The Role of Zinc in Alzheimer′s Disease

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063 · 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

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

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

Iron accumulation in Alzheimer disease is a source of redox-generated free radicals

Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357 · 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

Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial

Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988 · see citing works

Reconstitution of γ-secretase activity

Edbauer, D., Winkler, E., Regula, J. T., Pesold, B., Steiner, H., & Haass, C. (2003) · Nature Cell Biology · doi:10.1038/ncb960 · Cited by 882 · see citing works

Micromolar concentrations of Zn2+ antagonize NMDA and GABA responses of hippocampal neurons

Westbrook, G. L., & Mayer, M. L. (1987) · Nature · doi:10.1038/328640a0 · Cited by 852 · see citing works

Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc‐binding environments (HEXXHXXGXXH and Met‐turn) and topologies and should be grouped into a common family, the ‘metzincins’

Bode, W., Gomis‐Rüth, F. X., & Stöckler, W. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80312-i · Cited by 762 · see citing works

Mammalian Zinc Transporters: Nutritional and Physiologic Regulation

Lichten, L. A., & Cousins, R. J. (2009) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-033009-083312 · Cited by 732 · 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

An overview of APP processing enzymes and products.

Chow, V. W., Mattson, M. P., Wong, P. C., & Gleichmann, M. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8104-z · Cited by 684 · 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

Zinc Selectively Blocks the Action of N -Methyl-D-Aspartate on Cortical Neurons

Peters, S., Koh, J., & Choi, D. W. (1987) · Science · doi:10.1126/science.2883728 · Cited by 667 · 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

High-Affinity Zinc Inhibition of NMDA NR1–NR2A Receptors

Paoletti, P., Ascher, P., & Neyton, J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05711.1997 · Cited by 650 · 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

The worldwide societal costs of dementia: Estimates for 2009

Wimo, A., Winblad, B. G., & Jönsson, L. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.01.010 · Cited by 628 · 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 · cited 1× · see citing works

Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo

Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., & Holtzman, D. M. (2006) · Nature Medicine · doi:10.1038/nm1438 · Cited by 599 · see citing works

Zinc is a novel intracellular second messenger

Yamasaki, S., Sakata-Sogawa, K., Hasegawa, A., Suzuki, T., Kabu, K., Sato, E., Kurosaki, T., Yamashita, S., Tokunaga, M., Nishida, K., et al. (2007) · Journal of Cell Biology · doi:10.1083/jcb.200702081 · Cited by 592 · 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

Roles of amyloid β-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment

Butterfield, D. A., Reed, T., Newman, S. F., & Sultana, R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.037 · Cited by 564 · 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

Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene.

Cole, T., Wenzel, H., Kafer, K. E., Schwartzkroin, P., & Palmiter, R. (1999) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.96.4.1716 · Cited by 560 · 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

Neurons Regulate Extracellular Levels of Amyloid β-Protein via Proteolysis by Insulin-Degrading Enzyme

Vekrellis, K., Ye, Z., Qiu, W. Q., Walsh, D. M., Hartley, D. M., Chesneau, V., Rosner, M. R., & Selkoe, D. J. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-05-01657.2000 · Cited by 495 · see citing works

The Actions of Synaptically Released Zinc at Hippocampal Mossy Fiber Synapses

Vogt, K. E., Mellor, J. R., Tong, G., & Nicoll, R. A. (2000) · Neuron · doi:10.1016/s0896-6273(00)81149-6 · Cited by 491 · 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

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

Zinc at glutamatergic synapses

Paoletti, P., Vergnano, A. M., Barbour, B., & Casado, M. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.061 · Cited by 417 · see citing works

Matrix Metalloproteinases Expressed by Astrocytes Mediate Extracellular Amyloid-β Peptide Catabolism

Yin, K.-J., Cirrito, J. R., Yan, P., Hu, X., Xiao, Q., Pan, X., Bateman, R., Song, H., Hsu, F.-F., Turk, J., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2085-06.2006 · Cited by 381 · see citing works

SYMPOSIUM: Clearance of Aβ from the Brain in Alzheimer's Disease: Aβ‐Degrading Enzymes in Alzheimer's Disease

Miners, J. S., Baig, S., Palmer, J. C., Palmer, L. E., Kehoe, P. G., & Love, S. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00132.x · Cited by 380 · 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

Synaptically released zinc: Physiological functions and pathological effects

Frederickson, C. J., & Bush, A. I. (2001) · BioMetals · doi:10.1023/a:1012934207456 · Cited by 360 · see citing works

Structural aspects of the metzincin clan of metalloendopeptidases

Gomis‐Rüth, F. X. (2003) · Molecular Biotechnology · doi:10.1385/mb:24:2:157 · Cited by 339 · 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

Effect of zinc on NMDA receptor-mediated channel currents in cortical neurons

Christine, C. W., & Choi, D. W. (1990) · Journal of Neuroscience · doi:10.1523/jneurosci.10-01-00108.1990 · Cited by 299 · see citing works

Amyloid-β peptide levels in brain are inversely correlated with insulysin activity levels <i>in vivo</i>

Miller, B. C., Eckman, E. A., Sambamurti, K., Dobbs, N., Chow, K. M., Eckman, C. B., Hersh, L. B., & Thiele, D. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031520100 · Cited by 294 · 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

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

Cellular prion protein regulates β-secretase cleavage of the Alzheimer's amyloid precursor protein

Parkin, E. T., Watt, N. T., Hussain, I., Eckman, E. A., Eckman, C. B., Manson, J. C., Baybutt, H. N., Turner, A. J., & Hooper, N. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609621104 · Cited by 274 · see citing works

Rapid Translocation of Zn2+From Presynaptic Terminals Into Postsynaptic Hippocampal Neurons After Physiological Stimulation

Li, Y., Hough, C. J., Suh, S. W., Sarvey, J. M., & Frederickson, C. J. (2001) · Journal of Neurophysiology · doi:10.1152/jn.2001.86.5.2597 · Cited by 263 · see citing works

Alzheimer disease: progress or profit?

