The DOI matches its Crossref record; 132 of the 134 references it cites were found in a registry or an index.
The Role of Zinc in Alzheimer′s Disease
Open accessAbstract
Zinc, the most abundant trace metal in the brain, has numerous functions, both in health and in disease. Zinc is released into the synaptic cleft of glutamatergic neurons alongside glutamate from where it interacts and modulates NMDA and AMPA receptors. In addition, zinc has multifactorial functions in Alzheimer′s disease (AD). Zinc is critical in the enzymatic nonamyloidogenic processing of the amyloid precursor protein (APP) and in the enzymatic degradation of the amyloid‐ β (A β ) peptide. Zinc binds to A β promoting its aggregation into neurotoxic species, and disruption of zinc homeostasis in the brain results in synaptic and memory deficits. Thus, zinc dyshomeostasis may have a critical role to play in the pathogenesis of AD, and the chelation of zinc is a potential therapeutic approach.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Mechanistically, high concentrations of Zinc released into the synaptic cleft can induce neurotoxicity through NMDAR and AMPAR inhibition [548].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [548]
In the citing paper
“Zinc may aggravate AD pathogenesis, as zinc can bind Aβ and promote Aβ accumulation. In addition, the accumulation of zinc can cause synaptic and memory defects [548].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [548]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
2 retracted
RETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009) · Nature · doi:10.1038/nature07767 · Cited by 992
RetractedEndogenous Zinc in Neurological Diseases
Koh, J.-Y. (2005) · Journal of Clinical Neurology · doi:10.3988/jcn.2005.1.2.121 · Cited by 12
RetractedAlzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
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
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
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
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
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 1,365
Edwards, D. R., Handsley, M. M., & Pennington, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,163
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
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 914
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
Bode, W., Gomis‐Rüth, F. X., & Stöckler, W. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80312-i · Cited by 762
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 749
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
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
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 695
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
Hartmann, D. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2615 · Cited by 680
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 668
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 667
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 658
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
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
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×
“Although fibroblasts from ADAM10−/− mice showed no deficiency in α-secretase activity, probably due to compensation by ADAM17 [60], a recent detailed study has provided strong evidence that ADAM10 is the physiologically relevant constitutive α-secretase in primary neurons [61].”
BackgroundHuman 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
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
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
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
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
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
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
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 498
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
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
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
Self-citationLee, 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
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
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 393
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
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
Synaptically released zinc: Physiological functions and pathological effects
Frederickson, C. J., & Bush, A. I. (2001) · BioMetals · doi:10.1023/a:1012934207456 · Cited by 360
Structural aspects of the metzincin clan of metalloendopeptidases
Gomis‐Rüth, F. X. (2003) · Molecular Biotechnology · doi:10.1385/mb:24:2:157 · Cited by 349
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 306
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 305
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
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 301
Amyloid-β peptide levels in brain are inversely correlated with insulysin activity levels in vivo
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
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
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
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
Self-citationLi, 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
Alzheimer disease: progress or profit?
Mount, C., & Downton, C. (2006) · Nature Medicine · doi:10.1038/nm0706-780 · Cited by 262
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
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
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
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 238
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 237
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
Kanemitsu, H., Tomiyama, T., & Mori, H. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00898-x · Cited by 228
McMahon, R. J., & Cousins, R. J. (1998) · Journal of Nutrition · doi:10.1093/jn/128.4.667 · Cited by 223
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
Zinc Metalloproteases In Health And Disease
(1996) · CRC Press eBooks · doi:10.1201/9781482272765 · Cited by 221
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 221
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 219
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
Liu, S.-T., Howlett, G. J., & Barrow, C. J. (1999) · Biochemistry · doi:10.1021/bi990205o · Cited by 199
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
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 193
