Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Aβ42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease
Abstract
Metals are found associated with beta-pleated sheets of Abeta42 in vivo and may be involved in their formation. Metal chelation has been proposed as a therapy for Alzheimer's disease on the basis that it may safely dissolve precipitated Abeta peptides. We have followed fibrillisation of Abeta42 in the presence of an additional metal ion (Al(III), Fe(III), Zn(II), Cu(II)) over a period of 32 weeks and we have investigated the dissolution of these aged peptide aggregates in the presence of both desferrioxamine (DFO) and ethylenediaminetetraacetic acid (EDTA). Abeta42 either alone or in the presence of Al(III) or Fe(III) formed beta-pleated sheets of plaque-like amyloids which were dissolved upon incubation with either chelator. Zn(II) inhibited whilst Cu(II) prevented the formation of beta-pleated sheets of Abeta42and neither of these influences were affected by incubation of the aged peptide aggregates with either DFO or EDTA. Freshly prepared solutions of Abeta42 either alone or in the presence of added Al(III) or Fe(III) did not form beta-pleated amyloid in the presence of DFO when incubated for up to 8 weeks. EDTA did not prevent beta-pleated amyloid formation in the same treatments and promoted beta-pleated amyloid formation in the presence of either Zn(II) or Cu(II). The presence of significant concentrations of Al(III) and Fe(III) as contaminants of 'Abeta42 only' preparations suggested that both of these metals were involved in either triggering the formation or stabili…
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Exley et al. showed that both sub- and superstoichiometric concentrations of Cu2+ prevent aggregation of Aβ42 into ThT-positive β-sheet-rich amyloid fibrils.
“Exley et al. have used fluorescence assays and transmission electron microscopy (TEM) to show that both sub- and superstoichiometric concentrations of Cu2+ prevent aggregation of Aβ42 into thioflavin T (ThT)-positive β-sheet-rich amyloid fibrils.17−19”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [17]
Cu2+ by itself is not toxic to N2A cells, but the presence of Cu2+ and either monomeric Aβ42 or soluble Aβ42 oligomers exhibits enhanced cell toxicity.
“while Cu2+ by itself is not toxic to N2A cells, the presence of Cu2+ and either monomeric Aβ42 or soluble Aβ42 oligomers exhibits enhanced cell toxicity.17,18”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [17]
Cites
Still being checked.
Cited by
Sorted by citations
Aggregation-Induced Emission: Together We Shine, United We Soar!
Mei, J., Leung, N. L. C., Kwok, R. T. K., Lam, J. W. Y., & Tang, B. Z. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00263 · Cited by 8,270 · see citing works
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 672 · see citing works
Interactions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's disease
Zucca, F. A., Segura-Aguilar, J., Ferrari, E., Muñoz, P., Paris, I., Sulzer, D., Sarna, T., Casella, L., & Zecca, L. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.09.012 · Cited by 659 · see citing works
Agrawal, M., Saraf, S., Saraf, S., Antimisiaris, S. G., Chougule, M. B., Shoyele, S. A., & Alexander, A. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.05.011 · Cited by 630 · see citing works
Amyloidogenic Protein–Membrane Interactions: Mechanistic Insight from Model Systems
Butterfield, S. M., & Lashuel, H. A. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200906670 · Cited by 586 · see citing works
Lee, W., Loo, C., Bebawy, M., Luk, F., Mason, R. S., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 539 · see citing works
Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530 · see citing works
Kawahara, M., & Kato-Negishi, M. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/276393 · Cited by 509 · see citing works
Brain Insulin Resistance and Deficiency as Therapeutic Targets in Alzheimers Disease
de la Monte, S. M. (2012) · Current Alzheimer Research · doi:10.2174/156720512799015037 · Cited by 446 · see citing works
Han, T., Feng, X., Tong, B., Shi, J., Chen, L., Zhi, J., & Dong, Y. (2011) · Chemical Communications · doi:10.1039/c1cc15681k · Cited by 371 · see citing works
Iron Toxicity in Diseases of Aging: Alzheimer's Disease, Parkinson's Disease and Atherosclerosis
Altamura, S., & Muckenthaler, M. U. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1010 · Cited by 369 · see citing works
Role of Metal Ions in the Self-assembly of the Alzheimer’s Amyloid-β Peptide
Faller, P., Hureau, C., & Berthoumieu, O. (2013) · Inorganic Chemistry · doi:10.1021/ic4003059 · Cited by 355 · see citing works
Iron and Alzheimer’s Disease: From Pathogenesis to Therapeutic Implications
Liu, J., Fan, Y., Yang, Z., Wang, Z., & Guo, C. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00632 · Cited by 286 · see citing works
Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900321 · Cited by 285 · see citing works
Role of Environmental Contaminants in the Etiology of Alzheimer’s Disease: A Review
Yegambaram, M., Manivannan, B., Beach, T. G., & Halden, R. U. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150204121719 · Cited by 277 · see citing works
Low levels of copper disrupt brain amyloid-β homeostasis by altering its production and clearance
Singh, I., Sagare, A. P., Coma, M., Perlmutter, D., Gelein, R. M., Bell, R. D., Deane, R. J., Zhong, E., Parisi, M., Ciszewski, J. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302212110 · Cited by 253 · see citing works
Homeostasis and metabolism of iron and other metal ions in neurodegenerative diseases
Chen, L., Shen, Q.-Q., Liu, Y.-J., Zhang, Y., Sun, L., Ma, X.-Z., Song, N., & Xie, J.-X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02071-0 · Cited by 261 · see citing works
High‐resolution NMR studies of the zinc‐binding site of the Alzheimer's amyloid β‐peptide
Danielsson, J., Pierattelli, R., Banci, L., & Gräslund, A. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05563.x · Cited by 253 · see citing works
X‐ray fluorescence microprobe imaging in biology and medicine
Paunesku, T., Vogt, S., Maser, J. M., Lai, B. C. H., & Woloschak, G. E. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21047 · Cited by 251 · see citing works
Clioquinol: Review of its Mechanisms of Action and Clinical Uses in Neurodegenerative Disorders
Bareggi, S. R., & Cornelli, U. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00231.x · Cited by 247 · see citing works
Tõugu, V., Tiiman, A., & Palumaa, P. (2011) · Metallomics · doi:10.1039/c0mt00073f · Cited by 222 · see citing works
Mandel, S. A., Amit, T., Weinreb, O., Reznichenko, L., & Youdim, M. B. H. (2008) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2008.00060.x · Cited by 222 · see citing works
Guo, C., Wang, T., Zheng, W. H., Shan, Z., Teng, W., & Wang, Z. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.05.009 · Cited by 200 · see citing works
Iron(II) Binding to Amyloid-β, the Alzheimer’s Peptide
Garah, F. E., Bijani, C., Coppel, Y., Faller, P., & Hureau, C. (2011) · Inorganic Chemistry · doi:10.1021/ic201233b · Cited by 199 · see citing works
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 · see citing works
Metal swap between Zn7-metallothionein-3 and amyloid-β–Cu protects against amyloid-β toxicity
Meloni, G., Sonois, V., Delaine, T., Guilloreau, L., Gillet, A., Teissié, J., Faller, P., & Vašák, M. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.89 · Cited by 190 · see citing works