Mount, C., & Downton, C. (2006) · Nature Medicine · doi:10.1038/nm0706-780 · Cited by 262 · 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

Lipid Peroxidation and Free Radical Scavengers in Alzheimer’s Disease

Jeandel, C., Nicolas, M. B., Dubois, F., Belleville, F., Penin, F., & Cuny, G. (2009) · Gerontology · doi:10.1159/000213037 · Cited by 250 · see citing works

Zinc and copper: Pharmacological probes and endogenous modulators of neuronal excitability

Mathie, A. A., Sutton, G. L., Clarke, C. E., & Veale, E. L. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.11.004 · Cited by 246 · see citing works

Chapter 6 Zinc-containing neurons in hippocampus and related CNS structures

Frederickson, C. J., & Danscher, G. (1990) · Progress in brain research · doi:10.1016/s0079-6123(08)61242-x · Cited by 239 · see citing works

Mossy fiber Zn2+ spillover modulates heterosynapticN-methyl- d -aspartate receptor activity in hippocampal CA3 circuits

Ueno, S., Tsukamoto, M., Hirano, T., Kikuchi, K., Yamada, M. K., Nishiyama, N., Nagano, T., Matsuki, N., & Ikegaya, Y. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200204066 · 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

Human neprilysin is capable of degrading amyloid β peptide not only in the monomeric form but also the pathological oligomeric form

Kanemitsu, H., Tomiyama, T., & Mori, H. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00898-x · Cited by 228 · see citing works

Mammalian Zinc Transporters ,

McMahon, R. J., & Cousins, R. J. (1998) · Journal of Nutrition · doi:10.1093/jn/128.4.667 · Cited by 223 · see citing works

Zinc toxicity on cultured cortical neurons: Involvement of N-methyl-d-aspartate receptors

Koh, J., & Choi, D. W. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90282-8 · Cited by 222 · see citing works

Zinc Metalloproteases In Health And Disease

(1996) · CRC Press eBooks · doi:10.1201/9781482272765 · Cited by 221 · 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

Differential Sensitivity of RecombinantN-Methyl-d-Aspartate Receptor Subtypes to Zinc Inhibition

Chen, N., Moshaver, A., & Raymond, L. A. (1997) · Molecular Pharmacology · doi:10.1124/mol.51.6.1015 · Cited by 215 · see citing works

Degradation of the Amyloid β-Protein by the Novel Mitochondrial Peptidasome, PreP

Falkevall, A., Alikhani, N., Bhushan, S., Pavlov, P. F., Busch, K., Johnson, K. A., Eneqvist, T., Tjernberg, L. O., Ankarcrona, M., & Glaser, E. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602532200 · Cited by 202 · see citing works

Histidine-13 Is a Crucial Residue in the Zinc Ion-Induced Aggregation of the Aβ Peptide of Alzheimer's Disease

Liu, S.-T., Howlett, G. J., & Barrow, C. J. (1999) · Biochemistry · doi:10.1021/bi990205o · Cited by 199 · see citing works

Regulation of Steady-state β-Amyloid Levels in the Brain by Neprilysin and Endothelin-converting Enzyme but Not Angiotensin-converting Enzyme

Eckman, E. A., Adams, S. K., Troendle, F. J., Stodola, B. A., Kahn, M. A., Fauq, A. H., Xiao, H. D., Bernstein, K. E., & Eckman, C. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605827200 · Cited by 196 · see citing works

Low Micromolar Zinc Accelerates the Fibrillization of Human Tau via Bridging of Cys-291 and Cys-322

Mo, Z., Zhu, Y.-Z., Zhu, H., Fan, J.-B., Chen, J., & Liang, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.058883 · Cited by 189 · see citing works

Neprilysin: An Enzyme Candidate to Slow the Progression of Alzheimer's Disease

El‐Amouri, S. S., Zhu, H., Yu, J., Marr, R. A., Verma, I. M., & Kindy, M. S. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.070620 · Cited by 188 · see citing works

Reactive Oxygen Species-mediated β-Cleavage of the Prion Protein in the Cellular Response to Oxidative Stress

Watt, N. T., Taylor, D. R., Gillott, A., Thomas, D. A., Perera, W. S. S., & Hooper, N. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507327200 · Cited by 179 · see citing works

Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains

Danscher, G., Jensen, K. B., Frederickson, C. J., Kemp, K., Andreasen, A., Juhl, S., Stoltenberg, M., & Ravid, R. (1997) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(97)00079-4 · Cited by 174 · see citing works

Evidence for Chelatable Zinc in the Extracellular Space of the Hippocampus, But Little Evidence for Synaptic Release of Zn

Kay, A. R. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-17-06847.2003 · Cited by 171 · see citing works

The inhibition of single N‐methyl‐D‐aspartate‐activated channels by zinc ions on cultured rat neurones.

Legendre, P., & Westbrook, G. L. (1990) · The Journal of Physiology · doi:10.1113/jphysiol.1990.sp018266 · Cited by 171 · see citing works

Expression and functional profiling of neprilysin, insulin‐degrading enzyme, and endothelin‐converting enzyme in prospectively studied elderly and Alzheimer’s brain

Wang, S., Wang, R., Chen, L., Bennett, D. A., Dickson, D. W., & Wang, D. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06899.x · Cited by 170 · see citing works

Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease

Syme, C. D., & Viles, J. H. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.09.012 · Cited by 167 · see citing works

Age-dependent decline of neprilysin in Alzheimer's disease and normal brain: Inverse correlation with Aβ levels

Hellström‐Lindahl, E., Ravid, R., & Nordberg, A. K. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.010 · Cited by 163 · see citing works

Loss of Neprilysin Function Promotes Amyloid Plaque Formation and Causes Cerebral Amyloid Angiopathy

Farris, W., Schütz, S. G., Cirrito, J. R., Shankar, G. M., Sun, X., George, A., Leissring, M. A., Walsh, D. M., Qiu, W. Q., Holtzman, D. M., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070105 · Cited by 155 · see citing works

Cerebrospinal fluid levels of transition metals in patients with Parkinson's disease

Jiménez‐Jiménez, F. J., Molina, J. A., Aguilar, M. V., Meseguer, I., Mateos-Vega, C. J., González‐Muñoz, M. J., de Bustos, F., Martínez‐Salio, A., Pareja, M. O., Zurdo, M., et al. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050073 · Cited by 151 · 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

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

Binding of Zn(II), Cu(II), and Fe(II) ions to alzheimer's Aß peptide studied by fluorescence

Garzon-Rodriguez, W., Yatsimirsky, A. K., & Glabe, C. G. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00357-1 · Cited by 148 · see citing works

Aging-related down-regulation of neprilysin, a putative β-amyloid-degrading enzyme, in transgenic Tg2576 Alzheimer-like mouse brain is accompanied by an astroglial upregulation in the vicinity of β-amyloid plaques

Apelt, J., Ach, K., & Schliebs, R. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00030-2 · 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

Removing zinc from synaptic vesicles does not impair spatial learning, memory, or sensorimotor functions in the mouse

Cole, T. B., Martyanova, A., & Palmiter, R. D. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03220-0 · Cited by 135 · see citing works

Zinc‐Induced Aggregation of Human and Rat β‐Amyloid Peptides In Vitro

Esler, W. P., Stimson, E. R., Jennings, J. M., Ghilardi, J. R., Mantyh, P. W., & Maggio, J. E. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66020723.x · Cited by 135 · see citing works

Evolutionary Descent of Prion Genes from the ZIP Family of Metal Ion TransportersPreprint

Schmitt‐Ulms, G., Ehsani, S., Watts, J. C., Westaway, D. A., & Wille, H. (2009) · Nature Precedings · doi:10.1371/journal.pone.0007208 · Cited by 135 · see citing works

