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

Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer disease.

Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363

8-Hydroxyquinoline Schiff-base compounds as antioxidants and modulators of copper-mediated Aβ peptide aggregation

Gomes, L. M., Vieira, R. P., Jones, M. R., Wang, M. C. P., Dyrager, C., de Souza-Fagundes, E. M., Silva, J. G. D., Storr, T., & Beraldo, H. D. O. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.04.011 · Cited by 94

Manganese, Copper, and Zinc in Cerebrospinal Fluid from Patients with Multiple Sclerosis

Melø, T. M., Larsen, C. B., White, L. R., Aasly, J. O., Sjøbakk, T. E., Flaten, T. P., Sonnewald, U., & Syversen, T. L. M. (2003) · Biological Trace Element Research · doi:10.1385/bter:93:1-3:1 · Cited by 92

Amyloid beta and the longest-lived rodent: the naked mole-rat as a model for natural protection from Alzheimer's disease

Edrey, Y. H., Medina, D. X., Gaczynska, M. E., Osmulski, P. A., Oddo, S., Caccamo, A., & Buffenstein, R. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.03.032 · Cited by 95

Lead (Pb) exposure and its effect on APP proteolysis and Aβ aggregation

Basha, M. R., Murali, M., Siddiqi, H. K., Ghosal, K., Siddiqi, O. K., Lashuel, H. A., Ge, Y., Lahiri, D. K., & Zawia, N. H. (2005) · The FASEB Journal · doi:10.1096/fj.05-4375fje · Cited by 74

Transglutaminases and Transglutaminase‐Catalyzed Cross‐Links Colocalize with the Pathological Lesions in Alzheimer's Disease Brain

Wilhelmus, M. M. M., Grunberg, S. C. S., Bol, J. G. J. M., van Dam, A., Hoozemans, J. J. M., Rozemüller, A. J. M., & Drukarch, B. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00197.x · Cited by 90

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

Perrone, L., Mothes-Martin, E., Vignes, M., Mockel, A., Figueroa, C. M., Miquel, M., Maddelein, M., & Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900474 · Cited by 93

Characterization of copper binding to the peptide amyloid‐β(1–16) associated with Alzheimer's disease

Ma, Q., Hu, J. N., Wu, W., Liu, H., Du, J., Fu, Y., Wu, Y., Lei, P., Zhao, Y., & Li, Y. (2006) · Biopolymers · doi:10.1002/bip.20523 · Cited by 91

Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Suzuki, K., Miura, T., & Takeuchi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5263 · Cited by 90

Exacerbation of Copper Toxicity in Primary Neuronal Cultures Depleted of Cellular Glutathione

White, A. R., Bush, A. I., Beyreuther, K. T., Masters, C. L., & Cappai, R. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722092.x · Cited by 89

Restored degradation of the Alzheimer’s amyloid‐β peptide by targeting amyloid formation

Crouch, P. J., Tew, D. J., Du, T., Nguyen, D., Caragounis, A., Filiz, G., Blake, R. E., Trounce, I. A., Soon, C. P. W., Laughton, K. M., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05870.x · Cited by 88

Trace Copper(II) or Zinc(II) Ions Drastically Modify the Aggregation Behavior of Amyloid-β1–42: An AFM Study

Innocenti, M., Salvietti, E., Guidotti, M., Casini, A., Bellandi, S., Foresti, M. L., Gabbiani, C., Pozzi, A., Zatta, P. F., & Luigi Messori, A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1338 · Cited by 87

Inhibitory action of macrocyclic platiniferous chelators on metal-induced Aβ aggregation

Wang, X., Wang, X., Zhang, C., Jiao, Y., & Guo, Z. (2012) · Chemical Science · doi:10.1039/c2sc01100j · Cited by 87

A nontransgenic mouse model shows inducible amyloid-β (Aβ) peptide deposition and elucidates the role of apolipoprotein E in the amyloid cascade

Dolev, I., & Michaelson, D. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404458101 · Cited by 102

