The DOI matches its Crossref record; 76 of the 76 references it cites were found in a registry or an index.
Metal ions, Alzheimer's disease and chelation therapy
Open accessAbstract
Metal ions, Alzheimer's disease and chelation therapy: In the last few years, various studies have been providing evidence that metal ions are critically involved in the pathogenesis of major neurological diseases (Alzheimer, Parkinson). Metal ion chelators have been suggested as potential therapies for diseases involving metal ion imbalance. Neurodegeneration is an excellent target for exploiting the metal chelator approach to therapeutics. In contrast to the direct chelation approach in metal ion overload disorders, in neurodegeneration the goal seems to be a better and subtle modulation of metal ion homeostasis, aimed at restoring ionic balance. Thus, moderate chelators able to coordinate deleterious metals without disturbing metal homeostasis are needed. To date, several chelating agents have been investigated for their potential to treat neurodegeneration, and a series of 8-hydroxyquinoline analogues showed the greatest potential for the treatment of neurodegenerative diseases.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“It is known to transfer metal ions from extracellular environment to intra cellular environment of the cell to maintain metal ion balance and also dissolves Ab-Cu2+/Zn2+aggregates [125, 126].”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [125]
Experimental — accuracy not yet measuredIn the citing paper
“Clioquinol from class 8-hydroxyquinoline has shown better results in treating neurodegenerative disease.”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [125]
In the citing paper
“Interaction of metals with Aβ leads to the generation of ROS as well as abnormal metal ion homeostasis which is linked to the pathogenesis of AD.”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [125]
In the citing paper
“It is a bi-dentate ligand which has 2:1 activity against copper and zinc ions.”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [125]
In the citing paper
“Metal chelators are agents that break the Aβ-metal complex and restore metal ion homeostasis and hence reduce neuro toxicity.”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [125]
In the citing paper
“Consequently, the emergence of CQ as an anti-AD drug has been halted due to potential neurotoxicity and undesirable mutagenic contaminants (Budimir et al., 2011).”
From An update on the novel and approved drugs for Alzheimer disease (2022) · cites this paper as Budimir et al., 2011
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
The 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
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174
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
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
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
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
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
Research works printed but not linked: 2
- C. P. Ferri, R. Sousa, E. Albanese, W. S. Ribeiro and M. Honyashiki, World Alzheimer Report 2009 - Executive Summary (Eds. M. Prince and J. Jadeson), Alzheimer's Disease International, London 2009, pp. 1-22; http://www.alz.co.uk/adi/publications.html
- R. Cherny, 1999, Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion, J. Biol. Chem, 274, 23223, 10.1074/jbc.274.33.23223 · DOI · Paper page
Cited by
Sorted by citations
Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease
Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820
“Chelators do not exhibit strong specific activity towards metal ions as it can deplete its level and lead to abnormal metal ion concentration [125].”
BackgroundExploration of the medical periodic table: towards new targets
Barry, N. P. E., & Sadler, P. J. (2013) · Chemical Communications · doi:10.1039/c3cc41143e · Cited by 720
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683
The outdoor air pollution and brain health workshop