Zinc Binding to Alzheimer's Aβ(1–16) Peptide Results in Stable Soluble Complex

Kozin, S. A., Zirah, S., Rebuffat, S., Hoa, G. H. B., & Debey, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5284 · Cited by 131 · see citing works

Proteolytic mechanisms in amyloid-β metabolism: therapeutic implications for Alzheimer's disease

Vardy, E. R. L. C., Catto, A. J., & Hooper, N. M. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.08.004 · Cited by 130 · see citing works

Aluminum-triggered structural modifications and aggregation of β-amyloids

Ricchelli, F., Drago, D., Filippi, B., Tognon, G., & Zatta, P. F. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5141-0 · Cited by 128 · see citing works

Copper-Binding Amyloid Precursor Protein Undergoes a Site-Specific Fragmentation in the Reduction of Hydrogen Peroxide

Multhaup, G., Ruppert, T., Schlicksupp, A., Hesse, L., Bill, E., Pipkorn, R., Masters, C. L., & Beyreuther, K. T. (1998) · Biochemistry · doi:10.1021/bi980022m · Cited by 128 · see citing works

Neprilysin and Amyloid Beta Peptide Degradation

Hersh, L. B., & Rodgers, D. W. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954703 · Cited by 127 · see citing works

Labeling of the neurons of origin of zinc-containing pathways by intraperitoneal injections of sodium selenite

Slomianka, L., Danscher, G., & Frederickson, C. J. (1990) · Neuroscience · doi:10.1016/0306-4522(90)90076-g · Cited by 119 · see citing works

Zn ²⁺ currents are mediated by calcium‐permeable AMPA/Kainate channels in cultured murine hippocampal neurones

Jia, Y., Jeng, J., Sensi, S. L., & Weiss, J. H. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.020172 · Cited by 118 · see citing works

The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily.

Bush, A. I., Pettingell, W. H., Paradis, M. D., Tanzi, R. E., & Wasco, W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47062-7 · Cited by 117 · see citing works

Aggregation and Metal‐Binding Properties of Mutant Forms of the Amyloid Aβ Peptide of Alzheimer's Disease

Clements, A., Allsop, D., Walsh, D. M., & Williams, C. H. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66020740.x · Cited by 116 · see citing works

Examining the zinc binding site of the amyloid‐β peptide

Yang, D., McLaurin, J., Qin, K., Westaway, D. A., & Fraser, P. E. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01767.x · Cited by 113 · see citing works

Zinc Binding to Amyloid-β: Isothermal Titration Calorimetry and Zn Competition Experiments with Zn Sensors

Talmard, C., Bouzan, A., & Faller, P. (2007) · Biochemistry · doi:10.1021/bi701355j · Cited by 111 · see citing works

Mechanism of zinc‐induced phosphorylation of p70 S6 kinase and glycogen synthase kinase 3β in SH‐SY5Y neuroblastoma cells

An, W., Björkdahl, C., Liu, R., Cowburn, R. F., Winblad, B. G., & Pei, J.-J. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02948.x · Cited by 106 · 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

Effects of Clioquinol on Metal-Triggered Amyloid-β Aggregation Revisited

Mancino, A. M., Hindo, S. S., Kochi, A., & Lim, M. H. (2009) · Inorganic Chemistry · doi:10.1021/ic9014256 · Cited by 102 · see citing works

Amyloid‐Beta Peptide Forms Monomeric Complexes With CuII and ZnII Prior to Aggregation

Talmard, C., Guilloreau, L., Coppel, Y., Mazarguil, H., & Faller, P. (2006) · ChemBioChem · doi:10.1002/cbic.200600319 · Cited by 96 · see citing works

Altered expression of zinc transporters-4 and -6 in mild cognitive impairment, early and late Alzheimer’s disease brain

Smith, J. L., Xiong, S., Markesbery, W. R., & Lovell, M. A. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.02.049 · Cited by 94 · see citing works

Interaction between the zinc(II) and the heparin binding site of the Alzheimer's disease βA4 amyloid precursor protein (APP)

Multhaup, G., Bush, A. I., Pollwein, P., & Masters, C. L. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01176-1 · Cited by 92 · see citing works

Immunohistochemical localization of neprilysin in the human cerebral cortex: inverse association with vulnerability to amyloid β-protein (Aβ) deposition

Akiyama, H., Kondo, H., Ikeda, K., Kato, M., & McGeer, P. L. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02390-3 · Cited by 92 · see citing works

Alterations in zinc transporter protein-1 (ZnT-1) in the brain of subjects with mild cognitive impairment, early, and late-stage alzheimer’s disease

Lovell, M. A., Smith, J. L., Xiong, S., & Markesbery, W. R. (2005) · Neurotoxicity Research · doi:10.1007/bf03033884 · Cited by 91 · see citing works

A potential role for alterations of zinc and zinc transport proteins in the progression of Alzheimer's disease

Lovell, M. A. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0992 · Cited by 87 · see citing works

Characterization of the ZnII Binding to the Peptide Amyloid‐β1–16 linked to Alzheimer's Disease

Mekmouche, Y., Coppel, Y., Hochgräfe, K., Guilloreau, L., Talmard, C., Mazarguil, H., & Faller, P. (2005) · ChemBioChem · doi:10.1002/cbic.200500057 · Cited by 85 · see citing works

Fluorescence microscopy of stimulated Zn(II) release from organotypic cultures of mammalian hippocampus using a carbonic anhydrase-based biosensor system

Thompson, R. B., Whetsell, W. O., Maliwal, B. P., Fierke, C. A., & Frederickson, C. J. (2000) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(99)00183-1 · Cited by 85 · see citing works

The AβCs of Aβ-cleaving Proteases

Leissring, M. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800022200 · Cited by 84 · see citing works

Synaptically-released zinc inhibits N-methyl-d-aspartate receptor activation at recurrent mossy fiber synapses

Molnár, P., & Nadler, J. V. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02720-2 · Cited by 79 · see citing works

Radioiodinated clioquinol as a biomarker for β‐amyloid: Zn2+ complexes in Alzheimer's disease

Opazo, C., Luza, S., Villemagne, V. L., Volitakis, I., Rowe, C. C., Barnham, K. J., Altschul, D., Masters, C. L., Cherny, R. A., & Bush, A. I. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00196.x · Cited by 76 · see citing works

α‐Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

Fahrenholz, F., GILBERT, S., Kojro, E., Lammich, S., & Postina, R. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06925.x · Cited by 75 · see citing works

Zinc-Induced Augmentation of Excitatory Synaptic Currents and Glutamate Receptor Responses in Hippocampal CA3 Neurons

Lin, D. D., Cohen, A. S., & Coulter, D. A. (2001) · Journal of Neurophysiology · doi:10.1152/jn.2001.85.3.1185 · Cited by 75 · see citing works

Plaque-Associated Overexpression of Insulin-Degrading Enzyme in the Cerebral Cortex of Aged Transgenic Tg2576 Mice With Alzheimer Pathology

