Cited by 244Alzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.

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

Open access

Yoshiike, Yuji, Tanemura, Kentaro, Murayama, Ohoshi, Akagi, Takumi, Murayama, Miyuki, Sato, Shinji, Sun, Xiaoyan, Tanaka, Nobuo, Takashima, Akihiko·2001·Journal of Biological Chemistry

DOI 10.1074/jbc.m010706200

Open this paper in CoChat — free account

Abstract

Amyloid-beta protein (A beta) aggregates in the brain to form senile plaques. By using thioflavin T, a dye that specifically binds to fibrillar structures, we found that metals such as Zn(II) and Cu(II) normally inhibit amyloid beta-aggregation. Another method for detecting A beta, which does not distinguish the types of aggregates, showed that these metals induce a non-beta-sheeted aggregation, as reported previously. Secondary structural analysis and microscopic studies revealed that metals induced A beta to make non-fibrillar aggregates by disrupting beta-sheet formation. These non-fibrillar A beta aggregates displayed much weaker Congo Red birefringence, and in separate cell culture experiments, were less toxic than self beta-aggregates, as demonstrated by 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide assay. The toxicity of soluble A beta was enhanced in the presence of Cu(II), which suggests the previously hypothesized role of A beta in generating oxidative stress. Finally, under an acidic condition, similar to that in the inflammation associated with senile plaques, beta-aggregation was robustly facilitated at one specific concentration of Zn(II) in the presence of heparin. However, because a higher concentration of Zn(II) virtually abolished this abnormal phenomenon, and at normal pH any concentrations strongly inhibit beta-aggregation and its associated cytotoxicity, including its anti-oxidative nature we suggest that Zn(II) has an overall protective ef…

Integrity signals

Registry

Crossref · 10.1074/jbc.m010706200

Cites

60 of 60 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

We couldn’t retrieve this paper’s full text, 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?

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
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
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
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill
Hansen, M., Nielsen, S. E., & Berg, K. (1989) · Journal of Immunological Methods · doi:10.1016/0022-1759(89)90397-9 · Cited by 3,488
Thioflavine T interaction with synthetic Alzheimer's disease β ‐amyloid peptides: Detection of amyloid aggregation in solution
LeVine, H. (1993) · Protein Science · doi:10.1002/pro.5560020312 · Cited by 2,284
Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
Circular Dichroism and the Conformational Analysis of Biomolecules
Fasman, G. D. (1996) · Springer eBooks · doi:10.1007/978-1-4757-2508-7 · Cited by 1,950
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
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417

