Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide

VMD: visual molecular dynamics

Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952 · see citing works

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works

Protein Misfolding, Functional Amyloid, and Human Disease

Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,435 · see citing works

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063 · see citing works

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 · see citing works

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · see citing works

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

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 · see citing works

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 · see citing works

Alzheimer's Disease Is a Synaptic Failure

Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420 · see citing works

Pathways towards and Away from Alzheimer’s Disease

Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052 · see citing works

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120 · see citing works

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 · see citing works

Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)

Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729 · see citing works

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 · see citing works

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447 · see citing works

Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins

Peisach, J., & Blumberg, W. E. (1974) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(74)90298-7 · Cited by 1,362 · see citing works

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 1,357 · see citing works

The metallobiology of Alzheimer's disease

Bush, A. I. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00067-5 · Cited by 1,315 · see citing works

Release of endogenous Zn2+ from brain tissue during activity

Assaf, S. Y., & Chung, S. (1984) · Nature · doi:10.1038/308734a0 · Cited by 1,113 · see citing works

The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction

Huang, X., Atwood, C., Hartshorn, M. A., Multhaup, G., Goldstein, L. E., Scarpa, R. C., Cuajungco, M. P., Gray, D. N., Lim, J. T., Moir, R. D., et al. (1999) · Biochemistry · doi:10.1021/bi990438f · Cited by 1,107 · see citing works

Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors

Finney, L. A., & O'Halloran, T. V. (2003) · Science · doi:10.1126/science.1085049 · Cited by 1,100 · see citing works

Neurobiology of Zinc and Zinc-Containing Neurons

Frederickson, C. J. (1989) · International review of neurobiology · doi:10.1016/s0074-7742(08)60279-2 · Cited by 1,070 · see citing works

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

Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009 · see citing works

Ascorbate regulation and its neuroprotective role in the brain

Rice, M. E. (2000) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01543-x · Cited by 835 · see citing works

Stimulation-induced uptake and release of zinc in hippocampal slices

Howell, G. A., Welch, M. G., & Frederickson, C. (1984) · Nature · doi:10.1038/308736a0 · Cited by 820 · see citing works

Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

Huang, X., Cuajungco, M. P., Atwood, C. S., Hartshorn, M. A., Tyndall, J. D. A., Hanson, G. R., Stokes, K. C., Leopold, M., Multhaup, G., Goldstein, L. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762 · see citing works

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 653 · see citing works

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar‐Affinity Copper Binding Site on Amyloid β1‐42

Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751219.x · Cited by 641 · see citing works

The redox chemistry of the Alzheimer's disease amyloid β peptide

Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608 · see citing works

Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer’s disease

Miller, L. M., Wang, Q., Telivala, T. P., Smith, R., Lanzirotti, A., & Judith Miklossy, A. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.09.004 · Cited by 588 · see citing works

Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid

Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 580 · see citing works

Metal Binding and Oxidation of Amyloid-β within Isolated Senile Plaque Cores: Raman Microscopic Evidence

Dong, J., Atwood, C., Anderson, V. E., Siedlak, S. L., Smith, M. A., Perry, G. L., & CAREY, P. R. (2003) · Biochemistry · doi:10.1021/bi0272151 · Cited by 560 · see citing works

Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer’s disease: possible relation to oxidative stress.

Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (1996) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(96)00203-1 · Cited by 540 · see citing works

Molecular structure of amyloid fibrils: insights from solid-state NMR

Tycko, R. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004173 · Cited by 529 · see citing works

Solution NMR Studies of the Aβ(1−40) and Aβ(1−42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation

Hou, L., Shao, H., Zhang, Y., Li, H. L., Menon, N. K., Neuhaus, E. B., Brewer, J. M., Byeon, I. L., Ray, D. G., Vitek, M. P., et al. (2004) · Journal of the American Chemical Society · doi:10.1021/ja036813f · Cited by 525 · see citing works

Small assemblies of unmodified amyloid $beta;-protein are the proximate neurotoxin in Alzheimer?s disease

Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 487 · see citing works

Aqueous Dissolution of Alzheimer's Disease Aβ Amyloid Deposits by Biometal Depletion

Cherny, R. A., Legg, J. T., McLean, C. A., Fairlie, D. P., Huang, X., Atwood, C. S., Beyreuther, K., Tanzi, R. E., Masters, C. L., & Bush, A. I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23223 · Cited by 482 · see citing works

Amyloid Precursor Protein, Presenilins, and α-Synuclein: Molecular Pathogenesis and Pharmacological Applications in Alzheimer’s Disease

Suh, Y.-H., & Checler, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.469 · Cited by 467 · see citing works

Aluminum, Iron, and Zinc Ions Promote Aggregation of Physiological Concentrations of β‐Amyloid Peptide

Mantyh, P. W., Ghilardi, J. R., Rogers, S. D., DeMaster, E., Allen, C. J., Stimson, E. R., & Maggio, J. E. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03639.x · Cited by 464 · see citing works

Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease

Syme, C. D., Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313572200 · Cited by 459 · see citing works

Trace amounts of copper in water induce β-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease

Sparks, D. L., & Schreurs, B. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1832769100 · Cited by 455 · see citing works

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 452 · see citing works

Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice

Lee, J., Cole, T. B., Palmiter, R. D., Suh, S. W., & Koh, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092034699 · Cited by 432 · see citing works

Redox‐Active Metals, Oxidative Stress, and Alzheimer's Disease Pathology

HUANG, X., MOIR, R. D., TANZI, R. E., BUSH, A. I., & ROGERS, J. T. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.012 · Cited by 425 · see citing works

Imaging of Copper, Zinc, and Other Elements in Thin Section of Human Brain Samples (Hippocampus) by Laser Ablation Inductively Coupled Plasma Mass Spectrometry

Becker, J. S., Zoriy, M. V., Pickhardt, C., Palomero‐Gallagher, N., & Zilles, K. (2005) · Analytical Chemistry · doi:10.1021/ac040184q · Cited by 359 · see citing works

Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

Brown, D. R., & Kozłowski, H. (2004) · Dalton Transactions · doi:10.1039/b401985g · Cited by 343 · see citing works

Modulation of A beta adhesiveness and secretase site cleavage by zinc.