Leal, M. C., Dorfman, V. B., Fernández-Gamba, A. C., Frangione, B., Wısnıewskı, T., Castaño, E. M., Sigurdsson, E. M., & Morelli, L. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000235853.70092.ba · Cited by 74 · see citing works

Serum Zinc Levels and Alzheimer's Disease

Rulon, L. L., Robertson, J. D., Lovell, M. A., Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (2000) · Biological Trace Element Research · doi:10.1385/bter:75:1-3:79 · Cited by 71 · see citing works

Investigations of the Molecular Mechanism of Metal-Induced Aβ (1−40) Amyloidogenesis

Lim, K. H., Kim, Y. K., & Chang, Y. (2007) · Biochemistry · doi:10.1021/bi701112z · Cited by 71 · see citing works

Zinc binding properties of the amyloid fragment Aβ(1–16) studied by electrospray-ionization mass spectrometry

Zirah, S., Rebuffat, S., Kozin, S. A., Debey, P., Fournier, F., Lesage, D., & Tabet, J. (2003) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(03)00221-5 · Cited by 70 · see citing works

A direct inhibitory effect of insulin on a cytosolic proteolytic complex containing insulin-degrading enzyme and multicatalytic proteinase.

Duckworth, W. C., Bennett, R. G., & Hamel, F. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31430-8 · Cited by 63 · see citing works

A putative role of the Amyloid Precursor Protein Intracellular Domain (AICD) in transcription.

Słomnicki, L., & Leśniak, W. (2008) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2008-1691 · Cited by 60 · see citing works

ADAM19 is tightly associated with constitutive Alzheimer’s disease APP α-secretase in A172 cells

Tanabe, C., Hotoda, N., Sasagawa, N., Sehara‐Fujisawa, A., Maruyama, K., & Ishiura, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.181 · Cited by 57 · see citing works

Effect of amphetamine on extrastriatal D2 dopamine receptor binding in the primate brain: A PET study

Chou, Y.-H., Halldin, C., & Farde, L. (2000) · Synapse · doi:10.1002/1098-2396(200011)38:2 · Cited by 57 · see citing works

Zn2+ Sensitivity of High- and Low-Voltage Activated Calcium Channels

Sun, H., Hui, K., Lee, D. W. K., & Feng, Z. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.103333 · Cited by 52 · see citing works

Dual effect of Zn2+ on multiple types of voltage-dependent Ca2+ currents in rat palaeocortical neurons

Magistretti, J., Castelli, L., Taglietti, V., & Tanzi, F. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00865-5 · Cited by 52 · 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. R. E., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420864 · Cited by 51 · see citing works

Prion Protein is Reduced in Aging and in Sporadic but not in Familial Alzheimer's Disease

Whitehouse, I. J., Jackson, C. D., Turner, A. J., & Hooper, N. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101071 · Cited by 43 · see citing works

Dominant roles of the polybasic proline motif and copper in the PrP23-89-mediated stress protection response

Haigh, C. L., Drew, S. C., Boland, M. P., Masters, C. L., Barnham, K. J., Lawson, V., & Collins, S. J. (2009) · Journal of Cell Science · doi:10.1242/jcs.043604 · Cited by 43 · see citing works

Influence of Location of a Fluorescent Zinc Probe in Brain Slices on Its Response to Synaptic Activation

Kay, A. R., & Tóth, K. (2005) · Journal of Neurophysiology · doi:10.1152/jn.00959.2005 · Cited by 34 · see citing works

Measurement of presynaptic zinc changes in hippocampal mossy fibers.

Quinta-Ferreira, M., Matias, C., Arif, M., & Dionísio, J. C. (2004) · Brain Research · doi:10.1016/j.brainres.2004.07.054 · Cited by 30 · see citing works

Endothelin-Converting Enzyme in the Human Vasculature: Evidence for Differential Conversion of Big Endothelin-3 by Endothelial and Smooth-Muscle Cells

Davenport, A. P., Kuc, R. E., & Mockridge, J. W. (1998) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-199800001-00002 · Cited by 23 · see citing works

Zinc ion as modulator effects on excitability and synaptic transmission in hippocampal CA1 neurons in Wistar rats

Tian, Y., Yang, Z. R., & Zhang, T. (2010) · Neuroscience Research · doi:10.1016/j.neures.2010.07.2030 · Cited by 23 · see citing works

Fluorescence imaging study of extracellular zinc at the hippocampal mossy fiber synapse

Bastian, C., & Li, Y. V. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.04.047 · Cited by 13 · see citing works

The biological roles of zinc and families of zinc metalloproteases

Hooper, N. M. (1996) · CRC Press eBooks · doi:10.1201/9781482272765-10 · Cited by 9 · see citing works

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works

Bioinorganic Chemistry of Alzheimer’s Disease

Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 672 · see citing works

Copper, zinc and iron in neurodegenerative diseases (Alzheimer's, Parkinson's and prion diseases)

Kozłowski, H., Łuczkowski, M., Remelli, M., & Valensin, D. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.013 · Cited by 438 · see citing works

Iron dyshomeostasis, lipid peroxidation and perturbed expression of cystine/glutamate antiporter in Alzheimer’s disease: Evidence of ferroptosis

Ashraf, A., Jeandriens, J., Parkes, H. G., & So, P. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101494 · Cited by 304 · see citing works

Glyphosate’s Suppression of Cytochrome P450 Enzymes and Amino Acid Biosynthesis by the Gut Microbiome: Pathways to Modern Diseases

Samsel, A., & Seneff, S. (2013) · Entropy · doi:10.3390/e15041416 · Cited by 293 · see citing works

Zinc in the central nervous system: From molecules to behavior

Gower‐Winter, S. D., & Levenson, C. W. (2012) · BioFactors · doi:10.1002/biof.1012 · Cited by 206 · see citing works

Metal ions, Alzheimer's disease and chelation therapy

Budimir, A. (2011) · Acta Pharmaceutica · doi:10.2478/v10007-011-0006-6 · Cited by 202 · see citing works

Zinc oxide nanoparticles for therapeutic purposes in cancer medicine

Wiesmann, N., Tremel, W., & Brieger, J. (2020) · Journal of Materials Chemistry B · doi:10.1039/d0tb00739k · Cited by 187 · see citing works

Chronic Aluminum Intake Causes Alzheimer's Disease: Applying Sir Austin Bradford Hill's Causality Criteria

Walton, J. R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132204 · Cited by 124 · see citing works

Whole-blood metabolomics of dementia patients reveal classes of disease-linked metabolites

Teruya, T., Chen, Y.-J., Fukuji, Y., Kondoh, H., & Yanagida, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022857118 · Cited by 119 · see citing works

Metal Binding Dictates Conformation and Function of the Amyloid Precursor Protein (APP) E2 Domain

Dahms, S. O., Könnig, I., Roeser, D., Gührs, K., Mayer, M., Kaden, D., Multhaup, G., & Than, M. E. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.12.057 · Cited by 110 · see citing works

