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

Nucleoside-5′-phosphorothioate analogues are biocompatible antioxidants dissolving efficiently amyloid beta–metal ion aggregates

Amir, A., Shmuel, E., Zagalsky, R., Sayer, A. H., Nadel, Y., & Fischer, B. (2012) · Dalton Transactions · doi:10.1039/c2dt30631j · Cited by 17

Intertwined Pathologies of Amyloid-β and Metal Ions in Alzheimer’s Disease: Metal–Amyloid-β

Nam, G., & Lim, M. H. (2019) · Chemistry Letters · doi:10.1246/cl.190281 · Cited by 16

A fluorescent light-up probe for selective detection of Al3+ and its application in living cell imaging

Li, Z., Wang, Q., Wang, J., Jing, X., Wang, S., Xiao, L., & Li, L. (2019) · Inorganica Chimica Acta · doi:10.1016/j.ica.2019.119231 · Cited by 16

Experimental approaches to assess metallotoxicity and ageing in models of Alzheimer's disease

Platt, B. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-102-307 · Cited by 16

Mutual Stimulation of Beta-Amyloid Fibrillogenesis by Clioquinol and Divalent Metals

Bolognin, S., Zatta, P. F., Drago, D., Parnigotto, P. P., Ricchelli, F., & Tognon, G. (2008) · NeuroMolecular Medicine · doi:10.1007/s12017-008-8046-x · Cited by 16

Surface Functionalization of Exposed Core Glass Optical Fiber for Metal Ion Sensing

Bachhuka, A., Heng, S. C. H., Vasilev, K. A., Kostecki, R., Abell, A. D., & Ebendorff‐Heidepriem, H. (2019) · Sensors · doi:10.3390/s19081829 · Cited by 15

Coordinating to Three Histidine Residues: Cu(II) Promotes Oligomeric and Fibrillar Amyloid-β Peptide to Precipitate in a Non-β Aggregation Manner

Yang, X., Huang, H., Chen, L., Xu, W. X., & Jiang, Z.-F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1186 · Cited by 13

Peptide‐Modified Mo Polyoxometalate Nanoparticles Suppress Zn2+‐Induced Aβ Aggregation

Liu, Y., Sun, J., Gong, Y., Zhou, H., Chen, X., Zhu, X., Zhao, Y., Wen, Y., Qin, X., & Liu, J. (2019) · ChemNanoMat · doi:10.1002/cnma.201900057 · Cited by 13

Solvent-tuned discriminant sensing of Al 3+ , Mg 2+ and HF 2 − by vanilinyl-picolinyl hydrazide Schiff base

Purkait, R., & Sinha, C. (2019) · New Journal of Chemistry · doi:10.1039/c9nj00325h · Cited by 13

Copper is a potent inhibitor of the propensity for human ProIAPP1-48 to form amyloid fibrils in vitro

Exley, C., Mold, M. J., Shardlow, E., Shuker, B., Ikpe, B., Wu, L., & Fraser, P. E. (2012) · journal of Diabetes Research and Clinical Metabolism · doi:10.7243/2050-0866-1-3 · Cited by 12

Reciprocal modulation of Aβ42 aggregation by copper and homocysteine

Keskitalo, S., Farkas, M., Hanenberg, M., Szodorai, A., Kulic, L., Semmler, A., Weller, M., Nitsch, R. M., & Linnebank, M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00237 · Cited by 13

Nucleoside-2′,3′/3′,5′-bis(thio)phosphate antioxidants are also capable of disassembly of amyloid beta 42 -Zn( ii )/Cu( ii ) aggregates via Zn( ii )/Cu( ii )-chelation

Hevroni, B. L., Major, D. T., Dixit, M., Mhashal, A. R., Das, S., & Fischer, B. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00613b · Cited by 12

Self-plasticized, lumogallion-based fluorescent optical sensor for the determination of aluminium (III) with ultra-low detection limits

Mendecki, L., Granados-Fócil, S., Jendrlin, M., Mold, M. J., & Radu, A. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.12.021 · Cited by 12

Amyloid cascade hypothesis, tau synthesis, and role of oxidative stress in AD

Vyas, J., Raytthatha, N., & Prajapati, B. G. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-13205-6.00023-6 · Cited by 13

Oral phytate supplementation on the progression of mild cognitive impairment, brain iron deposition and diabetic retinopathy in patients with type 2 diabetes: a concept paper for a randomized double blind placebo controlled trial (the PHYND trial)

Pujol, A., Sanchís, P., Tamayo, M. I., Nicolau, J., Grases, F., Espino, A., Estremera, A., Rigo, E., Amengual, G. J., Rodríguez, M., et al. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1332237 · Cited by 11

The folding of a metallopeptide

Gamba, I., Rama, G., Ortega‐Carrasco, E., Berardozzi, R., Sánchez‐Pedregal, V. M., Bari, L. D., Maréchal, J., Vázquez, M. E., & Vázquez, M. E. (2015) · Dalton Transactions · doi:10.1039/c5dt02797g · Cited by 11

Sub-lethal levels of amyloid β-peptide oligomers decrease non-transferrin-bound iron uptake and do not potentiate iron toxicity in primary hippocampal neurons

SanMartín, C. D., Paula-Lima, A. C., Hidalgo, C., & Núñez, M. T. (2012) · BioMetals · doi:10.1007/s10534-012-9545-7 · Cited by 11

Assessing Surface Coverage of Aminophenyl Bonding Sites on Diazotised Glassy Carbon Electrodes for Optimised Electrochemical Biosensor Performance

Tehrani, Z., Abbasi, H. Y., Devadoss, A., Evans, J. E., & Guy, O. J. (2021) · Nanomaterials · doi:10.3390/nano11020416 · Cited by 11

Fabrication of a luminescent chemosensor for selective detection of Al 3+ used as an adjuvant in pharmaceutical drugs

Saha, S., Mondal, S., & Sahoo, P. (2022) · Organic & Biomolecular Chemistry · doi:10.1039/d2ob02044k · Cited by 11

Dietary interventions in mitigating the impact of environmental pollutants on Alzheimer’s disease – A review

Khandayataray, P., & Murthy, M. K. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.11.020 · Cited by 11

Influence of Metal Cations on the Viscoelastic Properties of Escherichia coli Biofilms

Sarlet, A., Ruffine, V., Blank, K. G., & Bidan, C. M. (2023) · ACS Omega · doi:10.1021/acsomega.2c06438 · Cited by 10

Interaction of Metal Ions with the His13-His14 Sequence Relevant to Alzheimer’s Disease

Kong, X., Zhao, Z., Lei, X., 张冰冰, Dai, D., & Jiang, L. (2015) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.5b01443 · Cited by 10

Quantum chemical molecular dynamics and metadynamics simulation of aluminium binding to amyloid-β and related peptides

Platts, J. A. (2020) · Royal Society Open Science · doi:10.1098/rsos.191562 · Cited by 10

Interaction of Zinc, Ascorbic Acid, and Folic Acid in Glycation with Albumin as Protein Model

Tupe, R. S., & Agte, V. V. (2010) · Biological Trace Element Research · doi:10.1007/s12011-010-8610-8 · Cited by 10

Aluminum does not enhance β-amyloid toxicity in rat hippocampal cultures

Nday, C. M., Drever, B. D., Salifoglou, T., & Platt, B. (2010) · Brain Research · doi:10.1016/j.brainres.2010.07.008 · Cited by 10

Revisiting Cu(II) Bound Amyloid-β40 and Amyloid-β42 Peptides: Varying Coordination Chemistries

Coskuner‐Weber, O. (2018) · Journal of the Turkish Chemical Society Section A Chemistry · doi:10.18596/jotcsa.424144 · Cited by 8

Selective recognition of aluminum ions using an esculetin@Q[8] host–guest supramolecular fluorescent probe

Luo, G., Meng, Y., Zhang, L., Li, X., Tao, Z., & Zhang, Q. (2021) · New Journal of Chemistry · doi:10.1039/d1nj04782e · Cited by 8

Intracellular tracing of amyloid vaccines through direct fluorescent labelling

Mold, M. J., Kumar, M., Mirza, A., Shardlow, E., & Exley, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-20845-9 · Cited by 7

Nanoscale chemical speciation of β-amyloid/iron aggregates using soft X-ray spectromicroscopy

Everett, J. L., Brooks, J., Collingwood, J. F., & Telling, N. D. (2021) · Inorganic Chemistry Frontiers · doi:10.1039/d0qi01304h · Cited by 7

Monitoring the early aggregatory behaviour and size of Aβ1-42 in the absence & presence of metal ions using dynamic light scattering

Shardlow, E., Khan, B., & Exley, C. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126766 · Cited by 7

A High Performance 2-Hydroxynaphthalene Acylhydrazone Fluorescent Chemosensor for Detection of Al3+ Ions Through ESIPT and PET Signalling Mechanism

Liu, X., Wang, Y., Liu, J., Tian, J., & Xu, F. (2022) · Journal of Cluster Science · doi:10.1007/s10876-022-02258-x · Cited by 7

Organosilicon Therapy in Alzheimer's Disease?