Bush, A. I., Pettingell, W. H., Paradis, M. D., & Tanzi, R. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32694-7 · Cited by 331 · see citing works

Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Aβ production in APP23 transgenic mice

Bayer, T. A., Schäfer, S., Simons, A., Kemmling, A., Kamer, T., Tepest, R., Eckert, A., Schüssel, K., Eikenberg, O., Sturchler, C., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332818100 · Cited by 325 · see citing works

Metals and Alzheimer's disease

Adlard, P. A., & Bush, A. I. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-102-303 · Cited by 324 · see citing works

Metal complexing agents as therapies for Alzheimer’s disease

Bush, A. I. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00120-3 · Cited by 310 · see citing works

Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer’s disease 1 1Edited by P. E. Wright

Shao, H., Jao, S., Ma, K., & Zagorski, M. G. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2348 · Cited by 308 · see citing works

Structural Changes of Region 1-16 of the Alzheimer Disease Amyloid β-Peptide upon Zinc Binding and in Vitro Aging

Zirah, S., Kozin, S. A., Mazur, A. K., Blond, A., Cheminant, M., Ségalas-Milazzo, I., Debey, P., & Rebuffat, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504454200 · Cited by 304 · see citing works

Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability.

Kardos, J., Kovács, I., Hajós, F., Kálmán, M., & Simonyi, M. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90565-x · Cited by 298 · see citing works

Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Aβ42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease

House, E., Collingwood, J., Khan, A., Korchazkina, O., Berthon, G., & Exley, C. (2004) · Journal of Alzheimer's Disease · doi:10.3233/jad-2004-6310 · Cited by 294 · see citing works

NMDA Receptor Activation Mediates Copper Homeostasis in Hippocampal Neurons

Schlief, M. L., Craig, A. M., & Gitlin, J. D. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3699-04.2005 · Cited by 291 · see citing works

Dual Nanomolar and Picomolar Zn(II) Binding Properties of Metallothionein

Krężel, A., & Maret, W. (2007) · Journal of the American Chemical Society · doi:10.1021/ja071979s · Cited by 283 · see citing works

Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice

Li, F., Calingasan, N. Y., Yu, F., Mauck, W. M., Toidze, M., Almeida, C. G., Takahashi, R. H., Carlson, G. A., Beal, M. F., Lin, M. T. S., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02455.x · Cited by 276 · see citing works

Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State

Guilloreau, L., Combalbert, S., Sournia‐Saquet, A., Mazarguil, H., & Faller, P. (2007) · ChemBioChem · doi:10.1002/cbic.200700111 · Cited by 273 · see citing works

Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease β‐amyloid

Barnham, K. J., Hæffner, F., Ciccotosto, G. D., Curtain, C. C., Tew, D. J., Mavros, C., Beyreuther, K. T., Carrington, D., Masters, C. L., Cherny, R. A., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-1890fje · Cited by 262 · see citing works

C-Terminal Domain of the Membrane Copper Transporter Ctr1 from Saccharomyces cerevisiae Binds Four Cu(I) Ions as a Cuprous-Thiolate Polynuclear Cluster: Sub-femtomolar Cu(I) Affinity of Three Proteins Involved in Copper Trafficking

Xiao, Z., Loughlin, F. E., George, G. N., Howlett, G. J., & Wedd, A. G. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0390350 · Cited by 255 · see citing works

Structural Analysis of Alzheimer's β(1–40) Amyloid: Protofilament Assembly of Tubular Fibrils

Malinchik, S., Inouye, H., Szumowski, K. E., & Kirschner, D. A. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77812-9 · Cited by 253 · see citing works

High‐resolution NMR studies of the zinc‐binding site of the Alzheimer's amyloid β‐peptide

Danielsson, J., Pierattelli, R., Banci, L., & Gräslund, A. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05563.x · Cited by 253 · see citing works

New Insights on How Metals Disrupt Amyloid β-Aggregation and Their Effects on Amyloid-β Cytotoxicity

Yoshiike, Y., Tanemura, K., Murayama, O., Akagi, T., Murayama, M., Sato, S., Sun, X., Tanaka, N., & Takashima, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010706200 · Cited by 244 · see citing works

Zinc takes the center stage: its paradoxical role in Alzheimer’s disease

Cuajungco, M. P., & Faget, K. Y. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(02)00219-9 · Cited by 242 · see citing works

Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer?s A? peptides

Huang, X., Atwood, C., Moir, R. D., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0602-8 · Cited by 241 · see citing works

Concentrations of extracellular free zinc (pZn)e in the central nervous system during simple anesthetization, ischemia and reperfusion

Frederickson, C. J., Giblin, L. J., Krężel, A., McAdoo, D. J., Muelle, R. N., Zeng, Y., Balaji, R. V., Masalha, R., Thompson, R. B., Fierke, C. A., et al. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2005.08.030 · Cited by 230 · see citing works

Coordination abilities of the 1–16 and 1–28 fragments of β-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study

Kowalik‐Jankowska, T., Ruta, M., Wiśniewska, K., & Łankiewicz, L. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(03)00128-4 · Cited by 222 · see citing works

NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque‐competence, Aβ(1–40)ox and Aβ(1–42)ox

Riek, R., Güntert, P., Döbeli, H., Wipf, B., & Wüthrich, K. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02537.x · Cited by 220 · see citing works

In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopy

Choo, L.-P., Wetzel, D. L., HALLIDAY, W. C., Jackson, M., LeVine, S. M., & Mantsch, H. H. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79411-0 · Cited by 220 · see citing works

Redox metals and neu rodegenerative disease

Sayre, L. M., Perry, G. L., & Smith, M. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80035-0 · Cited by 217 · see citing works

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 216 · see citing works

Zinc-Amyloid β Interactions on a Millisecond Time-Scale Stabilize Non-fibrillar Alzheimer-Related Species

Noy, D., Solomonov, I., Sinkevich, O., Arad, T., Kjær, K., & Sagi, I. (2008) · Journal of the American Chemical Society · doi:10.1021/ja076282l · Cited by 215 · see citing works

Insights into the Amyloid Folding Problem from Solid-State NMR

Tycko, R. (2003) · Biochemistry · doi:10.1021/bi027378p · Cited by 214 · see citing works

Identifying the Minimal Copper- and Zinc-binding Site Sequence in Amyloid-β Peptides