Zinc Ionophore Activity of Quercetin and Epigallocatechin-gallate: From Hepa 1-6 Cells to a Liposome Model

Dabbagh-Bazarbachi, H., Clergeaud, G., Quesada, I., Ortiz, M., O’Sullivan, C. K., & Fernández-Larrea, J. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5014633 · Cited by 109 · see citing works

The physiological role of drug transporters

Liang, Y., Li, S., & Chen, L. (2015) · Protein & Cell · doi:10.1007/s13238-015-0148-2 · Cited by 109 · see citing works

Absence of amyloid β oligomers at the postsynapse and regulated synaptic Zn2+ in cognitively intact aged individuals with Alzheimer’s disease neuropathology

Bjorklund, N. L., Reese, L. C., Sadagoparamanujam, V.-M., Ghirardi, V., Woltjer, R. L., & Taglialatela, G. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-23 · Cited by 98 · see citing works

Deciphering the Molecular Profile of Plaques, Memory Decline and Neuron Loss in Two Mouse Models for Alzheimer’s Disease by Deep Sequencing

Bouter, Y., Kacprowski, T., Weißmann, R., Dietrich, K., Borgers, H., Brauß, A., Sperling, C., Wirths, O., Albrecht, M., Jensen, L. R., et al. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00075 · Cited by 91 · see citing works

Trehalose Improves Cognition in the Transgenic Tg2576 Mouse Model of Alzheimer’s Disease

Portbury, S. D., Hare, D. J., Sgambelloni, C., Perronnes, K., Portbury, A. J., Finkelstein, D. I., & Adlard, P. A. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170322 · Cited by 87 · see citing works

New coumarin-benzotriazole based hybrid molecules as inhibitors of acetylcholinesterase and amyloid aggregation

Singh, A., Sharma, S., Arora, S., Attri, S., Kaur, P., Gulati, H. K., Bhagat, K., Kumar, N., Singh, H., Singh, J. V., et al. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127477 · Cited by 85 · see citing works

Copper and iron in Alzheimer's disease: a systematic review and its dietary implications

Loef, M., & Walach, H. (2011) · British Journal Of Nutrition · doi:10.1017/s000711451100376x · Cited by 85 · see citing works

Could Alzheimer’s Disease Originate in the Periphery and If So How So?

Morris, G., Berk, M., Maes, M. H. J., & Puri, B. K. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1092-y · Cited by 83 · see citing works

The Chemistry of Neurodegeneration: Kinetic Data and Their Implications

Pavlin, M., Repič, M., Vianello, R., & Mavri, J. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9284-1 · Cited by 75 · see citing works

Environmental toxins and Alzheimer's disease progression

Vasefi, M., Ghaboolian-Zare, E., Abedelwahab, H., & Osu, A. I. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104852 · Cited by 69 · see citing works

The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?

Fichou, Y., Al‐Hilaly, Y. K., Devred, F., Smet‐Nocca, C., Tsvetkov, P. O., Verelst, J., Winderickx, J., Geukens, N., Vanmechelen, E., Perrotin, A., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0682-x · Cited by 63 · see citing works

Zinc diet and Alzheimer's disease: a systematic review

Loef, M., von Stillfried, N., & Walach, H. (2012) · Nutritional Neuroscience · doi:10.1179/1476830512y.0000000010 · Cited by 56 · see citing works

Molecular mechanism of zinc neurotoxicity in Alzheimer’s disease

Narayanan, S. E., Rehuman, N. A., Harilal, S., Vincent, A., Rajamma, R. G., Behl, T., Uddin, M. S., Ashraf, G. M., & Mathew, B. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-10477-w · Cited by 70 · see citing works

Synthesis, spectroscopic characterization, insulin-enhancment, and competitive DNA binding activity of a new Zn(ii) complex with a vitamin B6 derivative—a new fluorescence probe for Zn(ii)

Mukherjee, T., Pessoa, J. C., Kumar, A., & Sarkar, A. R. (2012) · Dalton Transactions · doi:10.1039/c2dt12298g · Cited by 54 · see citing works

Limbic system pathologies associated with deficiencies and excesses of the trace elements iron, zinc, copper, and selenium

Torres-Vega, A., Pliego‐Rivero, B., Otero, G., Gómez‐Oliván, L. M., & Vieyra-Reyes, P. (2012) · Nutrition Reviews · doi:10.1111/j.1753-4887.2012.00521.x · Cited by 54 · see citing works

Novel Fluorinated 8-Hydroxyquinoline Based Metal Ionophores for Exploring the Metal Hypothesis of Alzheimer’s Disease

Liang, S. H., Southon, A. G., Fraser, B. H., Krause‐Heuer, A. M., Zhang, B., Shoup, T. M., Lewis, R., Volitakis, I., Han, Y., Greguric, I. D., et al. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00281 · Cited by 52 · see citing works

Zinc as Allosteric Ion Channel Modulator: Ionotropic Receptors as Metalloproteins

Peralta, F. A., & Huidobro-Toro, J. P. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17071059 · Cited by 51 · see citing works

Metal Nanoparticles in Alzheimer’s Disease

Behera, A., Sa, N., Pradhan, S. P., Swain, S., & Sahu, P. K. (2023) · Journal of Alzheimer's Disease Reports · doi:10.3233/adr-220112 · Cited by 50 · see citing works

Acetylcholinesterase and Aβ Aggregation Inhibition by Heterometallic Ruthenium(II)–Platinum(II) Polypyridyl Complexes

Vyas, N. A., Singh, S. B., Kumbhar, A. S., Ranade, D. S., Walke, G. R., Kulkarni, P. P., Jani, V., Sonavane, U., Joshi, R., & Rapole, S. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b00091 · Cited by 49 · see citing works

Metabolic relationship between diabetes and Alzheimer's Disease affected by Cyclo(His-Pro) plus zinc treatment

Song, M. K., Bischoff, D. S., Song, A. M., Uyemura, K., & Yamaguchi, D. T. (2016) · BBA Clinical · doi:10.1016/j.bbacli.2016.09.003 · Cited by 48 · see citing works

Degradation of Alzheimer’s Amyloid-β by a Catalytically Inactive Insulin-Degrading Enzyme

Sahoo, B. R., Panda, P. K., Liang, W. G., Tang, W., Ahuja, R., & Ramamoorthy, A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166993 · Cited by 47 · see citing works

DNA damage, copper and lead associates with cognitive function among older adults

Meramat, A. A., Rajab, N. F., Shahar, S., & Sharif, R. (2016) · The journal of nutrition health & aging · doi:10.1007/s12603-016-0759-1 · Cited by 44 · see citing works

Highly selective colorimetric detection of Zn(II) ions using label-free silver nanoparticles

Lee, S., Nam, Y.-S., Lee, H., Lee, Y., & Lee, K. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.06.141 · Cited by 43 · see citing works

Neuroprotective and cognitive enhancing effects of a multi-targeted food intervention in an animal model of neurodegeneration and depression