Block, M. L., Elder, A., Auten, R. L., Bilbo, S. D., Chen, H., Chen, J.-C., Cory-Slechta, D. A., Costa, D., Diaz-Sanchez, D., Dorman, D. C., et al. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.08.014 · Cited by 539
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
Krämer, J., Kang, R., Grimm, L., Cola, L. D., Picchetti, P., & Biedermann, F. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00746 · Cited by 464
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
Guzior, N., Wi.eckowska, A., Panek, D., & Malawska, B. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666141106122628 · Cited by 323
Rajasekhar, K., Chakrabarti, M., & Govindaraju, T. (2015) · Chemical Communications · doi:10.1039/c5cc05264e · Cited by 243
Milardi, D., Gazit, E., Radford, S. E., Xu, Y., Gallardo, R. U., Caflisch, A., Westermark, G. T., Westermark, P., Rosa, C. L., & Ramamoorthy, A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00981 · Cited by 199
Polyphenols as Potential Metal Chelation Compounds Against Alzheimer’s Disease
Lakey‐Beitia, J., Burillo, A., Penna, G. L., Hegde, M. L., & Rao, K. S. J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200185 · Cited by 193
Mitochondrial DNA Oxidative Damage and Repair in Aging and Alzheimer's Disease
Santos, R. X., Correia, S. C., Zhu, X., Smith, M. A., Moreira, P. I., Castellani, R. J., Nunomura, A., & Perry, G. L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5039 · Cited by 182
Insights of 8-hydroxyquinolines: A novel target in medicinal chemistry
Gupta, R., Luxami, V., & Paul, K. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104633 · Cited by 159
Functional dissection of astrocyte-secreted proteins: Implications in brain health and diseases
Jha, M. K., Kim, J.-H., Song, G. J., Lee, W., Lee, I. K., Lee, H., An, S. S. A., Kim, S., & Suk, K. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.12.003 · Cited by 156
Dietary strategies for improving iron status: balancing safety and efficacy
Prentice, A. M., Mendoza, Y. A., Pereira, D. I. A., Cerami, C., Wegmüller, R., Constable, A., & Spieldenner, J. (2016) · Nutrition Reviews · doi:10.1093/nutrit/nuw055 · Cited by 150
Role of natural products for the treatment of Alzheimer’s disease
Noori, T., Dehpour, A. R., Sureda, A., Sobarzo-Sanchez, E., & Shirooie, S. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173974 · Cited by 141
Oxidant/antioxidant imbalance and the risk of Alzheimer's disease
Moneim, A. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150325182702 · Cited by 136
López, N., Tormo, C., Blas, I. D., Llinares, I., & Alom, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121528 · Cited by 135
An update on the novel and approved drugs for Alzheimer disease
Alhazmi, H. A., & Albratty, M. (2022) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2022.10.004 · Cited by 122
Zinc Binding Directly Regulates Tau Toxicity Independent of Tau Hyperphosphorylation
Huang, Y., Wu, Z., Cao, Y., Lang, M., Lu, B., & Zhou, B. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.047 · Cited by 116
Pape, V. F. S., Tóth, S., Füredi, A., Szebényi, K., Lovrics, A., Szabó, P. T., Wiese, M., & Szakács, G. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.03.078 · Cited by 114
A New Paradigm for Enzymatic Control of α-Cleavage and β-Cleavage of the Prion Protein
McDonald, A. J., Dibble, J. P., Evans, E. G. B., & Millhauser, G. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.502351 · Cited by 107
Esmieu, C., Guettas, D., Conte‐Daban, A., Sabater, L., Faller, P., & Hureau, C. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b00995 · Cited by 103
A new simple Schiff base fluorescence “on” sensor for Al 3+ and its living cell imaging
Kumar, J., Sarma, M. J., Phukan, P., & Das, D. K. (2015) · Dalton Transactions · doi:10.1039/c4dt03932g · Cited by 94
Gomes, L. M., Vieira, R. P., Jones, M. R., Wang, M. C. P., Dyrager, C., de Souza-Fagundes, E. M., Silva, J. G. D., Storr, T., & Beraldo, H. D. O. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.04.011 · Cited by 94
Prati, 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
A Review on Bioactive Anthraquinone and Derivatives as the Regulators for ROS
Zhao, L., & Zheng, L. (2023) · Molecules · doi:10.3390/molecules28248139 · Cited by 85