Flagged first, then by citations

Show all 60 references

Research works printed but not linked: 2

Simmons, 1994, Mol. Pharmacol., 45, 373
Snow, 1988, Am. J. Pathol., 133, 456

Sorted by citations

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
Expression of Concern: Potent anti‐amyloidogenic and fibril‐destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease
Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., & Yamada, M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01976.x · Cited by 681
“Ten lM fAb(1–40) were incubated with 0 or 0.2% DMSO, or 10 lM Myr + 0.2% DMSO at pH 7.5 at 37 C. ThT fluorescence was regularly monitored as described in Yoshiike et al. (2001).”
BackgroundMethodInfluentialSelf-citation
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683
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
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
Curcumin and its Derivatives: Their Application in Neuropharmacology and Neuroscience in the 21st Century
Lee, W., Loo, C., Bebawy, M., Luk, F., Mason, R. S., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 552
Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530
Biological metals and metal-targeting compounds in major neurodegenerative diseases
Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497
Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer’s disease animal models
Baum, L., & Ng, A. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6403 · Cited by 483
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
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 360
Granular Tau Oligomers as Intermediates of Tau Filaments
Maeda, S., Sahara, N., Saito, Y., Murayama, M., Yoshiike, Y., Kim, H., Miyasaka, T., Murayama, S., Ikai, A., & Takashima, A. (2007) · Biochemistry · doi:10.1021/bi061359o · Cited by 330
Self-citation
A Novel Function of Monomeric Amyloid β-Protein Serving as an Antioxidant Molecule against Metal-Induced Oxidative Damage
Zou, K., Gong, J.-S., Yanagisawa, K., & Michikawa, M. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04833.2002 · Cited by 305
“In support of these findings, a recent study has clearly demonstrated that zinc and copper induce non- -sheeted A aggregation but inhibit -sheeted aggregation and fibril formation (Yoshiike et al., 2001).”
Result
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
Amyloid-β: a chameleon walking in two worlds: a review of the trophic and toxic properties of amyloid-β
Atwood, C., Obrenovich, M. E., Liu, T., Chan, H., Perry, G. L., Smith, M. A., & Martins, R. N. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(03)00174-7 · Cited by 297
Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease
Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 291
Aluminium in Alzheimer?s disease: are we still at a crossroad?
Gupta, V. B., Anitha, S., Hegde, M. L., Zecca, L., Garruto, R. M., Ravid, R., Shankar, S. K., Stein, R., Shanmugavelu, P., & Rao, K. S. J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4317-3 · Cited by 294
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 288
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
Clioquinol: Review of its Mechanisms of Action and Clinical Uses in Neurodegenerative Disorders
Bareggi, S. R., & Cornelli, U. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00231.x · Cited by 251
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
Hydrogen Peroxide Is Generated during the Very Early Stages of Aggregation of the Amyloid Peptides Implicated in Alzheimer Disease and Familial British Dementia
Tabner, B. J., El‐Agnaf, O. M. A., Turnbull, S., German, M. J., Paleologou, K. E., Hayashi, Y., Cooper, L. J., Fullwood, N. J., & Allsop, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500238200 · Cited by 243
Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics
Masters, C. L., Cappai, R., Barnham, K. J., & Villemagne, V. L. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03989.x · Cited by 242
“(2006) 97, 1700–1725 and fibril formation or (ii) lowering the pH (Yoshiike et al. 2001).”
Background
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 224
A Rapid Label-Free Electrochemical Detection and Kinetic Study of Alzheimer's Amyloid Beta Aggregation
Vestergaard, M. C. M., Kerman, K., Saito, M., Nagatani, N., Takamura, Y., & Tamiya, E. (2005) · Journal of the American Chemical Society · doi:10.1021/ja052522q · Cited by 218
Implications of the kynurenine pathway and quinolinic acid in Alzheimer's disease
Guillemin, G. J., & Brew, B. J. (2002) · Redox Report · doi:10.1179/135100002125000550 · 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
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
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
Distinct Effects of Zn2+, Cu2+, Fe3+, and Al3+ on Amyloid-β Stability, Oligomerization, and Aggregation
Chen, W.-T., Liao, Y., Yu, H.-M., Cheng, I. H.-J., & Chen, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177246 · Cited by 199
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
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