Exley, C. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11305 · Cited by 7

Preparation and characterization of a highly soluble Aβ1-42 peptide variant

LeVatte, M., Lipfert, M., Ladner-Keay, C. L., & Wishart, D. S. (2019) · Protein Expression and Purification · doi:10.1016/j.pep.2019.105480 · Cited by 7

Conformation Control of Amyloid Filaments by Repeated Thermal Perturbation

Lee, S. W., Choi, H., Lee, G., Choi, Y., Lee, H., Kim, G., Lee, H., Lee, W., Park, J., & Yoon, D. S. (2021) · ACS Macro Letters · doi:10.1021/acsmacrolett.1c00525 · Cited by 7

Perphenazine–Macrocycle Conjugates Rapidly Sequester the Aβ42 Monomer and Prevent Formation of Toxic Oligomers and Amyloid

Ball, S. R., Adamson, J. S. P., Sullivan, M. A., Zimmermann, M. R., Lo, V., Sanz-Hernández, M., Jiang, X., Kwan, A. H., McKenzie, A. D. J., Werry, E. L., et al. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00498 · Cited by 6

The pH effects on thermal amyloid fibrillation kinetics of hen egg‐white lysozyme using new normalization factor for Raman spectroscopy

Liu, D., Chen, N., Zhang, T., Zhou, X., & Liu, S. (2024) · Journal of Raman Spectroscopy · doi:10.1002/jrs.6674 · Cited by 6

Targeting Amyloids with Coated Nanoparticles: A Review on Potential Combinations of Nanoparticles and Bio-Compatible Coatings

Warerkar, O. D., Mudliar, N. H., Momin, M. M., & Singh, P. K. (2023) · Critical Reviews in Therapeutic Drug Carrier Systems · doi:10.1615/critrevtherdrugcarriersyst.2023046209 · Cited by 7

Designing drug-delivery systems for the nervous system using nanotechnology: opportunities and challenges

Liu‐Snyder, P., & Webster, T. J. (2006) · Expert Review of Medical Devices · doi:10.1586/17434440.3.6.683 · Cited by 6

Modified EDTA selectively recognized Cu2+ and its application in the disaggregation of β-amyloid-Cu (II)/Zn (II) aggregates

Chang, R., Chen, X., Yu, H., Tan, G., Wen, H., Huang, J., & Hao, Z. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.110929 · Cited by 6

Multimodal Therapeutic Approach Using Donor‐Engineered AIE Photosensitizer to Combat Multifaceted Aspects of Alzheimer's Disease

Ghosh, P., Mukhopadhyay, S., Singh, M., Ghosh, S. S., & Iyer, P. K. (2025) · Small · doi:10.1002/smll.202506572 · Cited by 5

The Aggregation Potential of the 1–15- and 1–16-Fragments of the Amyloid β Peptide and Their Influence on the Aggregation of Aβ40

Shabestari, M. H., Plug, T., Motazacker, M. M., Meeuwenoord, N. J., Filippov, D. V., Meijers, J. C. M., & Huber, M. (2013) · Applied Magnetic Resonance · doi:10.1007/s00723-013-0469-3 · Cited by 5

Sialic Acid Hydroxamate: A Potential Antioxidant and Inhibitor of Metal‐Induced β‐Amyloid Aggregates

Yadav, R., Murthy, R. V., & Kikkeri, R. V. (2015) · ChemBioChem · doi:10.1002/cbic.201500162 · Cited by 5

Rapid and high-throughput colorimetric screening for anti-aggregation reagents of protein conformational diseases by using gold nanoplasmonic particles

Kim, H. Y., Kwon, J. A., Kang, T., & Choi, I. (2017) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2017.01.004 · Cited by 5

Iron Serum Markers Profile in Frontotemporal Lobar Degeneration

Luca, A. D., Fostinelli, S., Ferrari, C., Binetti, G. G., Benussi, L., Borroni, B., Rossi, L. C., Rongioletti, M. C. A., Ghidoni, R., & Squitti, R. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201047 · Cited by 5

Modifiers of Protein Aggregation—From Nonspecific to Specific Interactions

Levy‐Sakin, M., Scherzer‐Attali, R., & Gazit, E. (2012) · Wiley eBooks · doi:10.1002/9781118183373.ch15 · Cited by 5