Iraji, A., Firuzi, O., Khoshneviszadeh, M., Tavakkoli, M., Mahdavi, M. R., Nadri, H., Edraki, N., & Miri, R. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.09.057 · Cited by 83
The protective role of plant biophenols in mechanisms of Alzheimer's disease
Omar, S. H., Scott, C., Hamlin, A. S., & Obied, H. K. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2017.02.016 · Cited by 84
Nanomaterials toward the treatment of Alzheimer’s disease: Recent advances and future trends
Zeng, H., Qi, Y., Zhang, Z., Liu, C., Peng, W., & Zhang, Y. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.01.014 · Cited by 83
Palanimuthu, D., Poon, R., Sahni, S., Anjum, R., Hibbs, D. E., Lin, H.-Y. J., Bernhardt, P. V., Kalinowski, D. S., & Richardson, D. R. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.08.021 · Cited by 82
Wu, W., Dai, Y.-C., Li, N., Dong, Z., Gu, T., Shi, Z., Xue, X., Tang, Y., & Duan, J. (2017) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2016.1210139 · Cited by 75
The Role of Copper in Tau-Related Pathology in Alzheimer’s Disease
Zubčić, K., Hof, P. R., Šimić, G., & Jembrek, M. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.572308 · Cited by 71
Copper-mediated β-amyloid toxicity and its chelation therapy in Alzheimer's disease
Singh, S. K., Balendra, V., Obaid, A. A., Esposto, J., Tikhonova, M. A., Gautam, N. K., & Pöeggeler, B. (2022) · Metallomics · doi:10.1093/mtomcs/mfac018 · Cited by 68
dos Santos, A. L. S., Sodré, C. L., Valle, R. S., da Silva, B. A. S., Abi-chacra, É. A., Silva, L. V., Souza-Gonçalves, A. L., Sangenito, L. S., Gonçalves, D. D. S., Souza, L. O., et al. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712800609788 · Cited by 71
Design and synthesis of donepezil analogues as dual AChE and BACE-1 inhibitors
Gabr, M. T., & Abdel‐Raziq, M. S. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.06.031 · Cited by 65
A Schiff base fluorescence probe for highly selective turn-on recognition of Zn2+
Zhu, J., Zhang, Y., Chen, Y., Sun, T., Tang, Y., Huang, Y., Yang, Q., Ma, D., Wang, Y., & Wang, M. (2016) · Tetrahedron Letters · doi:10.1016/j.tetlet.2016.12.041 · Cited by 63
Ghorai, A., Mondal, J., Chandra, R., & Patra, G. K. (2015) · Dalton Transactions · doi:10.1039/c5dt01376c · Cited by 62
Strategies, Development, and Pitfalls of Therapeutic Options for Alzheimer's Disease
Haas, C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110986 · Cited by 61
Freitas, L. V. D., da Silva, C. C. P., Ellena, J., Costa, L. A. S., & Rey, N. A. (2013) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2013.06.105 · Cited by 60
Copper Ion Binding Site in β-Amyloid Peptide
Yugay, D., Goronzy, D. P., Kawakami, L. M., Claridge, S. A., Song, T., Yan, Z., Xie, Y., Gilles, J., Yang, Y., & Weiss, P. S. (2016) · Nano Letters · doi:10.1021/acs.nanolett.6b02590 · Cited by 60
Pape, V. F. S., May, N. V., Gál, G. T., Szatmári, I., Szeri, F., Fülöp, F., Szakács, G., & Enyedy, É. A. (2018) · Dalton Transactions · doi:10.1039/c8dt03088j · Cited by 58
Nuclear and mitochondrial DNA oxidation in Alzheimer's disease
Santos, R. X., Correia, S. C., Zhu, X., Lee, H.-G., Petersen, R. B., Nunomura, A., Smith, M. A., Perry, G., & Moreira, P. I. (2012) · Free Radical Research · doi:10.3109/10715762.2011.648188 · Cited by 57
Cell Death via Lipid Peroxidation and Protein Aggregation Diseases
Iuchi, K., Takai, T., & Hisatomi, H. (2021) · Biology · doi:10.3390/biology10050399 · Cited by 56
Cheng, B., Gong, H., Li, X., Sun, Y., Chen, H., Zhang, X., Wu, Q., Zheng, L., & Huang, K. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24216 · Cited by 51
Transition metal nickel prevents Tau aggregation in Alzheimer's disease
Gorantla, N. V., Das, R., Balaraman, E., & Chinnathambi, S. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.11.176 · Cited by 50
Oxidative Stress in Alzheimer’s Disease: Molecular Hallmarks of Underlying Vulnerability
Uddin, M. S., & Kabir, M. T. (2019) · Springer eBooks · doi:10.1007/978-981-13-9636-6_5 · Cited by 50
Jiaranaikulwanitch, J., Govitrapong, P., Fokin, V. V., & Vajragupta, O. (2012) · Molecules · doi:10.3390/molecules17078312 · Cited by 49