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
Neurotoxic, Redox-competent Alzheimer's β-Amyloid Is Released from Lipid Membrane by Methionine Oxidation
Barnham, K. J., Ciccotosto, G. D., Tickler, A. K., Ali, F. E. A., Smith, D. G., Williamson, N. A., Lam, Y.-H., Carrington, D., Tew, D. J., Kocak, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305494200 · Cited by 191
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 187
Zn(II)‐ and Cu(II)‐induced non‐fibrillar aggregates of amyloid‐β (1–42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators
Tõugu, V., Karafin, A., Zovo, K., Chung, R. S., Howells, C., West, A. K., & Palumaa, P. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06269.x · Cited by 181
“Later it was found that the metal-induced Ab aggregates are predominantly nonfibrillar (Yoshiike et al. 2001; Raman et al. 2005), however, enhanced fibril formation in the presence of metal ions has also been observed (Klug et al. 2003; Ricchelli et al. 2005).”
BackgroundResult
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
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 183
Advances in the Understanding of Mammalian Copper Transporters
Wang, Y., Hodgkinson, V. L., Zhu, S., Weisman, G. A., & Petris, M. J. (2011) · Advances in Nutrition · doi:10.3945/an.110.000273 · Cited by 177
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
Biometal Dyshomeostasis and Toxic Metal Accumulations in the Development of Alzheimer’s Disease
Li, Y. H., Jiao, Q., Xu, H., Du, X., Shi, L., Jia, F., & Jiang, H. F. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00339 · Cited by 173
“Relative to iron and copper, zinc binds to Aβ with a greater affinity upon a wide range of pH (Yoshiike et al., 2001).”
Background
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
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 159
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
Propargylamine-derived multitarget-directed ligands: fighting Alzheimer’s disease with monoamine oxidase inhibitors
Bolea, I., Gella, A., & Unzeta, M. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0948-y · Cited by 158
Liberation of Copper from Amyloid Plaques: Making a Risk Factor Useful for Alzheimer’s Disease Treatment
Geng, J., Li, M. C., Wu, L. J., Ren, J., & Qu, X. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3003813 · Cited by 153
Alzheimer’s disease: How metal ions define β-amyloid function
Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 154
Metals and Neuronal Metal Binding Proteins Implicated in Alzheimer’s Disease
Cristóvão, J. S., Santos, R., & Gomes, C. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9812178 · Cited by 146
“In spite of contradictory findings, there seems to be a consensus that (a) superstoichiometric levels of Cu and Zn result in insoluble and amorphous aggregates rather than organized fibrils [49, 52–55]; (b) equimolar Zn and Cu induce amorphous aggregates, which slowly convert to fibrils [56, 57]; and (c) at subequimol…”
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
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
Vitamin A exhibits potent antiamyloidogenic and fibril-destabilizing effects in vitro
Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., & Yamada, M. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.05.035 · Cited by 134
Self-citation
The role of copper ions in pathophysiology and fluorescent sensors for the detection thereof
Verwilst, P., Sunwoo, K., & Kim, J. S. (2015) · Chemical Communications · doi:10.1039/c4cc10366a · Cited by 133
Role of metals in Alzheimer’s disease
Das, N., Raymick, J. B., & Sarkar, S. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00765-w · Cited by 132
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation
Abelein, A., Gräslund, A., & Danielsson, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1421961112 · Cited by 123
Cu(II) Mediates Kinetically Distinct, Non-amyloidogenic Aggregation of Amyloid-β Peptides
Pedersen, J. T., Østergaard, J., Rozlosnik, N., Gammelgaard, B., & Heegaard, N. H. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220863 · Cited by 123
Nordihydroguaiaretic acid potently breaks down pre‐formed Alzheimer's β‐amyloid fibrils in vitro
Ono, K., Hasegawa, K., Yoshiike, Y., Takashima, A., Yamada, M., & Naiki, H. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00904.x · Cited by 121
Self-citation
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
Aggregation Pathways of the Amyloid β(1–42) Peptide Depend on Its Colloidal Stability and Ordered β-Sheet Stacking
Jiang, D., Rauda, I. E., Han, S., Chen, S., & Zhou, F. (2012) · Langmuir · doi:10.1021/la3021436 · Cited by 117
S -Nitrosothiols React Preferentially with Zinc Thiolate Clusters of Metallothionein III through Transnitrosation
Chen, Y., Irie, Y., Keung, W. M., & Maret, W. (2002) · Biochemistry · doi:10.1021/bi020030+ · Cited by 115
The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway
Abelein, A., Abrahams, J. P., Danielsson, J., Gräslund, A., Jarvet, J., Luo, J., Tiiman, A., & Wärmländer, S. K. T. S. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1131-8 · Cited by 115