Investigation of Methylsulfonamide’s Capability to Prevent Zn 2+ -Induced Aβ Peptide Aggregation Based on Zn 2+ Coordination within the Zinc Binding Region of Aβ for Treatment of Alzheimer’s Disease (AD)

Ataman, D., Cansız, C. S., Turğut, M., Dağ, Ç., & Duman, M. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00238 · Cited by 4

The Influence of Ca2+ and Zn2+ on the Amyloid Fibril Formation by β-Casein

Wang, J., Liu, J., Du, G., An, Y., Zhao, C., & Zeng, B. (2020) · Protein and Peptide Letters · doi:10.2174/0929866527666200318143533 · Cited by 4

Neurological Disorders Associated with Iron Misdistribution: The Therapeutic Potential of Siderophores

Kakhlon, O., Breuer, B., Münnich, A., & Cabantchik, Z. I. (2010) · Humana Press eBooks · doi:10.1007/978-1-60327-514-9_11 · Cited by 4

Neuroprotective, and memory enhancement effects of Salvia aristata and its phenolic constituents: an in vitro, and in vivo study

Dabaghian, F., Delnavazi, M., Hariri, R., Akbarzadeh, T., Tayarani‐Najaran, Z., Ardekani, M. R. S., Sharifzadeh, M. S., & Khanavi, M. (2025) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-025-04902-1 · Cited by 3

Novel Schiff Base of E-2-(((4-Aminophenyl)imino)methyl)-5-(difluoromethoxy)phenol Fluorescence Chemosensor for Detection of Al3+, Fe2+, Cu2+ Ions and its Application towards Live Cell Imaging

Iyappan, M., Dhineshkumar, E., & Anbuselvan, C. (2020) · Asian Journal of Chemistry · doi:10.14233/ajchem.2020.22394 · Cited by 3

Aggregation-Induced Emission and Applications of Aryl-Substituted Pyrrole Derivatives

Tong, B., & Dong, Y. (2013) · Wiley eBooks · doi:10.1002/9781118735183.ch24 · Cited by 3

Fast voltammetry of metals at carbon-fiber microelectrodes: rapid determination of solution formation constants

Pathirathna, P., Siriwardhane, T., Morgan, S. L., McElmurry, S. P., & Hashemi, P. (2016) · The Analyst · doi:10.1039/c6an01401a · Cited by 3

Investigating the geometrical preferences of a flexible benzimidazolone-based linker in the synthesis of coordination polymers

Jones, C. L., Marsden, E. A., Nevin, A. C., Kariuki, B. M., Bhadbhade, M. M., Martin, A. D., & Easun, T. L. (2017) · Royal Society Open Science · doi:10.1098/rsos.171064 · Cited by 3

Toxic Exposure and Life Style Factors on Ageing Brain Neurodegenerative Disease, Alzheimer’s and Parkinson’s: Role of Natural Antioxidants to Ameliorate the Condition

Naha, N., Das, M., & Banerjee, A. (2018) · Journal of Alcoholism and Drug Dependence · doi:10.4172/2329-6488.1000309 · Cited by 3

Directly probing the dissociation effects of graphene oxide nanosheets on hIAPP fibrils

Li, S., Lin, D., Hu, X., & Yang, X. (2018) · Nanotechnology · doi:10.1088/1361-6528/aae143 · Cited by 3

Nanoparticles for the Treatment of A lzheimer's Disease: Theoretical Rationale, Present Status and Future Perspectives

Liu, G., Men, P., Perry, G. L., & Smith, M. A. (2003) · Wiley eBooks · doi:10.1002/9783527610419.ntls0122 · Cited by 3

Significant omissions of copper-amyloid research in ‘Metal Ions in Neurodegenerative Diseases’ special issue (CCR 256 (19,20) 2012)

Exley, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.08.012 · Cited by 2

Conditioned Media Therapy in Alzheimer's Disease: Current Findings and Future Challenges

Firoozi, A., Shadi, M., Aghaei, Z., & Namavar, M. R. (2023) · Current Stem Cell Research & Therapy · doi:10.2174/1574888x18666230523155659 · Cited by 2

Metal ions and beta amyloid: conformational modifications and biological aspects

Granzotto, A., & Zatta, P. F. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_7 · Cited by 2

The Amyloid _-Protein and Alzheimer's Disease

Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2

Investigating the therapeutic potential of 1,2,3,4,6 penta-O-galloyl-β-D-glucose in Alzheimer’s disease: a scoping review