Amyloid beta modulators and neuroprotection in Alzheimer's disease: a critical appraisal
Kuruva, C. S., & Reddy, P. H. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.10.010 · Cited by 52
Overdosing on iron: Elevated iron and degenerative brain disorders
D’Mello, S. R., & Kindy, M. S. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220953065 · Cited by 49
Anwar, S., Rehman, W. U., Hussain, R., Khan, S., Alanazi, M. M., Alsaif, N. A., Khan, Y., Iqbal, S., Naz, A., & Hashmı, M. A. (2023) · Pharmaceuticals · doi:10.3390/ph16070909 · Cited by 48
Recent Advances in Targeting Transition Metals (Copper, Iron, and Zinc) in Alzheimer’s Disease
Singh, R., Panghal, A., Jadhav, K., Thakur, A., Verma, R. K., Singh, C., Goyal, M., Kumar, J., & Namdeo, A. G. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04256-8 · Cited by 50
Multi-target iron-chelators improve memory loss in a rat model of sporadic Alzheimer's disease
Šalković‐Petrišić, M., Knezović, A., Barilar, J. O., Smailović, U., Trkulja, V., Riederer, P. F., Amit, T., Mandel, S. A., & Youdim, M. B. H. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.06.026 · Cited by 47
A Molecular Electron Density Theory Study of the Chemical Reactivity of Cis- and Trans-Resveratrol
Frau, J., Muñoz, F., & Glossman‐Mitnik, D. (2016) · Molecules · doi:10.3390/molecules21121650 · Cited by 46
Hauser‐Davis, R. A., Freitas, L. V. D., Cukierman, D. S., Cruz, W. S., Miotto, M., Landeira-Fernández, J., Valiente‐Gabioud, A. A., Fernández, C. O., & Rey, N. A. (2015) · Metallomics · doi:10.1039/c5mt00003c · Cited by 45
Conte‐Daban, A., Day, A. H., Faller, P., & Hureau, C. (2016) · Dalton Transactions · doi:10.1039/c6dt02308h · Cited by 48
Duarte, M. C., Lage, L. M. D. R., Lage, D. P., Mesquita, J. T., Salles, B. C. S., Lavorato, S. N., Menezes‐Souza, D., Roatt, B. M., Alves, R. J., Tavares, C. A. P., et al. (2016) · Veterinary Parasitology · doi:10.1016/j.vetpar.2016.01.002 · Cited by 44
Banerjee, S., Brandão, P., & Saha, A. (2016) · RSC Advances · doi:10.1039/c6ra21217d · Cited by 44
Oxidative Stress and Amyloid Toxicity: Insights From Yeast
França, M. B., Lima, K., & Eleuthério, E. C. A. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25803 · Cited by 43
Cukierman, D. S., Accardo, E., Gomes, R. G., Falco, A. D., Miotto, M., Freitas, M. C. R., Lanznaster, M., Fernández, C. O., & Rey, N. A. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1606-0 · Cited by 42
Kim, D.-K., Park, J., & Choi, B. (2014) · The Journal of Toxicological Sciences · doi:10.2131/jts.39.625 · Cited by 38
Hauser‐Davis, R. A., Silva, J. A. N., Rocha, R. C. C., Saint’Pierre, T. D., Ziolli, R. L., & Arruda, M. A. Z. (2015) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2015.09.001 · Cited by 37
Sgarlata, C., Arena, G., Bonomo, R. P., Giuffrida, A., & Tabbı̀, G. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.12.002 · Cited by 36
Rebalancing metal dyshomeostasis for Alzheimer’s disease therapy
Yang, G., Liu, H., Ma, D., & Leung, C. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01712-y · Cited by 36
Osmani̇ye, D., Ahmad, I., Sağlık, B. N., Levent, S., Patel, H., Özkay, Y., & Kaplancıklı, Z. A. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2139762 · Cited by 35
Duarte, A. E., de Menezes, I. R. A., Morais‐Braga, M. F. B., Leite, N. F., Barros, L. M., Waczuk, E. P., da Silva, M. P., Boligon, A. A., da Rocha, J. B. T., Souza, D. O., et al. (2016) · Molecules · doi:10.3390/molecules21060743 · Cited by 34
Pugazhendhi, A., Shafreen, R. B., Devi, K. P., & Suganthy, N. (2018) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2018.02.081 · Cited by 33
A benzyl carbazate-based fluorescent chemosensor for detecting Zn2+: Application to zebrafish
Kim, S., Lee, H., So, H., Lee, H., Kim, K., & Kim, C. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117787 · Cited by 33
Sağlık, B. N., Levent, S., Osmani̇ye, D., Evren, A. E., Karaduman, A. B., Özkay, Y., & Kaplancıklı, Z. A. (2022) · ACS Omega · doi:10.1021/acsomega.2c06906 · Cited by 33
Guglielmi, P., Secci, D., Petzer, A., Bagetta, D., Chimenti, P., Rotondi, G., Ferrante, C., Recinella, L., Leone, S., Alcaro, S., et al. (2019) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2019.1653864 · Cited by 33
