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

Amyloid‐β: A vascular sealant that protects against hemorrhage?

Atwood, C. S., Bishop, G. M., Perry, G., & Smith, M. A. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10388 · Cited by 44

Soluble Amyloid β1−28−Copper(I)/Copper(II)/Iron(II) Complexes Are Potent Antioxidants in Cell-Free Systems

Baruch-Suchodolsky, R., & Fischer, B. (2008) · Biochemistry · doi:10.1021/bi800114g · Cited by 44

Zinc, copper, and carnosine attenuate neurotoxicity of prion fragment PrP106-126

Kawahara, M., Koyama, H., Nagata, T., & Sadakane, Y. (2011) · Metallomics · doi:10.1039/c1mt00015b · Cited by 44

Stabilization of native amyloid β-protein oligomers by Copper and Hydrogen peroxide Induced Cross-linking of Unmodified Proteins (CHICUP)

Williams, T. L., Serpell, L. C., & Urbanc, B. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.12.001 · Cited by 45

Enhanced Emission from Single Isolated Gold Quantum Dots Investigated Using Two-Photon-Excited Fluorescence Near-Field Scanning Optical Microscopy

Abeyasinghe, N., Kumar, S., Sun, K., Mansfield, J. F., Jin, R. M., & Goodson, T. G., III (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b07737 · Cited by 44

Glycosylated tetrahydrosalens as multifunctional molecules for Alzheimer's therapy

Storr, T., Scott, L. E., Bowen, M. L., Green, D. E., Thompson, K. H., Schugar, H. J., & Orvig, C. (2009) · Dalton Transactions · doi:10.1039/b902545f · Cited by 44

Ubiquitin Stability and the Lys 63‐Linked Polyubiquitination Site Are Compromised on Copper Binding

Milardi, D., Arnesano, F., Grasso, G., Magrì, A. L., Tabbı̀, G., Scintilla, S., Natile, G., & Rizzarelli, E. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200701987 · Cited by 44

Links between copper and cholesterol in Alzheimer's disease

Hung, Y. H., Bush, A. I., & Fontaine, S. L. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00111 · Cited by 44

A label-free and signal-on electrochemiluminescence strategy for sensitive amyloid-beta assay

Qin, H., Gao, X. P., Yang, X., Cao, W., & Liu, S. (2019) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2019.111438 · Cited by 43

Human Aβ1–42 reduces iron‐induced toxicity in rat cerebral cortex

Bishop, G. M., & Robinson, S. R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10661 · Cited by 43

Electrically pulsatile responsive drug delivery platform for treatment of Alzheimer’s disease

Wu, L. J., Wang, J., Gao, N., Ren, J., Zhao, A., & Qu, X. (2015) · Nano Research · doi:10.1007/s12274-015-0750-x · Cited by 43

Amyloid-β: a (life) preserver for the brain

Obrenovich, M. E., Joseph, J. A., Atwood, C., Perry, G. L., & Smith, M. A. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00038-6 · Cited by 44

Recent Development in the Understanding of Molecular and Cellular Mechanisms Underlying the Etiopathogenesis of Alzheimer’s Disease

Afsar, A., Castro, M. D. C. C., Soladogun, A. S., & Li, Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087258 · Cited by 45

Calorimetric investigation of copper(II) binding to Aβ peptides: thermodynamics of coordination plasticity

Sacco, C., Skowronsky, R. A., Gade, S., Kenney, J. M., & Spuches, A. M. (2012) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-012-0874-3 · Cited by 42

Aβ under stress: the effects of acidosis, Cu 2+ -binding, and oxidation on amyloid β-peptide dimers

Liao, Q., Owen, M. C., Bali, S., Barz, B., & Strodel, B. (2018) · Chemical Communications · doi:10.1039/c8cc02263a · Cited by 42

X-ray Absorption Spectroscopy Investigations of Copper(II) Coordination in the Human Amyloid β Peptide

Summers, K. L., Schilling, K. M., Roseman, G. P., Markham, K. A., Dolgova, N. V., Kröll, T., Sokaras, D., Millhauser, G. L., Pickering, I. J., & George, G. N. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b00507 · Cited by 42

Metal homeostasis in Alzheimer’s disease

White, A. R., Barnham, K. J., & Bush, A. I. (2006) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.6.5.711 · Cited by 42

Insight into Potential Cu(II)-Binding Motifs in the Four Pseudorepeats of Tau Protein

Shin, B., & Saxena, S. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp204410h · Cited by 42

Catabolic attacks of membrane-bound angiotensin-converting enzyme on the N-terminal part of species-specific amyloid-beta peptides.

