Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619

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

Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921

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

Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus

Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611

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

The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene

Tanzi, R. E., Petrukhin, K. E., Чернов, И. П., Pellequer, J., Wasco, W., Ross, B., Romano, D., Parano, E., Pavone, P., Brzustowicz, L. M., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-344 · Cited by 1,367

Iron accumulation in Alzheimer disease is a source of redox-generated free radicals

Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,365

The initial stage of structural transformation of Aβ42 peptides from the human and mole rat in the presence of Fe2+ and Fe3+: Related to Alzheimer's disease

Vahed, M., Sweeney, A., Shirasawa, H., & Vahed, M. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107128 · Cited by 19

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

Acid–Base Homeostasis and Implications to the Phenotypic Behaviors of Cancer

Zhou, Y., Chang, W., Lu, X., Wang, J., Zhang, C., & Xu, Y. (2022) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2022.06.003 · Cited by 19

Modeling Cu2+-Aβ complexes from computational approaches

Alí‐Torres, J., Mirats, A., Maréchal, J., Rodrı́guez-Santiago, L., & Sodupe, M. (2015) · AIP Advances · doi:10.1063/1.4921072 · Cited by 19

Inhibition of Cu2+-mediated generation of reactive oxygen species by the small heat shock protein αB-crystallin: The relative contributions of the N- and C-terminal domains

Prabhu, S., Srinivas, V., Ramakrishna, T., Raman, B., & Rao, C. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.021 · Cited by 20

Prion Proteins Leading to Neurodegeneration

Mendola, D. L., Pietropaolo, A., Pappalardo, G., Zannoni, C., & Rizzarelli, E. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898415 · Cited by 19

Synthesis, Characterization and Potential Applications of Multifunctional PEO-PPOPEO- Magnetic Drug Delivery System

Dehvari, K., & Lin, K. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712803530584 · Cited by 19

In vitro study on potential pharmacological activity of curcumin analogues and their copper complexes

Ferrari, É., Benassi, R., Saladini, M., Orteca, G., Gažová, Z., & Šipošová, K. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12847 · Cited by 19

Effects of Metal Ions on Aβ42 Peptide Conformations from Molecular Simulation Studies

Khatua, P., Mondal, S., & Bandyopadhyay, S. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00098 · Cited by 19

Amyloid beta peptides electrochemistry: A review

Paquim, A.-M. C., & Oliveira‐Brett, A. M. (2021) · Current Opinion in Electrochemistry · doi:10.1016/j.coelec.2021.100837 · Cited by 19

Zinc-induced aggregation of Aβ (10–21) potentiates its action on voltage-gated potassium channel

Zhang, C., & Yang, P. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.04.044 · Cited by 19

MMP-7 cleaves amyloid β fragment peptides and copper ion inhibits the degradation

Taniguchi, M., Matsuura, K., Nakamura, R., Kojima, A., Konishi, M., & Akizawa, T. (2017) · BioMetals · doi:10.1007/s10534-017-0048-4 · Cited by 21

Novel multi-target compounds in the quest for new chemotherapies against Alzheimer’s disease: An experimental and theoretical study

Martínez, A., Zahran, M., Gomez, M., Cooper, C., Guevara, J., Ekengard, E., Nordlander, E., Alcendor, R. R., & Hambleton, S. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.08.019 · Cited by 19

Rapid Characterization of Amyloid-β Side-Chain Oxidation by Tandem Mass Spectrometry and the Scoring Algorithm for Spectral Analysis

Schiewe, A. J., Margol, L., Soreghan, B. A., Thomas, S. N., & Yang, A. J. (2004) · Pharmaceutical Research · doi:10.1023/b:pham.0000032994.36343.02 · Cited by 19

Copper(II) Can Kinetically Trap Arctic and Italian Amyloid-β40 as Toxic Oligomers, Mimicking Cu(II) Binding to Wild-Type Amyloid-β42: Implications for Familial Alzheimer’s Disease

Tian, Y., Shang, Q., Liang, R., & Viles, J. H. (2024) · JACS Au · doi:10.1021/jacsau.3c00687 · Cited by 18

Modulating Metals As A Therapeutic Strategy For Alzheimer’s Disease

Hung, L. W., & Barnham, K. J. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.32 · Cited by 18