Designing Recognition Molecules and Tailoring Functional Surfaces for In Vivo Monitoring of Small Molecules in the Brain

Zhang, L., & Tian, Y. (2018) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00543 · Cited by 86

Re‐evaluation of the existing health‐based guidance values for copper and exposure assessment from all sources

More, S. J., Bampidis, V., Benford, D., Bragard, C., Halldorsson, T. I., Hernández, A. F., Bennekou, S. H., Koutsoumanis, K., Lambré, C., Machera, K. A., et al. (2023) · EFSA Journal · doi:10.2903/j.efsa.2023.7728 · Cited by 99

A review of genome mutation and Alzheimer's disease

Thomas, P., & Fenech, M. F. (2006) · Mutagenesis · doi:10.1093/mutage/gel055 · Cited by 88

Lipid peroxidation and 4-hydroxy-2-nonenal formation by copper ion bound to amyloid-β peptide

Hayashi, T., Shishido, N., Nakayama, K., Nunomura, A., Smith, M. A., Perry, G. L., & Nakamura, M. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.013 · Cited by 84

PARP-1 Modulates Amyloid Beta Peptide-Induced Neuronal Damage

Martire, S., Fuso, A., Rotili, D., Tempera, I., Giordano, C., Zottis, I. D., Muzi, A., Vernole, P., Graziani, G., Lococo, E., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072169 · Cited by 85

Amyloid-like Conformation and Interaction for the Self-Assembly in Barnacle Underwater Cement

Nakano, M., & Kamino, K. (2014) · Biochemistry · doi:10.1021/bi500965f · Cited by 84

Amyloid‐β‐induced toxicity of primary neurons is dependent upon differentiation‐associated increases in tau and cyclin‐dependent kinase 5 expression

Liu, T., Perry, G. L., Chan, H. W., Verdile, G., Martins, R. N., Smith, M. A., & Atwood, C. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02196.x · Cited by 85

Bis (thiosemicarbazonato) Cu-64 Complexes for Positron Emission Tomography Imaging of Alzheimer's Disease

Fodero‐Tavoletti, M. T., Villemagne, V. L., Paterson, B. M., White, A. R., Li, Q., Camakaris, J., O'Keefe, G. J., Cappai, R., Barnham, K. J., & Donnelly, P. S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1359 · Cited by 83

The role of iron as a mediator of oxidative stress in Alzheimer disease

Castellani, R. J., Moreira, P. I., Perry, G. L., & Zhu, X. (2012) · BioFactors · doi:10.1002/biof.1010 · Cited by 82

Metal Switch for Amyloid Formation: Insight into the Structure of the Nucleus

Morgan, D. M., Dong, J., Jacob, J., Lu, K., Apkarian, R. P., Thiyagarajan, P., & Lynn, D. G. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0273086 · Cited by 82

The neuroprotective peptide NAP inhibits the aggregation of the beta-amyloid peptide

Ashur‐Fabian, O., Segal-Ruder, Y., Skutelsky, E., Brenneman, D. E., Steingart, R. A., Giladi, E., & Gozes, I. (2003) · Peptides · doi:10.1016/j.peptides.2003.08.005 · Cited by 83

Anti-amyloidogenic therapies: strategies for prevention and treatment of Alzheimer’s disease

Hamaguchi, T., Ono, K., & Yamada, M. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5599-9 · Cited by 83

Contrasting, Species-Dependent Modulation of Copper-Mediated Neurotoxicity by the Alzheimer's Disease Amyloid Precursor Protein

White, A. R., Multhaup, G., Galatis, D., McKinstry, W. J., Parker, M. W., Pipkorn, R., Beyreuther, K. T., Masters, C. L., & Cappai, R. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-02-00365.2002 · Cited by 82

Gold Nanocage‐Based Dual Responsive “Caged Metal Chelator” Release System: Noninvasive Remote Control with Near Infrared for Potential Treatment of Alzheimer's Disease

Shi, P., Li, M., Ren, J., & Qu, X. (2013) · Advanced Functional Materials · doi:10.1002/adfm.201301015 · Cited by 82

Copper reduction by copper binding proteins and its relation to neurodegenerative diseases

Opazo, C., Barría, M. I., Ruiz, F. H., & Inestrosa, N. C. (2003) · BioMetals · doi:10.1023/a:1020795422185 · Cited by 83

Cross talk between neurometals and amyloidogenic proteins at the synapse and the pathogenesis of neurodegenerative diseases.