Sun, X., Becker, M., Pankow, K., Krause, E., Ringling, M., Beyermann, M., Maul, B., Walther, T., & Siems, W. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.03.058 · Cited by 48

Quenched hydrogen/deuterium exchange NMR characterization of amyloid‐β peptide aggregates formed in the presence of Cu2+ or Zn2+

Olofsson, A., Lindhagen‐Persson, M., Vestling, M., Sauer-Eriksson, A. E., & Öhman, A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07113.x · Cited by 42

Interaction of β-amyloid(1-40) peptide with pairs of metal ions: An electrospray ion trap mass spectrometric model study

Drochioiu, G., Manea, M., Drăguşanu, M., Murariu, M., Drăgan, E. S., Petre, B. A., Mező, G., & Przybylski, M. (2009) · Biophysical Chemistry · doi:10.1016/j.bpc.2009.05.008 · Cited by 41

Controlling amyloid growth in multiple dimensions

Dong, J., Lu, K., Lakdawala, A. S., Mehta, A. K., & Lynn, D. G. (2006) · Amyloid · doi:10.1080/13506120600960809 · Cited by 41

Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments

Wild, K., August, A., Pietrzik, C. U., & Kins, S. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00021 · Cited by 45

Novel therapeutics for Alzheimer's disease: an update.

Bonda, D., Lee, H. P., Lee, H., Friedlich, A. L., Perry, G. L., Zhu, X., & Smith, M. A. (2010) · PubMed · Cited by 41

Inhibition of the Escherichia coli RecA protein: zinc(II), copper(II) and mercury(II) trap RecA as inactive aggregates

Lee, A. M., & Singleton, S. F. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.08.018 · Cited by 41

Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions

Stirpe, A., Rizzuti, B., Pantusa, M., Bartucci, R., Sportelli, L., & Guzzi, R. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0346-4 · Cited by 41

Brain copper may protect from cognitive decline and Alzheimer’s disease pathology: a community-based study

Agarwal, P., Ayton, S., Agrawal, S., Dhana, K., Bennett, D. A., Barnes, L. L., Leurgans, S. E., Bush, A. I., & Schneider, J. A. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01802-5 · Cited by 41

Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases

Cordeiro, Y., Macedo, B., Silva, J. L., & Gomes, M. P. B. (2014) · Biophysical Reviews · doi:10.1007/s12551-013-0132-0 · Cited by 40

A highly selective dual-channel fluorescent probe for the detection of Zn2+ ion and pyrophosphate in micelle

Chang, M. J., & Lee, M. H. (2017) · Dyes and Pigments · doi:10.1016/j.dyepig.2017.11.057 · Cited by 40

Overexpression of aldehyde dehydrogenase 1A1 reduces oxidation‐induced toxicity in SH‐SY5Y neuroblastoma cells

Zhang, M., Shoeb, M., Goswamy, J., Liu, P., Xiao, T., Hogan, D., Campbell, G. A., & Ansari, N. H. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22230 · Cited by 40

Nanoprobing of the Effect of Cu2+ Cations on Misfolding, Interaction and Aggregation of Amyloid β Peptide

Lv, Z., Condron, M. M., Teplow, D. B., & Lyubchenko, Y. L. (2012) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-012-9416-6 · Cited by 40

Die Alzheimer‐Demenz: von der Pathologie zu therapeutischen Ansätzen

Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie · doi:10.1002/ange.200802808 · Cited by 41

Metallostasis and amyloid β-degrading enzymes

Grasso, G., Giuffrida, M. L., & Rizzarelli, E. (2012) · Metallomics · doi:10.1039/c2mt20105d · Cited by 41

Metals and cholesterol: two sides of the same coin in Alzheimer’s disease pathology

Wong, B. X. W., Hung, Y. H., Bush, A. I., & Duce, J. A. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00091 · Cited by 41

Resistance of human cerebrospinal fluid toin vitrooxidation is directly related to its amyloid-β content

Kontush, A., Donarski, N., & Beisiegel†, U. (2001) · Free Radical Research · doi:10.1080/10715760100301521 · Cited by 39

