S., Bennett, B. D., Babu-Khan, S., Denis, P., Fan, W., Kha, H., Zhang, J., Gong, Y., et al. (2001) · Nature Neuroscience · doi:10.1038/85059 · Cited by 1,001 · see citing works

Fluorescent chemosensors for Zn2+

Xu, Z., Yoon, J., & Spring, D. R. (2010) · Chemical Society Reviews · doi:10.1039/b916287a · Cited by 983 · see citing works

Aph-1, Pen-2, and Nicastrin with Presenilin Generate an Active γ-Secretase Complex

De Strooper, B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00205-8 · Cited by 965 · see citing works

Oxidative damage in Alzheimer's

Smith, M. A., Perry, G. L., Richey, P. L., Sayrec, L. M., Anderson, V. E., Beal, M. F., & Kowall, N. W. (1996) · Nature · doi:10.1038/382120b0 · Cited by 897 · see citing works

Aβ Oligomers Induce Neuronal Oxidative Stress through an N-Methyl-D-aspartate Receptor-dependent Mechanism That Is Blocked by the Alzheimer Drug Memantine

De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882 · see citing works

BACE1 is the major β-secretase for generation of Aβ peptides by neurons

Cai, H., Wang, Y.-S., McCarthy, D., Wen, H., Borchelt, D., Price, D. L., & Wong, P. (2001) · Nature Neuroscience · doi:10.1038/85064 · Cited by 791 · see citing works

Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

Huang, X., Cuajungco, M. P., Atwood, C. S., Hartshorn, M. A., Tyndall, J. D. A., Hanson, G. R., Stokes, K. C., Leopold, M., Multhaup, G., Goldstein, L. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762 · see citing works

Zinc in the physiology and pathology of the CNS

Sensi, S. L., Paoletti, P., Bush, A. I., & Sekler, I. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2734 · Cited by 759 · see citing works

Safety, efficacy, and biomarker findings of PBT2 in targeting Aβ as a modifying therapy for Alzheimer's disease: a phase IIa, double-blind, randomised, placebo-controlled trial

Lannfelt, L., Blennow, K., Zetterberg, H., Batsman, S., Ames, D., Harrison, J., Masters, C. L., Targum, S., Bush, A. I., Murdoch, R., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70167-4 · Cited by 725 · see citing works

ZnT-3, a putative transporter of zinc into synaptic vesicles

Palmiter, R. D., Cole, T. B., Quaife, C. J., & Findley, S. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14934 · Cited by 708 · see citing works

Chromium(III) and the glucose tolerance factor

Schwarz, K., & Mertz, W. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90479-5 · Cited by 691 · see citing works

Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease

Duce, J. A., Tsatsanis, A., Cater, M. A., James, S., Robb, E. L., Wikhe, K., Leong, S. L., Perez, K. A., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 682 · see citing works

The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts

Hartmann, D. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2615 · Cited by 680 · see citing works

Rapid Restoration of Cognition in Alzheimer's Transgenic Mice with 8-Hydroxy Quinoline Analogs Is Associated with Decreased Interstitial Aβ

Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., Volitakis, I., Liu, X., Smith, J. P., Perez, K., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.018 · Cited by 672 · see citing works

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 653 · see citing works

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar‐Affinity Copper Binding Site on Amyloid β1‐42

Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751219.x · Cited by 641 · see citing works

A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model

Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20864 · Cited by 638 · see citing works

ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons

Kuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621 · see citing works

Arsenic Epidemiology and Drinking Water Standards

Smith, A. H., Lopipero, P. A., Bates, M. N., & Steinmaus, C. M. (2002) · Science · doi:10.1126/science.1072896 · Cited by 620 · see citing works

Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer’s disease

Miller, L. M., Wang, Q., Telivala, T. P., Smith, R., Lanzirotti, A., & Judith Miklossy, A. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.09.004 · Cited by 588 · see citing works

Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid

Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 580 · see citing works

Metal Binding and Oxidation of Amyloid-β within Isolated Senile Plaque Cores: Raman Microscopic Evidence

Dong, J., Atwood, C., Anderson, V. E., Siedlak, S. L., Smith, M. A., Perry, G. L., & CAREY, P. R. (2003) · Biochemistry · doi:10.1021/bi0272151 · Cited by 560 · see citing works

An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript

Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., Leiter, L., McPhee, J., Sarang, S. S., Utsuki, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207435200 · Cited by 551 · see citing works

Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer’s disease: possible relation to oxidative stress.

Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (1996) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(96)00203-1 · Cited by 540 · see citing works

Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide

Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530 · see citing works

Activation of superoxide dismutases: Putting the metal to the pedal

Culotta, V., Yang, M., & O’Halloran, T. V. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.003 · Cited by 509 · see citing works

Electrochemical Analysis of Protein Nitrotyrosine and Dityrosine in the Alzheimer Brain Indicates Region-Specific Accumulation

Hensley, K., Maidt, M. L., Yu, Z., Sang, H., Markesbery, W. R., & Floyd, R. A. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-20-08126.1998 · Cited by 508 · see citing works

Aqueous Dissolution of Alzheimer's Disease Aβ Amyloid Deposits by Biometal Depletion

Cherny, R. A., Legg, J. T., McLean, C. A., Fairlie, D. P., Huang, X., Atwood, C. S., Beyreuther, K., Tanzi, R. E., Masters, C. L., & Bush, A. I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23223 · Cited by 482 · see citing works

A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients

Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475 · see citing works

Alzheimer's Disease (AD)-Like Pathology in Aged Monkeys after Infantile Exposure to Environmental Metal Lead (Pb): Evidence for a Developmental Origin and Environmental Link for AD

Wu, J., Basha, R. M., Brock, B., Cox, D. P., Cardozo‐Pelaez, F., McPherson, C. A., Harry, J., Rice, D. C., Maloney, B., Chen, D., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4405-07.2008 · Cited by 473 · see citing works

Cellular distribution of transferrin, ferritin, and iron in normal and aged human brains

Connor, J. R., Menzies, S. L., Martin, S. M. S., & Mufson, E. J. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490270421 · Cited by 472 · see citing works

A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains

Connor, J. R., Menzies, S. L., Martin, S. M. S., & Mufson, E. J. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310111 · Cited by 468 · see citing works

Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease

Syme, C. D., Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313572200 · Cited by 459 · see citing works

