Rapid induction of Alzheimer A beta amyloid formation by zinc

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

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659

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

The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,780

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

A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513

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

Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type

Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,399

Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene

Chartier-Harlin, M.-C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L., Goate, A., Rossor, M., Roques, P., Hardy, J., et al. (1991) · Nature · doi:10.1038/353844a0 · Cited by 1,214

Nutrient patterns and brain biomarkers of Alzheimer's disease in cognitively normal individuals

Berti, V., Murray, J., Davies, M., Spector, N. C., Tsui, W. H., Li, Y., Williams, S. K., Pirraglia, E., Vallabhajosula, S., McHugh, P. F., et al. (2014) · The journal of nutrition health & aging · doi:10.1007/s12603-014-0534-0 · Cited by 156

Aβ as a bioflocculant: implications for the amyloid hypothesis of Alzheimer’s disease

Robinson, S. R., & Bishop, G. M. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00342-6 · Cited by 155

Increased tau Phosphorylation in Apolipoprotein E4 Transgenic Mice Is Associated with Activation of Extracellular Signal-regulated Kinase

Harris, F. M., Brecht, W. J., Xu, Q., Mahley, R. W., & Huang, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408127200 · Cited by 151

The art of building multifunctional metal-binding agents from basic molecular scaffolds for the potential application in neurodegenerative diseases

Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151

Alzheimer’s disease: How metal ions define β-amyloid function

Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 154

Enhanced Amyloidogenic Processing of the β-Amyloid Precursor Protein in Gene-targeted Mice Bearing the Swedish Familial Alzheimer's Disease Mutations and a “Humanized” Aβ Sequence

Reaume, A. G., Howland, D. S., Trusko, S. P., Savage, M. J., Lang, D. M., Greenberg, B. D., Siman, R., & Scott, R. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23380 · Cited by 150

Genetic and Epigenetic Etiology Underlying Autism Spectrum Disorder

Yoon, S. H., Choi, J., Lee, W. Y., & Do, J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9040966 · Cited by 175

Aqueous Fluorescence Turn-on Sensor for Zn2+ with a Tetraphenylethylene Compound

Sun, F., Zhang, G., Zhang, D., Xue, L., & Jiang, H. (2011) · Organic Letters · doi:10.1021/ol2026735 · Cited by 149

Modulating Amyloid Self-Assembly and Fibril Morphology with Zn(II)

Dong, J., Shokes, J. E., Scott, R. A., & Lynn, D. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja055973j · Cited by 149

The Role of Zinc in Alzheimer′s Disease

Watt, N. T., Whitehouse, I. J., & Hooper, N. M. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/971021 · Cited by 148

Nanoparticle–chelator conjugates as inhibitors of amyloid-β aggregation and neurotoxicity: A novel therapeutic approach for Alzheimer disease

Liu, G., Men, P., Kudo, W., Perry, G., & Smith, M. A. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.03.064 · Cited by 148

Multi-Target Directed Donepezil-Like Ligands for Alzheimer's Disease

Unzeta, M., Esteban, G., Bolea, I., Fogel, W. A., Ramsay, R. R., Youdim, M. B. H., Tipton, K. F., & Marco, J. L. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00205 · Cited by 154

Oxidative processes in Alzheimer's disease: the role of Aβ-metal interactions

Lynch, T. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00112-1 · Cited by 151

Binding of Zn(II), Cu(II), and Fe(II) ions to alzheimer's Aß peptide studied by fluorescence

Garzon-Rodriguez, W., Yatsimirsky, A. K., & Glabe, C. G. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00357-1 · Cited by 148

Impact of antioxidants, zinc, and copper on cognition in the elderly

Age-Related Eye Disease Study Research Group (2004) · Neurology · doi:10.1212/01.wnl.0000142969.19465.8f · Cited by 149

Transgenic mouse models of Alzheimer's disease: phenotype and application.