Rapid label-free detection of metal-induced Alzheimer’s amyloid β peptide aggregation by electrochemical method

Geng, J., Yu, H., Ren, J., & Qu, X. (2008) · Electrochemistry Communications · doi:10.1016/j.elecom.2008.09.020 · Cited by 38

Comparison between the Aggregation of Human and Rodent Amyloid β-Proteins in GM1 Ganglioside Clusters

Ueno, H., YAMAGUCHI, T. J., Fukunaga, S., Okada, Y., Yano, Y., Hoshino, M., & Matsuzaki, K. (2014) · Biochemistry · doi:10.1021/bi501239q · Cited by 38

Copper mediated amyloid-β binding to Transthyretin

Ciccone, L., Fruchart‐Gaillard, C., Mourier, G., Savko, M., Nencetti, S., Orlandini, E., Servent, D., Stura, E. A., & Shepard, W. (2018) · Scientific Reports · doi:10.1038/s41598-018-31808-5 · Cited by 38

Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro

Sasanian, N., Bernson, D., Horváth, I., Wittung-Stafshede, P. E., & Esbjörner, E. K. (2020) · Biomolecules · doi:10.3390/biom10060924 · Cited by 38

“What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine

Abdelrahman, S., Alghrably, M., Lachowicz, J. I., Emwas, A.-H. M., Hauser, C. A. E., & Jaremko, M. (2020) · Molecules · doi:10.3390/molecules25225245 · Cited by 38

Zinc and Copper inhibit nerve growth factor-mediated protection from oxidative stress-induced apoptosis

Wang, W., Post, J. I., Dow, K. E., Shin, S. H., Riopelle, R. J., & Ross, G. M. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00929-x · Cited by 38

Possible involvement of copper(II) in Alzheimer disease.

Kowalik‐Jankowska, T., Ruta-Dolejsz, M., Wiśniewska, K., Łankiewicz, L., & Kozłowski, H. (2002) · Environmental Health Perspectives · doi:10.1289/ehp.02110s5869 · Cited by 38

Oxidative and hydrolytic properties of β‐amyloid

Brzyska, M., Bacia, A., & Elbaum, D. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02248.x · Cited by 38

Study of the non‐covalent interaction between amyloid‐β‐peptide and melatonin using electrospray ionization mass spectrometry

Bazoti, F. N., Tsarbopoulos, A., Markides, K. E., & Bergquist, J. (2005) · Journal of Mass Spectrometry · doi:10.1002/jms.738 · Cited by 38

Low concentrations of aggregated β-amyloid induce neurite formation via the neurotrophin receptor p75

Susen, K., & Blöchl, A. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0671-3 · Cited by 38

Binding Affinities for Models of Biologically Available Potential Cu(II) Ligands Relevant to Alzheimer's Disease: An ab Initio Study

Rickard, G. A., Gómez‐Balderas, R., Brunelle, P., Raffa, D. F., & Rauk, A. (2005) · The Journal of Physical Chemistry A · doi:10.1021/jp052303r · Cited by 38

Do glutathione and copper interact to modify Alzheimer's disease pathogenesis?

Ho, T., Ahmadi, S., & Kerman, K. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.01.025 · Cited by 37

PtCl2(phen) disrupts the metal ions binding to amyloid-β peptide

Ma, G., Wang, E., Hao, W., Wei, K., Zhu, P., & Liu, Y. (2013) · Metallomics · doi:10.1039/c3mt20262c · Cited by 37

Development of an Efficient Biosensor for the In Vivo Monitoring of Cu+ and pH in the Brain: Rational Design and Synthesis of Recognition Molecules

Liu, W., Dong, H. Y., Zhang, L., & Tian, Y. (2017) · Angewandte Chemie · doi:10.1002/ange.201710863 · Cited by 37

Copper in Alzheimer’s disease: Implications in amyloid aggregation and neurotoxicity

Gámez, P., & Caballero, A. B. (2015) · AIP Advances · doi:10.1063/1.4921314 · Cited by 37

Investigation of the effects of copper ions on protein aggregation using a model system

Capanni, C., Luigi Messori, A., Orioli, P., Chiti, F., Stefani, M., Ramponi, G., Taddei, N., & Gabrielli, S. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3447-3 · Cited by 40

An ultrathin graphitic carbon nitride nanosheet: a novel inhibitor of metal-induced amyloid aggregation associated with Alzheimer's disease

Li, M., Guan, Y., Ding, C., Chen, Z., Ren, J., & Qu, X. (2016) · Journal of Materials Chemistry B · doi:10.1039/c6tb01215a · Cited by 37

Unusual Cyclodextrin Derivatives as a New Avenue to Modulate Self‐ and Metal‐Induced Aβ Aggregation

Oliveri, V., Bellia, F., Pietropaolo, A., & Vecchio, G. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201502155 · Cited by 36

The Efficacy and Pharmacological Mechanism of Zn7MT3 to Protect against Alzheimer’s Disease

Xu, W., Xu, Q., Cheng, H., & Tan, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-12800-x · Cited by 36

Amyloid-β peptide (1–42) aggregation induced by copper ions under acidic conditions

Bin, Y., Li, X., He, Y., Chen, S., & Xiang, J. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt044 · Cited by 36

Copper inducing Aβ42 rather than Aβ40 nanoscale oligomer formation is the key process for Aβ neurotoxicity

Jin, L., Wu, W., Li, Q., Zhao, Y., & Li, Y. (2011) · Nanoscale · doi:10.1039/c1nr11029b · Cited by 36

Spatial memory deficits in a mouse model of late-onset Alzheimer’s disease are caused by zinc supplementation and correlate with amyloid-beta levels

Flinn, J. M., Bozzelli, P. L., Adlard, P. A., & Railey, A. M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00174 · Cited by 37

Expression Pattern of Scavenger Receptors and Amyloid-β Phagocytosis of Astrocytes and Microglia in Culture are Modified by Acidosis: Implications for Alzheimer’s Disease

Eugenín, J. L., Vecchiola, A., Murgas, P., Arroyo, P., Cornejo, F., & Rommy von Bernhardi, M. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160083 · Cited by 35

Review of Amyotrophic Lateral Sclerosis, Parkinson’s and Alzheimer’s diseases helps further define pathology of the novel paradigm for Alzheimer’s with heavy metals as primary disease cause

Cavaleri, F. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.10.009 · Cited by 36

Aβ(25–35) and its C‐ and/or N‐blocked derivatives: Copper driven structural features and neurotoxicity

Giuffrida, M. L., Grasso, G., Ruvo, M., Pedone, C., Saporito, A., Marasco, D., Pignataro, B., Cascio, C., Copani, A., & Rizzarelli, E. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21135 · Cited by 35

On the metal ion (Zn2+, Cu2+) coordination with beta-amyloid peptide: DFT computational study

Marino, T., Russo, N., Toscano, M., & Pavelka, M. (2010) · Interdisciplinary Sciences Computational Life Sciences · doi:10.1007/s12539-010-0086-x · Cited by 35

Natural antioxidants in prevention and management of Alzheimer's disease

Zhao, Y. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/419 · Cited by 35

X‐ray photoelectron spectroscopic and Raman analysis of silk fibroin–Cu(II) films

Li, Z., Chen, X., Dai, W., & Shao, Z. (2006) · Biopolymers · doi:10.1002/bip.20472 · Cited by 35

Amyloid β

Cappai, R., & White, A. R. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00027-8 · Cited by 35

Aluminum speciation studies in biological fluids Part 5. A quantitative investigation of Al(III) complex equilibria with desferrioxamine, 2,3-dihydroxybenzoic acid, Tiron, CP20 (L1), and CP94 under physiological conditions, and computer-aided assessment of the aluminum-mobilizing capacities of these ligands in vivo

Desroches, S., Biron, F., & Berthon, G. (1999) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(99)00029-x · Cited by 36

The Neuroprotective Activities of the Novel Multi-Target Iron-Chelators in Models of Alzheimer’s Disease, Amyotrophic Lateral Sclerosis and Aging

Kupershmidt, L., & Youdim, M. B. H. (2023) · Cells · doi:10.3390/cells12050763 · Cited by 36

Current biomarkers and treatment strategies in Alzheimer disease: An overview and future perspectives

Bhole, R. P., Chikhale, R. V., & Rathi, K. M. (2023) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2023.11.003 · Cited by 34

Model studies of cholesterol and ascorbate oxidation by copper complexes: Relevance to Alzheimer’s disease β-amyloid metallochemistry