Inhibition of the Human Thioredoxin System

Carvalho, C. M. L., Chew, E., Hashemy, S. I., Lu, J., & Holmgren, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710133200 · Cited by 456 · see citing works

ADAMs family members as amyloid precursor protein α‐secretases

Allinson, T. M. J., Parkin, E. T., Turner, A. J., & Hooper, N. M. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10737 · Cited by 441 · see citing works

Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice

Lee, J., Cole, T. B., Palmiter, R. D., Suh, S. W., & Koh, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092034699 · Cited by 432 · see citing works

PBT2 Rapidly Improves Cognition in Alzheimer's Disease: Additional Phase II Analyses

Faux, N. G., Ritchie, C. W., Gunn, A. P., Rembach, A., Tsatsanis, A., Bedő, J., Harrison, J., Lannfelt, L., Blennow, K., Zetterberg, H., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1390 · Cited by 406 · see citing works

Iron, Neuromelanin and ferritin content in the substantia nigra of normal subjects at different ages: consequences for iron storage and neurodegenerative processes

Zecca, L., Gallorini, M., Schünemann, V., Trautwein, A. X., Gerlach, M., Riederer, P., Vezzoni, P., & Tampellini, D. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00186.x · Cited by 401 · see citing works

Rapid Communication: Characterization of β‐Amyloid Peptide from Human Cerebrospinal Fluid

Vigo‐Pelfrey, C., Lee, D., Keim, P., Lieberburg, I., & Schenk, D. B. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09841.x · Cited by 385 · see citing works

Cognitive Loss in Zinc Transporter-3 Knock-Out Mice: A Phenocopy for the Synaptic and Memory Deficits of Alzheimer's Disease?

Adlard, P. A., Parncutt, J. M., Finkelstein, D. I., & Bush, A. I. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5255-09.2010 · Cited by 376 · see citing works

Regional distribution of iron and iron‐regulatory proteins in the brain in aging and Alzheimer's disease

Connor, J. R., Snyder, B. S., Beard, J. L., Fine, R. E., & Mufson, E. J. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310214 · Cited by 374 · see citing works

Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β

Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371 · see citing works

Aggregation of Secreted Amyloid β-Protein into Sodium Dodecyl Sulfate-stable Oligomers in Cell Culture

Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydel, R. E., Teplow, D. B., & Selkoe, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9564 · Cited by 364 · see citing works

The Fetal Basis of Amyloidogenesis: Exposure to Lead and Latent Overexpression of Amyloid Precursor Protein and β-Amyloid in the Aging Brain

Basha, R. M., Wei, W., Bakheet, S. A., Benitez, N. B., Siddiqi, H. K., Ge, Y., Lahiri, D. K., & Zawia, N. H. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4335-04.2005 · Cited by 353 · see citing works

Overexpression of Alzheimer's Disease Amyloid-β Opposes the Age-dependent Elevations of Brain Copper and Iron

Maynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., White, A. R., Beyreuther, K. T., Masters, C. L., Bush, A. I., & Li, Q. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204379200 · Cited by 352 · see citing works

Mass spectrometric characterization of brain amyloid beta isoform signatures in familial and sporadic Alzheimer’s disease

Portelius, E., Bogdanovic, N., Gustavsson, M. K., Volkmann, I., Brinkmalm, G., Zetterberg, H., Winblad, B., & Blennow, K. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0690-1 · Cited by 348 · see citing works

Modulation of A beta adhesiveness and secretase site cleavage by zinc.

Bush, A. I., Pettingell, W. H., Paradis, M. D., & Tanzi, R. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32694-7 · Cited by 331 · see citing works

Zinc-induced Alzheimer's Aβ1–40 Aggregation Is Mediated by Conformational Factors

Huang, X., Atwood, C., Moir, R. D., Hartshorn, M. A., Vonsattel, J., Tanzi, R. E., & Bush, A. I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26464 · Cited by 313 · see citing works

Structural Changes of Region 1-16 of the Alzheimer Disease Amyloid β-Peptide upon Zinc Binding and in Vitro Aging

Zirah, S., Kozin, S. A., Mazur, A. K., Blond, A., Cheminant, M., Ségalas-Milazzo, I., Debey, P., & Rebuffat, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504454200 · Cited by 304 · see citing works

Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states

Miller, Y., Ma, B., & Nussinov, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913114107 · Cited by 303 · see citing works

Putative function of ADAM9, ADAM10, and ADAM17 as APP -secretase

Asai, M., Hattori, C., Szabó, B., Sasagawa, N., Maruyama, K., Tanuma, S.-I., & Ishiura, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02999-6 · Cited by 303 · see citing works

Longitudinal, Quantitative Assessment of Amyloid, Neuroinflammation, and Anti-Amyloid Treatment in a Living Mouse Model of Alzheimer's Disease Enabled by Positron Emission Tomography

Maeda, J., Ji, B., Irie, T., Tomiyama, T., Maruyama, M., Okauchi, T., Staufenbiel, M., Iwata, N., Ono, M., Saido, T. C., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0673-07.2007 · Cited by 300 · see citing works

NMDA Receptor Activation Mediates Copper Homeostasis in Hippocampal Neurons

Schlief, M. L., Craig, A. M., & Gitlin, J. D. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3699-04.2005 · Cited by 291 · see citing works

ALZHEIMERʼS DISEASE

GOODMAN, L. (1953) · The Journal of Nervous and Mental Disease · doi:10.1097/00005053-195308000-00001 · Cited by 287 · see citing works

A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease

Bush, A. I., Multhaup, G., Moir, R. D., Williamson, T. G., Small, D. H., Rumble, B. A., Pollwein, P., Beyreuther, K. T., & Masters, C. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85394-2 · Cited by 286 · see citing works

Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics

Duce, J. A., & Bush, A. I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.003 · Cited by 281 · see citing works

AMPA receptor activation potentiates zinc neurotoxicity

Weiss, J. H., Hartley, D. M., Koh, J., & Choi, D. W. (1993) · Neuron · doi:10.1016/0896-6273(93)90240-r · Cited by 279 · see citing works

Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain

Barnham, K. J., McKinstry, W. J., Multhaup, G., Galatis, D., Morton, C. J., Curtain, C. C., Williamson, N. A., White, A. R., Hinds, M. G., Norton, R. S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300629200 · Cited by 274 · see citing works

Elevated cortical zinc in Alzheimer disease

Religa, D., Strozyk, D., Cherny, R. A., Volitakis, I., Haroutunian, V., Winblad, B. G., Näslund, J., & Bush, A. I. (2006) · Neurology · doi:10.1212/01.wnl.0000223644.08653.b5 · Cited by 272 · see citing works

Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains.