Understanding Aspects of Aluminum Exposure in A lzheimer's Disease Development
Kandimalla, R. J. L., Vallamkondu, J., Corgiat, E. B., & Gill, K. D. (2015) · Brain Pathology · doi:10.1111/bpa.12333 · Cited by 182 · see citing works
Hureau, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.037 · Cited by 178 · see citing works
A brief overview of amyloids and Alzheimer's disease
Ow, S., & Dunstan, D. E. (2014) · Protein Science · doi:10.1002/pro.2524 · Cited by 178 · see citing works
Telling, N. D., Everett, J. L., Collingwood, J. F., Dobson, J., van der Laan, G., Gallagher, J. J., Wang, J., & Hitchcock, A. P. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.07.014 · Cited by 170 · see citing works
Self-citationChallenges Associated with Metal Chelation Therapy in Alzheimer's Disease
Hegde, M. L., Bharathi, P., Suram, A., Venugopal, C., Jagannathan, R., Poddar, P., Srinivas, P., Sambamurti, K., Rao, K. S. J., Ščančar, J., et al. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1068 · Cited by 166 · see citing works
Yumoto, S., Kakimi, S., Ohsaki, A., & Ishikawa, A. (2009) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.07.023 · Cited by 166 · see citing works
Mandel, S., Amit, T., Bar-Am, O., & Youdim, M. B. H. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.06.001 · Cited by 164 · see citing works
Walton, J. R., & Wang, M.-X. (2009) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.07.027 · Cited by 158 · see citing works
Mitochondrial iron homeostasis and its dysfunctions in neurodegenerative disorders
Mena, N. P., Urrutia, P. J., Lourido, F., Carrasco, C. M., & Núñez, M. T. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.02.001 · Cited by 154 · see citing works
Roles of Oxidative Stress in Synaptic Dysfunction and Neuronal Cell Death in Alzheimer’s Disease
Plascencia-Villa, G., & Perry, G. (2023) · Antioxidants · doi:10.3390/antiox12081628 · Cited by 149 · see citing works
Neuroprotective mechanisms of ayurvedic antidementia botanical <i>Bacopa monniera</i>
Dhanasekaran, M., Tharakan, B., Holcomb, L. A., Hitt, A. R., Young, K. A., & Manyam, B. V. (2007) · Phytotherapy Research · doi:10.1002/ptr.2195 · Cited by 148 · see citing works
Collingwood, J. F., Chong, R. K. K., Kasama, T., Cervera-Gontard, L., Dunin-Borkowski, R. E., Perry, G., Pósfai, M., Siedlak, S. L., Simpson, E. T., Smith, M. A., et al. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-14211 · Cited by 147 · see citing works
Self-citationFarr, A. C., & Xiong, M. P. (2020) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c00474 · Cited by 151 · see citing works
Why is the amyloid beta peptide of Alzheimer’s disease neurotoxic?
Rauk, A. (2008) · Dalton Transactions · doi:10.1039/b718601k · Cited by 139 · see citing works
Structure and function of amyloid in Alzheimer's disease
Morgan, C., Colombres, M., Núñez, M. T., & Inestrosa, N. C. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.10.004 · Cited by 136 · see citing works
Metal ions and oxidative protein modification in neurological disease.
Sayre, L. M., Moreira, P. I., Smith, M. A., & Perry, G. L. (2005) · PubMed · Cited by 135 · see citing works
A Synthetic Circuit for Mercury Bioremediation Using Self-Assembling Functional Amyloids
Tay, P. K. R., Nguyen, P. Q., & Joshi, N. S. (2017) · ACS Synthetic Biology · doi:10.1021/acssynbio.7b00137 · Cited by 133 · see citing works
Metal chelating ability and antioxidant properties of Curcumin-metal complexes – A DFT approach
Mary, C. P. V., Vijayakumar, S., & Shankar, R. (2017) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2017.10.022 · Cited by 133 · see citing works