(2003) · PubMed · doi:10.1097/01.fbp.0000088420.18414.ff · Cited by 147

Alzheimer's disease & metals: therapeutic opportunities

Kenche, V. B., & Barnham, K. J. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01221.x · Cited by 147

Acceleration of Amyloid β-Peptide Aggregation by Physiological Concentrations of Calcium

Isaacs, A. M., Senn, D. B., Yuan, M., Shine, J. P., & Yankner, B. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602061200 · Cited by 149

Assessment of ZnT3 and PSD95 protein levels in Lewy body dementias and Alzheimer's disease: association with cognitive impairment

Whitfield, D., Vallortigara, J., Alghamdi, A., Howlett, D. R., Hortobágyi, T., Johnson, M., Attems, J., Newhouse, S., Ballard, C. G., Thomas, A. J., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.06.015 · Cited by 144

Alzheimer's centennial legacy: prospects for rational therapeutic intervention targeting the A amyloid pathway

Masters, C. L., & Beyreuther, K. (2006) · Brain · doi:10.1093/brain/awl251 · Cited by 145

Thiamine deficiency induces oxidative stress and exacerbates the plaque pathology in Alzheimer's mouse model

Karuppagounder, S. S., Xu, H., Shi, Q., Chen, L. H., Pedrini, S., Pechman, D., Baker, H., Beal, M. F., Gandy, S., & Gibson, G. E. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.12.013 · Cited by 144

Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer's amyloidogenesis

Dedeoglu, A., Cormier, K., Payton, S., Tseitlin, K. A., Kremsky, J. N., Lai, L., Li, X., Moir, R. D., Tanzi, R. E., Bush, A. I., et al. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.08.016 · Cited by 141

Prion protein facilitates uptake of zinc into neuronal cells

Watt, N. T., Taylor, D. R., Kerrigan, T. L., Jarosz-Griffiths, H., Rushworth, J. V., Whitehouse, I. J., & Hooper, N. M. (2012) · Nature Communications · doi:10.1038/ncomms2135 · Cited by 137

Neuronal Zinc Exchange with the Blood Vessel Wall Promotes Cerebral Amyloid Angiopathy in an Animal Model of Alzheimer's Disease

Friedlich, A. L., Lee, J., van Groen, T., Cherny, R. A., Volitakis, I., Cole, T. B., Palmiter, R. D., Koh, J., & Bush, A. I. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0297-04.2004 · Cited by 138

Blood cadmium levels and Alzheimer’s disease mortality risk in older US adults

Min, J., & Min, K. (2016) · Environmental Health · doi:10.1186/s12940-016-0155-7 · Cited by 138

The Interaction between Apolipoprotein E and Alzheimer's Amyloid β-Peptide Is Dependent on β-Peptide Conformation

Golabek, A. A., Soto, C. A., Vogel, T., & Wısnıewskı, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10602 · Cited by 137

The “Nonamyloidogenic” p3 Fragment (Amyloid β17-42) Is a Major Constituent of Down's Syndrome Cerebellar Preamyloid

Lalowski, M. M., Golabek, A. A., Lemere, C. A., Selkoe, D. J., Wı́sniewski, H. M., Beavis, R. C., Frangione, B., & Wısnıewskı, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.52.33623 · Cited by 134

Neuroprotective features of carnosine in oxidative driven diseases

Bellia, F., Vecchio, G., Cuzzocrea, S., Calabrese, V., & Rizzarelli, E. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.009 · Cited by 142

The role of intracellular zinc release in aging, oxidative stress, and Alzheimer’s disease

McCord, M. C., & Aizenman, E. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00077 · Cited by 142

Iron, Copper, and Zinc Concentration in Aβ Plaques in the APP/PS1 Mouse Model of Alzheimer’s Disease Correlates with Metal Levels in the Surrounding Neuropil

James, S., Churches, Q. I., de Jonge, M. D., Birchall, I. E., Streltsov, V. A., McColl, G., Adlard, P. A., & Hare, D. J. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00362 · Cited by 136

Structure and function of amyloid in Alzheimer's disease

Morgan, C., Colombres, M., Núñez, M. T., & Inestrosa, N. C. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.10.004 · Cited by 146

Histochemically Reactive Zinc in Plaques of the Swedish Mutant β-Amyloid Precursor Protein Transgenic Mice

Lee, J., Mook‐Jung, I., & Koh, J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-11-j0002.1999 · Cited by 136

The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity

Sharma, A. K., Pavlova, S. T., Kim, J., Kim, J., & Mirica, L. M. (2013) · Metallomics · doi:10.1039/c3mt00161j · Cited by 135

Structural and thermodynamical properties of CuII amyloid-β16/28 complexes associated with Alzheimer’s disease