Borre, Y. E., Panagaki, T., Koelink, P. J., Morgan, M. E., Hendriksen, H., Garssen, J., Kraneveld, A. D., Olivier, B., & Oosting, R. S. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.11.009 · Cited by 42 · see citing works

Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments

Wild, K., August, A., Pietrzik, C. U., & Kins, S. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00021 · Cited by 41 · see citing works

Unified theory of Alzheimer’s disease (UTAD): implications for prevention and curative therapy

Nehls, M. (2016) · Journal of Molecular Psychiatry · doi:10.1186/s40303-016-0018-8 · Cited by 41 · see citing works

Histidine-rich branched peptides as Cu( ii ) and Zn( ii ) chelators with potential therapeutic application in Alzheimer's disease

Lakatos, A., Gyurcsik, B., May, N. V., Csendes, Z., Wéber, E., Fülöp, L., & Kiss, T. (2011) · Dalton Transactions · doi:10.1039/c1dt10989h · Cited by 39 · see citing works

Subcellular localised small molecule fluorescent probes to image mobile Zn 2+

Fang, L., & Watkinson, M. (2020) · Chemical Science · doi:10.1039/d0sc04568c · Cited by 39 · see citing works

A Novel hAPP/htau Mouse Model of Alzheimer's Disease: Inclusion of APP With Tau Exacerbates Behavioral Deficits and Zinc Administration Heightens Tangle Pathology

Lippi, S. L. P., Smith, M. L., & Flinn, J. M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00382 · Cited by 35 · see citing works

Neurotoxicity of metal mixtures

Andrade, V., dos Santos, A. P. M., & Aschner, M. (2021) · Advances in neurotoxicology · doi:10.1016/bs.ant.2020.12.003 · Cited by 36 · see citing works

Examining the homeostatic distribution of metals and Zn isotopes in Göttingen minipigs

Mahan, B., Moynier, F., Jørgensen, A. L., Habekost, M., & Siebert, J. (2018) · Metallomics · doi:10.1039/c8mt00179k · Cited by 35 · see citing works

Selective colorimetric sensing of Zn(II) ions using green-synthesized silver nanoparticles: Ficus benjamina extract as reducing and stabilizing agent

Puente, C., Gómez, I., Kharisov, B. I., & López, I. A. (2018) · Materials Research Bulletin · doi:10.1016/j.materresbull.2018.11.045 · Cited by 34 · see citing works

Serum zinc levels and in vivo beta-amyloid deposition in the human brain

Kim, J. W., Byun, M. S., Yi, D., Lee, J. H., Jung, G., Jung, G., Lee, J.-Y., Kang, K. M., Sohn, C., Lee, D. Y., et al. (2021) · Alzheimer s Research & Therapy · doi:10.1186/s13195-021-00931-3 · Cited by 35 · see citing works

Selective, quantitative measurement of releasable synaptic zinc in human autopsy hippocampal brain tissue from Alzheimer's disease patients

Bjorklund, N. L., Sadagoparamanujam, V. M., & Taglialatela, G. (2011) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2011.09.008 · Cited by 34 · see citing works

Zinc involvement in opioid addiction and analgesia – should zinc supplementation be recommended for opioid-treated persons?

Ciubotariu, D., Ghiciuc, C. M., & Lupușoru, C. E. (2015) · Substance Abuse Treatment Prevention and Policy · doi:10.1186/s13011-015-0025-2 · Cited by 33 · see citing works

Oxidative stress in zinc-induced dopaminergic neurodegeneration: Implications of superoxide dismutase and heme oxygenase-1

Singh, B. K., Kumar, A., Ahmad, I., Kumar, V., Patel, D. K., Jain, S. K., & Singh, C. (2011) · Free Radical Research · doi:10.3109/10715762.2011.607164 · Cited by 32 · see citing works

Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ

Huang, J. Q., Ringuet, M. T., Whitten, A. E., Caria, S., Lim, Y. W., Badhan, R., Anggono, V., & Lee, M. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa076 · Cited by 32 · see citing works

Multivariate effects of pH, salt, and Zn2+ ions on Aβ40 fibrillation

Wang, H., Wu, J., Sternke‐Hoffmann, R., Zheng, W., Mörman, C., & Luo, J. (2022) · Communications Chemistry · doi:10.1038/s42004-022-00786-1 · Cited by 28 · see citing works

A Synthetic Peptide with the Putative Iron Binding Motif of Amyloid Precursor Protein (APP) Does Not Catalytically Oxidize Iron

Ebrahimi, K. H., Hagedoorn, P., & Hagen, W. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040287 · Cited by 28 · see citing works

Second Sphere Interactions in Amyloidogenic Diseases

Roy, M., Nath, A. K., Pal, I., & Dey, S. G. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00941 · Cited by 28 · see citing works

PET Neuroimaging Studies of [18F]CABS13 in a Double Transgenic Mouse Model of Alzheimer’s Disease and Nonhuman Primates

Liang, S. H., Holland, J. P., Stephenson, N. A., Kassenbrock, A. R., Rotstein, B. H., Daignault, C. P., Lewis, R., Collier, L., Hooker, J. M., & Vasdev, N. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00055 · Cited by 27 · see citing works

Machine learning techniques to discover genes with potential prognosis role in Alzheimer’s disease using different biological sources

Martínez-Ballesteros, M., García-Heredia, J. M., Nepomuceno-Chamorro, I. A., & Riquelme, J. C. (2016) · Information Fusion · doi:10.1016/j.inffus.2016.11.005 · Cited by 26 · see citing works

Zinc Modulates Several Transcription-Factor Regulated Pathways in Mouse Skeletal Muscle Cells

Ferdowsi, P. V., Ng, R., Adulcikas, J., Sohal, S. S., & Myers, S. (2020) · Molecules · doi:10.3390/molecules25215098 · Cited by 25 · see citing works

Supplementation with zinc in rats enhances memory and reverses an age-dependent increase in plasma copper

Sandusky‐Beltran, L. A., Manchester, B. L., & McNay, E. C. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.07.007 · Cited by 25 · see citing works

RTHLVFFARK-NH2: A potent and selective modulator on Cu2+-mediated amyloid-β protein aggregation and cytotoxicity

Meng, J., Zhang, H., Dong, X., Liu, F., & Sun, Y. P. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.01.012 · Cited by 25 · see citing works

Small Molecules as Regulators of Liquid–Liquid Phase Separation: Mechanisms and Strategies for New Drug Discovery

Usman, A., Yusuf, A., Isah, M. B., Dang, M., & Zhang, X. (2025) · The FASEB Journal · doi:10.1096/fj.202501476r · Cited by 24 · see citing works

Beneficial consequences of probiotic on mitochondrial hippocampus in Alzheimer’s disease

Beltagy, D. M., Nawar, N. F., Mohamed, T. M., Tousson, E., & El-Keey, M. M. (2021) · Journal of Complementary and Integrative Medicine · doi:10.1515/jcim-2020-0156 · Cited by 24 · see citing works

