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

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

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

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

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 1,163

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

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

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 306

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 307

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 208

Metal ions, Alzheimer's disease and chelation therapy

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

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 194

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 126

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 122

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

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

The physiological role of drug transporters

Liang, Y., Li, S., & Chen, L. (2015) · Protein & Cell · doi:10.1007/s13238-015-0148-2 · Cited by 118

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

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 76

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

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 86

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 87

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 86

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

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 70

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 67

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

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 71

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

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 55

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

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

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

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

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

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 48

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 45

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

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

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 45

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 29

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

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 24

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

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

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 26

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 25

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

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

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 25

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

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 21

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 22

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 18

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 19

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 19

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

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 15

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

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 14

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

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

Metal‐mediated Targeting in the Body

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

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

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

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

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

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

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

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 10

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

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

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

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

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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 11

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Xu, L., Wang, X., & Wang, X. (2013) · European Biophysics Journal · doi:10.1007/s00249-013-0906-0 · Cited by 11

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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

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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

Emerging Evidence of Golgi Stress Signaling for Neuropathies

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

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

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

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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

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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

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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 9

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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

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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

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

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

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

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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

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