Hæffner, F., Smith, D. G., Barnham, K. J., & Bush, A. I. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.09.011 · Cited by 34

Protective effect of zinc on amyloid-ß 25–35 and 1–40 mediated toxicity

Cardoso, S. M., Rego, A. C., Pereira, C., & Oliveira, C. R. (2005) · Neurotoxicity Research · doi:10.1007/bf03033885 · Cited by 34

Characterization of the Binding of Cu(II) and Zn(II) to Transthyretin: Effects on Amyloid Formation

Wilkinson‐White, L. E., & Easterbrook‐Smith, S. B. (2007) · Biochemistry · doi:10.1021/bi700607z · Cited by 34

Metalloproteins and neuronal death

Brown, D. R. (2009) · Metallomics · doi:10.1039/b912601e · Cited by 34

Enhanced Histochemical Detection of Iron in Paraffin Sections of Mouse Central Nervous System Tissue

Sands, S. A., Leung-Toung, R., Wang, Y., Connelly, J., & LeVine, S. M. (2016) · ASN NEURO · doi:10.1177/1759091416670978 · Cited by 34

Modelling Alzheimer's disease: Insights fromin vivotoin vitrothree-dimensional culture platforms

Ranjan, V., Qiu, L., Tan, E., Zeng, L., & Zhang, Y. (2018) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.2728 · Cited by 41

Cu(II) Potentiation of Alzheimer Aβ1-40 Cytotoxicity and Transition on its Secondary Structure

Dai, X., Sun, Y., & Jiang, Z.-F. (2006) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2006.00228.x · Cited by 34

Effect of Zinc Ions on the Cytotoxicity Induced by the Amyloid β -Peptide

Moreira, P. I., Pereira, C., Santos, M. S., & Oliveira, C. R. (2000) · Antioxidants and Redox Signaling · doi:10.1089/ars.2000.2.2-317 · Cited by 34

Bioluminescence imaging reveals inhibition of tumor cell proliferation by Alzheimer's amyloid β protein

Zhao, H., Zhu, J., Cui, K., Xu, X., O'Brien, M., Wong, K. K., Kesari, S., Xia, W., & Wong, S. T. (2009) · Cancer Cell International · doi:10.1186/1475-2867-9-15 · Cited by 33

Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements

Giannozzi, P., Jansen, K., Penna, G. L., Minicozzi, V., Morante, S., Rossi, G. C., & Stellato, F. (2011) · Metallomics · doi:10.1039/c2mt00148a · Cited by 33

Emerging evidence for the neuroprotective role of α-synuclein

Lee, H., Zhu, X., Takeda, A., Perry, G. L., & Smith, M. A. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.04.024 · Cited by 37

Exploring the differences between mouse mAβ1–42 and human hAβ1–42 for Alzheimer's disease related properties and neuronal cytotoxicity

Lv, X., Li, W., Luo, Y., Wang, D., Zhu, C., Huang, Z., & Tan, X. (2013) · Chemical Communications · doi:10.1039/c3cc40779a · Cited by 33

Alzheimer's Amyloid-β as a Preventive Antioxidant for Brain Lipoproteins

Kontush, A. (2001) · Cellular and Molecular Neurobiology · doi:10.1023/a:1012629603390 · Cited by 34

Mechanism of Copper(II) Inhibiting Alzheimer's Amyloid β-Peptide from Aggregation: A Molecular Dynamics Investigation

Jiao, Y., & Yang, P. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp0673359 · Cited by 34

On the generation of OH(.) radical species from H2O2 by Cu(I) amyloid beta peptide model complexes: A DFT investigation

Prosdocimi, T., De Gioia, L., Zampella, G., & Bertini, L. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1322-y · Cited by 32

On the Conformational Dynamics of β-Amyloid Forming Peptides: A Computational Perspective

Saravanan, K. M., Zhang, H., Zhang, H., Xi, W., & Wei, Y. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00532 · Cited by 33

A new evidence for DNA nicking property of amyloid β-peptide (1–42): Relevance to Alzheimer’s disease

Suram, A., Hegde, M. L., & Rao, K. S. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.015 · Cited by 32

Amyloid-β precursor protein expression and modulation in human embryonic stem cells: A novel role for human chorionic gonadotropin