Molecular Tweezers: Supramolecular Hosts with Broad-Spectrum Biological Applications

Shahpasand‐Kroner, H., Siddique, I. A., Malik, R., Linares, G. R., Ivanova, M. I., Ichida, J. K., Weil, T., Münch, J., Sánchez‐García, E., Klärner, F., et al. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000654 · Cited by 25 · see citing works

Diminished brain resilience syndrome: A modern day neurological pathology of increased susceptibility to mild brain trauma, concussion, and downstream neurodegeneration

Seneff, S., & Morley, W. A. (2014) · Surgical Neurology International · doi:10.4103/2152-7806.134731 · Cited by 24 · see citing works

Peroxidase activity of heme bound amyloid β peptides associated with Alzheimer's disease

Roy, M., Pal, I., Nath, A. K., & Dey, S. G. (2020) · Chemical Communications · doi:10.1039/c9cc09758a · Cited by 24 · see citing works

Bioinformatic analysis of the human brain extracellular matrix proteome in neurodegenerative disorders

Freitas, A., Aroso, M., Rocha, S., Ferreira, R. M., Vitorino, R. M. P., & Gómez-Lázaro, M. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15316 · Cited by 20 · see citing works

Lipid rafts: linking prion protein to zinc transport and amyloid-β toxicity in Alzheimer's disease

Watt, N. T., Jarosz-Griffiths, H., & Hooper, N. M. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00041 · Cited by 20 · see citing works

Comparative Analysis of the Inhibitory Mechanism of Aβ 1–42 Aggregation by Diruthenium Complexes

Manna, S. L., Panzetta, V., Natale, C. D., Cipollone, I., Monti, M., Netti, P. A., Terán, A., Sánchez, A. E., Herrero, S., Merlino, A., et al. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c01218 · Cited by 19 · see citing works

Phytochemical analysis and anticholinesterase activity of aril of Myristica fragrans Houtt

Rastegari, A., Manayi, A., Rezakazemi, M., Eftekhari, M., Khanavi, M., Akbarzadeh, T., & Saeedi, M. (2022) · BMC Chemistry · doi:10.1186/s13065-022-00897-9 · Cited by 18 · see citing works

Curcumin Dictates Divergent Fates for the Central Salt Bridges in Amyloid- β 40 and Amyloid- β 42

Chandra, B., Mithu, V. S., Bhowmik, D., Das, A. K., Sahoo, B., Maiti, S., & Madhu, P. K. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.02.043 · Cited by 18 · see citing works

Recent development in plant-mediated zinc oxide nanoparticles with biomedical applications

Ravi, P., & Babu, S. (2025) · Chemical Physics Impact · doi:10.1016/j.chphi.2025.100870 · Cited by 17 · see citing works

Copper Modulates Adult Neurogenesis in Brain Subventricular Zone

Liu, L. L., van Rijn, R. M., & Zheng, W. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179888 · Cited by 16 · see citing works

Upper rim modified calix[4]arene towards selective turn-on fluorescence sensor for spectroscopically silent metal ions

Anandababu, A., Anandan, S., Syed, A., Marraiki, N., & Ashokkumar, M. (2020) · Inorganica Chimica Acta · doi:10.1016/j.ica.2020.120133 · Cited by 16 · see citing works

Extracellular Zn2+-Dependent Amyloid-β1–42 Neurotoxicity in Alzheimer’s Disease Pathogenesis

Sato, Y., Takiguchi, M., Tamano, H., & Takeda, A. (2020) · Biological Trace Element Research · doi:10.1007/s12011-020-02131-w · Cited by 13 · see citing works

Zinc binding with l-dopa peptides

Veldkamp, K., Tubergen, P. J., Swartz, M. A., DeVries, J. T., & Tatko, C. D. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.02.006 · Cited by 13 · see citing works

Insight into inhibition of the human amyloid beta protein precursor (APP: PDB ID 3UMI) using (E)-N-(pyridin-2-ylmethylene)arylamine (L R ) models: structure elucidation of a family of ZnX 2 -L R complexes

Baul, T. S. B., Kundu, S., Singh, P., Shaveta, S., & da Silva, M. F. C. G. (2014) · Dalton Transactions · doi:10.1039/c4dt03151b · Cited by 13 · see citing works

Metal‐mediated Targeting in the Body

Tang, X., & Liang, X. (2012) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12090 · Cited by 13 · see citing works

Combining conformational sampling and selection to identify the binding mode of zinc-bound amyloid peptides with bifunctional molecules

Xu, L., Gao, K., Bao, C., & Wang, X. (2012) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-012-9588-4 · Cited by 11 · see citing works

Zinc Modulation of Neuronal Calcium Sensor Proteins: Three Modes of Interaction with Different Structural Outcomes

Baksheeva, V. E., Tsvetkov, P. O., Zalevsky, A. O., Vladimirov, V. I., Gorokhovets, N. V., Zinchenko, D. V., Permyakov, S. E., Devred, F., & Zernii, E. Y. (2022) · Biomolecules · doi:10.3390/biom12070956 · Cited by 11 · see citing works

A novel 3D-printed centrifugal ultrafiltration method reveals in vivo glycation of human serum albumin decreases its binding affinity for zinc

Jacobs, M., Pinger, C. W., Castiaux, A. D., Maloney, K. J., & Spence, D. M. (2020) · Metallomics · doi:10.1039/d0mt00123f · Cited by 11 · see citing works

Imbalances in Copper or Zinc Concentrations Trigger Further Trace Metal Dyshomeostasis in Amyloid-Beta Producing Caenorhabditis elegans

Metaxas, A. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.755475 · Cited by 10 · see citing works

Cyclen-based chelators for the inhibition of Aβ aggregation: Synthesis, anti-oxidant and aggregation evaluation

Safadi, M. E., Bhadbhade, M. M., Shimmon, R., Baker, A. T., & McDonagh, A. M. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.07.060 · Cited by 10 · see citing works

Extracellular Zn2+-independently attenuated LTP by human amyloid β1-40 and rat amyloid β1-42

Tamano, H., Takiguchi, M., Shimaya, R., Adlard, P. A., Bush, A. I., & Takeda, A. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.05.037 · Cited by 10 · see citing works

Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling

Baksheeva, V. E., Baldin, A. V., Zalevsky, A. O., Nazipova, A. A., Kazakov, A. S., Vladimirov, V. I., Gorokhovets, N. V., Devred, F., Philippov, P. P., Bazhin, A. V., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212602 · Cited by 9 · see citing works

A Brain-Penetrating Foldamer Rescues Aβ Aggregation-Associated Alzheimer’s Disease Phenotypes in In Vivo Models

Baysah, C. Z., Dohoney, R. A., Palanikumar, L., Stillman, N. H., Penney, A. L., Sola, A. D., Paredes, D., Magzoub, M. M., & Kumar, S. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00753 · Cited by 9 · see citing works

