Cited by 537Alzheimer's disease research and treatmentsMetal complexes synthesis and propertiesTrace Elements in Health

The DOI matches its Crossref record; 133 of the 134 references it cites were found in a registry or an index.

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

Faller, Peter, Hureau, Christelle·2009·Dalton Trans.

Open this paper in CoChat — free account

Abstract

In the present perspective, we give a critical review on the coordination chemistry of the metal ions copper and zinc to the amyloid-beta (Abeta) peptide; such complexes have been linked to Alzheimer's disease. We focus on two main issues: the identification of the coordination sphere of the Cu(ii) and Zn(ii) ions and the affinity of these metal ions towards the peptide. With the aim to come up with as few as possible valuable structural models and binding affinity values, we critically review the divergent propositions reported in the literature and take into account the experimental differences and the limits of the methods used in the published studies. We propose that: (i) the conditional dissociation constant of the Cu(Abeta) complexes lies in the range of 10 pM to 100 nM, with a preference for the region between 100 pM to 1 nM. (ii) Two most likely coordination modes for the predominant form of the Cu(Abeta) complexes at physiological pH can be retained, both being 3N1O distorted square planar. In the first model, the Cu(ii) ion is coordinated by the Ntau atoms of the three His residues and the carboxylate of the Asp1. In the second model, both the N-terminus and the carboxylate functions of Asp1 are ligated together with the Ntau of His6 and of His13 (or His14). An equilibrium between these two forms at room temperature, and a preferentially freezing out of the second one would explain most of the divergences in the published results (in particular, between those obtai…

Integrity signals

Registry

Crossref · 10.1039/b813398k

Cites

133 of 133 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
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
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 6,497
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
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
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
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
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
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
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
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
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
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
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
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
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
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
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 1,117
Release of endogenous Zn2+ from brain tissue during activity
Assaf, S. Y., & Chung, S. (1984) · Nature · doi:10.1038/308734a0 · Cited by 1,113
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
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
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
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
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
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
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 658
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
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
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
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 587
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
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
Molecular structure of amyloid fibrils: insights from solid-state NMR
Tycko, R. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004173 · Cited by 529
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
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 494
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
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 476
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 466
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
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
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
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
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
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
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
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
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 329
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
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
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
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 306
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
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
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
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
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 277
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
Self-citation
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
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
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
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
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 245
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
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
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
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
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
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
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
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
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 216
Insights into the Amyloid Folding Problem from Solid-State NMR
Tycko, R. (2003) · Biochemistry · doi:10.1021/bi027378p · Cited by 214
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
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 204
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 204
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
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
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
Self-citation
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 188
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 188
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
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
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 176
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
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
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
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
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
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
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
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
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
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
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
Self-citation
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
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
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
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
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
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
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 116
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
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 115
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
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
Self-citation
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 110
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
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
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
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
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
Self-citation
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
Characterization of copper binding to the peptide amyloid‐β(1–16) associated with Alzheimer's disease
Ma, Q., Hu, J. N., Wu, W., Liu, H., Du, J., Fu, Y., Wu, Y., Lei, P., Zhao, Y., & Li, Y. (2006) · Biopolymers · doi:10.1002/bip.20523 · Cited by 91
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
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
Self-citation
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
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
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
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
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
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 63
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
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 59
Self-citation
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
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
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
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
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
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
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
Untitled work
(2001) · doi:10.1002/1521-3773(20010618)40:12

Research works printed but not linked: 3

Multhaup, 1999, Met. Ions Biol. Syst., 36, 365
Sayre, 2005, Ann Ist Super Sanita, 41, 143
Krezel, 2008, J. Biol. Chem., 13, 401

Sorted by citations

Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683
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 612
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 446
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
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 404

See all 537

Authors: Faller, P., & Hureau, C.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: Faller, Peter
ORCID: Faller, Peter
Hureau, Christelle
Venue: Dalton Trans.
Publisher: Royal Society of Chemistry (RSC)
Published: 2009
Issue: 7
Pages: 1080-1094
ISSN: 1477-9226 (ISSN-L)
1477-9234
DOI: 10.1039/b813398k
OpenAlex: W2062820102
Cited by: 530
References: 134
Citations by year: 2026: 12 · 2025: 19 · 2024: 17 · 2023: 20 · 2022: 14 · 2021: 25 · 2020: 23 · 2019: 29 · 2018: 34 · 2017: 37 · 2016: 25 · 2015: 28 · 2014: 36 · 2013: 40 · 2012: 58
FWCI: 4.03
Type: journal article
Language: en
Open access: closed
Locations: Dalton Transactions (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Oncology › Metal complexes synthesis and properties
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: amyloid-beta, copper(II) complexes, zinc(II) complexes, metal-peptide coordination, Alzheimer's disease, coordination sphere, dissociation constant, binding affinity, square-planar coordination, histidine ligands, structural model
MeSH terms: Alzheimer Disease, Copper, Humans, Peptide Fragments, Zinc, Chemistry, Bioinorganic, Amyloid beta-Peptides

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks