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.
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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
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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
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009
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
Intramuscular desferrioxamine in patients with Alzheimer's disease
MCLACHLAN, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)92978-b · Cited by 764
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
Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., Volitakis, I., Liu, X., Smith, J. P., Perez, K., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.018 · Cited by 672
Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo
Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620
EXPERIMENTAL PRODUCTION OF NEUROFIBRILLARY DEGENERATION
KLATZO, I., Wı́sniewski, H. M., & STREICHER, E. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196504000-00002 · Cited by 609
The redox chemistry of the Alzheimer's disease amyloid β peptide
Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608
Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid
Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 587
Therapeutics for Alzheimer's Disease Based on the Metal Hypothesis
Bush, A. I., & Tanzi, R. E. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.001 · Cited by 582
Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (1996) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(96)00203-1 · Cited by 540
E PIDEMIOLOGY OF N EURODEGENERATION
Mayeux, R. P. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.043002.094919 · Cited by 531
Copper in the brain and Alzheimer’s disease
Hung, Y. H., Bush, A. I., & Cherny, R. A. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0600-y · Cited by 503
A Portrait of Alzheimer Secretases--New Features and Familiar Faces
Esler, W. P., & Wolfe, M. S. (2001) · Science · doi:10.1126/science.1064638 · Cited by 493
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
Kozłowski, H., Janicka-Kłos, A., Brasuń, J., Gaggelli, E., Valensin, D., & Valensin, G. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.05.011 · Cited by 481
Alzheimer's disease: Aβ, tau and synaptic dysfunction
LaFerla, F. M., & Oddo, S. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.02.009 · Cited by 477
Good, P. F., Perl, D. P., Bierer, L. M., & Schmeidler, J. (1992) · Annals of Neurology · doi:10.1002/ana.410310310 · Cited by 476
A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients
Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475
Mantyh, P. W., Ghilardi, J. R., Rogers, S. D., DeMaster, E., Allen, C. J., Stimson, E. R., & Maggio, J. E. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03639.x · Cited by 466
NEURODEGENERATIVE DISEASES: New Concepts of Pathogenesis and Their Therapeutic Implications
Skovronsky, D., Lee, V. M. ‐., & Trojanowski, J. Q. (2006) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.1.110304.100113 · Cited by 433
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy
Gaeta, A., & Hider, R. C. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706416 · Cited by 411
Rapid Communication: Characterization of β‐Amyloid Peptide from Human Cerebrospinal Fluid
Vigo‐Pelfrey, C., Lee, D., Keim, P., Lieberburg, I., & Schenk, D. B. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09841.x · Cited by 385
Alzheimer's disease, metal ions and metal homeostatic therapy
Zatta, P., Drago, D., Bolognin, S., & Sensi, S. L. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.05.002 · Cited by 369
EXPERIMENTAL PRODUCTION OF NEUROFIBRILLARY DEGENERATION
Terry, R. D., & Peña, C. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196504000-00003 · Cited by 332
Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332
Metal complexing agents as therapies for Alzheimer’s disease
Bush, A. I. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00120-3 · Cited by 310
Di Vaira, M., Bazzicalupi, C., Orioli, P., Messori, L., Bruni, B., & Zatta, P. (2004) · Inorganic Chemistry · doi:10.1021/ic0494051 · Cited by 292
Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics
Duce, J. A., & Bush, A. I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.003 · Cited by 288
Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900321 · Cited by 285
Hureau, C., & Faller, P. (2009) · Biochimie · doi:10.1016/j.biochi.2009.03.013 · Cited by 259
The C‐Terminus of the β Protein is Critical in Amyloidogenesis a
Jarrett, J., Berger, E. P., & Lansbury, P. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23043.x · Cited by 257
Zinc takes the center stage: its paradoxical role in Alzheimer’s disease
Cuajungco, M. P., & Faget, K. Y. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(02)00219-9 · Cited by 245
Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., YOSHIMASU, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 245
Zheng, H., Gal, S., Weiner, L. M., Bar‐Am, O., Warshawsky, A., Fridkin, M., & Youdim, M. B. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03340.x · Cited by 215
REVIEW: tau protein pathology in Alzheimer’s disease and related disorders
Tolnay, M., & Probst (1999) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.1999.00182.x · Cited by 214
Cui, Z., Lockman, P. R., Atwood, C., Hsu, C. C., Gupte, A., ALLEN, D., & Mumper, R. J. (2004) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2004.07.009 · Cited by 203
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
Lee, J., Friedman, J. E., Angel, I., Kozak, A., & Koh, J. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.01.005 · Cited by 190
Boll, M.-C., Alcaraz-Zubeldia, M., Montes, S., & Rios, C. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9610-3 · Cited by 173
Metal Ion-dependent Effects of Clioquinol on the Fibril Growth of an Amyloid β Peptide
Raman, B., Ban, T., Yamaguchi, K., Sakai, M., Kawai, T., Naiki, H., & Goto, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500309200 · Cited by 158
Minding metals: Tailoring multifunctional chelating agents for neurodegenerative disease
Perez, L. R., & Franz, K. J. (2010) · Dalton Trans. · doi:10.1039/b919237a · Cited by 156
The Role of Zinc in Alzheimer′s Disease
Watt, N. T., Whitehouse, I. J., & Hooper, N. M. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/971021 · Cited by 148
Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer's amyloidogenesis
Dedeoglu, A., Cormier, K., Payton, S., Tseitlin, K. A., Kremsky, J. N., Lai, L., Li, X., Moir, R. D., Tanzi, R. E., Bush, A. I., et al. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.08.016 · Cited by 141
Grossi, C., Francese, S., Casini, A., Rosi, M. C., Luccarini, I., Fiorentini, A., Gabbiani, C., Luigi Messori, A., Moneti, G., & Casamenti, F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1063 · Cited by 131
Ma, Q., Li, Y., Du, J., Liu, H., Kanazawa, K., Nemoto, T., Nakanishi, H., & Zhao, Y. (2006) · Peptides · doi:10.1016/j.peptides.2005.09.002 · Cited by 123
Changes in uptake of vitamin B12 and trace metals in brains of mice treated with clioquinol
Yassin, M. S., Ekblom, J., Xilinas, M., Gottfries, C. G., & Oreland, L. (2000) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(99)00297-x · Cited by 123
The amyloid‐β peptide and its role in Alzheimer's disease
Clippingdale, A. B., Wade, J. D., & Barrow, C. J. (2001) · Journal of Peptide Science · doi:10.1002/psc.324 · Cited by 103
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
Subacute myelo‐optico‐neuropathy: Clioquinol intoxication in humans and animals
Tateishi, J. (2000) · Neuropathology · doi:10.1046/j.1440-1789.2000.00296.x · Cited by 92
Shin, R., Kruck, T. P. A., Murayama, H., & Kitamoto, T. (2003) · Brain Research · doi:10.1016/s0006-8993(02)03893-3 · Cited by 88
Cherny, R. A., Barnham, K. J., Lynch, T., Volitakis, I., Li, Q.-X., McLean, C., Multhaup, G., Beyreuther, K. T., Tanzi, R. E., Masters, C. L., et al. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4285 · Cited by 85
Potential pathogenic role of β-amyloid1–42–aluminum complex in Alzheimer's disease
Drago, D., Bettella, M., Bolognin, S., Cendron, L., Ščančar, J., Milačić, R., Ricchelli, F., Casini, A., Luigi Messori, A., Tognon, G., et al. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.014 · Cited by 82
Hydroxyquinoline based binders: Promising ligands for chelatotherapy?
Budimir, A., Humbert, N., Elhabiri, M., Nierengarten, I., Biruš, M., & Albrecht‐Gary, A. (2010) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2010.08.014 · Cited by 71
Self-citationInvestigations 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
Aggregation of tau protein by aluminum
Scott, C. W., Fieles, A. W., Sygowski, L. A., & Caputo, C. B. (1993) · Brain Research · doi:10.1016/0006-8993(93)90940-o · Cited by 60
Bis-8-hydroxyquinoline ligands as potential anti-Alzheimer agents
Deraeve, C., Piti, M., Mazarguil, H., & Meunier, B. (2007) · New Journal of Chemistry · doi:10.1039/b616085a · Cited by 53
Therapeutic Treatments for Alzheimer's Disease Based on Metal Bioavailability
Crouch, P. J., Barnham, K. J., Bush, A. I., & White, A. R. (2006) · Drug News & Perspectives · doi:10.1358/dnp.2006.19.8.1021492 · Cited by 36
Moret, V., Laras, Y., Pietrancosta, N., Garino, C., Quéléver, G., Rolland, A., Mallet, B., Norreel, J.-C., & Kraus, J. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.03.026 · Cited by 29
Zheng, H., Youdim, M. B. H., Weiner, L. M., & Fridkin, M. (2005) · Journal of Peptide Research · doi:10.1111/j.1399-3011.2005.00289.x · Cited by 27
Vibrational spectra of clioquinol and its Cu(II) complex
Wagner, C. C., Calvo, S., Torre, M. H., & Baran, E. J. (2006) · Journal of Raman Spectroscopy · doi:10.1002/jrs.1654 · Cited by 24
Boldron, C., der Auwera, I. V., Deraeve, C., Gornitzka, H., Wera, S., Pitié, M., LEUVEN, F. V., & Meunier, B. (2005) · ChemBioChem · doi:10.1002/cbic.200500220 · Cited by 21
Molecular Determinants of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2007) · Future Neurology · doi:10.2217/14796708.2.4.397 · Cited by 9
The amyloid‐β peptide and its role in Alzheimer's disease
Clippingdale, A. B., Wade, J. D., & Barrow, C. J. (2001) · Journal of Peptide Science · doi:10.1002/psc.324.abs · Cited by 5
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
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“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
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
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