Minicozzi, V., Stellato, F., Comai, M., Serra, M. D., Potrich, C., Meyer‐Klaucke, W., & Morante, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707109200 · Cited by 209 · see citing works

Redox Reactions of Copper Complexes Formed with Different β-Amyloid Peptides and Their Neuropathalogical Relevance

Jiang, D., Men, L., Wang, J., Zhang, Y., Chickenyen, S., Wang, Y., & Zhou, F. (2007) · Biochemistry · doi:10.1021/bi700508n · Cited by 202 · see citing works

In vivo reduction of amyloid-β by a mutant copper transporter

Phinney, A. L., Drisaldi, B., Schmidt, S. D., Lugowski, S. J., Coronado, V. A., Liang, Y., Horne, P., Yang, J., Sekoulidis, J., Coomaraswamy, J., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332851100 · Cited by 201 · see citing works

Metal Ions, pH, and Cholesterol Regulate the Interactions of Alzheimer's Disease Amyloid-β Peptide with Membrane Lipid

Curtain, C. C., Ali, F. E. A., Smith, D. G., Bush, A. I., Masters, C. L., & Barnham, K. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205455200 · Cited by 200 · see citing works

Histidine-13 Is a Crucial Residue in the Zinc Ion-Induced Aggregation of the Aβ Peptide of Alzheimer's Disease

Liu, S.-T., Howlett, G. J., & Barrow, C. J. (1999) · Biochemistry · doi:10.1021/bi990205o · Cited by 199 · see citing works

Metal swap between Zn7-metallothionein-3 and amyloid-β–Cu protects against amyloid-β toxicity

Meloni, G., Sonois, V., Delaine, T., Guilloreau, L., Gillet, A., Teissié, J., Faller, P., & Vašák, M. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.89 · Cited by 190 · see citing works

Copper-mediated Amyloid-β Toxicity Is Associated with an Intermolecular Histidine Bridge

Smith, D. P., Smith, D. G., Curtain, C. C., Boas, J. F., Pilbrow, J. R., Ciccotosto, G. D., Lau, T., Tew, D. J., Perez, K. A., Wade, J. D., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600417200 · Cited by 186 · see citing works

Copper and Alzheimer's disease

Donnelly, P. S., Xiao, Z., & Wedd, A. G. (2007) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2007.01.678 · Cited by 185 · see citing works

Evidence for release of copper in the brain: Depolarization‐induced release of newly taken‐up 67copper

Hartter, D. E., & Barnea, A. (1988) · Synapse · doi:10.1002/syn.890020408 · Cited by 185 · see citing works

N-Terminal Deletions Modify the Cu2+Binding Site in Amyloid-β

Karr, J. W., Akintoye, H., Kaupp, L. J., & Szalai, V. A. (2005) · Biochemistry · doi:10.1021/bi047611e · Cited by 178 · see citing works

Changes in apparent pH on freezing aqueous buffer solutions and their relevance to biochemical electron-paramagnetic-resonance spectroscopy

Williams-Smith, D. L., Bray, R. C., Barber, M. J., Tsopanakis, A. D., & Vincent, S. P. (1977) · Biochemical Journal · doi:10.1042/bj1670593 · Cited by 175 · see citing works

NMR Reveals Anomalous Copper(II) Binding to the Amyloid Aβ Peptide of Alzheimer's Disease

Hou, L., & Zagorski, M. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja046032u · Cited by 169 · see citing works

Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease

Syme, C. D., & Viles, J. H. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.09.012 · Cited by 167 · see citing works

The Amyloid β Peptide (Aβ 1 - 40 ) Is Thermodynamically Soluble at Physiological Concentrations

Sengupta, P., Garai, K., Sahoo, B., Shi, Y., Callaway, D. J. E., & Maiti, S. (2003) · Biochemistry · doi:10.1021/bi0341410 · Cited by 166 · see citing works

Amyloid-β Binds Cu ²⁺ in a Mononuclear Metal Ion Binding Site

Karr, J. W., Kaupp, L. J., & Szalai, V. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0488028 · Cited by 160 · see citing works

Metal Ion-dependent Effects of Clioquinol on the Fibril Growth of an Amyloid β Peptide

Raman, B., Ban, T., Yamaguchi, K., Sakai, M., Kawai, T., Naiki, H., & Goto, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500309200 · Cited by 158 · see citing works

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 · see citing works

Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity

Rózga, M., Sokołowska, M., Protas, A. M., & Bal, W. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0244-8 · Cited by 142 · see citing works

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 136 · see citing works

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 · see citing works

Metal ions and oxidative protein modification in neurological disease.

Sayre, L. M., Moreira, P. I., Smith, M. A., & Perry, G. L. (2005) · PubMed · Cited by 135 · see citing works

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 · see citing works

Cu(II) complexation by “non-coordinating” N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid (HEPES buffer)☆

Sokołowska, M., & Bal, W. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.05.007 · Cited by 133 · see citing works

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 · see citing works

Aluminum-triggered structural modifications and aggregation of β-amyloids

Ricchelli, F., Drago, D., Filippi, B., Tognon, G., & Zatta, P. F. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5141-0 · Cited by 128 · see citing works

Metal binding in amyloid β-peptides shows intra- and inter-peptide coordination modes

Stellato, F., Menestrina, G., Serra, M. D., Potrich, C., Tomazzolli, R., Meyer‐Klaucke, W., & Morante, S. (2006) · European Biophysics Journal · doi:10.1007/s00249-005-0041-7 · Cited by 120 · see citing works

Cu(II) Binding to Monomeric, Oligomeric, and Fibrillar Forms of the Alzheimer’s Disease Amyloid-β Peptide

Karr, J. W., & Szalai, V. A. (2008) · Biochemistry · doi:10.1021/bi702423h · Cited by 119 · see citing works

Effect of the Two Conserved Prolines of Human Growth Inhibitory Factor (Metallothionein-3) on Its Biological Activity and Structure Fluctuation: Comparison with a Mutant Protein

Hasler, D. W., Jensen, L. T., Zerbe, O., Winge, D. R., & Vašák, M. (2000) · Biochemistry · doi:10.1021/bi001569f · Cited by 118 · see citing works