Guilloreau, L., Damian, L., Coppel, Y., Mazarguil, H., Winterhalter, M., & Faller, P. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0154-1 · Cited by 134

Metal exposure and Alzheimer’s pathogenesis

Liu, G., Huang, W., Moir, R. D., Vanderburg, C. R., Lai, B. C. H., Peng, Z., Tanzi, R. E., Rogers, J. T., & Huang, X. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.12.011 · Cited by 135

Fluorescent Zinc Sensor with Minimized Proton-Induced Interferences: Photophysical Mechanism for Fluorescence Turn-On Response and Detection of Endogenous Free Zinc Ions

Kwon, J. E., Lee, S., You, Y., Baek, K.-H., Ohkubo, K., Cho, J., Fukuzumi, S., Shin, I., Park, S. Y., & Nam, W. (2012) · Inorganic Chemistry · doi:10.1021/ic300476e · Cited by 134

Zinc, Carnosine, and Neurodegenerative Diseases

Kawahara, M., Tanaka, K.-I., & Kato-Negishi, M. (2018) · Nutrients · doi:10.3390/nu10020147 · Cited by 134

Amyloid accomplices and enforcers

Alexandrescu, A. T. (2004) · Protein Science · doi:10.1110/ps.04887005 · Cited by 137

Engineering metal ion coordination to regulate amyloid fibril assembly and toxicity

Dong, J., Canfield, J. M., Mehta, A. K., Shokes, J. E., Tian, B., Childers, W. S., Simmons, J. A., Mao, Z., Scott, R. A., Warncke, K., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702669104 · Cited by 134

Alzheimer's disease: An overview of amyloid beta dependent pathogenesis and its therapeutic implications along with in silico approaches emphasizing the role of natural products

Awasthi, M., Singh, S., Pandey, V. P., & Dwivedi, U. N. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.01.008 · Cited by 139

Zinc-binding structure of a catalytic amyloid from solid-state NMR

Lee, M., Wang, T., Makhlynets, O. V., Wu, Y., Polizzi, N. F., Wu, H., Gosavi, P. M., Stöhr, J., Korendovych, I. V., DeGrado, W. F., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706179114 · Cited by 133

Inhibition of the formation of amyloid β‐protein fibrils using biocompatible nanogels as artificial chaperones

Ikeda, K., Okada, T., Sawada, S., Akiyoshi, K., & Matsuzaki, K. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.009 · Cited by 133

Lithium deficiency and the onset of Alzheimer’s disease

Aron, L., Ngian, Z., Qiu, C., Choi, J., Liang, M., Drake, D., Hamplova, S. E., Lacey, E. K., Roche, P., Yuan, M., et al. (2025) · Nature · doi:10.1038/s41586-025-09335-x · Cited by 153

Zinc in the Brain: Friend or Foe?

Choi, S., Hong, D. K., Choi, B. Y., & Suh, S. W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238941 · Cited by 140

Zinc Binding to Alzheimer's Aβ(1–16) Peptide Results in Stable Soluble Complex

Kozin, S. A., Zirah, S., Rebuffat, S., Hoa, G. H. B., & Debey, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5284 · Cited by 131

Disease-modifying treatments for Alzheimer’s disease

Galimberti, D., & Scarpini, E. A. (2011) · Therapeutic Advances in Neurological Disorders · doi:10.1177/1756285611404470 · Cited by 128

Biometals and Their Therapeutic Implications in Alzheimer's Disease

Ayton, S., Lei, P., & Bush, A. I. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0312-z · Cited by 134

A Highly Selective Chemosensor for Al(III) and Zn(II) and Its Coordination with Metal Ions

Cao, W., Zheng, X., Sun, J.-P., Wong, W., Fang, D., Zhang, J., & Jin, L. (2014) · Inorganic Chemistry · doi:10.1021/ic402811x · Cited by 130

Zinc: indications in brain disorders

Prakash, A. K., Bharti, K., & Majeed, A. B. A. (2015) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12110 · Cited by 131

Formation of Bradykinin: A Major Contributor to the Innate Inflammatory Response

Joseph, K., & Kaplan, A. P. (2005) · Advances in immunology · doi:10.1016/s0065-2776(04)86005-x · Cited by 129

Clioquinol Decreases Amyloid-β Burden and Reduces Working Memory Impairment in a Transgenic Mouse Model of Alzheimer's Disease

