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Alzheimer's disease, metal ions and metal homeostatic therapy
Abstract
Mounting evidences support the idea that endogenous 'biometals', such as copper, iron, zinc and exogenous ones such as aluminum, can be involved as factors or cofactors in the etiopathogenesis of a variety of neurodegenerative diseases. Alzheimer's disease (AD) is a multifactorial neurodegenerative condition associated with pathological accumulation of amyloid plaques and with the appearance of deposit of neurofibrillary tangles. In AD, the process of beta-amyloid (Abeta) misfolding and plaque aggregation is greatly influenced by alterations in the homeostasis of the aforementioned metal ions. Here, we discuss the most recent evidences that associate metal ion dyshomeostasis with the development of AD. As for aluminum, a role for this ion in AD pathogenesis is still controversial. Thus, here, we also critically review new findings that argue for and against the 'aluminum hypothesis'. Finally, it is discussed how therapeutic strategies aimed at restoring metal homeostasis can delay and modify the progression of AD-related neurodegeneration.
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“Post-mortem examination of the brain suggested that bio-available metals (i.e., copper, zinc, and iron) are found in high concentration in the amyloid plaques.”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [15]
In the citing paper
“However, use of non-specific chelators (i.e., CQ) that do not interact selectively with the Aβ–metal species exhibit adverse side effects that will likely limit their long term clinical use.3,28,29,31,44,46–48”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [28]
In the citing paper
“as well as lead to formation of reactive oxygen species (ROS) and oxidative stress.3,26–31,33–36”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [28]
In the citing paper
“Copper, iron and zinc deposits are observed within the core and periphery of senile plaques, and co-localize with Aβ [539].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [539]
In the citing paper
“Subsequently, there is evidence suggesting that metals similar to iron, zinc, or copper may have a role in AD-related pathogenesis [166].”
From The Multifaceted Role of Neuroprotective Plants in Alzheimer’s Disease Treatment (2022) · cites this paper as [166]
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879
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
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942
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
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
The Dialysis Encephalopathy Syndrome
Alfrey, A. C., LeGendre, G. R., & Kaehny, W. D. (1976) · New England Journal of Medicine · doi:10.1056/nejm197601222940402 · Cited by 1,628
Flagged first, then by citations
2 of the 118 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Lovestone, 1997, The phosphorylation of tau: a critical stage in neurodevelopment and neurodegenerative processes, Neuroscience, 78, 309
Cited by
Sorted by citations
Zhang, J., Zhang, Y., Wang, J., Xia, Y., Zhang, J., & Chen, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01911-3 · Cited by 1,138
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
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683
Metabolism and functions of copper in brain
Scheiber, I. F., Mercer, J. F. B., & Dringen, R. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.01.002 · Cited by 524
Kawahara, M., & Kato-Negishi, M. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/276393 · Cited by 509
8-Hydroxyquinolines: a review of their metal chelating properties and medicinal applications
Prachayasittikul, V., Prachayasittikul, V., Prachayasittikul, S., & Ruchirawat, S. (2013) · Drug Design Development and Therapy · doi:10.2147/dddt.s49763 · Cited by 461
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
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361
Misfolded proteins in Alzheimer's disease and type II diabetes
DeToma, A. S., Salamekh, S., Ramamoorthy, A., & Lim, M. H. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15112f · Cited by 363
Copper: Effects of Deficiency and Overload
Scheiber, I. F., Dringen, R., & Mercer, J. F. B. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_11 · Cited by 349
Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease
Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 291
Choi, J.-S., Braymer, J. J., Nanga, R. P. R., Ramamoorthy, A., & Lim, M. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006091107 · Cited by 264