Vallée, B. L., Coleman, J., & Auld, D. S. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.3.999 · Cited by 271 · see citing works

Iron, zinc and copper in the Alzheimer's disease brain: A quantitative meta-analysis. Some insight on the influence of citation bias on scientific opinion

Schrag, M., Mueller, C., Oyoyo, U. E., Smith, M. A., & Kirsch, W. M. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.05.001 · Cited by 266 · see citing works

Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease β‐amyloid

Barnham, K. J., Hæffner, F., Ciccotosto, G. D., Curtain, C. C., Tew, D. J., Mavros, C., Beyreuther, K. T., Carrington, D., Masters, C. L., Cherny, R. A., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-1890fje · Cited by 262 · see citing works

Formation of hydrogen peroxide and hydroxyl radicals from Aβ and α-synuclein as a possible mechanism of cell death in Alzheimer’s disease and Parkinson’s disease

Tabner, B. J., Turnbull, S., El‐Agnaf, O. M. A., & Allsop, D. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00801-8 · Cited by 261 · see citing works

Iron deposits in multiple sclerosis and Alzheimer's disease brains

LeVine, S. M. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00470-8 · Cited by 258 · see citing works

Imbalances of trace elements related to oxidative damage in Alzheimer's disease brain.

Cornett, C., Markesbery, W. R., & Ehmann, W. D. (1998) · PubMed · Cited by 253 · see citing works

Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia

Grundke, I., Fleming, J. T., Tung, Y. C., Lassmann, H., Iqbal, K., & Joshi, J. G. (1990) · Acta Neuropathologica · doi:10.1007/bf00334497 · Cited by 253 · see citing works

High‐resolution NMR studies of the zinc‐binding site of the Alzheimer's amyloid β‐peptide

Danielsson, J., Pierattelli, R., Banci, L., & Gräslund, A. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05563.x · Cited by 253 · see citing works

Zn2+ Ions: Modulators of Excitatory and Inhibitory Synaptic Activity

Smart, T. G., Hosie, A. M., & Miller, P. S. (2004) · The Neuroscientist · doi:10.1177/1073858404263463 · Cited by 247 · see citing works

Pleomorphic Copper Coordination by Alzheimer’s Disease Amyloid-β Peptide

Drew, S. C., Noble, C. J., Masters, C. L., Hanson, G. R., & Barnham, K. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja808073b · Cited by 242 · see citing works

Taurine prevents the neurotoxicity of β‐amyloid and glutamate receptor agonists: activation of GABA receptors and possible implications for Alzheimer's disease and other neurological disorders

Louzada, P., Lima, A. C. P., Mendonça-Silva, D., Noël, F., de Mello, F. G., & Ferreira, S. (2004) · The FASEB Journal · doi:10.1096/fj.03-0739com · Cited by 239 · see citing works

Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP<i>In Vivo</i>Is Prevented by Immunotargeting Cellular Prion Protein

Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237 · see citing works

Brain iron metabolism: Neurobiology and neurochemistry

Ke, Y., & Qian, Z. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.07.009 · Cited by 236 · see citing works

Elevation of serum copper levels in Alzheimer’s disease

Squitti, R., Lupoi, D., Pasqualetti, P., Forno, G. D., Vernieri, F., Chiovenda, P., Rossi, L. C., Cortesi, M., Cassetta, E., & Rossini, P. M. (2002) · Neurology · doi:10.1212/wnl.59.8.1153 · Cited by 236 · see citing works

A Role for Synaptic Zinc in Activity-Dependent Aβ Oligomer Formation and Accumulation at Excitatory Synapses

Deshpande, A., Kawai, H., Metherate, R., Glabe, C. G., & Busciglio, J. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5980-08.2009 · Cited by 232 · see citing works

Metal Ions Differentially Influence the Aggregation and Deposition of Alzheimer's β-Amyloid on a Solid Template

Ha, C., Ryu, J., & Park, C. B. (2007) · Biochemistry · doi:10.1021/bi7000032 · Cited by 231 · see citing works

Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease.

Basun, H., Forssell, L. G., Wetterberg, L., & Winblad, B. G. (1991) · PubMed · Cited by 228 · see citing works

Extracellular phosphorylation of the amyloid β‐peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease

Kumar, S., Rezaei‐Ghaleh, N., Terwel, D., Thal, D. R., Richard, M., Hoch, M., Donald, J. M. M., Wüllner, U., Glebov, K., Heneka, M. T., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.138 · Cited by 220 · see citing works

Iron Promotes the Toxicity of Amyloid β Peptide by Impeding Its Ordered Aggregation

Liu, B., Moloney, A. M., Meehan, S., Morris, K. L., Thomas, S. E., Serpell, L. C., Hider, R. C., Marciniak, S. J., Lomas, D. A., & Crowther, D. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158980 · Cited by 217 · see citing works

Homodimerization of Amyloid Precursor Protein and Its Implication in the Amyloidogenic Pathway of Alzheimer's Disease

Scheuermann, S., Hambsch, B., Hesse, L., Stumm, J., Schmidt, C., Beher, D., Bayer, T. A., Beyreuther, K. T., & Multhaup, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105410200 · Cited by 216 · see citing works

Binding of zinc(II) and copper(II) to the full‐length Alzheimer’s amyloid‐β peptide

Tõugu, V., Tiiman, A., & Palumaa, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05061.x · Cited by 216 · see citing works

Truncated beta‐amyloid peptide species in pre‐clinical Alzheimer's disease as new targets for the vaccination approach

Sergeant, N., Bombois, S., Ghestem, A., Drobecq, H., Kostanjevečki, V., Missiaen, C., Wattez, A., David, J. P., Vanmechelen, E., Sergheraert, C., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01818.x · Cited by 213 · see citing works

Identifying the Minimal Copper- and Zinc-binding Site Sequence in Amyloid-β Peptides

Minicozzi, V., Stellato, F., Comai, M., Serra, M. D., Potrich, C., Meyer‐Klaucke, W., & Morante, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707109200 · Cited by 209 · see citing works