Grossi, C., Francese, S., Casini, A., Rosi, M. C., Luccarini, I., Fiorentini, A., Gabbiani, C., Luigi Messori, A., Moneti, G., & Casamenti, F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1063 · Cited by 131

Copper, β-amyloid, and Alzheimer's disease: Tapping a sensitive connection

Bush, A. I., Masters, C. L., & Tanzi, R. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135061100 · Cited by 128

Metal protein attenuating compounds for the treatment of Alzheimer's dementia

Sampson, E. L., Jenagaratnam, L., & McShane, R. H. (2014) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd005380.pub5 · Cited by 128

Signal transduction during amyloid-β-peptide neurotoxicity: role in Alzheimer disease

Fuentealba, R. A., Farı́as, G. G., Scheu, J., Bronfman, M., Marzolo, M., & Inestrosa, N. C. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.07.018 · Cited by 126

Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases

Breydo, L., & Uversky, V. N. (2011) · Metallomics · doi:10.1039/c1mt00106j · Cited by 129

Revisiting the Amyloid Cascade Hypothesis: From Anti-Aβ Therapeutics to Auspicious New Ways for Alzheimer’s Disease

Uddin, M. S., Kabir, M. T., Rahman, M. S., Behl, T., Jeandet, P., Ashraf, G. M., Najda, A., Bin-Jumah, M. N., El-Seedi, H. R., & Abdel‐Daim, M. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165858 · Cited by 131

Amyloid plaques in PSAPP mice bind less metal than plaques in human Alzheimer's disease

Leskovjan, A. C., Lanzirotti, A., & Miller, L. M. (2009) · NeuroImage · doi:10.1016/j.neuroimage.2009.05.063 · Cited by 129

Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation

Abelein, A., Gräslund, A., & Danielsson, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421961112 · Cited by 123

Therapeutic Redistribution of Metal Ions To Treat Alzheimer’s Disease

Crouch, P. J., & Barnham, K. J. (2012) · Accounts of Chemical Research · doi:10.1021/ar300074t · Cited by 125

Alzheimer’s disease due to loss of function: A new synthesis of the available data

Kepp, K. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.004 · Cited by 123

Mesoporous Silica Nanoparticle‐based H2O2 Responsive Controlled‐Release System Used for Alzheimer's Disease Treatment

Geng, J., Li, M., Wu, L., Chen, C., & Qu, X. (2012) · Advanced Healthcare Materials · doi:10.1002/adhm.201200067 · Cited by 124

Transient receptor potential channels in Alzheimer's disease

Yamamoto, S., Wajima, T., Hara, Y., Nishida, M., & Mori, Y. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.03.006 · Cited by 127

Ionic effects of the Alzheimer's disease β-amyloid precursor protein and its metabolic fragments

Fraser, S. P., Suh, Y.-H., & Djamgoz, M. B. A. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)10079-5 · Cited by 127

Zinc and Disease of the Brain

Koh, J. (2001) · Molecular Neurobiology · doi:10.1385/mn:24:1-3:099 · Cited by 124

Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation through Src dependent PP2A (tyrosine 307) phosphorylation

Xiong, Y., Jing, X.-P., Zhou, X.-W., Wang, X.-L., Yang, Y., Sun, X.-Y., Qiu, M., Cao, F.-Y., Lu, Y.-M., Liu, R., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.07.003 · Cited by 122

Rodent Aβ Modulates the Solubility and Distribution of Amyloid Deposits in Transgenic Mice

Jankowsky, J. L., Younkin, L. H., Gonzales, V., Fadale, D. J., Slunt, H. H., Lester, H. A., Younkin, S. G., & Borchelt, D. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611050200 · Cited by 122

Metal imaging in neurodegenerative diseases

Bourassa, M. W., & Miller, L. M. (2012) · Metallomics · doi:10.1039/c2mt20052j · Cited by 125

Cu(II) Mediates Kinetically Distinct, Non-amyloidogenic Aggregation of Amyloid-β Peptides

Pedersen, J. T., Østergaard, J., Rozlosnik, N., Gammelgaard, B., & Heegaard, N. H. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220863 · Cited by 123

Metal ions influx is a double edged sword for the pathogenesis of Alzheimer’s disease

Wang, P., & Wang, Z. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.10.003 · Cited by 123