Metal-associated amyloid-β species in Alzheimer's disease
Pithadia, A. S., & Lim, M. H. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.01.016 · Cited by 259
Neuroprotective Herbs for the Management of Alzheimer’s Disease
Gregory, J., Vengalasetti, Y. V., Bredesen, D. E., & Rao, R. V. (2021) · Biomolecules · doi:10.3390/biom11040543 · Cited by 264
Vural, H., Demirin, H., Kara, Y. B., Eren, İ., & Delibaş, N. (2010) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2010.02.002 · Cited by 235
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Maqbool, M., Mobashir, M., & Hoda, N. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.10.018 · Cited by 235
Tõugu, V., Tiiman, A., & Palumaa, P. (2011) · Metallomics · doi:10.1039/c0mt00073f · Cited by 224
Fluorescent Diagnostic Probes in Neurodegenerative Diseases
Zhou, J., Jangili, P., Son, S., Ji, M. S., Won, M., & Kim, J. S. (2020) · Advanced Materials · doi:10.1002/adma.202001945 · Cited by 204
Metal ions, Alzheimer's disease and chelation therapy
Budimir, A. (2011) · Acta Pharmaceutica · doi:10.2478/v10007-011-0006-6 · Cited by 202
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Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202
Agis-Torres, A., Sollhuber, M., Fernandez, M., & Sanchez-Montero, J. M. (2014) · Current Neuropharmacology · doi:10.2174/1570159x113116660047 · Cited by 202
Chen, W.-T., Liao, Y., Yu, H.-M., Cheng, I. H.-J., & Chen, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177246 · Cited by 199
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Mitochondrial iron metabolism and its role in neurodegeneration
Horowitz, M. P., & Greenamyre, J. T. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100354 · Cited by 195
Corona, C., Masciopinto, F., Silvestri, E., Viscovo, A. D., Lattanzio, R., Sorda, R. L., Ciavardelli, D., Goglia, F., Piantelli, M., Canzoniero, L. M. T., et al. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.73 · Cited by 189
Self-citationLee, S., Zheng, X., Krishnamoorthy, J., Savelieff, M. G., Park, H. M., Brender, J., Kim, J. H., Derrick, J. S., Kochi, A., Lee, H. J., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja409801p · Cited by 186
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
Leal, S. S., Botelho, H. M., & Gomes, C. M. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.04.004 · Cited by 187
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Loef, M., Schrauzer, G. N., & Walach, H. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110414 · Cited by 182
Is aluminum exposure a risk factor for neurological disorders?
Ayaz, A., & Eroglu, E. I. (2018) · Journal of Research in Medical Sciences · doi:10.4103/jrms.jrms_921_17 · Cited by 168
Aluminum, copper, iron and zinc differentially alter amyloid-Aβ1–42 aggregation and toxicity
Bolognin, S., Luigi Messori, A., Drago, D., Gabbiani, C., Cendron, L., & Zatta, P. F. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.02.009 · Cited by 165
Self-citationXie, S., Wang, X., Li, J., Yang, L., & Kong, L. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.03.051 · Cited by 160
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Gupta, R., Luxami, V., & Paul, K. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104633 · Cited by 159
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Bolognin, S., Luigi Messori, A., & Zatta, P. F. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8102-1 · Cited by 159
Self-citationFasae, K. D., Abolaji, A. O., Faloye, T. R., Odunsi, A., Oyetayo, B. O., Enya, J. I., Rotimi, J. A., Akinyemi, R., Whitworth, A. J., & Aschner, M. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126779 · Cited by 161
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Yoon, S. H., Choi, J., Lee, W. Y., & Do, J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9040966 · Cited by 175
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Cristóvão, J. S., Santos, R., & Gomes, C. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9812178 · Cited by 146
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Colomina, M. T., & Peris‐Sampedro, F. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-60189-2_9 · Cited by 146
Derry, P. J., Hegde, M. L., Jackson, G. R., Kayed, R., Tour, J. M., Tsai, A.-L., & Kent, T. A. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101716 · Cited by 146
Najafi, Z., Mahdavi, M. R., Saeedi, M., Karimpour‐Razkenari, E., Edraki, N., Sharifzadeh, M. S., Khanavi, M., & Akbarzadeh, T. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.10.056 · Cited by 141