Distinct Effects of Zn2+, Cu2+, Fe3+, and Al3+ on Amyloid-β Stability, Oligomerization, and Aggregation

Chen, W.-T., Liao, Y., Yu, H.-M., Cheng, I. H.-J., & Chen, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177246 · Cited by 200 · see citing works

Metal Ions, pH, and Cholesterol Regulate the Interactions of Alzheimer's Disease Amyloid-β Peptide with Membrane Lipid

Curtain, C. C., Ali, F. E. A., Smith, D. G., Bush, A. I., Masters, C. L., & Barnham, K. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205455200 · Cited by 200 · see citing works

Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1–16 Amyloid‐β Peptide: A Key Role of the First Two N‐Terminus Residues

Dorlet, P., Gambarelli, S., Faller, P., & Hureau, C. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904567 · Cited by 196 · see citing works

Dietary arsenic intakes in the United States: FDA Total Diet Study, September 1991-December 1996

Tao, S. S.-H., & Bolger, P. M. (1999) · Food Additives & Contaminants · doi:10.1080/026520399283759 · Cited by 194 · see citing works

Lysosomal Membrane Damage in Soluble Aβ-Mediated Cell Death in Alzheimer's Disease

Ditaranto, K., Tekirian, T. L., & Yang, A. J. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0364 · Cited by 192 · see citing works

The Amyloid-β Peptide of Alzheimer’s Disease Binds Cu I in a Linear Bis-His Coordination Environment: Insight into a Possible Neuroprotective Mechanism for the Amyloid-β Peptide

Shearer, J., & Szalai, V. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805940m · Cited by 189 · see citing works

Dityrosine: Preparation, Isolation, and Analysis

Malencik, D. A., Sprouse, J. F., Swanson, C. A., et al. (1996) · Analytical Biochemistry · doi:10.1006/abio.1996.0454 · Cited by 188 · see citing works

Copper-mediated Amyloid-β Toxicity Is Associated with an Intermolecular Histidine Bridge

Smith, D. P., Smith, D. G., Curtain, C. C., Boas, J. F., Pilbrow, J. R., Ciccotosto, G. D., Lau, T., Tew, D. J., Perez, K. A., Wade, J. D., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600417200 · Cited by 186 · see citing works

Oxidation of Cholesterol by Amyloid Precursor Protein and β-Amyloid Peptide

Nelson, T. J., & Alkon, D. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409071200 · Cited by 185 · see citing works

Role of the Menkes copper-transporting ATPase in NMDA receptor-mediated neuronal toxicity

Schlief, M. L., West, T., Craig, A. M., Holtzman, D. M., & Gitlin, J. D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605390103 · Cited by 184 · see citing works

Copper in Alzheimer's Disease: A Meta-Analysis of Serum, Plasma, and Cerebrospinal Fluid Studies

Bucossi, S., Ventriglia, M., Panetta, V., Salustri, C., Pasqualetti, P., Mariani, S., Siotto, M., Rossini, P. M., & Squitti, R. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101473 · Cited by 183 · see citing works

Amyloid Precursor Proteins Inhibit Heme Oxygenase Activity and Augment Neurotoxicity in Alzheimer's Disease

Takahashi, M., Doré, S., Ferris, C. D., Tomita, T., Sawa, A., Wolosker, H., Borchelt, D., Iwatsubo, T., Kim, S., Thinakaran, G., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)00125-2 · Cited by 181 · see citing works

MR evaluation of age-related increase of brain iron in young adult and older normal males

Bartzokis, G., Beckson, M., Hance, D. B., Marx, P., Foster, J., & Marder, S. R. (1997) · Magnetic Resonance Imaging · doi:10.1016/s0730-725x(96)00234-2 · Cited by 181 · see citing works

Iron: The Redox-active Center of Oxidative Stress in Alzheimer Disease

Castellani, R. J., Moreira, P. I., Liu, G., Dobson, J., Perry, G., Smith, M. A., & Zhu, X. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9360-7 · Cited by 180 · see citing works

Copper in Alzheimer's Disease: A Meta-Analysis of Serum, Plasma, and Cerebrospinal Fluid Studies

Ventriglia, M., Bucossi, S., Panetta, V., & Squitti, R. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120244 · Cited by 180 · see citing works

N-Terminal Deletions Modify the Cu2+Binding Site in Amyloid-β

Karr, J. W., Akintoye, H., Kaupp, L. J., & Szalai, V. A. (2005) · Biochemistry · doi:10.1021/bi047611e · Cited by 178 · see citing works

Vascular oxidative stress in Alzheimer disease

Zhu, X., Smith, M. A., Honda, K., Aliev, G. M., Moreira, P. I., Nunomura, A., Casadesús, G., Harris, P. L. R., Siedlak, S. L., & Perry, G. L. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.01.039 · Cited by 175 · see citing works

Iron, Transferrin, and Ferritin in the Rat Brain During Development and Aging

Roskams, A. J., & Connor, J. R. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63020709.x · Cited by 173 · see citing works

Fenton chemistry and oxidative stress mediate the toxicity of the β‐amyloid peptide in a Drosophila model of Alzheimer’s disease

Rival, T., Page, R. M., Chandraratna, D. S., Sendall, T. J., Ryder, E. J., Liu, B., Lewis, H. D., Rosahl, T. W., Hider, R. C., Camargo, L. M., et al. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06701.x · Cited by 168 · see citing works

Excess of serum copper not related to ceruloplasmin in Alzheimer disease

Squitti, R., Pasqualetti, P., Forno, G. D., Moffa, F., Cassetta, E., Lupoi, D., Vernieri, F., Rossi, L. C., Baldassini, M., & Rossini, P. M. (2005) · Neurology · doi:10.1212/01.wnl.0000154531.79362.23 · Cited by 166 · see citing works

Alanine-2 Carbonyl is an Oxygen Ligand in Cu 2+ Coordination of Alzheimer’s Disease Amyloid-β Peptide − Relevance to N-Terminally Truncated Forms

Drew, S. C., Masters, C. L., & Barnham, K. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903669a · Cited by 166 · see citing works

Mitochondrial enzyme-deficient hippocampal neurons and choroidal cells in AD

Cottrell, D. A., Blakely, E. L., Johnson, M. A., Ince, P. G., & Turnbull, D. M. (2001) · Neurology · doi:10.1212/wnl.57.2.260 · Cited by 163 · see citing works