Appraising the Role of Iron in Brain Aging and Cognition: Promises and Limitations of MRI Methods
Daugherty, A. M., & Raz, N. (2015) · Neuropsychology Review · doi:10.1007/s11065-015-9292-y · Cited by 131 · see citing works
Exley, C. (2006) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2005.086553 · Cited by 129 · see citing works
Self-citationAmit, T., Avramovich‐Tirosh, Y., Youdim, M. B. H., & Mandel, S. (2008) · The FASEB Journal · doi:10.1096/fj.07-8627rev · Cited by 126 · see citing works
Uddin, M. S., Kabir, M. T., Rahman, M. S., Behl, T., Jeandet, P., Ashraf, G. M., Najda, A., Bin-Jumah, M. N., El-Seedi, H. R., & Abdel‐Daim, M. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165858 · Cited by 127 · see citing works
Walton, J. R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132204 · Cited by 124 · see citing works
Shi, X., Wang, H., Han, T., Feng, X., Tong, B., Shi, J., Zhi, J., & Dong, Y. (2012) · Journal of Materials Chemistry · doi:10.1039/c2jm33393g · Cited by 120 · see citing works
Poudel, P., & Park, S. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14040835 · Cited by 124 · see citing works
Molecular mechanisms of aluminum neurotoxicity: Update on adverse effects and therapeutic strategies
Skalny, A. V., Aschner, M., Jiang, Y., Gluhcheva, Y. G., Tizabi, Y., Łobiński, R., & Tinkov, A. A. (2021) · Advances in neurotoxicology · doi:10.1016/bs.ant.2020.12.001 · Cited by 123 · see citing works
Maity, S. B., & Bharadwaj, P. K. (2013) · Inorganic Chemistry · doi:10.1021/ic301915s · Cited by 112 · see citing works
Rana, M., & Sharma, A. K. (2018) · Metallomics · doi:10.1039/c8mt00203g · Cited by 113 · see citing works
Multifunctional Neuroprotective Derivatives of Rasagiline as Anti-Alzheimer's Disease Drugs
Weinreb, O., Mandel, S. A., Bar‐Am, O., Yogev‐Falach, M., Avramovich‐Tirosh, Y., Amit, T., & Youdim, M. B. H. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.10.030 · Cited by 109 · see citing works
Effect of Zinc Binding on β-Amyloid Structure and Dynamics: Implications for Aβ Aggregation
Rezaei‐Ghaleh, N., Giller, K., Becker, S., & Zweckstetter, M. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.06.062 · Cited by 107 · see citing works
The Role of Adenosine in Alzheimers Disease
Rahman, A. (2009) · Current Neuropharmacology · doi:10.2174/157015909789152119 · Cited by 104 · see citing works
Metal binding sites in amyloid oligomers: Complexes and mechanisms
Miller, Y., Ma, B., & Nussinov, R. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.12.022 · Cited by 103 · see citing works
The coordination chemistry of aluminium in neurodegenerative disease
Exley, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.02.020 · Cited by 103 · see citing works
Self-citationMold, M., Ouro-Gnao, L., Wieckowski, B. M., & Exley, C. (2013) · Scientific Reports · doi:10.1038/srep01256 · Cited by 101 · see citing works
Self-citationAge-related differences in iron content of subcortical nuclei observed in vivo: A meta-analysis
Daugherty, A. M., & Raz, N. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.12.040 · Cited by 101 · see citing works
Copper(II) inhibits the formation of amylin amyloid in vitro
Ward, B., Walker, K., & Exley, C. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.09.010 · Cited by 99 · see citing works
Self-citationThe Relevance of Metals in the Pathophysiology of Neurodegeneration, Pathological Considerations
Jellinger, K. A. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00002-8 · Cited by 99 · see citing works
Chelation therapy for neurodegenerative diseases
Bolognin, S., Drago, D., Luigi Messori, A., & Zatta, P. F. (2009) · Medicinal Research Reviews · doi:10.1002/med.20148 · Cited by 97 · see citing works