Aggregation and Metal‐Binding Properties of Mutant Forms of the Amyloid Aβ Peptide of Alzheimer's Disease

Clements, A., Allsop, D., Walsh, D. M., & Williams, C. H. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66020740.x · Cited by 116 · see citing works

Quantification of the Binding Constant of Copper(II) to the Amyloid-Beta Peptide

Hatcher, L. Q., Hong, L., Bush, W. D., Carducci, T. M., & Simon, J. D. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp710806s · Cited by 114 · see citing works

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 · see citing works

Methylation of the Imidazole Side Chains of the Alzheimer Disease Amyloid-β Peptide Results in Abolition of Superoxide Dismutase-like Structures and Inhibition of Neurotoxicity

Tickler, A. K., Smith, D. G., Ciccotosto, G. D., Tew, D. J., Curtain, C. C., Carrington, D., Masters, C. L., Bush, A. I., Cherny, R. A., Cappai, R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414178200 · Cited by 113 · see citing works

Zinc Binding to Amyloid-β: Isothermal Titration Calorimetry and Zn Competition Experiments with Zn Sensors

Talmard, C., Bouzan, A., & Faller, P. (2007) · Biochemistry · doi:10.1021/bi701355j · Cited by 111 · see citing works

Zinc Lowers Amyloid-β Toxicity by Selectively Precipitating Aggregation Intermediates

Garai, K., Sahoo, B., Kaushalya, S. K., Desai, R., & Maiti, S. (2007) · Biochemistry · doi:10.1021/bi700798b · Cited by 110 · see citing works

Cupric–amyloid β peptide complex stimulates oxidation of ascorbate and generation of hydroxyl radical

Dikalov, S., Vitek, M. P., & Mason, R. P. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.11.004 · Cited by 109 · see citing works

Role of Aspartate-1 in Cu(II) Binding to the Amyloid-β Peptide of Alzheimer's Disease

Karr, J. W., & Szalai, V. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068952d · Cited by 105 · see citing works

Synthesis and X-ray Absorption Spectroscopy Structural Studies of Cu(I) Complexes of HistidylHistidine Peptides: The Predominance of Linear 2-Coordinate Geometry

Himes, R. A., Park, G. Y., Barry, A. N., Blackburn, N. J., & Karlin, K. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0708013 · Cited by 104 · see citing works

NMR Studies of the Zn 2+ Interactions with Rat and Human β-Amyloid (1−28) Peptides in Water-Micelle Environment

Gaggelli, E., Janicka-Kłos, A., Jankowska, E., Kozłowski, H., Migliorini, C., Molteni, E., Valensin, D., Valensin, G., & Wieczerzak, E. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp075168m · Cited by 102 · see citing works

Amyloid‐Beta Peptide Forms Monomeric Complexes With CuII and ZnII Prior to Aggregation

Talmard, C., Guilloreau, L., Coppel, Y., Mazarguil, H., & Faller, P. (2006) · ChemBioChem · doi:10.1002/cbic.200600319 · Cited by 96 · see citing works

Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1–10, 1–16 fragments of human and mouse β-amyloid peptide

Kowalik-Jankowska, T., Ruta, M., Wiśniewska, K., Łankiewicz, L., & Dyba, M. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.03.001 · Cited by 92 · see citing works

Studies on human lactoferrin by electron paramagnetic resonance, fluorescence, and resonance Raman spectroscopy

Ainscough, E. W., Brodie, A. M., Plowman, J. E., Bloor, S. J., Loehr, J. S., & Loehr, T. M. (1980) · Biochemistry · doi:10.1021/bi00558a026 · Cited by 91 · see citing works

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 89 · see citing works

Characterization of the ZnII Binding to the Peptide Amyloid‐β1–16 linked to Alzheimer's Disease

Mekmouche, Y., Coppel, Y., Hochgräfe, K., Guilloreau, L., Talmard, C., Mazarguil, H., & Faller, P. (2005) · ChemBioChem · doi:10.1002/cbic.200500057 · Cited by 85 · see citing works

Direct Evidence That All Three Histidine Residues Coordinate to Cu(II) in Amyloid-β1−16

Shin, B., & Saxena, S. (2008) · Biochemistry · doi:10.1021/bi801014x · Cited by 83 · see citing works

A method based on ICP-MS for the analysis of Alzheimer's amyloid plaques.

Beauchemin, D., & Kisilevsky, R. (1998) · Analytical Chemistry · doi:10.1021/ac970783f · Cited by 79 · see citing works

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 · see citing works

Investigations of the Molecular Mechanism of Metal-Induced Aβ (1−40) Amyloidogenesis

Lim, K. H., Kim, Y. K., & Chang, Y. (2007) · Biochemistry · doi:10.1021/bi701112z · Cited by 71 · see citing works

Zinc binding properties of the amyloid fragment Aβ(1–16) studied by electrospray-ionization mass spectrometry

Zirah, S., Rebuffat, S., Kozin, S. A., Debey, P., Fournier, F., Lesage, D., & Tabet, J. (2003) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(03)00221-5 · Cited by 70 · see citing works

The Aggregated State of Amyloid‐β Peptide In Vitro Depends on Cu2+ Ion Concentration

Jun, S., & Saxena, S. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200700318 · Cited by 61 · see citing works

Oxidative switches in functioning of mammalian copper chaperone Cox17

Voronova, A., Meyer‐Klaucke, W., Meyer, T. F., Rompel, A., Krebs, B., Kazantseva, J., Sillard, R., & Palumaa, P. (2007) · Biochemical Journal · doi:10.1042/bj20070804 · Cited by 60 · see citing works

A spectroscopic and voltammetric study of the pH-dependent Cu(II) coordination to the peptide GGGTH: relevance to the fifth Cu(II) site in the prion protein

Hureau, C., Charlet, L., Dorlet, P., Gonnet, F., Spadini, L., Anxolabéhère‐Mallart, E., & Girerd, J. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0118-5 · Cited by 58 · see citing works

Determining Thermodynamic Parameters from Isothermal Calorimetric Isotherms of the Binding of Macromolecules to Metal Cations Originally Chelated by a Weak Ligand

Hong, L., Bush, W. D., Hatcher, L. Q., & Simon, J. D. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp075747r · Cited by 55 · see citing works