Lee, M., Yu, W., Shih, Y., Chen, C., Guo, Z., Huang, S., Chan, J. C. C., & Chen, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-23122-x · Cited by 141
Zhao, L., Wang, J., Wang, Y.-R., & Fa, X.-Z. (2012) · Brain Research · doi:10.1016/j.brainres.2012.11.019 · Cited by 140
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Sharma, A. K., Pavlova, S. T., Kim, J., Kim, J., & Mirica, L. M. (2013) · Metallomics · doi:10.1039/c3mt00161j · Cited by 135
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Santos, M. A., Marques, S. M., & Chaves, S. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.08.008 · Cited by 131
Becerril-Ortega, J., Bordji, K., Fréret, T., Rush, T., & Buisson, A. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.04.019 · Cited by 127
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Wang, P., & Wang, Z. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.10.003 · Cited by 123
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Hussain, M. I., Syed, Q. A., Khattak, M. N. K., Hafez, B., Reigosa, M. J., & El‐Keblawy, A. A. (2019) · Biologia · doi:10.2478/s11756-019-00242-x · Cited by 126
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Serafini, M. M., Catanzaro, M., Rosini, M., Racchi, M., & Lanni, C. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.08.004 · Cited by 119
Migliorini, C., Porciatti, E., Łuczkowski, M., & Valensin, D. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.004 · Cited by 117
Nikoomanzari, E., Karbasi, M., Melo, W., Moris, H., Babaei, K., Giannakis, S., & Fattah‐alhosseini, A. (2022) · Chemical Engineering Journal · doi:10.1016/j.cej.2022.136003 · Cited by 112
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Mueed, Z., Tandon, P., Maurya, S. K., Deval, R., Kamal, M. A., & Poddar, N. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.01017 · Cited by 111
Li, S., Wang, X., & Kong, L. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.10.068 · Cited by 110
Prati, F., Cavalli, A., & Bolognesi, M. (2016) · Molecules · doi:10.3390/molecules21040466 · Cited by 110
Liu, R., Meng, F., Zhang, L., Liu, A., Qin, H., Lan, X., Li, L., & Du, G. (2011) · Molecules · doi:10.3390/molecules16032084 · Cited by 103
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Guerrini, L., Arenal, R., Mannini, B., Chiti, F., Pini, R., Matteini, P., & Álvarez‐Puebla, R. A. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b01056 · Cited by 98
Li, S., Wang, X., Xie, S., Jiang, N., Wang, K. D. G., Yao, H., Sun, H., & Kong, L. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.09.024 · Cited by 97
Frontiers in Probing Alzheimer’s Disease Biomarkers with Fluorescent Small Molecules
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Resveratrol and Alzheimer’s disease: message in a bottle on red wine and cognition
Granzotto, A., & Zatta, P. F. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00095 · Cited by 99
Self-citationPrati, F., Bergamini, C., Fato, R., Soukup, O., Korábečný, J., Andrisano, V., Bartolini, M., & Bolognesi, M. L. (2016) · ChemMedChem · doi:10.1002/cmdc.201600014 · Cited by 91
Braymer, J. J., Choi, J.-S., DeToma, A. S., Wang, C., Nam, K., Kampf, J. W., Ramamoorthy, A., & Lim, M. H. (2011) · Inorganic Chemistry · doi:10.1021/ic2012205 · Cited by 89
The missing link in the amyloid cascade of Alzheimer’s disease – Metal ions
Tiiman, A., Palumaa, P., & Tõugu, V. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.023 · Cited by 92
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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
Luqman, M., Ali, Y., Zaghloul, M. M. Y., Sheikh, F. A., Chan, V., & Abdal‐hay, A. (2023) · Journal of Materials Research and Technology · doi:10.1016/j.jmrt.2023.04.219 · Cited by 86
Zhang, C., Du, Q.-Y., Chen, L.-D., Wu, W., Liao, S., Yu, L., & Liang, X. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.03.077 · Cited by 85
Hu, J.-Y., Zhang, D.-L., Liu, X., Li, X.-S., Cheng, X., Chen, J., Du, H., & Liang, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.022 · Cited by 81
Kupershmidt, L., Weinreb, O., Amit, T., Mandel, S. A., Bar‐Am, O., & Youdim, M. B. H. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.03.040 · Cited by 80
Aluminium and Iron in Humans: Bioaccumulation, Pathology, and Removal
Peto, M. V. (2010) · Rejuvenation Research · doi:10.1089/rej.2009.0995 · Cited by 84
Weinreb, O., Amit, T., Mandel, S. A., Kupershmidt, L., & Youdim, M. B. H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2929 · Cited by 80
Huang, M. Y., Xie, S., Jiang, N., Lan, J., Kong, L., & Wang, X. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.12.034 · Cited by 77