Molecular structure of tetraaqua adenosine 5′-triphosphate aluminium(III) complex: A study involving Raman spectroscopy, theoretical DFT and potentiometry

Tenório, T. D. S., Silva, A. M., Ramos, J. M., Buarque, C. D., & Felcman, J. (2012) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2012.12.019 · Cited by 18

Novel bis-(−)-nor-meptazinol derivatives act as dual binding site AChE inhibitors with metal-complexing property

Zheng, W., Li, J., Qiu, Z., Xia, Z., Li, W., Yu, L., Chen, H., Chen, J., Chen, Y., Hu, Z., et al. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.07.018 · Cited by 18

The nickel-chelator dimethylglyoxime inhibits human amyloid beta peptide in vitro aggregation

Benoit, S. L., & Maier, R. J. (2021) · Scientific Reports · doi:10.1038/s41598-021-86060-1 · Cited by 18

Novel phage peptides attenuate beta amyloid-42 catalysed hydrogen peroxide production and associated neurotoxicity

Taddei, K., Laws, S. M., Verdile, G., Munns, S. E., D'Costa, K. J., Harvey, A. R., Martins, I. J., Hill, F., Levy, E., Shaw, J. E., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.03.023 · Cited by 18

Role of Protein Conformational Dynamics and DNA Integrity in Relevance to Neuronal Cell Death in Neurodegeneration

Gupta, V. B., Hegde, M. L., & Rao, K. S. J. (2006) · Current Alzheimer Research · doi:10.2174/156720506778249452 · Cited by 18

The Amyloid β Protein

Lazo, N. D., Maji, S. K., Fradinger, E. A., Bitan, G., & Teplow, D. B. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch17 · Cited by 18

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

A novel device of array nanochannels integrated electrochemical detector for detection of amyloid β aggregation and inhibitor screening

Wang, C., Liu, H., Li, Y., Cao, J., Zheng, B., Xia, X., & Feng, F. (2016) · Electrochemistry Communications · doi:10.1016/j.elecom.2016.02.016 · Cited by 17

Amyloids of multiple species: are they helpful in survival?

Upadhyay, A., & Mishra, A. (2018) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12399 · Cited by 17

Copper Downregulates Neprilysin Activity Through Modulation of Neprilysin Degradation

Li, M., Sun, M., Liu, Y., Yu, J. H., Yang, H., Fan, D., & Chui, D. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1218 · Cited by 17

Chronic Exposure to High Levels of Zinc or Copper has Little Effect on Brain Metal Homeostasis or Aβ Accumulation in Transgenic APP-C100 Mice

Maynard, C. J., Cappai, R., Volitakis, I., Laughton, K. M., Masters, C. L., Bush, A. I., & Li, Q. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9401-7 · Cited by 17

Aggregation of Aβ(1–42) in the presence of short peptides: conformational studies

Laczkó, I., Vass, E., Soós, K., Fülöp, L., Zarándi, M., & Penke, B. (2008) · Journal of Peptide Science · doi:10.1002/psc.990 · Cited by 17

Mercury Reduces the Enzymatic Activity of Neprilysin in Differentiated SH-SY5Y Cells

Chin-Chan, M., Segovia, J., Quintanar, L., Arcos‐López, T., Hersh, L. B., Chow, K. M., Rodgers, D. W., & Quintanilla‐Vega, B. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv037 · Cited by 17

A synthetic amyloid lawn system for high-throughput analysis of amyloid toxicity and drug screening

Girigoswami, K., Ku, S. H., Ryu, J., & Park, C. B. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.03.022 · Cited by 17

New curcumin-derived ligands and their affinity towards Ga 3+ , Fe 3+ and Cu 2+ : spectroscopic studies on complex formation and stability in solution

Rigamonti, L., Orteca, G., Asti, M., Basile, V., Imbriano, C., Saladini, M., & Ferrari, É. (2018) · New Journal of Chemistry · doi:10.1039/c8nj00535d · Cited by 17

Copper(II) complexation by fragment of central part of FBP28 protein from Mus musculus

Makowska, J., Żamojć, K., Wyrzykowski, D., Wiczk, W. M., & Chmurzyński, L. (2018) · Biophysical Chemistry · doi:10.1016/j.bpc.2018.08.002 · Cited by 17