Kawahara, M., Kato-Negishi, M., & Tanaka, K. (2017) · Metallomics · doi:10.1039/c7mt00046d · Cited by 80

Molecular Dynamics Study of the Beta Amyloid Peptide of Alzheimer's Disease and Its Divalent Copper Complexes

Raffa, D. F., & Rauk, A. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp0689621 · Cited by 80

Amyloidosis of Alzheimer's Aβ peptides: solid‐state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies

Antzutkin, O. N. (2004) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.1341 · Cited by 80

β‐Amyloid aggregation and heterogeneous nucleation

Srivastava, A. K., Pittman, J. M., Zerweck, J., Venkata, B. S., Moore, P. C., Sachleben, J. R., & Meredith, S. C. (2019) · Protein Science · doi:10.1002/pro.3674 · Cited by 82

The state versus amyloid-β: the trial of the most wanted criminal in Alzheimer disease

Rottkamp, C. A., Atwood, C., Joseph, J. A., Nunomura, A., Perry, G. L., & Smith, M. A. (2002) · Peptides · doi:10.1016/s0196-9781(02)00069-4 · Cited by 81

Metals in alzheimer's disease: a systemic perspective

Squitti, R. (2011) · Frontiers in bioscience · doi:10.2741/3938 · Cited by 80

Imaging hydrogen peroxide in Alzheimer’s disease via cascade signal amplification

Yang, J., Yang, J., Liang, S. H., Xu, Y., Moore, A. V., & Ran, C. (2016) · Scientific Reports · doi:10.1038/srep35613 · Cited by 78

Neurotoxic β-amyloid oligomers cause mitochondrial dysfunction—the trigger for PANoptosis in neurons

Meng, X., Song, Q., Liu, Z., Liu, X., Wang, Y., & Liu, J. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1400544 · Cited by 84

Selective Cu2+ Binding, Redox Silencing, and Cytoprotective Effects of the Small Heat Shock Proteins αA- and αB-Crystallin

Ahmad, M. F., Singh, D., Taiyab, A., Ramakrishna, T., Raman, B., & Rao, C. M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.068 · Cited by 78

Cu(II) interaction with N-terminal fragments of human and mouse β-amyloid peptide

Kowalik‐Jankowska, T. (2001) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(01)00226-4 · Cited by 78

Imaging real-time aggregation of amyloid beta protein (1–42) by atomic force microscopy

Parbhu, A. N., Lin, H., Thimm, J. C., & Lal, R. (2002) · Peptides · doi:10.1016/s0196-9781(02)00061-x · Cited by 77

Increase in the conformational flexibility of β2‐microglobulin upon copper binding: A possible role for copper in dialysis‐related amyloidosis

Villanueva, J., Hoshino, M., Katou, H., Kardos, J., Hasegawa, K., Naiki, H., & Goto, Y. (2004) · Protein Science · doi:10.1110/ps.03445704 · Cited by 77

The modulation of metal bio‐availability as a therapeutic strategy for the treatment of Alzheimer's disease

Crouch, P. J., White, A. R., & Bush, A. I. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05918.x · Cited by 78

Towards a Unified Vision of Copper Involvement in Alzheimer's Disease: A Review Connecting Basic, Experimental, and Clinical Research

Pal, A., Siotto, M., Prasad, R., & Squitti, R. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-141194 · Cited by 76

Radioiodinated clioquinol as a biomarker for β‐amyloid: Zn2+ complexes in Alzheimer's disease