Does Inorganic Mercury Play a Role in Alzheimer's Disease? A Systematic Review and an Integrated Molecular Mechanism

Mutter, J., Curth, A., Naumann, J., Deth, R. C., & Walach, H. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100705 · Cited by 163 · see citing works

Aluminum, copper, iron and zinc differentially alter amyloid-Aβ1–42 aggregation and toxicity

Bolognin, S., Luigi Messori, A., Drago, D., Gabbiani, C., Cendron, L., & Zatta, P. F. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.02.009 · Cited by 162 · see citing works

Copper(ii) and iron(ii) ion sensing with semiconducting polymer dots

Chan, Y., Jin, Y., Wu, C., et al. (2011) · Chemical Communications · doi:10.1039/c0cc04929h · Cited by 162 · see citing works

TRACE ELEMENTS AND COGNITIVE IMPAIRMENT: AN ELDERLY COHORT STUDY

SMORGON, C., Mari, E., Atti, A. R., Nora, E. D., Zamboni, P., Calzoni, F., Passaro, A., & Fellin, R. (2004) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2004.04.050 · Cited by 156 · see citing works

The emerging role of ICP-MS in proteomic analysis

Bettmer, J., Montes‐Bayón, M., Encinar, J. R., Fernández‐Sánchez, M. L., de la Campa, M. D. R. F., & Sanz‐Medel, A. (2009) · Journal of Proteomics · doi:10.1016/j.jprot.2009.05.003 · Cited by 156 · see citing works

Zinc and copper modulate Alzheimer Aβ levels in human cerebrospinal fluid

Altschul, D., Launer, L. J., Adlard, P. A., Cherny, R. A., Tsatsanis, A., Volitakis, I., Blennow, K., Petrovitch, H., White, L. R., & Bush, A. I. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.10.012 · Cited by 154 · see citing works

Modulating Amyloid Self-Assembly and Fibril Morphology with Zn(II)

Dong, J., Shokes, J. E., Scott, R. A., & Lynn, D. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja055973j · Cited by 149 · see citing works

Increased Expression but Reduced Activity of Antioxidant Enzymes in Alzheimer's Disease

Omar, R., Chyan, Y., Andorn, A. C., Poeggeler, B., Robakis, N. K. R. K., & Pappolla, M. A. (1999) · Journal of Alzheimer s Disease · doi:10.3233/jad-1999-1301 · Cited by 149 · see citing works

Zinc-induced Neurotoxicity Mediated by Transient Receptor Potential Melastatin 7 Channels

Inoue, K., Branigan, D. L., & Xiong, Z. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040485 · Cited by 148 · see citing works

In vivo MR evaluation of age-related increases in brain iron.

Bartzokis, G., Mintz, J., Sultzer, D. L., Marx, P., Herzberg, J., Phelan, C., & Marder, S. R. (1994) · PubMed Central · Cited by 140 · see citing works

Serum zinc is decreased in Alzheimer’s disease and serum arsenic correlates positively with cognitive ability

Baum, L., Chan, I. H. S., Cheung, S. K. K., Goggins, W. B., Mok, V., LAM, L. C. W., Leung, V., Hui, E., Ng, C., Woo, J., et al. (2009) · BioMetals · doi:10.1007/s10534-009-9277-5 · Cited by 139 · see citing works

A potential pathogenetic role of iron in Alzheimer's disease

Silvestri, L., & Camaschella, C. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00356.x · Cited by 139 · see citing works

Assessment of copper status: effect of age and gender on reference ranges in healthy adults

MILNE, D. B., & Johnson, P. E. (1993) · Clinical Chemistry · doi:10.1093/clinchem/39.5.883 · Cited by 138 · see citing works

Amyloidogenic Processing but Not Amyloid Precursor Protein (APP) Intracellular C-terminal Domain Production Requires a Precisely Oriented APP Dimer Assembled by Transmembrane GXXXG Motifs

Kienlen‐Campard, P., Tasiaux, B., Hees, J. V., Li, M., Huysseune, S., Sato, T., Fei, J. Z., Aimoto, S., Courtoy, P. J., Smith, S. O., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707142200 · Cited by 138 · see citing works

Neuronal Zinc Exchange with the Blood Vessel Wall Promotes Cerebral Amyloid Angiopathy in an Animal Model of Alzheimer's Disease

Friedlich, A. L., Lee, J., van Groen, T., Cherny, R. A., Volitakis, I., Cole, T. B., Palmiter, R. D., Koh, J., & Bush, A. I. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0297-04.2004 · Cited by 138 · see citing works

Iron: A Pathological Mediator of Alzheimer Disease?

Bishop, G. M., Robinson, S. R., Liu, Q., Perry, G. L., Atwood, C., & Smith, M. A. (2002) · Developmental Neuroscience · doi:10.1159/000065696 · Cited by 138 · see citing works

Subclinical Zinc Deficiency in Alzheimer’s Disease and Parkinson’s Disease

Brewer, G., Kanzer, S., Zimmerman, E., Molho, E., Celmins, D. F., Heckman, S. M., & Dick, R. (2010) · American Journal of Alzheimers Disease & Other Dementias · doi:10.1177/1533317510382283 · Cited by 137 · see citing works

Alzheimer disease β-amyloid activity mimics cholesterol oxidase

Puglielli, L., Friedlich, A. L., Setchell, K. D. R., Nagano, S., Opazo, C., Cherny, R. A., Barnham, K. J., Wade, J. D., Melov, S., Kovacs, D. M., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23610 · Cited by 134 · see citing works

Non-equivalent Roles for the First and Second Zinc Fingers of Protein Kinase Cδ

Szállási, Z., Bögi, K., Gohari, S., Bı́ró, T., Acs, P. I., & Blumberg, P. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18299 · Cited by 134 · see citing works

Diphenyl diselenide, a simple organoselenium compound, decreases methylmercury-induced cerebral, hepatic and renal oxidative stress and mercury deposition in adult mice

de Freitas, A. S., Funck, V. R., Rotta, M. D. S., et al. (2008) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2008.11.001 · Cited by 134 · see citing works

Increased brain iron coincides with early plaque formation in a mouse model of Alzheimer's disease

Leskovjan, A. C., Kretlow, A., Lanzirotti, A., Barrea, R. A., Vogt, S., & Miller, L. M. (2010) · NeuroImage · doi:10.1016/j.neuroimage.2010.11.073 · Cited by 134 · see citing works