Cu2+-induced modification of the kinetics of Aβ(1-42) channels

Bahadi, R., Farrelly, P. V., Kenna, B. L., Curtain, C. C., Masters, C. L., Cappai, R., Barnham, K. J., & Kourie, J. I. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00147.2003 · Cited by 17

Role of Metals in Neuronal Apoptosis: Challenges Associated with Neurodegeneration

Ravid, R., & Rao, K. S. J. (2006) · Current Alzheimer Research · doi:10.2174/156720506778249399 · Cited by 18

Aluminum ions accelerated the oxidative stress of copper-mediated melanin formation

Di, J., & Bi, S. (2003) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/s1386-1425(03)00127-6 · Cited by 17

Therapeutic targets in the biology of Alzheimerʼs disease

Bush, A. I. (2001) · Current Opinion in Psychiatry · doi:10.1097/00001504-200107000-00018 · Cited by 17

Decreased Brain pH Correlated With Progression of Alzheimer Disease Neuropathology: A Systematic Review and Meta-Analyses of Postmortem Studies

Hagihara, H., & Miyakawa, T. (2024) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyae047 · Cited by 16

Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin

Mijin, N., Milošević, J. R., Stevanović, S., Petrović, P. M., Lolić, A., Urbič, T., & Polović, N. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108292 · Cited by 16

Estrés oxidativo, péptido β-amiloide y enfermedad de Alzheimer

Manzano‐León, N., & Mas‐Oliva, J. (2006) · Gaceta Médica de México · Cited by 16

In silico strategies for the selection of chelating compounds with potential application in metal-promoted neurodegenerative diseases

Rodríguez‐Rodríguez, C., Rimola, A., Alí‐Torres, J., Sodupe, M., & Gonzalez-Duarte, P. (2010) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-010-9396-7 · Cited by 16

Coordination properties of a metal chelator clioquinol to Zn 2+ studied by static DFT and ab initio molecular dynamics

Rodrı́guez-Santiago, L., Alí‐Torres, J., Vidossich, P., & Sodupe, M. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp01615k · Cited by 16

Effect of C-Terminal Residues of Aβ on Copper Binding Affinity, Structural Conversion and Aggregation

Huang, S.-H., Ke, S., Lin, T.-H., Huang, H.-B., & Chen, Y.-C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090385 · 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

Differential effects of transition metal cations on the conformation and biological activities of nerve growth factor

Maitra, R., Shamovsky, I. L., Wang, W., Solc, M., Lawrance, G. M., Dostaler, S. M., Ross, G. M., & Riopelle, R. J. (2000) · Neurotoxicity Research · doi:10.1007/bf03033341 · Cited by 16

Rapid Formation of a Preoligomeric Peptide–Metal–Peptide Complex Following Copper(II) Binding to Amyloid β Peptides

Pedersen, J. T., Teilum, K., Heegaard, N. H. H., Østergaard, J., Adolph, H., & Hemmingsen, L. (2011) · Angewandte Chemie · doi:10.1002/ange.201006335 · Cited by 16

Protection of Green Tea Polyphenols against Neurodegenerative Diseases: Evidence and Possible Mechanisms

Zhao, B., & Zhao, B. (2025) · Journal of Nutrition · doi:10.1016/j.tjnut.2025.02.010 · Cited by 15

Fluorescent Protein-Based Metal Biosensors

Nam, K. H. (2023) · Chemosensors · doi:10.3390/chemosensors11040216 · Cited by 15

The Use of Polyphenols for the Treatment of Alzheimer’s Disease

Sathya, S., & Devi, K. P. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811959-4.00015-8 · Cited by 15

Physiological Metals Can Induce Conformational Changes in Transthyretin Structure: Neuroprotection or Misfolding Induction?