Opazo, C., Luza, S., Villemagne, V. L., Volitakis, I., Rowe, C. C., Barnham, K. J., Altschul, D., Masters, C. L., Cherny, R. A., & Bush, A. I. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00196.x · Cited by 76

Recent advances in the design and applications of amyloid-β peptide aggregation inhibitors for Alzheimer’s disease therapy

Jokar, S., Khazaei, S., Behnammanesh, H., Shamloo, A., Erfani, M., Beiki, D., & Bavi, O. (2019) · Biophysical Reviews · doi:10.1007/s12551-019-00606-2 · Cited by 76

Efficacy and mechanism of cGAMP to suppress Alzheimer’s disease by elevating TREM2

Xu, Q., Xu, W., Cheng, H., Yuan, H., & Tan, X. (2019) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2019.07.004 · Cited by 75

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 International Edition · doi:10.1002/anie.201006335 · Cited by 75

Cellular acidification as a new approach to cancer treatment and to the understanding and therapeutics of neurodegenerative diseases

Harguindey, S., Stanciu, D., Devesa, J., Alfarouk, K. O., Cardone, R. A., Orozco, J. D. P., Devesa, P., Rauch, C., Orive, G., Anitua, E., et al. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.02.003 · Cited by 75

Curcumin derivatives as metal-chelating agents with potential multifunctional activity for pharmaceutical applications

Ferrari, É., Benassi, R., Sacchi, S., Pignedoli, F., Asti, M., & Saladini, M. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.06.002 · Cited by 75

Copper(II) interaction with amyloid-β: Affinity and speciation

Arena, G., Pappalardo, G., Sóvágó, I., & Rizzarelli, E. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.012 · Cited by 74

Presenilins Promote the Cellular Uptake of Copper and Zinc and Maintain Copper Chaperone of SOD1-dependent Copper/Zinc Superoxide Dismutase Activity

Greenough, M. A., Volitakis, I., Li, Q., Laughton, K. M., Evin, G. M., Ho, M., Dalziel, A. H., Camakaris, J., & Bush, A. I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163964 · Cited by 74

Ferroptosis: A potential therapeutic target for neurodegenerative diseases

Vitalakumar, D., Sharma, A., & Flora, S. J. S. (2021) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22830 · Cited by 75

Quantification of the Binding Properties of Cu2+ to the Amyloid Beta Peptide: Coordination Spheres for Human and Rat Peptides and Implication on Cu2+-Induced Aggregation

Hong, L., Carducci, T. M., Bush, W. D., Dudzik, C. G., Millhauser, G. L., & Simon, J. D. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp103272v · Cited by 73

Amyloid-Induced Aggregation and Precipitation of Soluble Proteins: An Electrostatic Contribution of the Alzheimer's β(25−35) Amyloid Fibril

Konno, T. (2001) · Biochemistry · doi:10.1021/bi002156h · Cited by 72

Brain proteins that mind metals: a neurodegenerative perspective

Brown, D. R. (2009) · Dalton Transactions · doi:10.1039/b822135a · Cited by 72

Inhibition of Amyloid-β Aggregation by Cobalt(III) Schiff Base Complexes: A Computational and Experimental Approach

Iscen, A., Brue, C. R., Roberts, K. F., Kim, J., Schatz, G. C., & Meade, T. J. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06388 · Cited by 73

The molecular mechanisms of the anti-amyloid effects of phenols

Shoval, H., Lichtenberg, D. A., & Gazit, E. (2007) · Amyloid · doi:10.1080/13506120601116674 · Cited by 71

Applications and bioefficacy of the functional food supplement fermented papaya preparation

Aruoma, O. I., Hayashi, Y., Marotta, F., Mantello, P., Rachmilewitz, E. A., & Montagnier, L. (2010) · Toxicology · doi:10.1016/j.tox.2010.09.006 · Cited by 71