The galvanization of β-amyloid in Alzheimer's disease

Bush, A. I., & Tanzi, R. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122249699 · Cited by 122

Current therapeutic targets for the treatment of Alzheimer’s disease

Grill, J. D., & Cummings, J. L. (2010) · Expert Review of Neurotherapeutics · doi:10.1586/ern.10.29 · Cited by 123

Serum zinc, copper, insulin and lipids in Alzheimer's disease epsilon 4 apolipoprotein E allele carriers*

González, G., Martín, M., Cacho, Breñas, Arroyo, García‐Berrocal, Navajo, & González‐Buitrago (1999) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.1999.00471.x · Cited by 120

Zinc, human diseases and aging

Fabris, Ν., & Mocchegiani, E. (1995) · Aging Clinical and Experimental Research · doi:10.1007/bf03324297 · Cited by 123

Intracellular routing of human amyloid protein precursor: Axonal delivery followed by transport to the dendrites

Simons, M., Ikonen, E., Tienari, P. J., Arregui, A. C., Mönning, U., Beyreuther, K. T., & Dotti, C. G. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490410114 · Cited by 123

Colorimetric Sensor Array for Discrimination of Heavy Metal Ions in Aqueous Solution Based on Three Kinds of Thiols as Receptors

He, W., Luo, L., Liu, Q., & Chen, Z. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b00076 · Cited by 119

Nanoparticles as potential clinical therapeutic agents in Alzheimer’s disease: focus on selenium nanoparticles

Nazıroğlu, M., Muhamad, S., & Pecze, L. (2017) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2017.1324781 · Cited by 118

Copper, Zinc, and the Metallobiology of Alzheimer Disease

Bush, A. I. (2003) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-200307000-00005 · Cited by 117

Impacts of Cd(II) on the conformation and self-aggregation of Alzheimer's tau fragment corresponding to the third repeat of microtubule-binding domain

Jiang, L., Yao, T., Zhu, Z.-L., Wang, C., & Ji, L. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.08.014 · Cited by 117

Characterization of metal profiles in serum during the progression of Alzheimer's disease

González‐Domínguez, R., García‐Barrera, T., & Gómez‐Ariza, J. L. (2013) · Metallomics · doi:10.1039/c3mt00301a · Cited by 119

Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation

Hane, F. T., & Leonenko, Z. (2014) · Biomolecules · doi:10.3390/biom4010101 · Cited by 120

Amyloid-Beta (Aβ) D7H Mutation Increases Oligomeric Aβ42 and Alters Properties of Aβ-Zinc/Copper Assemblies

Chen, W.-T., Hong, C., Lin, Y.-T., Chang, W.-H., Huang, H.-T., Liao, J., Chang, Y.-J., Hsieh, Y.-F., Cheng, C.-Y., Liu, H.-C., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035807 · Cited by 119

The conformation of Alzheimer's β peptide determines the rate of amyloid formation and its resistance to proteolysis

Soto, C. A., & Castaño, E. M. (1996) · Biochemical Journal · doi:10.1042/bj3140701 · Cited by 116

The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily.

Bush, A. I., Pettingell, W. H., Paradis, M. D., Tanzi, R. E., & Wasco, W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47062-7 · Cited by 117

Interaction of Amyloid Beta-Protein with Anionic Phospholipids: Possible Involvement of Lys28 and C-Terminus Aliphatic Amino Acids

Chauhan, A., Ray, I., & Chauhan, V. P. S. (2000) · Neurochemical Research · doi:10.1023/a:1007509608440 · Cited by 117

Structural characterization of Cu2+, Ni2+ and Zn2+ binding sites of model peptides associated with neurodegenerative diseases

Migliorini, C., Porciatti, E., Łuczkowski, M., & Valensin, D. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.004 · Cited by 117

Aggregation Pathways of the Amyloid β(1–42) Peptide Depend on Its Colloidal Stability and Ordered β-Sheet Stacking

Jiang, D., Rauda, I. E., Han, S., Chen, S., & Zhou, F. (2012) · Langmuir · doi:10.1021/la3021436 · Cited by 117

Elemental imbalances in the olfactory pathway in Alzheimer's disease

Samudralwar, D. L., Diprete, C. C., Ni, B. F., Ehmann, W. D., & Markesbery, W. R. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(95)00018-w · Cited by 116