Kaviani, S., Izadyar, M., & Housaindokht, M. R. (2017) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2016.12.012 · Cited by 32
Svobodová, B., Mezeiová, E., Hepnarová, V., Hrabinová, M., Múčková, Ľ., Kobrlová, T., Jun, D., Soukup, O., Jimeno, M. L., Marco, J. L., et al. (2019) · Biomolecules · doi:10.3390/biom9080379 · Cited by 32
The Role of Trace Metals in Alzheimer’s Disease
Benedictis, C. A. D., Vilella, A., & Grabrucker, A. M. (2019) · Codon Publications eBooks · doi:10.15586/alzheimersdisease.2019.ch6 · Cited by 31
Insights of metal 8-hydroxylquinolinol complexes as the potential anticancer drugs
Zhou, X. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.112051 · Cited by 31
Stable iron isotope tracing reveals significant brain iron uptake in adult rats
Chen, J., Shahnavas, S., Singh, N. N., Ong, W.-Y., & Walczyk, T. (2012) · Metallomics · doi:10.1039/c2mt20226c · Cited by 31
Derivatives of Tenuazonic Acid as Potential New Multi-Target Anti-Alzheimer’s Disease Agents
Poliseno, V., Chaves, S., Brunetti, L., Loiodice, F., Carrieri, A., Laghezza, A., Tortorella, P., Magalhães, J. D., Cardoso, S. M., Santos, M. A., et al. (2021) · Biomolecules · doi:10.3390/biom11010111 · Cited by 30
Pape, V. F. S., Türk, D., Szabó, P. T., Wiese, M., Enyedy, É. A., & Szakács, G. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.12.015 · Cited by 30
Discovery of a novel fluorescent probe for the sensitive detection of β-amyloid deposits
Ren, W., Xu, M., Liang, S. H., Xiang, H., Tang, L., Zhang, M., Ding, D., Li, X., Zhang, H., & Hu, Y. (2015) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2015.08.030 · Cited by 31
Effects of aryl methanesulfonate derivatives on acetylcholinesterase and butyrylcholinesterase
Zilbeyaz, K., Stellenboom, N., Güney, M., Öztekіn, A., & Şentürk, M. (2018) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22210 · Cited by 29
Modification of Aβ Peptide Aggregation via Covalent Binding of a Series of Ru(III) Complexes
Gomes, L. M., Bataglioli, J. C., Jussila, A. J., Smith, J. R., Walsby, C. J., & Storr, T. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00838 · Cited by 29
Quinoxaline-based chromogenic and fluorogenic chemosensors for the detection of metal cations
da Silva, L. C., Machado, V. G., & Menezes, F. G. (2021) · Chemical Papers · doi:10.1007/s11696-020-01484-9 · Cited by 29
Drug-like chelating agents: a potential lead for Alzheimer's disease
Huang, W., Wei, W., & Shen, Z. (2014) · RSC Advances · doi:10.1039/c4ra09193k · Cited by 29
Fu, Y., Mu, Y., Lei, H., Wang, P., Li, X., Leng, Q., Han, L., Qu, X., Wang, Z., & Huang, X. (2016) · Molecules · doi:10.3390/molecules21101338 · Cited by 28
Kaur, P., & Sodhi, R. K. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.12.033 · Cited by 28
Dynamic nanoassemblies for imaging and therapy of neurological disorders
Zhang, L., Sun, H., Zhao, J., Lee, J., Low, L. E., Gong, L., Chen, Y., Wang, N., Zhu, C., Lin, P., et al. (2021) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2021.113832 · Cited by 27
Gök, H. N., Luca, S. V., Ay, S. T., Komsta, Ł., Salmas, R. E., Orhan, İ. E., & Skalicka‐Woźniak, K. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130775 · Cited by 27
Mumtaz, A., Majeed, A., Zaib, S., Rahman, S. U., Hameed, S., Saeed, A., Rafique, H., Mughal, E. U., Maalik, A., Hussain, I., et al. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103036 · Cited by 27
D'Acunto, C. W., Kaplánek, R., Gbelcová, H., Kejík, Z., Bříza, T., Vasina, L., Havlík, M., Ruml, T., & Král, V. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.084 · Cited by 26
Keyari, C. M., Kearns, A. K., Duncan, N. S., Eickholt, E. A., Abbott, G., Beall, H. D., & Diaz, P. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301689x · Cited by 25
A DFT study on the metal ion selectivity of deferiprone complexes
Kaviani, S., Izadyar, M., & Housaindokht, M. R. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107267 · Cited by 24
Revisiting Metal Toxicity in Neurodegenerative Diseases and Stroke: Therapeutic Potential.