Structural features of the Cu( ii ) complex with the rat Aβ(1–28) fragment

Gaggelli, E., Grzonka, Z., Kozłowski, H., Migliorini, C., Molteni, E., Valensin, D., & Valensin, G. (2008) · Chemical Communications · doi:10.1039/b713453c · Cited by 52 · see citing works

Ab initio modelling of the structure and redox behaviour of copper(I) bound to a His–His model peptide: relevance to the β-amyloid peptide of Alzheimer’s disease

Raffa, D. F., Rickard, G. A., & Rauk, A. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0175-9 · Cited by 50 · see citing works

Metal Binding and Radical Generation of Proteins in Human Neurological Diseases and Aging

Multhaup, G., & Masters, C. L. (2018) · Routledge eBooks · doi:10.1201/9780203747605-11 · Cited by 29 · see citing works

Complex formation between copper(II) and several β-amino alcohols in aqueous solution: a potentiometric and spectrophotometric study

Canepari, S., Carunchio, V., & Schina, R. (1999) · Polyhedron · doi:10.1016/s0277-5387(99)00262-4 · Cited by 9 · see citing works

Ring Expansion of a 4,4′‐Bipyridyl Derivative into π‐Conjugated Azepinoazepines

Yamaguchi, I., Tsutsui, S., & Sato, M. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200790137 · Cited by 7 · see citing works

The Aggregated State of Amyloid‐β Peptide In Vitro Depends on Cu2+ Ion Concentration

Jun, S., & Saxena, S. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200790133 · Cited by 4 · see citing works

Untitled work

(2001) · doi:10.1002/1521-3773(20010618)40:12

Bioinorganic Chemistry of Alzheimer’s Disease

Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 672 · see citing works

Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer’s Disease, Parkinson’s Disease, and Amyotrophic Lateral Sclerosis in the Last Decade

Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M. H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 603 · see citing works

Copper, zinc and iron in neurodegenerative diseases (Alzheimer's, Parkinson's and prion diseases)

Kozłowski, H., Łuczkowski, M., Remelli, M., & Valensin, D. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.013 · Cited by 438 · see citing works

Cellular zinc metabolism and zinc signaling: From biological functions to diseases and therapeutic targets

Chen, B., Yu, P., Chan, W. N., Xie, F., Zhang, Y., Liang, L., Leung, K. T., Lo, K. W., Yu, J., Tse, G. M. K., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01679-y · Cited by 420 · see citing works

Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases

Viles, J. H. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.003 · Cited by 403 · see citing works

Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease

Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H. (2013) · ACS Chemical Biology · doi:10.1021/cb400080f · Cited by 398 · see citing works

Misfolded proteins in Alzheimer's disease and type II diabetes

DeToma, A. S., Salamekh, S., Ramamoorthy, A., & Lim, M. H. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15112f · Cited by 359 · see citing works

Role of Metal Ions in the Self-assembly of the Alzheimer’s Amyloid-β Peptide

Faller, P., Hureau, C., & Berthoumieu, O. (2013) · Inorganic Chemistry · doi:10.1021/ic4003059 · Cited by 355 · see citing works

Medicinal Inorganic Chemistry Approaches to Passivation and Removal of Aberrant Metal Ions in Disease

Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332 · see citing works

Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states

Miller, Y., Ma, B., & Nussinov, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913114107 · Cited by 303 · see citing works

Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease

Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 288 · see citing works

Copper and Zinc Binding to Amyloid‐β: Coordination, Dynamics, Aggregation, Reactivity and Metal‐Ion Transfer

Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900321 · Cited by 285 · see citing works

Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape

Miller, Y., Ma, B., & Nussinov, R. (2010) · Chemical Reviews · doi:10.1021/cr900377t · Cited by 284 · see citing works

Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics

Duce, J. A., & Bush, A. I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.003 · Cited by 281 · see citing works

The role of metallobiology and amyloid-β peptides in Alzheimer's disease

Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07500.x · Cited by 266 · see citing works

Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity

Choi, J.-S., Braymer, J. J., Nanga, R. P. R., Ramamoorthy, A., & Lim, M. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006091107 · Cited by 264 · see citing works

Metal-associated amyloid-β species in Alzheimer's disease

Pithadia, A. S., & Lim, M. H. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.01.016 · Cited by 259 · see citing works

Interactions of Zn(ii) and Cu(ii) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity

Tõugu, V., Tiiman, A., & Palumaa, P. (2011) · Metallomics · doi:10.1039/c0mt00073f · Cited by 222 · see citing works

Copper(II) Binding to Amyloid-β Fibrils of Alzheimer’s Disease Reveals a Picomolar Affinity: Stoichiometry and Coordination Geometry Are Independent of Aβ Oligomeric Form

Sarell, C. J., Syme, C. D., Rigby, S. E. J., & Viles, J. H. (2009) · Biochemistry · doi:10.1021/bi900254n · Cited by 209 · see citing works

Fluorescent Diagnostic Probes in Neurodegenerative Diseases

Zhou, J., Jangili, P., Son, S., Ji, M. S., Won, M., & Kim, J. S. (2020) · Advanced Materials · doi:10.1002/adma.202001945 · Cited by 203 · see citing works

Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ₄₂Peptide

Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202 · see citing works

Substoichiometric Levels of Cu2+ Ions Accelerate the Kinetics of Fiber Formation and Promote Cell Toxicity of Amyloid-β from Alzheimer Disease

Sarell, C. J., Wilkinson, S. R., & Viles, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.171355 · Cited by 199 · see citing works

Iron(II) Binding to Amyloid-β, the Alzheimer’s Peptide

Garah, F. E., Bijani, C., Coppel, Y., Faller, P., & Hureau, C. (2011) · Inorganic Chemistry · doi:10.1021/ic201233b · Cited by 199 · see citing works

Alzheimer's disease and metabolic syndrome: A link from oxidative stress and inflammation to neurodegeneration

Rojas-Gutierrez, E., Muñoz‐Arenas, G., Treviño, S., Espinosa, B., Chávez, R., Rojas, K., Flores, G., Díaz, A., & Guevara, J. (2017) · Synapse · doi:10.1002/syn.21990 · Cited by 198 · see citing works

Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1–16 Amyloid‐β Peptide: A Key Role of the First Two N‐Terminus Residues