Aβ induces cell death by direct interaction with its cognate extracellular domain on APP (APP 597–624)

Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., Bredesen, D. E., Koo, E. H., Shaked, G. M., Kummer, M. P., Lu, D. C., Galvan, V., et al. (2006) · The FASEB Journal · doi:10.1096/fj.05-5032fje · Cited by 132 · see citing works

The Caenorhabditis elegans Aβ1–42 Model of Alzheimer Disease Predominantly Expresses Aβ3–42

McColl, G., Roberts, B. R., Gunn, A. P., Perez, K. A., Tew, D. J., Masters, C. L., Barnham, K. J., Cherny, R. A., & Bush, A. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.028514 · Cited by 131 · see citing works

Uptake and Distribution of Iron and Transferrin in the Adult Rat Brain

Morris, C. M., Keith, A. B., Edwardson, J. A., & Pullen, R. G. L. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08904.x · Cited by 131 · see citing works

Iron Mediates N-Methyl-d-aspartate Receptor-dependent Stimulation of Calcium-induced Pathways and Hippocampal Synaptic Plasticity

Muñoz, P., Humeres, A., Elgueta, C., Kirkwood, A., Hidalgo, C., & Núñez, M. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213785 · Cited by 128 · see citing works

BACE1 Cytoplasmic Domain Interacts with the Copper Chaperone for Superoxide Dismutase-1 and Binds Copper

Angeletti, B., Waldron, K. J., Freeman, K. B., Bawagan, H., Hussain, I., Miller, C. C. J., Lau, K., Tennant, M. E., Dennison, C., Robinson, N. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412034200 · Cited by 125 · see citing works

Increasing striatal iron content associated with normal aging

Martin, W. R. W., Ye, F. Q., & Allen, P. S. (1998) · Movement Disorders · doi:10.1002/mds.870130214 · Cited by 122 · see citing works

Synergy between the C2 allele of transferrin and the C282Y allele of the haemochromatosis gene (<i>HFE</i>) as risk factors for developing Alzheimer’s disease

Robson, K. J. H., Lehmann, D. J., Wimhurst, V. L. C., Livesey, K. J., Combrinck, M., Merryweather-Clarke, A. T., Warden, D. R., & Smith, A. D. (2004) · Journal of Medical Genetics · doi:10.1136/jmg.2003.015552 · Cited by 120 · see citing works

INTERACTIONS OF VITAMIN E AND SELENIUM WITH MERCURY AND SILVER

Ganther, H. E. (1980) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1980.tb21340.x · Cited by 116 · see citing works

β-Amyloid Modulation of Synaptic Transmission and Plasticity

Venkitaramani, D. V., Chin, J., Netzer, W. J., Gouras, G. K., Lesné, S., Malinow, R., & Lombroso, P. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3478-07.2007 · Cited by 115 · see citing works

Amyloid plaques arise from zinc-enriched cortical layers in APP/PS1 transgenic mice and are paradoxically enlarged with dietary zinc deficiency

Stoltenberg, M., Bush, A. I., Bach, G., Smidt, K., Larsen, A., Rungby, J., Lund, S. A., Doering, P., & Danscher, G. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.09.025 · Cited by 114 · see citing works

Differential Effects of Apolipoprotein E Isoforms on Metal-Induced Aggregation of Aβ Using Physiological Concentrations

Moir, R. D., Atwood, C., Romano, D., Laurans, M. H., Huang, X., Bush, A. I., Smith, J. D., & Tanzi, R. E. (1999) · Biochemistry · doi:10.1021/bi982437d · Cited by 111 · see citing works

Promotion of Oxidative Lipid Membrane Damage by Amyloid β Proteins

Murray, I. V. J., Sindoni, M. E., & Axelsen, P. H. (2005) · Biochemistry · doi:10.1021/bi050926p · Cited by 107 · see citing works

Evidence That the ZNT3 Protein Controls the Total Amount of Elemental Zinc in Synaptic Vesicles

Linkous, D. H., Flinn, J. M., Koh, J. Y., Lanzirotti, A., Bertsch, P. M., Jones, B. F., Giblin, L. J., & Frederickson, C. J. (2007) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.6a7035.2007 · Cited by 106 · see citing works

Role of Aspartate-1 in Cu(II) Binding to the Amyloid-β Peptide of Alzheimer's Disease

Karr, J. W., & Szalai, V. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068952d · Cited by 105 · see citing works

Alterations of Zinc Transporter Proteins ZnT‐1, ZnT‐4 and ZnT‐6 in Preclinical Alzheimer's Disease Brain

Ganna Lyubartseva, A., Smith, J. L., Markesbery, W. R., & Lovell, M. A. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00283.x · Cited by 103 · see citing works

Alterations in the interaction between iron regulatory proteins and their iron responsive element in normal and Alzheimer's diseased brains.

Piñero, D. J., Hu, J., & Connor, J. R. (2000) · PubMed · Cited by 102 · see citing works

Selective destabilization of soluble amyloid β oligomers by divalent metal ions

Garai, K., Sengupta, P., Sahoo, B., & Maiti, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.04.056 · Cited by 102 · see citing works

Crystal Structure of the Amyloid-β p3 Fragment Provides a Model for Oligomer Formation in Alzheimer's Disease

Streltsov, V. A., Varghese, J. N., Masters, C. L., & Nuttall, S. D. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4259-10.2011 · Cited by 101 · see citing works

Enhanced Toxicity and Cellular Binding of a Modified Amyloid β Peptide with a Methionine to Valine Substitution

Ciccotosto, G. D., Tew, D. J., Curtain, C. C., Smith, D., Carrington, D., Masters, C. L., Bush, A. I., Cherny, R. A., Cappai, R., & Barnham, K. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406465200 · Cited by 101 · see citing works

Association of transferrin C2 allele with late-onset Alzheimer's disease

Namekata, K., Imagawa, M., Terashi, A., Ohta, S., Oyama, F., & Ihara, Y. (1997) · Human Genetics · doi:10.1007/s004390050600 · Cited by 100 · see citing works

Chromium and parenteral nutrition.