Ciccone, L., Tonali, N., Shepard, W., Nencetti, S., & Orlandini, E. (2021) · Crystals · doi:10.3390/cryst11040354 · Cited by 16

New mescaline-related N-acylhydrazone and its unsubstituted benzoyl derivative: Promising metallophores for copper-associated deleterious effects relief in Alzheimer's disease

Carvalho, A., Barbosa, B. M., Flores, J. S., Gonçalves, P. D. C., Diniz, R., Cordeiro, Y., Fernández, C. O., Cukierman, D. S., & Rey, N. A. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.112033 · Cited by 15

Aβ8-20 Fragment as an Anti-Fibrillogenic and Neuroprotective Agent: Advancing toward Efficient Alzheimer’s Disease Treatment

Zimbone, S., Giuffrida, M. L., Sabatino, G., Natale, G. D., Tosto, R., Consoli, G. M. L., Milardi, D., Pappalardo, G., & Sciacca, M. F. M. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00720 · Cited by 15

Synthesis, Characterization, and Activity of a Triazine Bridged Antioxidant Small Molecule

Gonzalez, P., Pota, K., Turan, L. S., da Costa, V. C. P., Akkaraju, G. R., & Green, K. N. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00184 · Cited by 15

Impact of sphingosine and acetylsphingosines on the aggregation and toxicity of metal-free and metal-treated amyloid-β

Yi, Y., Lin, Y., Han, J., Lee, H. J., Park, N., Nam, G., Park, Y. S., Lee, Y., & Lim, M. H. (2020) · Chemical Science · doi:10.1039/d0sc04366d · Cited by 15

Complexation of peptide with Cu2+ responsible to inducing and enhancing the formation of α-helix conformation

Zou, J., & Sugimoto, N. (2000) · BioMetals · doi:10.1023/a:1009249816652 · Cited by 15

Effects of Zinc on Creatine Kinase: Activity Changes, Conformational Changes, and Aggregation

Tong, X., Zeng, X., & Hai‐Meng, Z. H. O. U. (2000) · Journal of Protein Chemistry · doi:10.1023/a:1007142117037 · Cited by 15

Effects of single and continuous administration of amyloid β-peptide (25–35) on adenylyl cyclase activity and the somatostatinergic system in the rat frontal and parietal cortex

Hervás‐Aguilar, A., Puebla‐Jiménez, L., Burgos‐Ramos, E., Aguado‐Llera, D., & Arilla, E. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.02.017 · Cited by 16

Amyloid-β: phylogenesis of a chameleon

Kontush, A., & Atwood, C. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.05.001 · Cited by 15

Mild Cognitive Impairment

(2006) · Wiley eBooks · doi:10.1002/9780470041000.cedt079 · Cited by 15

Aluminum Facilitation of the Iron-Mediated Oxidation of DOPA to Melanin

Di, J., & Bi, S. (2004) · Analytical Sciences · doi:10.2116/analsci.20.629 · Cited by 14

A Preliminary Study of Cu Exposure Effects upon Alzheimer’s Amyloid Pathology

Pilozzi, A. R., Yu, Z., Carreras, I., Cormier, K., Hartley, D. M., Rogers, J. T., Dedeoglu, A., & Huang, X. (2020) · Biomolecules · doi:10.3390/biom10030408 · Cited by 14

Paradigm shift redefining molecular, metabolic and structural events in Alzheimer’s disease involves a proposed contribution by transition metals. Defined lengthy preclinical stage provides new hope to circumvent advancement of disease- and age-related neurodegeneration

Cavaleri, F. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.01.044 · Cited by 14

Multi-elemental analysis of serum and amyloid fibrils in familial amyloid polyneuropathy patients

Susuki, S., Ando, Y., Sato, T., Nishiyama, M., Miyata, M., Suico, M. A., Shuto, T., & Kai, H. (2008) · Amyloid · doi:10.1080/13506120802006013 · Cited by 14

Influence of divalent copper, manganese and zinc ions on fibril nucleation and elongation of the amyloid-like yeast prion determinant Sup35p-NM

Suhre, M. H., Hess, S., Golser, A. V., & Scheibel, T. (2009) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.09.021 · Cited by 15

Structural Elements Regulating Amyloidogenesis: A Cholinesterase Model System

Jean, L., Lee, C. F., Shaw, M. K., & Vaux, D. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001834 · Cited by 15

The prion-like protein Doppel fails to interact with itself, the prion protein and the 37 kDa/67 kDa laminin receptor in the yeast two-hybrid system

Hundt, C., & Weiss, S. F. T. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.02.003 · Cited by 14

Cordycepin, a bioactive compound from Cordyceps spp ., moderates Alzheimer’s disease-associated pathology via anti-oxidative stress and autophagy activation