Porayette, P., Gallego, M. J., Kaltcheva, M. M., Meethal, S. V., & Atwood, C. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.021 · Cited by 32

The Cu(ii) complex of Aβ40 peptide in ammonium acetate solutions. Evidence for ternary species formation

Rózga, M., Protas, A. M., Jabłonowska, A., Dadlez, M., & Bal, W. (2009) · Chemical Communications · doi:10.1039/b819616h · Cited by 32

Effect of Imidazole on the Solubility of a His-Tagged Antibody Fragment

Hamilton, S., Odili, J. I., Pacifico, M. D., Wilson, G. D., & Kupsch, J. (2003) · Hybridoma and Hybridomics · doi:10.1089/153685903771797048 · Cited by 32

NMR studies of zinc binding in a multi-histidinic peptide fragment

Zoroddu, M. A., Medici, S., Peana, M., & Anedda, R. (2009) · Dalton Transactions · doi:10.1039/b914296g · Cited by 31

Metal attenuating therapies in neurodegenerative disease

Mot, A. I., Wedd, A. G., Sinclair, L., Brown, D. R., Collins, S. J., & Brazier, M. W. (2011) · Expert Review of Neurotherapeutics · doi:10.1586/ern.11.170 · Cited by 32

Amyloids: Regulators of Metal Homeostasis in the Synapse

Kawahara, M., Kato‐Negishi, M., & Tanaka, K. (2020) · Molecules · doi:10.3390/molecules25061441 · Cited by 31

Neurotoxicity from glutathione depletion is mediated by Cu-dependent p53 activation

Du, T., Ciccotosto, G. D., Cranston, G. A., Kocak, G., Masters, C. L., Crouch, P. J., Cappai, R., & White, A. R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.001 · Cited by 31

High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation

Žerovnik, E., Škerget, K., Žnidarič, M. T., Loeschner, C., Brazier, M. W., & Brown, D. R. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05426.x · Cited by 31

Molecular Basis for the Cu2+ Binding-Induced Destabilization of β2-Microglobulin Revealed by Molecular Dynamics Simulation

Deng, N., Yan, L., Singh, D. L., & Cieplak, P. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.064444 · Cited by 31

Metallo-complex activation of neuroprotective signalling pathways as a therapeutic treatment for Alzheimer’s disease

Bica, L., Crouch, P. J., Cappai, R., & White, A. R. (2008) · Molecular BioSystems · doi:10.1039/b816577g · Cited by 33

Tuning Reactivity of Diphenylpropynone Derivatives with Metal-Associated Amyloid-β Species via Structural Modifications

Liu, Y., Kochi, A., Pithadia, A. S., Lee, S., Nam, Y., Beck, M. W., He, X., Lee, D., & Lim, M. H. (2013) · Inorganic Chemistry · doi:10.1021/ic400851w · Cited by 30

The role of terminal amino group and histidine at the fourth position in the metal ion binding of oligopeptides revisited: Copper(II) and nickel(II) complexes of glycyl-glycyl-glycyl-histamine and its N-Boc protected derivative

Jancsó, A., Selmeczi, K., Gizzi, P., May, N. V., Gajda, T., & Henry, B. (2010) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2010.09.004 · Cited by 30

Current understanding of the interactions between metal ions and Apolipoprotein E in Alzheimer’s disease

Zhang, Y., Gao, H., Zheng, W., & Xu, H. J. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105824 · Cited by 31

Possible mechanisms of APP-mediated oxidative stress in Alzheimer’s disease1,2 1Guest Editors: Mark A. Smith and George Perry 2This article is part of a series of reviews on “Causes and Consequences of Oxidative Stress in Alzheimer’s Disease.” The full list of papers may be found on the homepage of the journal.

Multhaup, G., Scheuermann, S., Schlicksupp, A., Simons, A., Strauss, M., Kemmling, A., Oehler, C., Cappai, R., Pipkorn, R., & Bayer, T. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00806-7 · Cited by 30

Is Alzheimer's disease amyloidosis the result of a repair mechanism gone astray?

Kokjohn, T. A., Maarouf, C. L., & Roher, A. E. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.2429 · Cited by 31

Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer’s Aβ peptide

Garvey, M., Tepper, K., Haupt, C., Knüpfer, U., Klement, K., Meinhardt, J., Horn, U., Balbach, J., & Fändrich, M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.141 · Cited by 30

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