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 · see citing works
Nanoparticle and Iron Chelators as a Potential Novel Alzheimer Therapy
Liu, G., Men, P., Perry, G. L., & Smith, M. A. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-029-8_8 · Cited by 95 · see citing works
The Aluminium-Amyloid Cascade Hypothesis and Alzheimer’s Disease
Exley, C. (2005) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/0-387-23226-5_11 · Cited by 93 · see citing works
Self-citationDomingo, J. L. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-102-315 · Cited by 91 · see citing works
Khan, A., Dobson, J., & Exley, C. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.013 · Cited by 90 · see citing works
Self-citationHölscher, C. (2005) · Reviews in the Neurosciences · doi:10.1515/revneuro.2005.16.3.181 · Cited by 82 · see citing works
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 · see citing works
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 79 · see citing works
Fluorescence-Based Aluminum Ion Sensing Using a Surface-Functionalized Microstructured Optical Fiber
Warren-Smith, S. C., Heng, S. C. H., Ebendorff‐Heidepriem, H., Abell, A. D., & Monro, T. M. (2011) · Langmuir · doi:10.1021/la2002496 · Cited by 80 · see citing works
Xie, L., Zheng, W. H., Xin, N., Xie, J., Wang, T., & Wang, Z. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.05.016 · Cited by 79 · see citing works
Mapping and characterization of iron compounds in Alzheimer's tissue
Collingwood, J. F., & Dobson, J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-102-308 · Cited by 79 · see citing works
Self-citationRole of environmental pollutants in Alzheimer’s disease: a review
Mir, R. H., Sawhney, G., Pottoo, F. H., Mohi-ud-din, R., Madishetti, S., Jachak, S. M., Ahmed, Z., & Masoodi, M. H. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-09964-x · Cited by 78 · see citing works
Dey, S., Halder, S., Mukherjee, A. K., Ghosh, K., & Roy, P. S. (2015) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2015.03.060 · Cited by 77 · see citing works
Drago, D., Cavaliere, A., Mascetra, N., Ciavardelli, D., Ilio, C. D., Zatta, P. F., & Sensi, S. L. (2008) · Rejuvenation Research · doi:10.1089/rej.2008.0761 · Cited by 74 · see citing works
Liao, Z., Liu, Y., Han, S.-F., Wang, D., Zheng, J., Zheng, X., & Jin, L. (2017) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2017.01.074 · Cited by 74 · see citing works
Functional impairment in aged rats chronically exposed to human range dietary aluminum equivalents
Walton, J. R. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.11.012 · Cited by 73 · see citing works
Brain biometals and Alzheimer's disease – boon or bane?
Prakash, A. K., Dhaliwal, G. K., Kumar, P., & Majeed, A. B. A. (2016) · International Journal of Neuroscience · doi:10.3109/00207454.2016.1174118 · Cited by 70 · see citing works
Li, R.-Y., Wei, Z.-L., Wang, L., Zhang, Y., & Ru, J. (2020) · Microchemical Journal · doi:10.1016/j.microc.2020.105720 · Cited by 70 · see citing works
Damante, C. A., Ösz, K., Nagy, Z., Pappalardo, G., Grasso, G., Impellizzeri, G., Rizzarelli, E., & Sóvágó, I. (2009) · Inorganic Chemistry · doi:10.1021/ic9012334 · Cited by 70 · see citing works
Iron promotes protein insolubility and aging in C. elegans
Klang, I. M., Schilling, B., Sorensen, D. J., Sahu, A. K., Kapahi, P., Andersen, J. K., Swoboda, P., Killilea, D. W., Gibson, B. W., & Lithgow, G. J. (2014) · Aging · doi:10.18632/aging.100689 · Cited by 69 · see citing works
Mapping Brain Metals to Evaluate Therapies for Neurodegenerative Disease
Popescu, B. F. G., & Nichol, H. K. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00149.x · Cited by 68 · see citing works
Is there a role for copper in neurodegenerative diseases?