Anderson, R. A. (1995) · PubMed · Cited by 96 · see citing works

Site-Specific Nitration Differentially Influences τ Assembly in Vitro

Reynolds, M. R., Berry, R. W., & Binder, L. I. (2005) · Biochemistry · doi:10.1021/bi051028w · Cited by 96 · see citing works

Divalent metal transporter 1 is involved in amyloid precursor protein processing and Aβ generation

Zheng, W. H., Xin, N., Chi, Z., Zhao, B.-L., Zhang, J., Li, J., & Wang, Z. (2009) · The FASEB Journal · doi:10.1096/fj.09-135749 · Cited by 95 · see citing works

Correlation of R2 with total iron concentration in the brains of rhesus monkeys

Hardy, P., Gash, D., Yokel, R., Andersen, A., Ai, Y., & Zhang, Z.-M. (2005) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.20244 · Cited by 93 · see citing works

Acceleration of brain amyloidosis in an Alzheimer’s disease mouse model by a folate, vitamin B6 and B12-deficient diet

Zhuo, J., & Praticò, D. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.12.005 · Cited by 89 · see citing works

Methionine regulates copper/hydrogen peroxide oxidation products of Aβ

Ali, F. E. A., Separovic, F., Barrow, C. J., Cherny, R. A., Fraser, F. W., Bush, A. I., Masters, C. L., & Barnham, K. J. (2004) · Journal of Peptide Science · doi:10.1002/psc.626 · Cited by 87 · see citing works

In vitro peroxidase oxidation induces stable dimers of β-amyloid (1-42) through dityrosine bridge formation

Galeazzi, L., Ronchi, P., Franceschi, C., & Giunta, S. (1999) · Amyloid · doi:10.3109/13506129908993282 · Cited by 87 · see citing works

Intracellular copper deficiency increases amyloid-β secretion by diverse mechanisms

Cater, M. A., McInnes, K. T., Li, Q., Volitakis, I., Fontaine, S. L., Mercer, J. F. B., & Bush, A. I. (2008) · Biochemical Journal · doi:10.1042/bj20080103 · Cited by 86 · see citing works

ATP7A (Menkes protein) functions in axonal targeting and synaptogenesis

Meskini, R. E., Crabtree, K. L., Cline, L. B., Mains, R. E., Eipper, B. A., & Ronnett, G. V. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.11.018 · Cited by 82 · see citing works

Mapping and characterization of iron compounds in Alzheimer's tissue

Collingwood, J. F., & Dobson, J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-102-308 · Cited by 79 · see citing works

The Structure of Neuritic Plaques in the Cerebral Cortex of Aged Rats

Vaughan, D. W., & Peters, A. (1981) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-198107000-00009 · Cited by 78 · see citing works

Effect of aldehydes derived from oxidative deamination and oxidative stress on β-amyloid aggregation; pathological implications to Alzheimer’s disease

Chen, K., Kazachkov, M., & Yu, P. H. (2007) · Journal of Neural Transmission · doi:10.1007/s00702-007-0697-5 · Cited by 76 · see citing works

Presenilins Promote the Cellular Uptake of Copper and Zinc and Maintain Copper Chaperone of SOD1-dependent Copper/Zinc Superoxide Dismutase Activity

Greenough, M. A., Volitakis, I., Li, Q., Laughton, K. M., Evin, G. M., Ho, M., Dalziel, A. H., Camakaris, J., & Bush, A. I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163964 · Cited by 74 · see citing works

Copper binding to the Alzheimer’s disease amyloid precursor protein

Kong, G. K.-W., Miles, L. A., Crespi, G. A. N., Morton, C. J., Ng, H. L., Barnham, K. J., McKinstry, W. J., Cappai, R., & Parker, M. W. (2007) · European Biophysics Journal · doi:10.1007/s00249-007-0234-3 · Cited by 73 · see citing works

Solution Conformation and Heparin-induced Dimerization of the Full-length Extracellular Domain of the Human Amyloid Precursor Protein

Gralle, M., Oliveira, C. L. P., Guerreiro, L. H., McKinstry, W. J., Galatis, D., Masters, C. L., Cappai, R., Parker, M. W., Ramos, C. H. I., Torriani, I. L., et al. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.12.053 · Cited by 72 · see citing works

Copper Efflux from Murine Microvascular Cells Requires Expression of the Menkes Disease Cu-ATPase

Qian, Y., Tiffany‐Castiglioni, E., Welsh, J., & Harris, E. D. (1998) · Journal of Nutrition · doi:10.1093/jn/128.8.1276 · Cited by 72 · see citing works

Blood-Borne Amyloid-β Dimer Correlates with Clinical Markers of Alzheimer's Disease

Villemagne, V. L., Perez, K. A., Pike, K. E., Kok, W. M., Rowe, C. C., White, A. R., Bourgeat, P., Salvado, O., Bedő, J., Hutton, C. A., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5180-09.2010 · Cited by 71 · see citing works

The Environmental Toxin Arsenite Induces Tau Hyperphosphorylation

Giasson, B. I., Sampathu, D. M., Wilson, C., Vogelsberg-Ragaglia, V., Mushynski, W. E., & Lee, V. M. ‐. (2002) · Biochemistry · doi:10.1021/bi026813c · Cited by 66 · see citing works

Paradoxical Condensation of Copper with Elevated β-Amyloid in Lipid Rafts under Cellular Copper Deficiency Conditions

Hung, Y. H., Robb, E. L., Volitakis, I., Ho, M., Evin, G. M., Li, Q.-X., Culvenor, J. G., Masters, C. L., Cherny, R. A., & Bush, A. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019521 · Cited by 64 · see citing works

Membrane Localization of β-Amyloid 1–42 in Lysosomes

Liu, R., Zhou, Q., Ji, S., Zhou, Q., Feng, D., Wu, Y., & Sui, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.036798 · Cited by 64 · see citing works

Measurement of the Attachment and Assembly of Small Amyloid-β Oligomers on Live Cell Membranes at Physiological Concentrations Using Single-Molecule Tools

Nag, S., Chen, J., Irudayaraj, J., & Maiti, S. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.020 · Cited by 64 · see citing works

Serum copper and zinc in random samples of the population of Northern Ireland

McMaster, D., McCrum, E. E., Patterson, C., et al. (1992) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/56.2.440 · Cited by 64 · see citing works

Clinical findings in a patient withFGFR1 P252R mutation and comparison with the literature

Roscioli, T., Flanagan, S., Kumar, P., Masel, J., Gattas, M. R., Hyland, V. J., & Glass, I. A. (2000) · American Journal of Medical Genetics · doi:10.1002/1096-8628(20000703)93:1 · Cited by 62 · see citing works

Non-haem iron histochemistry of the normal and Alzheimer's disease hippocampus.