Yusufzai, S. K., Khan, M. S., Sulaiman, O., Osman, H., & Lamjin, D. N. (2018) · Chemistry Central Journal · doi:10.1186/s13065-018-0497-z · Cited by 78
Copper(II) interaction with amyloid-β: Affinity and speciation
Arena, G., Pappalardo, G., Sóvágó, I., & Rizzarelli, E. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.012 · Cited by 74
Sales, T. A., Prandi, I. G., de Castro, A. A., Leal, D. H. S., da Cunha, E. F. F., Kuča, K., & Ramalho, T. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081829 · Cited by 73
Vitamin D in Neurological Diseases
Plantone, D., Primiano, G., Manco, C., Locci, S., Servidei, S., & Stefano, N. D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010087 · Cited by 81
Pedersen, J. T., Hureau, C., Hemmingsen, L., Heegaard, N. H. H., Østergaard, J., Vašák, M., & Faller, P. (2012) · Biochemistry · doi:10.1021/bi201774z · Cited by 72
Du, K., Liu, M., Pan, Y., Zhong, X., & Wei, M. (2017) · Nutrients · doi:10.3390/nu9030231 · Cited by 70
Nanogels as Novel Nanocarrier Systems for Efficient Delivery of CNS Therapeutics
Zhang, Y., Zou, Z., Liu, S., Miao, S., & Liu, H. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.954470 · Cited by 69
Yang, X., Cai, P., Liu, Q., Wu, J., Yin, Y., Wang, X., & Kong, L. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.04.043 · Cited by 69
Sharma, A., Pachauri, V., & Flora, S. J. S. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01247 · Cited by 67
Molecular Mechanisms Underlying Neuroinflammation Elicited by Occupational Injuries and Toxicants
Pathak, D., & Sriram, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032272 · Cited by 72
Mannello, F., Tonti, G. A., Medda, V., Simone, P., & Darbre, P. D. (2011) · Journal of Applied Toxicology · doi:10.1002/jat.1641 · Cited by 65
Iron Pathophysiology in Alzheimer’s Diseases
Wang, T., Xu, S.-F., Fan, Y.-G., Li, L.-B., & Guo, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_5 · Cited by 64
Selenoprotein P and selenoprotein M block Zn2+-mediated Aβ42 aggregation and toxicity
Du, X., Li, H., Wang, Z., Qiu, S., Liu, Q., & Ni, J. (2013) · Metallomics · doi:10.1039/c3mt20282h · Cited by 67
The Relationship Between Copper, Iron, and Selenium Levels and Alzheimer Disease
Vaz, F. N. C., Fermino, B. L., Haskel, M. V. L., Wouk, J., Freitas, G. B. L. D., Fabbri, R., Montagna, E., da Rocha, J. B. T., & Bonini, J. S. (2017) · Biological Trace Element Research · doi:10.1007/s12011-017-1042-y · Cited by 62
Saini, N., Oelhafen, S., Hua, H., Georgiev, O., Schaffner, W., & Büeler, H. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.011 · Cited by 63
Air pollution, glymphatic impairment, and Alzheimer's disease
Hussain, R., Graham, U. M., Elder, A. C. P., & Nedergaard, M. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.08.010 · Cited by 66
Wang, X., Xia, C., Chen, S.-B., Tan, J., Ou, T., Huang, S., Li, D., Gu, L., & Huang, Z. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.10.018 · Cited by 60
Huang, W., Lv, D., Yu, H., Sheng, R., Kim, S. C., Wu, P., Luo, K., Li, J. X., & Hu, Y. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.06.042 · Cited by 58
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
Copper Chelators: Chemical Properties and Bio-medical Applications
Tegoni, M., Valensin, D., Toso, L., & Remelli, M. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140601161939 · Cited by 61
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Self-citation
Metadata
- Authors
- Zatta, P., Drago, D., Bolognin, S., & Sensi, S. L.
- Affiliations
- University of Padua (IT)
- University of California, Irvine (US)
- Corresponding author
- Zatta, Paolo
- Sensi, Stefano L.
- Venue
- Trends in Pharmacological Sciences
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 30
- Issue
- 7
- Pages
- 346-355
- ISSN
- 0165-6147 (ISSN-L)
- OpenAlex
- W2025615265
- Cited by
- 369
- References
- 118
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 23 · 2023: 22 · 2022: 18 · 2021: 15 · 2020: 24 · 2019: 19 · 2018: 21 · 2017: 17 · 2016: 25 · 2015: 13 · 2014: 28 · 2013: 19 · 2012: 29
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Pharmacological Sciences (publishedVersion)
- PubMed (publishedVersion)
- 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
- Alzheimer's disease, metal ions, metal homeostasis, copper, iron, zinc, aluminum, amyloid plaques, neurofibrillary tangles, neurodegeneration
- MeSH terms
- Alzheimer Disease, Animals, Homeostasis, Humans, Clioquinol, Metals, Plaque, Amyloid
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