Hohenheim Consensus Workshop: Copper

Schümann, K., Classen, H.-G., Dieter, H. H., König, J. S., Multhaup, G., Rükgauer, M., Summer, K., Bernhardt, J., & Biesalski, H.-K. (2002) · European Journal of Clinical Nutrition · doi:10.1038/sj.ejcn.1601315 · Cited by 71

Biochemical and structural analysis of the interaction between β-amyloid and fibrinogen

Zamolodchikov, D., Berk-Rauch, H. E., Oren, D. A., Stor, D. S., Singh, P. K., Kawasaki, M., Aso, K., Strickland, S., & Ahn, H. J. (2016) · Blood · doi:10.1182/blood-2016-03-705228 · Cited by 70

Polyphenolic Antioxidants and Neuronal Regeneration

Ataie, A., Ataie, R., & Shadifar, M. (2016) · Basic and Clinical Neuroscience Journal · doi:10.15412/j.bcn.03070201 · Cited by 75

Metal Loading Capacity of Aβ N-Terminus: a Combined Potentiometric and Spectroscopic Study of Zinc(II) Complexes with Aβ(1−16), Its Short or Mutated Peptide Fragments and Its Polyethylene Glycol−ylated Analogue

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

Rapid Exchange of Metal between Zn7–Metallothionein-3 and Amyloid-β Peptide Promotes Amyloid-Related Structural Changes

Pedersen, J. T., Hureau, C., Hemmingsen, L., Heegaard, N. H. H., Østergaard, J., Vašák, M., & Faller, P. (2012) · Biochemistry · doi:10.1021/bi201774z · Cited by 72

Mechanisms of Neurodegenerative Disorders

Wolozin, B. L., & Behl, C. (2000) · Archives of Neurology · doi:10.1001/archneur.57.6.793 · Cited by 70

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

Nicotine attenuates the β‐amyloid neurotoxicity through regulating metal homeostasis

Zhang, J., Liu, Q., Chen, Q., Liu, N.-Q., Li, F., Lu, Z., Qin, C., Zhu, H., Huang, Y., He, W., et al. (2006) · The FASEB Journal · doi:10.1096/fj.05-5214fje · Cited by 70

N-Aryl-substituted 3-(β-D-glucopyranosyloxy)-2-methyl-4(1H)-pyridinones as agents for Alzheimer's therapy

Scott, L. E., Telpoukhovskaia, M., Rodríguez-Rodríguez, C., Merkel, M., Bowen, M. L., Page, B. D. G., Green, D. E., Storr, T., Thomas, F., Allen, D. D., et al. (2011) · Chem. Sci. · doi:10.1039/c0sc00544d · Cited by 68

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 deficiency elicits glial and neuronal response typical of neurodegenerative disorders

Zucconi, G. G., Cipriani, S., Scattoni, R., Balgkouranidou, I., Hawkins, D. P., & Ragnarsdottir, K. V. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00793.x · Cited by 67

Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets

Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67

Modulation of protein kinase C by curcumin; inhibition and activation switched by calcium ions

Mahmmoud, Y. A. (2006) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706970 · Cited by 67

PET Imaging of Copper Trafficking in a Mouse Model of Alzheimer Disease

Torres, J. B., Andreozzi, E. M., Dunn, J., Siddique, M., Szanda, I., Howlett, D. R., Sunassee, K., & Blower, P. J. (2015) · Journal of Nuclear Medicine · doi:10.2967/jnumed.115.162370 · Cited by 67

Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimers disease

Wallin, C., Kulkarni, Y., Abelein, A., Jarvet, J., Liao, Q., Strodel, B., Olsson, L., Luo, J., Abrahams, J. P., Sholts, S. B., et al. (2016) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.03.009 · Cited by 67

Copper-Triggered Aggregation of Ubiquitin

Arnesano, F., Scintilla, S., Calò, V., Bonfrate, E., Ingrosso, C., Losacco, M., Pellegrino, T., Rizzarelli, E., & Natile, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007052 · Cited by 68