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 190
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
Self-citationWang, 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 177
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
Kay, A. R. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-17-06847.2003 · Cited by 171
Legendre, P., & Westbrook, G. L. (1990) · The Journal of Physiology · doi:10.1113/jphysiol.1990.sp018266 · Cited by 171
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
Hellström‐Lindahl, E., Ravid, R., & Nordberg, A. K. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.010 · Cited by 167
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 159
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
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
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
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
Apelt, J., Ach, K., & Schliebs, R. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00030-2 · Cited by 140
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
Cole, T. B., Martyanova, A., & Palmiter, R. D. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03220-0 · Cited by 135
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 135
Self-citationZinc‐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
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
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
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
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
Neprilysin and Amyloid Beta Peptide Degradation
Hersh, L. B., & Rodgers, D. W. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954703 · Cited by 127
Slomianka, L., Danscher, G., & Frederickson, C. J. (1990) · Neuroscience · doi:10.1016/0306-4522(90)90076-g · Cited by 119
Jia, Y., Jeng, J., Sensi, S. L., & Weiss, J. H. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.020172 · Cited by 118
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
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
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
Talmard, C., Bouzan, A., & Faller, P. (2007) · Biochemistry · doi:10.1021/bi701355j · Cited by 111
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 107
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
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
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
Smith, J. L., Xiong, S., Markesbery, W. R., & Lovell, M. A. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.02.049 · Cited by 94
Multhaup, G., Bush, A. I., Pollwein, P., & Masters, C. L. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01176-1 · Cited by 92
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
Lovell, M. A., Smith, J. L., Xiong, S., & Markesbery, W. R. (2005) · Neurotoxicity Research · doi:10.1007/bf03033884 · Cited by 91
Lovell, M. A. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0992 · Cited by 87
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
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
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 79
Molnár, P., & Nadler, J. V. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02720-2 · Cited by 79
The AβCs of Aβ-cleaving Proteases*
Leissring, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800022200 · Cited by 78
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
Lin, D. D., Cohen, A. S., & Coulter, D. A. (2001) · Journal of Neurophysiology · doi:10.1152/jn.2001.85.3.1185 · Cited by 76
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
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
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
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
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
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
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
Chou, Y.-H., Halldin, C., & Farde, L. (2000) · Synapse · doi:10.1002/1098-2396(200011)38:2 · Cited by 57
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
Magistretti, J., Castelli, L., Taglietti, V., & Tanzi, F. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00865-5 · Cited by 52
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
Self-citationHaigh, 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
Kay, A. R., & Tóth, K. (2005) · Journal of Neurophysiology · doi:10.1152/jn.00959.2005 · Cited by 33
Measurement of presynaptic zinc changes in hippocampal mossy fibers
Quinta-Ferreira, M. E., Matias, C. M., Arif, M., & Dionı́sio, J. C. (2004) · Brain Research · doi:10.1016/j.brainres.2004.07.054 · Cited by 32
Davenport, A. P., Kuc, R. E., & Mockridge, J. W. (1998) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-199800001-00002 · Cited by 23
Tian, Y., Yang, Z. R., & Zhang, T. (2010) · Neuroscience Research · doi:10.1016/j.neures.2010.07.2030 · Cited by 23
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
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
Self-citation
Research works printed but not linked: 1
- 10.1172/JCI200420864 · DOI · Paper page
Cited by
Sorted by citations
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
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683
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 446
Ashraf, A., Jeandriens, J., Parkes, H. G., & So, P. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101494 · Cited by 306
Samsel, A., & Seneff, S. (2013) · Entropy · doi:10.3390/e15041416 · Cited by 307
Metadata
- Authors
- Watt, N. T., Whitehouse, I. J., & Hooper, N. M.
- Affiliations
- University of Leeds (GB)
- Corresponding author
- Hooper, Nigel M.
- Venue
- International Journal of Alzheimer’s Disease
- Publisher
- Wiley
- Published
- 2010-12-20
- Volume
- 2011
- Issue
- 1
- Pages
- 971021-971021
- ISSN
- 2090-0252 (ISSN-L)
- 2090-8024
- PMC
- PMC3010690
- OpenAlex
- W2012671084
- Cited by
- 148
- References
- 134
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 12 · 2023: 10 · 2022: 10 · 2021: 12 · 2020: 19 · 2019: 5 · 2018: 8 · 2017: 10 · 2016: 7 · 2015: 8 · 2014: 6 · 2013: 4 · 2012: 11
- FWCI
- 4.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- International Journal of Alzheimer s Disease (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- Medical Research Council
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- zinc, Alzheimer's disease, zinc homeostasis, zinc dyshomeostasis, amyloid precursor protein, amyloid-beta, amyloid-beta aggregation, NMDA receptor, AMPA receptors, glutamatergic synapses, synaptic dysfunction, memory impairment, zinc chelation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review