Cerpa, W. F., Varela‐Nallar, L., Reyes, A. E., Minniti, A. N., & Inestrosa, N. C. (2005) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2005.07.011 · Cited by 67 · see citing works
Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67 · see citing works
Li, W., Tian, X., Huang, B., Li, H., Zhao, X., Gao, S., Zheng, J., Zhang, X., Zhou, H., Tian, Y., et al. (2015) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2015.09.059 · Cited by 66 · see citing works
Influence of Multiple Metal Ions on β-Amyloid Aggregation and Dissociation on a Solid Surface
Ryu, J., Girigoswami, K., Ha, C., Ku, S. H., & Park, C. B. (2008) · Biochemistry · doi:10.1021/bi800012e · Cited by 65 · see citing works
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 · see citing works
Cu(II) interaction with amyloid-β peptide: A review of neuroactive mechanisms in AD brains
Lin, C., Huang, H., & Jiang, Z.-F. (2010) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2010.06.003 · Cited by 63 · see citing works
Chemical imaging analysis of the brain with X-ray methods
Collingwood, J. F., & Adams, F. C. (2017) · Spectrochimica Acta Part B Atomic Spectroscopy · doi:10.1016/j.sab.2017.02.013 · Cited by 64 · see citing works
Self-citationGhorai, A., Mondal, J., Chandra, R., & Patra, G. K. (2015) · Dalton Transactions · doi:10.1039/c5dt01376c · Cited by 62 · see citing works
Gallagher, J. J., Finnegan, M. E., Grehan, B., Dobson, J., Collingwood, J. F., & Lynch, M. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110614 · Cited by 62 · see citing works
Self-citationFrisardi, V., Solfrizzi, V., Capurso, C. A., Kehoe, P. G., Imbimbo, B. P., Santamato, A., Dellegrazie, F., Seripa, D., Pilotto, A., Capurso, A., et al. (2010) · PubMed · doi:10.3233/jad-2009-1340 · Cited by 62 · see citing works
Mithu, V. S., Sarkar, B., Bhowmik, D., Chandrakesan, M., Maiti, S., & Madhu, P. K. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.023 · Cited by 62 · see citing works
Inhibitory effect of curcumin on the Al(III)-induced Aβ42 aggregation and neurotoxicity in vitro
Jiang, T., Zhi, X., Zhang, Y., Pan, L., & Zhou, P. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.04.015 · Cited by 61 · see citing works
Solfrizzi, V., Colacicco, A. M., D’Introno, A., Capurso, C. A., Parigi, A. D., Capurso, S. A., Torres, F., Capurso, A., & Panza, F. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-102-314 · Cited by 58 · see citing works
ZnO Nanoflower petals mediated amyloid degradation - An in vitro electrokinetic potential approach
Girigoswami, A., Ramalakshmi, M., Akhtar, N., Metkar, S. K., & Girigoswami, K. (2019) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.03.086 · Cited by 60 · see citing works
Exley, C., House, E., Polwart, A., & Esiri, M. M. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-120766 · Cited by 59 · see citing works
Self-citation
- Authors
- House, E., Collingwood, J., Khan, A., Korchazkina, O., Berthon, G., & Exley, C.
- Affiliations
- Keele University (GB)
- Centre for Science and Technology in Medicine, Keele University, Staffordshire, UK
- Université Toulouse III - Paul Sabatier (FR)
- Corresponding author
- Exley, Christopher
- Venue
- Journal of Alzheimer's Disease
- Publisher
- SAGE Publications
- Published
- 2004-06-03
- Volume
- 6
- Issue
- 3
- Pages
- 291-301
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- OpenAlex
- W1480108665
- Cited by
- 294
- References
- 0
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 8 · 2023: 6 · 2022: 8 · 2021: 17 · 2020: 15 · 2019: 20 · 2018: 16 · 2017: 16 · 2016: 9 · 2015: 16 · 2014: 8 · 2013: 15 · 2012: 27
- FWCI
- 6.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Alzheimer s Disease (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01 AG02030-01 A1)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- amyloid-beta 42, metal ions
- MeSH terms
- Aluminum, Alzheimer Disease, Brain, Chromatography, High Pressure Liquid, Copper, Edetic Acid, Humans, Iron, Peptide Fragments, Zinc, Chelation Therapy, Amyloid beta-Peptides, In Vitro Techniques
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