Kahil, E. A., Jackson, A., D’Souza, B., Gorman, G. S., & Jumbo‐Lucioni, P. P. (2025) · Natural Product Research · doi:10.1080/14786419.2025.2477226 · Cited by 1

Alzheimer’s disease and exposome: is there really a connection? Literature review and meta-analysis

Zayani, C. B. H. Y., Abdelhédi, R., & Gargouri, I. (2026) · Euro-Mediterranean Journal for Environmental Integration · doi:10.1007/s41207-025-01023-6 · Cited by 1

An Al 3+ ions-responsive blue emitting ionic liquid-based nano-optode and its implications for the detection of 2, 4, 6-trinitrophenol

Lama, S., & Das, S. K. (2026) · Analytical Methods · doi:10.1039/d6ay00179c · Cited by 1

Environmental Factors Preceding A40 Monomer to Oligomers and the Detection of Oligomers in Alzheimer's Disease Patient Serum

Matsunaga, Y., & Suenaga, M. (2012) · Journal of Amino Acids · doi:10.1155/2012/206520 · Cited by 1

Oxidative Stress and Alzheimer Disease: Mechanisms and Therapeutic Opportunities

Mondragón‐Rodríguez, S., García‐Sierra, F., Casadesús, G., Lee, H., Petersen, R. B., Perry, G. L., Zhu, X., & Smith, M. A. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-7104-3_18 · Cited by 1

Silica nanoparticles (SiNPs) derived from melon seed husk ameliorate Ni/Al mixture-mediated cognitive impairment in rats

Orish, C. N., Orisakwe, O. E., Anyachor, C. P., Ezejiofor, A. N., Ćirović, A., Ćirović, A., Dooka, B. D., & Ezealisiji, K. M. (2024) · Journal of Medicine and Life · doi:10.25122/jml-2024-0019 · Cited by 1

Environmental Aspects of Alzheimer's and Parkinson's Diseases Neuropathologies

Zouhairi, N., Hiba, O. E., Lahouaoui, H., Benammi, H., Chatoui, H., Elgot, A., Aimrane, A., Bitar, A., Kahime, K., Draoui, A., et al. (2019) · Advances in environmental engineering and green technologies book series · doi:10.4018/978-1-5225-7775-1.ch012 · Cited by 1

Construction of turn-on mode fluorescent sensor for Pb2+ and Al3+ with structure of phthalic acid and tetraphenylethylene core

Liu, J., & Dong, Y. Q. (2022) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2022-0190 · Cited by 1

Role of Environmental and Inflammatory Toxicity in Neuronal Cell Death

Somayajulu‐Nitu, M., Domazet-Damjanov, D., Matei, A., Schwartzenberger, E., Cohen, J. S., & Pandey, S. (2008) · The Open Toxicology Journal · doi:10.2174/1874340400802010026 · Cited by 1

Accumulation Of Subcortical Iron As A Modifier Of Volumetric And Cognitive Decline In Healthy Aging: Two Longitudinal Studies

Daugherty, A. M. (2014) · Human Biology · Cited by 1

PHYTOTHERAPIES AS NEW DRUG SOURCES

Liao, V. W. Y., Narlawar, R., Hibbs, D. E., & Groundwater, P. W. (2015) · doi:10.1002/9781119006039.ch14

Aluminium in the Diet, Cognitive Decline and Dementia

Frisardi, V., Solfrizzi, V., Kehoe, P. G., Imbimbo, B. P., Vendemiale, G., Capurso, A., & Panza, F. (2011) · Springer eBooks · doi:10.1007/978-0-387-92271-3_178

Alzheimer’s Disease and Metal Contamination: Aspects on Genotoxicity

de Lima, P. D. L., de Vasconcellos, M. C., Montenegro, R. C., & Burbano, R. M. R. (2011) · InTech eBooks · doi:10.5772/17659

Interaction entre le zinc(II) et le peptide amyloïde bêta lié à la maladie d'Alzheimer

Talmard, C. (2007)

Nutrition, Brain Aging, and Alzheimers Disease

Zhang, Y., Cao, P., Leonard, B. W., & Li, R. (2005) · Current Nutrition & Food Science · doi:10.2174/157340105774574875

An Investigation into the Role of Iron, Copper, and Gender in a Transgenic Mouse Model of Alzheimer's Disease.