Sorraksa, N., Heebkaew, N., Promjantuek, W., Kunhorm, P., Kaokean, P., Chaicharoenaudomung, N., & Noisa, P. (2023) · Journal of Asian Natural Products Research · doi:10.1080/10286020.2023.2258797 · Cited by 13

Chelating and antioxidant properties of l-Dopa containing tetrapeptide for the treatment of neurodegenerative diseases

Cacciatore, I., Marinelli, L., Stefano, A. D., Marco, V. D., Orlando, G., Gabriele, M., Gatta, D. M. P., Ferrone, A., Franceschelli, S., Speranza, L., et al. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.06.002 · Cited by 13

Probable Reasons for Neuron Copper Deficiency in the Brain of Patients with Alzheimer’s Disease: The Complex Role of Amyloid

Bagheri, S., Saboury, A. A., Haertlé, T., Rongioletti, M. C. A., & Saso, L. (2022) · Inorganics · doi:10.3390/inorganics10010006 · Cited by 14

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

A Lysozyme Concentration, pH, and Time-Dependent Isothermal Transformation Diagram Reveals Fibrous Amyloid and Non-Fibrous, Amorphous Aggregate Species

Burnett, L. C., Burnett, B. J., Li, B., Durrance, S. T., & Xu, S. (2014) · Open Journal of Biophysics · doi:10.4236/ojbiphy.2014.42006 · Cited by 13

Lead Exposure: Expression and Activity Levels of Oct-2 in the Developing Rat Brain

Bakheet, S. A., Basha, R. M., Cai, H., & Zawia, N. H. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl163 · Cited by 13

Correlation of Copper Interaction, Copper‐Driven Aggregation, and Copper‐Driven H2O2 Formation with Aβ40 Conformation

Yang, C.-A., Chen, Y.-H., Shyue-Chu, K., Chen, Y.-R., Huang, H.-B., Lin, T.-H., & Chen, Y.-C. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/607861 · Cited by 13

Why nutraceuticals do not prevent or treat Alzheimer's disease

Fisher, A. E. O., & Naughton, D. P. (2005) · Nutrition Journal · doi:10.1186/1475-2891-4-14 · Cited by 13

Copper catalysed oxidation of amino acids and Alzheimer's disease

Ali, F. E. A., Barnham, K. J., Barrow, C. J., & Separovic, F. (2003) · International Journal of Peptide Research and Therapeutics · doi:10.1007/bf02442571 · Cited by 13

Reversal of temperature‐induced conformational changes in the amyloid‐beta peptide, Aβ40, by the β‐sheet breaker peptides 16–23 and 17–24

Hatip, F. F. B., Suenaga, M., Yamada, T., & Matsunaga, Y. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00384.x · Cited by 12

Crystallization and preliminary X-ray diffraction analysis of the Fab fragment of WO2, an antibody specific for the Aβ peptides associated with Alzheimer's disease

Wun, K. S., Miles, L. A., Crespi, G. A. N., Wycherley, K., Ascher, D. B., Barnham, K. J., Cappai, R., Beyreuther, K. T., Masters, C. L., Parker, M. W., et al. (2008) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309108011718 · Cited by 12

Interaction of Metal Ions with Proteins as a Source of Inspiration for Biomimetic Materials

Smith, A. M. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622673-00001 · Cited by 12

Avoiding Alzheimer’s disease: The important causative role of divalent copper ingestion

Brewer, G. J. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219827907 · Cited by 12

Probing Alzheimer amyloid peptide aggregation using a cell-free fluorescent protein refolding method

Arslan, P. E., & Chakrabartty, A. (2009) · Biochemistry and Cell Biology · doi:10.1139/o09-038 · Cited by 12

Studies on the Interactions of Copper and Zinc Ions with β-Amyloid Peptides by a Surface Plasmon Resonance Biosensor

Yao, F., Zhang, R., Tian, H., & Li, X. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms130911832 · Cited by 12

Unravelling the Alzheimer's pathogenesis: Molecular and cellular pathways to neurodegeneration and therapeutic targets

Chauhan, P., Wadhwa, K., & Singh, G. (2025) · Pathology - Research and Practice · doi:10.1016/j.prp.2025.156109 · Cited by 12

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Frederickson, C. J., & Bush, A. I. (2001) · Springer eBooks · doi:10.1007/978-94-017-3728-9_10 · Cited by 11

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