Morris, C. M., Kerwin, J. M., & Ja, E. (1994) · PubMed · Cited by 61 · see citing works

Interactions of Aβ25−35 β-Barrel-like Oligomers with Anionic Lipid Bilayer and Resulting Membrane Leakage: An All-Atom Molecular Dynamics Study

Chang, Z., Luo, Y., Zhang, Y., et al. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp107558e · Cited by 57 · see citing works

Transcriptional activation of Alzheimer's β-amyloid precursor protein gene by stress

Dewji, N. N., Do, C., & Bayney, R. M. (1995) · Molecular Brain Research · doi:10.1016/0169-328x(95)00131-b · Cited by 56 · see citing works

Neuroprotection against Aβ and glutamate toxicity by melatonin: Are GABA receptors involved?

Paula-Lima, A. C., Louzada, P. R., Mello, F. G. D., & Ferreira, S. T. (2003) · Neurotoxicity Research · doi:10.1007/bf03033152 · Cited by 53 · see citing works

The role of iron in brain ageing and neurodegenerative disorders

Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819 · see citing works

History and progress of hypotheses and clinical trials for Alzheimer’s disease

Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723 · see citing works

The application of Ferroptosis in diseases

Qiu, Y., Cao, Y., Cao, W., Jia, Y., & Lu, N. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104919 · Cited by 415 · see citing works

SOD2 in mitochondrial dysfunction and neurodegeneration

Flynn, J. M., & Melov, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.027 · Cited by 390 · see citing works

Management of oxidative stress and other pathologies in Alzheimer’s disease

Simunkova, M., Alwasel, S. H., Alhazza, I. M., Jomova, K., Kollar, V., Rusko, M., & Valko, M. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02538-y · Cited by 303 · see citing works

NCOA4-Mediated Ferritinophagy: A Potential Link to Neurodegeneration

Quiles del Rey, M., & Mancias, J. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00238 · Cited by 227 · see citing works

Metals and Neuronal Metal Binding Proteins Implicated in Alzheimer’s Disease

Cristóvão, J. S., Santos, R., & Gomes, C. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9812178 · Cited by 146 · see citing works

Novel upregulation of amyloid-β precursor protein (APP) by microRNA-346 via targeting of APP mRNA 5′-untranslated region: Implications in Alzheimer’s disease

Long, J. M., Maloney, B., Rogers, J. T., & Lahiri, D. K. (2019) · Molecular Psychiatry · doi:10.1038/s41380-018-0266-3 · Cited by 141 · see citing works

Biochemically-defined pools of amyloid-β in sporadic Alzheimer’s disease: correlation with amyloid PET

Roberts, B. R., Lind, M., Wagen, A. Z., Rembach, A., Frugier, T., Li, Q.-X., Ryan, T. M., McLean, C. A., Doecke, J. D., Rowe, C. C., et al. (2017) · Brain · doi:10.1093/brain/awx057 · Cited by 143 · see citing works

Identification of key structural features of the elusive Cu–Aβ complex that generates ROS in Alzheimer’s disease

Cheignon, C., Jones, M., Atrián-Blasco, E., Kieffer, I., Faller, P., Collin, F., & Hureau, C. (2017) · Chemical Science · doi:10.1039/c7sc00809k · Cited by 132 · see citing works

Characterization of biometal profiles in neurological disorders

Pfaender, S., & Grabrucker, A. M. (2014) · Metallomics · doi:10.1039/c4mt00008k · Cited by 117 · see citing works

Copper prevents amyloid-β1–42 from forming amyloid fibrils under near-physiological conditions in vitro

Mold, M., Ouro-Gnao, L., Wieckowski, B. M., & Exley, C. (2013) · Scientific Reports · doi:10.1038/srep01256 · Cited by 101 · see citing works

Iron Deposition Leads to Hyperphosphorylation of Tau and Disruption of Insulin Signaling

Wan, W., Cao, L., Kalionis, B., Murthi, P., Xia, S., & Guan, Y. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00607 · Cited by 84 · see citing works

Unraveling the Burden of Iron in Neurodegeneration: Intersections with Amyloid Beta Peptide Pathology

Uranga, R. M., & Salvador, G. A. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2850341 · Cited by 48 · see citing works

Pratensein attenuates Aβ-induced cognitive deficits in rats: Enhancement of synaptic plasticity and cholinergic function

Wei, L., Lv, S., Huang, Q., Wei, J., Zhang, S., Huang, R., Lu, Z., & Lin, X. (2015) · Fitoterapia · doi:10.1016/j.fitote.2015.01.017 · Cited by 40 · see citing works

Network Analysis of a Membrane-Enriched Brain Proteome across Stages of Alzheimer’s Disease

Higginbotham, L., Dammer, E., Duong, D., Modeste, E., Montine, T., Lah, J., Levey, A., & Seyfried, N. (2019) · Proteomes · doi:10.3390/proteomes7030030 · Cited by 32 · see citing works

P4‐198: Liposomal delivery of a beta sheet blocker peptide for the treatment of Alzheimer's disease

Kumaraswamy, P., Sethuraman, S., & Krishnan, U. M. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.1902 · Cited by 3 · see citing works

A Molecular Dynamics Study on the Binding and Interaction of the Amyloid-Beta (1-42) Peptide with Phospholipid Bilayers

Davis, C. H., & Berkowitz, M. L. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.12.2338

Design of peptide-based inhibitor agent against amyloid-β aggregation: Molecular docking, synthesis and in vitro evaluation

Jokar, S., Erfani, M., Bavi, O., Khazaei, S., Sharifzadeh, M. S., Hajiramezanali, M., Beiki, D., & Shamloo, A. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104050 · Cited by 43 · see citing works

Processing and Secretion of Alzheimer's Disease Amyloid Precursor Protein.

Kinbara, K., KITAGAKI, H., Kinouchi, T., et al. (1994) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.174.209 · Cited by 3 · see citing works

Quantification of the Binding Constant of Copper(II) to the Amyloid-Beta Peptide

Hatcher, L. Q., Hong, L., Bush, W. D., Carducci, T. M., & Simon, J. D. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp710806s · Cited by 114 · see citing works