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
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 116
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
Surface Structure of Amyloid-β Fibrils Contributes to Cytotoxicity
Yoshiike, Y., Akagi, T., & Takashima, A. (2007) · Biochemistry · doi:10.1021/bi700455c · Cited by 110
Self-citation
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 110
“This type of aggregate has been noted before in the case of A (1–40) (27, 53, 54).”
BackgroundResult
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
Molecular Mechanisms of Metal Toxicity in the Pathogenesis of Alzheimer’s Disease
Kabir, M. T., Uddin, M. S., Zaman, S., Begum, Y., Ashraf, G. M., Bin-Jumah, M. N., BUNGAU, S. G., Mousa, S. A., & Abdel‐Daim, M. M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02096-w · Cited by 113
β‐Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH
Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109
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 112
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
Copper prevents amyloid-β1–42 from forming amyloid fibrils under near-physiological conditions in vitro
Mold, M., Ouro-Gnao, L., Wieckowski, B. M., & Exley, C. (2013) · Scientific Reports · doi:10.1038/srep01256 · Cited by 101
Altered microglial copper homeostasis in a mouse model of Alzheimer’s disease
Zheng, Z., White, C., Lee, J., Peterson, T. S., Bush, A. I., Sun, G. Y., Weisman, G. A., & Petris, M. J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06888.x · Cited by 103
“For example, copper can potentiate the ability of Ab to penetrate and disrupt membranes (Curtain et al. 2001, 2003), inhibit mitochondrial cytochrome c oxidase (Crouch et al. 2005) and kill neurons (Huang et al. 1999b; Yoshiike et al. 2001; Giuffrida et al. 2007).”
Background
The Metal Loading Ability of β-Amyloid N-Terminus: A Combined Potentiometric and Spectroscopic Study of Copper(II) Complexes with β-Amyloid(1−16), Its Short or Mutated Peptide Fragments, and Its Polyethylene Glycol (PEG)-ylated Analogue
Damante, C. A., Ösz, K., Nagy, Z., Pappalardo, G., Grasso, G., Impellizzeri, G., Rizzarelli, E., & Sóvágó, I. (2008) · Inorganic Chemistry · doi:10.1021/ic8006052 · Cited by 94
Ionic Strength Modulation of the Free Energy Landscape of Aβ 40 Peptide Fibril Formation
Abelein, A., Jarvet, J., Barth, A., Gräslund, A., & Danielsson, J. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b04511 · Cited by 92
8-Hydroxyquinoline Schiff-base compounds as antioxidants and modulators of copper-mediated Aβ peptide aggregation
Gomes, L. M., Vieira, R. P., Jones, M. R., Wang, M. C. P., Dyrager, C., de Souza-Fagundes, E. M., Silva, J. G. D., Storr, T., & Beraldo, H. D. O. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.04.011 · Cited by 94
Aluminum and other metals in Alzheimer's disease: A review of potential therapy with chelating agents
Domingo, J. L. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-102-315 · Cited by 91
“While it has been shown that zinc may serve twin roles by initiating amyloid deposition and then being involved in mechanisms attempting to quench oxidative stress and neurotoxicity derived from the amyloid mass [55], it has been also suggested that zinc has an overall protective effect against β-amyloid toxicity [15,…”
Background
Zinc Overload Enhances APP Cleavage and Aβ Deposition in the Alzheimer Mouse Brain
Wang, C., Wang, T., Zheng, W., Zhao, B., Danscher, G., Chen, Y., & Wang, Z. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015349 · Cited by 93
“At an early stage of AD, the elevated brain zinc results in the formation of zinc-Ab complex, which is of some benefit in protecting against zinc toxicity [42,43,44].”
Background
PEGylated phospholipid nanomicelles interact with β-amyloid(1–42) and mitigate its β-sheet formation, aggregation and neurotoxicity in vitro
Pai, A., Rubinstein, I., & Önyüksel, H. (2006) · Peptides · doi:10.1016/j.peptides.2006.04.022 · Cited by 83
Multifunctional roles of zinc in Alzheimer’s disease
Xie, Z., Wu, H., & Zhao, J. (2020) · NeuroToxicology · doi:10.1016/j.neuro.2020.07.003 · Cited by 94
Shedding Light on Alzheimer’s β-Amyloidosis: Photosensitized Methylene Blue Inhibits Self-Assembly of β-Amyloid Peptides and Disintegrates Their Aggregates
Lee, B. I., Suh, Y. S., Chung, Y. J., Yu, K., & Park, C. B. (2017) · Scientific Reports · doi:10.1038/s41598-017-07581-2 · Cited by 79
Rapid aggregation and assembly in aqueous solution of Aβ (25–35) peptide
Millucci, L., Raggiaschi, R., Franceschini, D., Terstappen, G. C., & Santucci, A. (2009) · Journal of Biosciences · doi:10.1007/s12038-009-0033-3 · Cited by 79
“We adopted a modifi ed procedure described by Yoshiike et al. (2001) .”
MethodInfluential
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
Radioiodinated clioquinol as a biomarker for β‐amyloid: Zn2+ complexes in Alzheimer's disease
Opazo, C., Luza, S., Villemagne, V. L., Volitakis, I., Rowe, C. C., Barnham, K. J., Altschul, D., Masters, C. L., Cherny, R. A., & Bush, A. I. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00196.x · Cited by 76