Copper Binding to the Neurotoxic Peptide PrP106–126: Thermodynamic and Structural Studies

Belosi, B., Gaggelli, E., Guerrini, R., Kozłowski, H., Łuczkowski, M., Mancini, F. M., Remelli, M., Valensin, D., & Valensin, G. (2004) · ChemBioChem · doi:10.1002/cbic.200300786 · Cited by 66

Fermented papaya preparation attenuates β-amyloid precursor protein: β-amyloid–mediated copper neurotoxicity in β-amyloid precursor protein and β-amyloid precursor protein Swedish mutation overexpressing SH-SY5Y cells

Zhang, J., Mori, A., Chen, Q., & Zhao, B. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.07.023 · Cited by 66

Bridging Type 2 Diabetes and Alzheimer's Disease: Assembling the Puzzle Pieces in the Quest for the Molecules With Therapeutic and Preventive Potential

de Matos, A. M., Macedo, M. P., & Rauter, A. P. (2017) · Medicinal Research Reviews · doi:10.1002/med.21440 · Cited by 68

Neurotoxicity from glutathione depletion is dependent on extracellular trace copper

White, A. R., & Cappai, R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10537 · Cited by 66

Murine Aβ over-production produces diffuse and compact Alzheimer-type amyloid deposits

Xu, G., Ran, Y., Fromholt, S. E., Fu, C., Yachnis, A. T., Golde, T. E., & Borchelt, D. R. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0252-9 · Cited by 65

Role of antioxidants and a nutrient rich diet in Alzheimer's disease

Veurink, G., Perry, G. L., & Singh, S. K. (2020) · Open Biology · doi:10.1098/rsob.200084 · Cited by 69

Soluble aggregates of the amyloid‐β protein selectively stimulate permeability in human brain microvascular endothelial monolayers

Gonzalez‐Velasquez, F. J., Kotarek, J. A., & Moss, M. A. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05618.x · Cited by 67

Modulation of mitochondrial membrane potential and reactive oxygen species production by copper in astrocytes

Gyulkhandanyan, A. V., Feeney, C. J., & Pennefather, P. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02029.x · Cited by 65

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 66

Neuroinflammation and Copper in Alzheimer’s Disease

Choo, X. Y., Alukaidey, L., White, A. R., & Grubman, A. (2013) · International Journal of Alzheimer s Disease · doi:10.1155/2013/145345 · Cited by 70

Characterization of New Specific Copper Chelators as Potential Drugs for the Treatment of Alzheimer’s Disease

Nguyen, M., Robert, A., Sournia‐Saquet, A., Vendier, L., & Meunier, B. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201402143 · Cited by 67

Magnesium Status in Alzheimer’s Disease: A Systematic Review

Veronese, N., Zurlo, A., Solmi, M., Luchini, C., Trevisan, C., Bano, G., Manzato, E., Sergi, G., & Rylander, R. (2016) · American Journal of Alzheimer's Disease & Other Dementias® · doi:10.1177/1533317515602674 · Cited by 64

Sources and triggers of oxidative damage in neurodegeneration

Angelova, P. R. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.003 · Cited by 67

Cerebrovascular requirement for sealant, anti-coagulant and remodeling molecules that allow for the maintenance of vascular integrity and blood supply

Atwood, C., Bowen, R. L., Smith, M. A., & Perry, G. L. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(03)00206-6 · Cited by 64

Beta-amyloid expression, release and extracellular deposition in aged rat brain slices

Marksteiner, J., & Humpel, C. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4002072 · Cited by 64

Acidosis, Acid-Sensing Ion Channels, and Neuronal Cell Death

Wang, Y., & Xu, T. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8204-2 · Cited by 64

Paradoxical Condensation of Copper with Elevated β-Amyloid in Lipid Rafts under Cellular Copper Deficiency Conditions

Hung, Y. H., Robb, E. L., Volitakis, I., Ho, M., Evin, G. M., Li, Q.-X., Culvenor, J. G., Masters, C. L., Cherny, R. A., & Bush, A. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019521 · Cited by 64