Brassica Vegetables: Rich Sources of Neuroprotective Compounds

Beretta, V. H., Palazzolo, C. T., Ramírez, D. A., & Camargo, A. B. (2021) · Springer eBooks · doi:10.1007/978-3-030-61721-9_24 · Cited by 9 · see citing works

Regulation of extracellular Zn2+homeostasis in the hippocampus as a therapeutic target for Alzheimer’s disease

Takeda, A., & Tamano, H. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2015.1029454 · Cited by 9 · see citing works

In vitro structure-specific Zn(II)-induced adipogenesis and structure-function bioreactivity correlations

Halevas, E. G., Tsave, O., Yavropoulou, M. P., Yovos, J. G., Hatzidimitriou, A. G., Psycharis, V., & Salifoglou, A. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.09.002 · Cited by 9 · see citing works

Nutrients in Alzheimer’s Disease: The Interaction of Diet, Drugs and Disease

Liyanage, S. I., Vilekar, P., & Weaver, D. F. (2019) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/cjn.2018.353 · Cited by 10 · see citing works

Characterization of the internal dynamics and conformational space of zinc-bound amyloid β peptides by replica-exchange molecular dynamics simulations

Xu, L., Wang, X., & Wang, X. (2013) · European Biophysics Journal · doi:10.1007/s00249-013-0906-0 · Cited by 9 · see citing works

Roles of ZnT86D in Neurodevelopment and Pathogenesis of Alzheimer Disease in a Drosophila melanogaster Model

Lee, B., Choi, B., Park, Y., Jang, S., Yuan, C., Lim, C., Lee, J. H., Song, G. J., & Cho, K. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911832 · Cited by 8 · see citing works

Synthesis, chemical characterization, and biological investigation of naturally isolated hesperidin and its metal complexes

Abdelgawad, A. A. M., El-Bassossy, T., & Ahmed, F. A. (2024) · Bulletin of the Chemical Society of Ethiopia · doi:10.4314/bcse.v38i2.8 · Cited by 7 · see citing works

Emerging Evidence of Golgi Stress Signaling for Neuropathies

Shirai, R., & Yamauchi, J. (2024) · Neurology International · doi:10.3390/neurolint16020024 · Cited by 7 · see citing works

Correlative analysis of metallomic gene expression and metal ion content within the mouse hippocampus

Mamsa, S. S. A., Ellison, G., Köhn‐Gaone, J., Inder-Smith, K. R., Evans, C. W., Graham, R. M., Howard, D. L., & Hackett, M. J. (2025) · Metallomics · doi:10.1093/mtomcs/mfaf009 · Cited by 7 · see citing works

Investigation of the Effects of Zinc Oxide Nanoparticles on Membrane Damage of Human Neuroblastoma Cell Lineage (SH-SY5Y) and Change of Tau Protein Structure by Spectroscopic Methods

(2021) · Biointerface Research in Applied Chemistry · doi:10.33263/briac125.60326045 · Cited by 7 · see citing works

Investigation of Cyclo-Z Therapeutic Effect on Insulin Pathway in Alzheimer's Rat Model: Biochemical and Electrophysiological Parameters

Acun, A. D., Kantar, D., Er, H., Erkan, O., Derin, N., & Yargıçoğlu, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03334-7 · Cited by 8 · see citing works

The Protective Role of Coffea arabica L. and Crocus sativus L. Against the Neurotoxicity Induced by Chronic Administration of Aluminium Chloride

Elsaid, F. G., Shati, A. A., & Hafez, E. S. E. (2011) · Journal of Pharmacology and Toxicology · doi:10.3923/jpt.2011.647.663 · Cited by 7 · see citing works

((E)-N-(4-(((2-Amino-5-phenylpyridin-3-yl)imino)methyl)pyridin-2-yl)cyclopropanecarboxamide) Ameliorated Aβ1–42-Induced Alzheimer’s Disease in SD Rats by Inhibiting Oxidative Stress and Apoptosis

Ding, Y., Wang, X., Ji, J., Zhang, X., Chen, M., Li, S., Zhang, Q., & Liu, P. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00655 · Cited by 7 · see citing works

Dual roles of tannins as polyphenols and metal complexing agents in the prevention and treatment of Alzheimer's disease: Exploring the potential of dietary interventions

Guan, Q., Cao, Y., Zhang, Y., Zhou, B., Wang, J., Baranenko, D., Cifuentes, A., Ibañez, E., Yuan, C., & Lu, W. (2025) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.105177 · Cited by 8 · see citing works

Difference in ability for extracellular Zn2+ influx between human and rat amyloid β1-42 and its significance

Tamano, H., Suzuki, H., Kobuchi, S., Adlard, P. A., Bush, A. I., & Takeda, A. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.01.005 · Cited by 6 · see citing works

Seeds

Mohammed, S. G. A. A., & Qoronfleh, M. W. (2020) · Advances in neurobiology · doi:10.1007/978-3-030-30402-7_13 · Cited by 6 · see citing works

Adrenergic β receptor activation reduces amyloid β1-42-mediated intracellular Zn2+ toxicity in dentate granule cells followed by rescuing impairment of dentate gyrus LTP

Tamano, H., Ishikawa, Y., Shioya, A., Itoh, R., Oneta, N., Shimaya, R., Egawa, M., Adlard, P. A., Bush, A. I., & Takeda, A. (2020) · NeuroToxicology · doi:10.1016/j.neuro.2020.06.001 · Cited by 6 · see citing works

Modulation of Mitochondrial Dynamics in Primary Hippocampal Cultures of 5xFAD Mice by Mdivi-1, MFP, and Exogenous Zinc

Chaplygina, A. V., & Zhdanova, D. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl44648 · Cited by 5 · see citing works

Griess’s Reagent-Based Azo Compounds Ameliorate Multifaceted Toxicity and Ferroptosis in Alzheimer’s Disease

Kumar, A., Mondal, T., Ramesh, M., Bhoi, J., Samanta, S., & Govindaraju, T. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00998 · Cited by 6 · see citing works

doi:10.4061/2011/971021 Review Article TheRoleofZincinAlzheimer’sDisease

Watt, N. T., Whitehouse, I. J., & Hooper, N. M. (2010)

Brain zinc metabolism and Alzheimer's disease

Zheng, W., & Zhan-you, W. (2012)

A potential role for zinc alterations in the pathogenesis of Alzheimer's disease

Ganna Lyubartseva, A., & Lovell, M. A. (2012) · BioFactors · doi:10.1002/biof.199 · Cited by 30 · see citing works

Disruption of brain zinc homeostasis promotes the pathophysiological progress of Alzheimer's disease.

Li, L.-B., & Wang, Z. (2016) · PubMed · doi:10.14670/hh-11-737 · Cited by 23 · see citing works

Zinc and Alzheimer's disease: is there a direct link?

Cuajungco, M. P., & Lees, G. J. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(97)00002-7 · Cited by 170 · see citing works