Groeber, C. M. (2013) · doi:10.13021/mars/5636

MEMORY, METALS AND ALZHEIMER'S DISEASE, SPRING 2006

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Coordination of Metal Ions to β-Amyloid Peptide: Impact on Alzheimer’s Disease

Faller, P., Penna, G. L., Hureau, C., & Furlan, S. (2013) · Modecular medicine and medicinal · doi:10.1142/9781848167551_0004

Direct Evaluation of Alzheimer’s Disease-Specific Oxidative Stress with Multiphoton Microscopy

Garcı́a-Alloza, M., Bacskai, B. J., & Dodwell, S. A. (2005) · Oxidative stress and disease · doi:10.1201/9781420026559.ch2

Animal Models of Metallic Dementia

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Iron and Monoamine Oxidase in Brain Function and Dysfunction

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Crystallization and dissolution studies of calcium oxalate monohydrate

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Differentiating the Substantia Nigra and Ventral Tegmental Area in Early-stage Parkinson's Disease Using Iron Imaging

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Aluminum

Jicha, G. A., & Carr, S. A. (2009) · Elsevier eBooks · doi:10.1016/b978-032305260-3.50031-9

Inorganic Nanomaterials as Promoters/Inhibitors of Amyloid Fibril Formation

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Perphenazine-macrocycle conjugates rapidly sequester the Aβ42 monomer and inhibit amyloid formationPreprint

Ball, S. R., Adamson, J. S. P., Sullivan, M. A., Zimmermann, M. R., Lo, V., Sanz-Hernández, M., Jiang, F. N., Kwan, A. H., Werry, E. L., Knowles, T. P. J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.16.384248

Faculty Opinions recommendation of Severe cerebral congophilic angiopathy coincident with increased brain aluminium in a resident of Camelford, Cornwall, UK.

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Nutrition, Brain Aging, and Alzheimer’s Disease

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Environmental Aspects of Alzheimer's and Parkinson's Diseases Neuropathologies

Zouhairi, N., Hiba, O. E., Lahouaoui, H., Benammi, H., Chatoui, H., Elgot, A., Aimrane, A., Bitar, A., Kahime, K., Draoui, A., et al. (2020) · IGI Global eBooks · doi:10.4018/978-1-7998-3441-0.ch005

Influence of divalent metal cations on α-lactalbumin fibril formation

Bogdanova, L. R., Nikiforova, A. A., Ziganshina, S. A., Zuev, Y. F., & Sedov, I. A. (2024) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-024-02071-z

Additional file 2 of CERTL reduces C16 ceramide, amyloid-β levels, and inflammation in a model of Alzheimer’s disease

Crivelli, S. M., Luo, Q., Stevens, J., Giovagnoni, C., van Kruining, D., Bode, G. H., den Hoedt, S., Hobo, B., Scheithauer, A.-L., Walter, J., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14053548

Additional file 1 of CERTL reduces C16 ceramide, amyloid-β levels, and inflammation in a model of Alzheimer’s disease

Crivelli, S. M., Luo, Q., Stevens, J., Giovagnoni, C., van Kruining, D., Bode, G. H., den Hoedt, S., Hobo, B., Scheithauer, A.-L., Walter, J., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14053545

Additional file 3 of CERTL reduces C16 ceramide, amyloid-β levels, and inflammation in a model of Alzheimer’s disease

Crivelli, S. M., Luo, Q., Stevens, J., Giovagnoni, C., van Kruining, D., Bode, G. H., den Hoedt, S., Hobo, B., Scheithauer, A.-L., Walter, J., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14053551

Valence-sensitive assembly of a Cu–amyloid peptide network

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BindingDB Entry 50001909: Novel multi-target compounds in the quest for new chemotherapies against Alzheimer's disease: An experimental and theoretical study.

BindingDB (2020) · UC San Diego · doi:10.7270/q29s1tk8

Zn(II)‐ and Cu(II)‐induced non‐fibrillar aggregates of amyloid‐β (1–42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators

Tõugu, V., Karafin, A., Zovo, K., Chung, R. S., Howells, C., West, A. K., & Palumaa, P. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06269.x · Cited by 181

Effect of metal chelators on the aggregation of beta-amyloid peptides in the presence of copper and iron

Tahmasebinia, F., & Emadi, S. (2017) · BioMetals · doi:10.1007/s10534-017-0005-2 · Cited by 73

Effect of metal chelators on the aggregation of Beta-Amyloid peptides in the presence of metal ions

Tahmasebinia, F., & Emadi, S. (2015) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.10927813

Amyloid-β Metal Interaction and Metal Chelation

Cuajungco, M. P., Frederickson, C. J., & Bush, A. I. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_12 · Cited by 68

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