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 64

Cu2+ accentuates distinct misfolding of Aβ(1–40) and Aβ(1–42) peptides, and potentiates membrane disruption

Matheou, C. J., Younan, N. D., & Viles, J. H. (2014) · Biochemical Journal · doi:10.1042/bj20141168 · Cited by 64

Differential protein expression of hippocampal cells associated with heavy metals (Pb, As, and MeHg) neurotoxicity: Deepening into the molecular mechanism of neurodegenerative diseases

Karri, V., Ramos, D., Bauzá‐Martinez, J., Odena, M. A., de Oliveira, E., Coort, S. L., Evelo, C. T., Mariman, E. C. M., Schuhmacher, M., & Kumar, V. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.06.020 · Cited by 65

Melatonin prevents free radical formation due to the interaction between β‐amyloid peptides and metal ions [Al(III), Zn(II), Cu(II), Mn(II), Fe(II)]

Zatta, P. F., Tognon, G., & Carampin, P. (2003) · Journal of Pineal Research · doi:10.1034/j.1600-079x.2003.00058.x · Cited by 64

Free copper and resting temporal EEG rhythms correlate across healthy, mild cognitive impairment, and Alzheimer’s disease subjects

Babiloni, C., Squitti, R., Percio, C. D., Cassetta, E., Ventriglia, M. C., Ferreri, F., Tombini, M., Frisoni, G. B., Binetti, G. G., Gurzì, M., et al. (2007) · Clinical Neurophysiology · doi:10.1016/j.clinph.2007.03.016 · Cited by 64

Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain 1 1Edited by A. Fersht

Davis, D. P., Gallo, G., Vogen, S. M., Dul, J. L., Sciarretta, K. L., Kumar, A. R., Wilton, R., Stevens, F. J., & Argon, Y. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5092 · Cited by 63

Control of Alzheimer's Amyloid Beta Toxicity by the High Molecular Weight Immunophilin FKBP52 and Copper Homeostasis in Drosophila

Sanokawa‐Akakura, R., Cao, W., Allan, K., Patel, K., Ganesh, A., Heiman, G. A., Burke, R., Kemp, F. W., Bogden, J. D., Camakaris, J., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008626 · Cited by 62

Antioxidant, anti‐inflammatory and epigenetic potential of curcumin in Alzheimer's disease

Abdul‐Rahman, T., Awuah, W. A., Mikhailova, T., Kalmanovich, J. B., Mehta, A., Ng, J. C., Coghlan, M. A., Zivcevska, M., Tedeschi, A. J., Oliveira, E. C., et al. (2024) · BioFactors · doi:10.1002/biof.2039 · Cited by 66

Strategies, Development, and Pitfalls of Therapeutic Options for Alzheimer's Disease

Haas, C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110986 · Cited by 61

Fibrillation in Human Serum Albumin Is Enhanced in the Presence of Copper(II)

PANDEY, N. K., Ghosh, S., & Dasgupta, S. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp103876p · Cited by 61

Metal Binding Modes of Alzheimer's Amyloid β-Peptide in Insoluble Aggregates and Soluble Complexes

Miura, T., Suzuki, K., Kohata, N., & Takeuchi, H. (2000) · Biochemistry · doi:10.1021/bi0002479 · Cited by 457

Roles of Cu2+ in the conformational transitions and dimerization of amyloid-beta peptide and its implications in Alzheimer's disease

Liao, Q. (2016)

Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Suzuki, K., Miura, T., & Takeuchi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5263 · Cited by 90

pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide

Ghalebani, L., Wahlström, A., Danielsson, J., Wärmländer, S. K. T. S., & Gräslund, A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.043 · Cited by 48

Binding of zinc(II) and copper(II) to the full‐length Alzheimer’s amyloid‐β peptide

Tõugu, V., Tiiman, A., & Palumaa, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05061.x · Cited by 219