Dorlet, P., Gambarelli, S., Faller, P., & Hureau, C. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904567 · Cited by 196 · see citing works

Overview of Alzheimer’s Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds

Singh, S. K., Srivastav, S., Yadav, A. K., Srikrishna, S., & Perry, G. L. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7361613 · Cited by 188 · see citing works

Rational Design of a Structural Framework with Potential Use to Develop Chemical Reagents That Target and Modulate Multiple Facets of Alzheimer’s Disease

Lee, S., Zheng, X., Krishnamoorthy, J., Savelieff, M. G., Park, H. M., Brender, J., Kim, J. H., Derrick, J. S., Kochi, A., Lee, H. J., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja409801p · Cited by 185 · see citing works

Metal ions as modulators of protein conformation and misfolding in neurodegeneration

Leal, S. S., Botelho, H. M., & Gomes, C. M. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.04.004 · Cited by 183 · see citing works

Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 1: An overview

Hureau, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.037 · Cited by 178 · see citing works

The Heterogeneous Nature of Cu 2+ Interactions with Alzheimer’s Amyloid-β Peptide

Drew, S. C., & Barnham, K. J. (2011) · Accounts of Chemical Research · doi:10.1021/ar200014u · Cited by 174 · see citing works

The Ongoing Search for Small Molecules to Study Metal-Associated Amyloid-β Species in Alzheimer’s Disease

Savelieff, M. G., DeToma, A. S., Derrick, J. S., & Lim, M. H. (2014) · Accounts of Chemical Research · doi:10.1021/ar500152x · Cited by 174 · see citing works

Cu(II) Affinity for the Alzheimer’s Peptide: Tyrosine Fluorescence Studies Revisited

Aliès, B., Renaglia, E., Rózga, M., Bal, W., Faller, P., & Hureau, C. (2012) · Analytical Chemistry · doi:10.1021/ac302629u · Cited by 172 · see citing works

Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance

Atrián‐Blasco, E., Gonzalez, P., Santoro, A., Aliès, B., Faller, P., & Hureau, C. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.007 · Cited by 168 · see citing works

Insights of 8-hydroxyquinolines: A novel target in medicinal chemistry

Gupta, R., Luxami, V., & Paul, K. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104633 · Cited by 159 · see citing works

Oxidative Stress and Cell Membranes in the Pathogenesis of Alzheimer's Disease

Axelsen, P. H., Komatsu, H., & Murray, I. V. J. (2011) · Physiology · doi:10.1152/physiol.00024.2010 · Cited by 158 · see citing works

Minding metals: Tailoring multifunctional chelating agents for neurodegenerative disease

Perez, L. R., & Franz, K. J. (2010) · Dalton Trans. · doi:10.1039/b919237a · Cited by 156 · see citing works

Towards the functional high-resolution coordination chemistry of blood plasma human serum albumin

Al-Harthi, S., Lachowicz, J. I., Nowakowski, M. E., Jaremko, M., & Jaremko, Ł. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.110716 · Cited by 154 · see citing works

High-resolution analytical imaging and electron holography of magnetite particles in amyloid cores of Alzheimer’s disease

Plascencia‐Villa, G., Ponce, A., Collingwood, J. F., Arellano-Jiménez, M. J., Zhu, X., Rogers, J. T., Betancourt, I., José–Yacamán, M., & Perry, G. L. (2016) · Scientific Reports · doi:10.1038/srep24873 · Cited by 152 · see citing works

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 · see citing works

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 151 · see citing works

Recent progress in multifunctional metal chelators as potential drugs for Alzheimer's disease

Santos, M. A., Chand, K., & Chaves, S. (2016) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2016.04.013 · Cited by 149 · see citing works

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 · see citing works

Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 2: Dependence of Cu(II) binding sites with Aβ sequences

Hureau, C., & Dorlet, P. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.034 · Cited by 148 · see citing works

Chelation therapy in Wilson's disease: from d-penicillamine to the design of selective bioinspired intracellular Cu(i) chelators

Delangle, P., & Mintz, E. (2012) · Dalton Transactions · doi:10.1039/c2dt12188c · Cited by 139 · see citing works

Affinity of copper and zinc ions to proteins and peptides related to neurodegenerative conditions (Aβ, APP, α-synuclein, PrP)

Zawisza, I. A., Rózga, M., & Bal, W. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.012 · Cited by 138 · see citing works

Deprotonation of the Asp1Ala2 Peptide Bond Induces Modification of the Dynamic Copper(II) Environment in the Amyloid‐β Peptide near Physiological pH

Hureau, C., Coppel, Y., Dorlet, P., Solari, P. L., Sayen, S., Guillon, E., Sabater, L., & Faller, P. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904512 · Cited by 137 · see citing works

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 · see citing works

Importance of dynamical processes in the coordination chemistry and redox conversion of copper amyloid-β complexes

Hureau, C., Balland, V., Coppel, Y., Solari, P. L., Fonda, E., & Faller, P. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0570-0 · Cited by 134 · see citing works

Heme–Cu Bound Aβ Peptides: Spectroscopic Characterization, Reactivity, and Relevance to Alzheimer’s Disease

Pramanik, D., Ghosh, C., & Dey, S. G. (2011) · Journal of the American Chemical Society · doi:10.1021/ja204628b · Cited by 133 · see citing works

Bioinorganic chemistry of copper coordination to alpha-synuclein: Relevance to Parkinson's disease

Binolfi, A., Quintanar, L., Bertoncini, C. W., Griesinger, C., & Fernández, C. O. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.004 · Cited by 132 · see citing works

Metal complexes of amino acids and amino acid side chain groups. Structures and properties

Shimazaki, Y., Takani, M., & Yamauchi, O. (2009) · Dalton Transactions · doi:10.1039/b905871k · Cited by 132 · see citing works

Bioinorganic Chemistry of Parkinson’s Disease: Structural Determinants for the Copper-Mediated Amyloid Formation of Alpha-Synuclein

Binolfi, A., Rodríguez, E. E., Valensin, D., D’Amelio, N., Ippoliti, E., Obal, G., Durán, R., Magistrato, A., Pritsch, O., Zweckstetter, M., et al. (2010) · Inorganic Chemistry · doi:10.1021/ic1016752 · Cited by 128 · see citing works