Supramolecular Vesicles Coassembled from Disulfide‐Linked Benzimidazolium Amphiphiles and Carboxylate‐Substituted Pillar[6]arenes that Are Responsive to Five Stimuli

Jiang, L., Huang, X., Chen, D., Yan, H., Li, X., & Du, X. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201611973 · Cited by 115

Formation of Toxic Fibrils of Alzheimer’s Amyloid β-Protein-(1–40) by Monosialoganglioside GM1, a Neuronal Membrane Component

Okada, T., Wakabayashi, M., Ikeda, K., & Matsuzaki, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.069 · Cited by 116

Amyloid plaques arise from zinc-enriched cortical layers in APP/PS1 transgenic mice and are paradoxically enlarged with dietary zinc deficiency

Stoltenberg, M., Bush, A. I., Bach, G., Smidt, K., Larsen, A., Rungby, J., Lund, S. A., Doering, P., & Danscher, G. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.09.025 · Cited by 114

Nitric oxide generators produce accumulation of chelatable zinc in hippocampal neuronal perikarya

Cuajungco, M. P., & Lees, G. J. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00463-6 · Cited by 116

Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1–42, in differentiated PC12 cells

Burdick, D., Kosmoski, J., Knauer, M. F., & Glabe, C. G. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01262-0 · Cited by 102

Progress in Alzheimer’s disease

Galimberti, D., & Scarpini, E. A. (2011) · Journal of Neurology · doi:10.1007/s00415-011-6145-3 · Cited by 114

A simple Schiff base as dual-responsive fluorescent sensor for bioimaging recognition of Zn 2+ and Al 3+ in living cells

Liu, H., Liu, T., Li, J., Zhang, Y., Li, J., Song, J., Qu, J., & Wong, W. (2018) · Journal of Materials Chemistry B · doi:10.1039/c8tb01743c · Cited by 113

Examining the zinc binding site of the amyloid‐β peptide

Yang, D., McLaurin, J., Qin, K., Westaway, D. A., & Fraser, P. E. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01767.x · Cited by 113

Alzheimer's Disease, β-Amyloid Protein and Zinc

Huang, X., Cuajungco, M. P., Atwood, C., Moir, R. D., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Nutrition · doi:10.1093/jn/130.5.1488s · Cited by 114

An Artificial Tongue Fluorescent Sensor Array for Identification and Quantitation of Various Heavy Metal Ions

Xu, W., Ren, C., Teoh, C. L., Peng, J., Gadre, S. H., Rhee, H., Lee, C.-L. K., & Chang, Y. (2014) · Analytical Chemistry · doi:10.1021/ac501953z · Cited by 113

The role of coordination chemistry in the development of copper and rhenium radiopharmaceuticals

Donnelly, P. S. (2011) · Dalton Transactions · doi:10.1039/c0dt01075h · Cited by 112

Serum Iron, Zinc, and Copper Levels in Patients with Alzheimer’s Disease: A Replication Study and Meta-Analyses

Wang, Z.-X., Tan, L., Wang, H.-F., Ma, J., Liu, J., Tan, M., Sun, J., Zhu, X., Jiang, T., & Yu, J. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-143108 · Cited by 112

Selective Aggregation of Endogenous β‐Amyloid Peptide and Soluble Amyloid Precursor Protein in Cerebrospinal Fluid by Zinc

Brown, A. M., Tummolo, D. M., Rhodes, K. J., Hofmann, J. R., Jacobsen, J. S., & Sonnenberg‐Reines, J. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031204.x · Cited by 55

The role of zinc in the cerebral deposition of A beta amyloid in Alzheimer's disease

Bush, A. I., & Re, T. (1995)

Role of Interaction between Zinc and Amyloid Beta in Pathogenesis of Alzheimer’s Disease

Kozin, S. A. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923140055 · Cited by 14

Zinc‐Induced Aggregation of Human and Rat β‐Amyloid Peptides In Vitro

Esler, W. P., Stimson, E. R., Jennings, J. M., Ghilardi, J. R., Mantyh, P. W., & Maggio, J. E. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66020723.x · Cited by 135

A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease

Bush, A. I., Multhaup, G., Moir, R. D., Williamson, T. G., Small, D. H., Rumble, B. A., Pollwein, P., Beyreuther, K. T., & Masters, C. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85394-2 · Cited by 286