Mitra, J., Vasquez, V., Hegde, P. M., Boldogh, I. R., MITRA, S. P., Kent, T. A., Rao, K. S. J., & Hegde, M. L. (2014) · PubMed · doi:10.14437/nrtoa-1-107 · Cited by 24
Wallin, C., Luo, J., Jarvet, J., Wärmländer, S. K. T. S., & Gräslund, A. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600105 · Cited by 26
Fernandes, L. D. P., Silva, J. M. B., Martins, D. O. S., Santiago, M. B., Martins, C. H. G., Jardim, A. C. G., Oliveira, G. S., Pivatto, M., Souza, R. A. C., Franca, E. D. F., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218355 · Cited by 22
Evidence of cadmium and mercury involvement in the Aβ42 aggregation process
Meleleo, D., Sblano, C., Storelli, M. M., & Mallamaci, R. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106453 · Cited by 22
Hoque, A., Islam, M. S., Khan, M. A., Ghosh, S., Sekh, M. A., Hussain, S., & Alam, M. A. (2022) · New Journal of Chemistry · doi:10.1039/d2nj03144b · Cited by 21
Hoque, A., Islam, M. S., Khan, S., Datta, B., Zangrando, E., Kole, G. K., & Alam, M. A. (2023) · Dalton Transactions · doi:10.1039/d3dt01512b · Cited by 21
Shervedani, R. K., Rezvaninia, Z., Sabzyan, H., & Boeini, H. Z. (2014) · Analytica Chimica Acta · doi:10.1016/j.aca.2014.03.041 · Cited by 20
Associative Interactions among Zinc, Apolipoprotein E, and Amyloid-β in the Amyloid Pathology
Oh, S. B., Kim, J. A., Park, S., & Lee, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030802 · Cited by 19
Aptamers Selected for Recognizing Amyloid β-Protein—A Case for Cautious Optimism
Rahimi, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030668 · Cited by 18
Metadata
- Authors
- Budimir, A.
- Affiliations
- University of Zagreb (HR)
- Corresponding author
- Budimir, Ana
- ORCID
- Budimir, Ana
- Venue
- Acta Pharmaceutica
- Publisher
- Walter de Gruyter GmbH
- Published
- 2011-03-01
- Volume
- 61
- Issue
- 1
- Pages
- 1-14
- ISSN
- 1330-0075 (ISSN-L)
- 1846-9558
- OpenAlex
- W2033807567
- Cited by
- 202
- References
- 75
- Citations by year
- 2026: 2 · 2025: 9 · 2024: 13 · 2023: 12 · 2022: 14 · 2021: 18 · 2020: 18 · 2019: 15 · 2018: 19 · 2017: 13 · 2016: 18 · 2015: 12 · 2014: 14 · 2013: 12 · 2012: 12
- FWCI
- 1.36
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Acta Pharmaceutica (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- University of Zagreb University Computing Centre (SRCE) (submittedVersion, other-oa)
- Repozitorij Farmaceutsko-biokemijskog fakulteta (Sveučilišta u Zagrebu) (submittedVersion, cc-by)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Heavy Metal Exposure and Toxicity
- Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
- Keywords
- metal ions, Alzheimer's disease, chelation therapy, metal chelators, neurodegeneration, metal homeostasis, Parkinson's disease, metal imbalance
- MeSH terms
- Alzheimer Disease, Animals, Chelating Agents, Homeostasis, Humans, Hydroxyquinolines, Ions, Metals, Neurodegenerative Diseases
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