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 126 · see citing works

Minimal Zn2+ Binding Site of Amyloid-β

Tsvetkov, P. O., Kulikova, A. A., Golovin, A. V., Tkachev, Y. V., Archakov, A. I., Kozin, S. A., & Makarov, A. А. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.09.015 · Cited by 126 · see citing works

Electrochemical and homogeneous electron transfers to the Alzheimer amyloid-β copper complex follow a preorganization mechanism

Balland, V., Hureau, C., & Savéant, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011315107 · Cited by 124 · see citing works

Hepatocyte Targeting and Intracellular Copper Chelation by a Thiol-Containing Glycocyclopeptide

Pujol, A. M., Cuillel, M., Renaudet, O., Lebrun, C., Charbonnier, P., Cassio, D., Gateau, C., Dumy, P., Mintz, E., & Delangle, P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja106206z · Cited by 123 · see citing works

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 · see citing works

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 121 · see citing works

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 116 · see citing works

Effect of Metals on Kinetic Pathways of Amyloid-β Aggregation

Hane, F. T., & Leonenko, Z. (2014) · Biomolecules · doi:10.3390/biom4010101 · Cited by 116 · see citing works

Cu and Zn interactions with Aβ peptides: consequence of coordination on aggregation and formation of neurotoxic soluble Aβ oligomers

Rana, M., & Sharma, A. K. (2018) · Metallomics · doi:10.1039/c8mt00203g · Cited by 113 · see citing works

Close Correlation of Monoamine Oxidase Activity with Progress of Alzheimer’s Disease in Mice, Observed by in Vivo Two-Photon Imaging

Kim, D., Baik, S. H., Kang, S., Cho, S. W., Bae, J., Cha, M.-Y., Sailor, M. J., Mook‐Jung, I., & Ahn, K. H. (2016) · ACS Central Science · doi:10.1021/acscentsci.6b00309 · Cited by 112 · see citing works

Pivotal role of carnosine in the modulation of brain cells activity: Multimodal mechanism of action and therapeutic potential in neurodegenerative disorders

Caruso, G., Caraci, F., & Jolivet, R. B. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.004 · Cited by 110 · see citing works

β-Amyloid Fibrils in Alzheimer Disease Are Not Inert When Bound to Copper Ions but Can Degrade Hydrogen Peroxide and Generate Reactive Oxygen Species

Mayes, J., Tinker, C. L., Kolosov, O., Zhang, H., Tabner, B. J., & Allsop, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525212 · Cited by 109 · see citing works

Ternary Complexes of Iron, Amyloid-β, and Nitrilotriacetic Acid: Binding Affinities, Redox Properties, and Relevance to Iron-Induced Oxidative Stress in Alzheimer’s Disease

Jiang, D., Li, X., Williams, R. S., Patel, S., Men, L., Wang, Y., & Zhou, F. (2009) · Biochemistry · doi:10.1021/bi900907a · Cited by 109 · see citing works

Cu2+ Affects Amyloid-β (1–42) Aggregation by Increasing Peptide-Peptide Binding Forces

Hane, F. T., Tran, G., Attwood, S. J., & Leonenko, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059005 · Cited by 109 · see citing works

Effect of Zinc Binding on β-Amyloid Structure and Dynamics: Implications for Aβ Aggregation

Rezaei‐Ghaleh, N., Giller, K., Becker, S., & Zweckstetter, M. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.06.062 · Cited by 107 · see citing works

Metal binding sites in amyloid oligomers: Complexes and mechanisms

Miller, Y., Ma, B., & Nussinov, R. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.12.022 · Cited by 103 · see citing works

Cellular Polyamines Promote Amyloid-Beta (Aβ) Peptide Fibrillation and Modulate the Aggregation Pathways

Luo, J., Yu, C., Yu, H., Borštnar, R., Kamerlin, S. C. L., Gräslund, A., Abrahams, J. P., & Wärmländer, S. K. T. S. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn300170x · Cited by 103 · see citing works

Molecular Dynamics Study of Zn(Aβ) and Zn(Aβ)2

Pan, L., & Patterson, J. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070681 · Cited by 102 · see citing works

Metal Binding of Alzheimer’s Amyloid-β and Its Effect on Peptide Self-Assembly

Abelein, A. (2023) · Accounts of Chemical Research · doi:10.1021/acs.accounts.3c00370 · Cited by 102 · see citing works

Biophysical Studies of the Amyloid β‐Peptide: Interactions with Metal Ions and Small Molecules

Wärmländer, S. K. T. S., Tiiman, A., Abelein, A., Luo, J., Jarvet, J., Söderberg, K. L., Danielsson, J., & Gräslund, A. (2013) · ChemBioChem · doi:10.1002/cbic.201300262 · Cited by 101 · see citing works

Copper-Targeting Approaches in Alzheimer’s Disease: How To Improve the Fallouts Obtained from in Vitro Studies

Esmieu, C., Guettas, D., Conte‐Daban, A., Sabater, L., Faller, P., & Hureau, C. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b00995 · Cited by 100 · see citing works

Reevaluation of Copper(I) Affinity for Amyloid‐β Peptides by Competition with Ferrozine—An Unusual Copper(I) Indicator

Aliès, B., Badei, B., Faller, P., & Hureau, C. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201102746 · Cited by 99 · see citing works

Myricetin: A Naturally Occurring Regulator of Metal‐Induced Amyloid‐β Aggregation and Neurotoxicity

DeToma, A. S., Choi, J., Braymer, J. J., & Lim, M. H. (2011) · ChemBioChem · doi:10.1002/cbic.201000790 · Cited by 99 · see citing works

Interplay of histidine residues of the Alzheimer’s disease Aβ peptide governs its Zn-induced oligomerization

Istrate, A., Kozin, S. A., Zhokhov, S. S., Mantsyzov, A. B., Kechko, O. I., Pastore, A., Makarov, A. А., & Polshakov, V. I. (2016) · Scientific Reports · doi:10.1038/srep21734 · Cited by 98 · see citing works

Neurodegenerative diseases and exposure to the environmental metals Mn, Pb, and Hg

Charlet, L., Chapron, Y., Faller, P., Kirsch, R., Stone, A. T., & Baveye, P. C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.012 · Cited by 96 · see citing works

Design, synthesis, and biological evaluation of curcumin analogues as multifunctional agents for the treatment of Alzheimer’s disease

Chen, S., Chen, Y., Li, Y., Chen, S., Tan, J., Ou, T., Gu, L., & Huang, Z. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.07.033 · Cited by 95 · see citing works

Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation

Stewart, K. L., & Radford, S. E. (2017) · Biophysical Reviews · doi:10.1007/s12551-017-0271-9 · Cited by 93 · see citing works

Metal complexes that bind to the amyloid-β peptide of relevance to Alzheimer’s disease

Gomes, L. M., Bataglioli, J. C., & Storr, T. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213255 · Cited by 93 · see citing works

Copper imbalance in Alzheimer’s disease: Convergence of the chemistry and the clinic

Kepp, K. P., & Squitti, R. (2019) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2019.06.018 · Cited by 90 · see citing works

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 89 · see citing works

Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production

Gerber, H., Wu, F., Dimitrov, M. I., Osuna, G. M. G., & Fraering, P. C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.754101 · Cited by 89 · see citing works

Development of Bifunctional Stilbene Derivatives for Targeting and Modulating Metal-Amyloid-β Species

Braymer, J. J., Choi, J.-S., DeToma, A. S., Wang, C., Nam, K., Kampf, J. W., Ramamoorthy, A., & Lim, M. H. (2011) · Inorganic Chemistry · doi:10.1021/ic2012205 · Cited by 88 · see citing works

The missing link in the amyloid cascade of Alzheimer’s disease – Metal ions

Tiiman, A., Palumaa, P., & Tõugu, V. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.023 · Cited by 88 · see citing works

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 · see citing works

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 · see citing works

fac -{Ru(CO) 3 } 2+ Selectively Targets the Histidine Residues of the β-Amyloid Peptide 1-28. Implications for New Alzheimer's Disease Treatments Based on Ruthenium Complexes

Valensin, D., Anzini, P., Gaggelli, E., Gaggelli, N., Tamasi, G., Cini, R., Gabbiani, C., Michelucci, E., Luigi Messori, A., Kozłowski, H., et al. (2010) · Inorganic Chemistry · doi:10.1021/ic902593e · Cited by 85 · see citing works

Reaction Rates and Mechanism of the Ascorbic Acid Oxidation by Molecular Oxygen Facilitated by Cu(II)-Containing Amyloid-β Complexes and Aggregates

Jiang, D., Li, X., Liu, L., Yagnik, G. B., & Zhou, F. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp9095375 · Cited by 83 · see citing works

Novel Tacrine-Hydroxyphenylbenzimidazole hybrids as potential multitarget drug candidates for Alzheimer's disease

Hiremathad, A., Keri, R. S., Esteves, A. R., Cardoso, S. M., Chaves, S., & Santos, M. A. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.023 · Cited by 82 · see citing works

Development and Application of a Nonbonded Cu2+ Model That Includes the Jahn–Teller Effect

Liao, Q., Kamerlin, S. C. L., & Strodel, B. (2015) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.5b01122 · Cited by 81 · see citing works

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 · see citing works

Specific metal ion binding sites in unstructured regions of proteins

Kozłowski, H., Potocki, S., Remelli, M., Rowińska‐Żyrek, M., & Valensin, D. (2013) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2013.01.024 · Cited by 80 · see citing works

pH-Dependent Cu(II) Coordination to Amyloid-β Peptide: Impact of Sequence Alterations, Including the H6R and D7N Familial Mutations.

Aliès, B., Eury, H., Bijani, C., Rechignat, L., Faller, P., & Hureau, C. (2011) · Inorganic Chemistry · doi:10.1021/ic201739n · Cited by 80 · see citing works

Copper(II) Coordination to Amyloid β: Murine versus Human Peptide

Eury, H., Bijani, C., Faller, P., & Hureau, C. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201005838 · Cited by 79 · see citing works

Identification of [PtCl2(phen)] Binding Modes in Amyloid‐β Peptide and the Mechanism of Aggregation Inhibition

Ma, G., Huang, F., Pu, X., Jia, L., Jiang, T., Li, L., & Liu, Y. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201101859 · Cited by 79 · see citing works

Zinc-induced dimerization of the amyloid-β metal-binding domain 1–16 is mediated by residues 11–14

Kozin, S. A., Mezentsev, Y. V., Kulikova, A. A., Indeykina, M. I., Golovin, A. V., Ivanov, A. S., Tsvetkov, P. O., & Makarov, A. А. (2011) · Molecular BioSystems · doi:10.1039/c0mb00334d · Cited by 78 · see citing works

Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar

Xiao, Z., Gottschlich, L., van der Meulen, R., Udagedara, S. R., & Wedd, A. G. (2013) · Metallomics · doi:10.1039/c3mt00032j · Cited by 77 · see citing works

Affinity of Cu+ for the Copper-Binding Domain of the Amyloid-β Peptide of Alzheimer’s Disease

Feaga, H. A., Maduka, R. C., Foster, M. N., & Szalai, V. A. (2011) · Inorganic Chemistry · doi:10.1021/ic100967s · Cited by 77 · see citing works

Toward a Rational Design to Regulate β-Amyloid Fibrillation for Alzheimer’s Disease Treatment

Han, X., & He, G. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00477 · Cited by 77 · see citing works

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 216 · see citing works

ChemInform Abstract: Bioinorganic Chemistry of Copper and Zinc Ions Coordinated to Amyloid‐β Peptide

Faller, P., & Hureau, C. (2009) · ChemInform · doi:10.1002/chin.200922264

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 · see citing works

Isothermal Titration Calorimetric Study of Amyloid b (Ab) Peptide Interaction with Cu2+ and Zn2+

Jin, L., Kaatz, L., Zbyszynski, P., & Behbahani, S. (2008) · The FASEB Journal · doi:10.1096/fasebj.22.1_supplement.1055.2

Cu(II)–Zn(II) Cross-Modulation in Amyloid–Beta Peptide Binding: An X-ray Absorption Spectroscopy Study

Santis, E. D., Minicozzi, V., Proux, O., Rossi, G. C., Silva, K. I., Lawless, M. J., Stellato, F., Saxena, S., & Morante, S. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b10264 · Cited by 21 · see citing works