“We and others have characterized Aβ as a metalloprotein able to coordinate Cu2+, Zn2+ and Fe3+ (Bush et al., 1994b; Atwood et al., 2000; Yoshiike et al., 2001; Opazo et al., 2002; Dong et al., 2003).”
Background
Rapid Formation of a Preoligomeric Peptide–Metal–Peptide Complex Following Copper(II) Binding to Amyloid β Peptides
Pedersen, J. T., Teilum, K., Heegaard, N. H. H., Østergaard, J., Adolph, H., & Hemmingsen, L. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201006335 · Cited by 75
Curcumin derivatives as metal-chelating agents with potential multifunctional activity for pharmaceutical applications
Ferrari, É., Benassi, R., Sacchi, S., Pignedoli, F., Asti, M., & Saladini, M. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.06.002 · Cited by 75
β-Sheet Structured β-Amyloid(1-40) Perturbs Phosphatidylcholine Model Membranes
de Planque, M. R. R., Raussens, V., Contera, S., Rijkers, D. T. S., Liskamp, R. M. J., Ruysschaert, J., Ryan, J. F., Separovic, F., & Watts, A. G. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.063 · Cited by 80
Copper(II) interaction with amyloid-β: Affinity and speciation
Arena, G., Pappalardo, G., Sóvágó, I., & Rizzarelli, E. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.012 · Cited by 74
Metal-Induced Conformational Changes of Human Metallothionein-2A: A Combined Theoretical and Experimental Study of Metal-Free and Partially Metalated Intermediates
Chen, S., Chen, L., & Russell, D. H. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5047878 · Cited by 74
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
Metal Loading Capacity of Aβ N-Terminus: a Combined Potentiometric and Spectroscopic Study of Zinc(II) Complexes with Aβ(1−16), Its Short or Mutated Peptide Fragments and Its Polyethylene Glycol−ylated Analogue
Damante, C. A., Ösz, K., Nagy, Z., Pappalardo, G., Grasso, G., Impellizzeri, G., Rizzarelli, E., & Sóvágó, I. (2009) · Inorganic Chemistry · doi:10.1021/ic9012334 · Cited by 70
Rapid Exchange of Metal between Zn7–Metallothionein-3 and Amyloid-β Peptide Promotes Amyloid-Related Structural Changes
Pedersen, J. T., Hureau, C., Hemmingsen, L., Heegaard, N. H. H., Østergaard, J., Vašák, M., & Faller, P. (2012) · Biochemistry · doi:10.1021/bi201774z · Cited by 72
Amyloid-β Metal Interaction and Metal Chelation
Cuajungco, M. P., Frederickson, C. J., & Bush, A. I. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_12 · Cited by 68
Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets
Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67
Is there a role for copper in neurodegenerative diseases?
Cerpa, W. F., Varela‐Nallar, L., Reyes, A. E., Minniti, A. N., & Inestrosa, N. C. (2005) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2005.07.011 · Cited by 67
“In vitro analysis showed that Cu did not affect Ab aggregation (Yoshiike et al., 2001) while other studies conclude that it enhance Ab aggregation (House et al.”
Background
Advances in Multi-Functional Ligands and the Need for Metal-Related Pharmacology for the Management of Alzheimer Disease
Sharma, A., Pachauri, V., & Flora, S. J. S. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01247 · Cited by 67
Curcumin Alters the Salt Bridge-containing Turn Region in Amyloid β(1–42) Aggregates
Mithu, V. S., Sarkar, B., Bhowmik, D., Das, A. K., Chandrakesan, M., Maiti, S., & Madhu, P. K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.519447 · Cited by 67
Cerebrovascular requirement for sealant, anti-coagulant and remodeling molecules that allow for the maintenance of vascular integrity and blood supply
Atwood, C., Bowen, R. L., Smith, M. A., & Perry, G. L. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(03)00206-6 · Cited by 64
Cu(II) interaction with amyloid-β peptide: A review of neuroactive mechanisms in AD brains
Lin, C., Huang, H., & Jiang, Z.-F. (2010) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2010.06.003 · Cited by 64
Cu2+ accentuates distinct misfolding of Aβ(1–40) and Aβ(1–42) peptides, and potentiates membrane disruption
Matheou, C. J., Younan, N. D., & Viles, J. H. (2014) · Biochemical Journal · doi:10.1042/bj20141168 · Cited by 64
Zn++ Binding Disrupts the Asp23-Lys28 Salt Bridge without Altering the Hairpin-Shaped Cross-β Structure of Aβ42 Amyloid Aggregates
Mithu, V. S., Sarkar, B., Bhowmik, D., Chandrakesan, M., Maiti, S., & Madhu, P. K. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.023 · Cited by 63

Authors: Yoshiike, Y., Tanemura, K., Murayama, O., Akagi, T., Murayama, M., Sato, S., Sun, X., Tanaka, N., & Takashima, A.
Affiliations: Tokyo Institute of Technology (JP)
RIKEN Center for Brain Science (JP)
Corresponding author: Takashima, Akihiko
ORCID: Tanemura, Kentaro
Sato, Shinji
Sun, Xiaoyan
Takashima, Akihiko
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2001-08
Volume: 276
Issue: 34
Pages: 32293-32299
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m010706200
OpenAlex: W2081099437
Cited by: 244
References: 60
Citations by year: 2026: 1 · 2025: 2 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 6 · 2020: 8 · 2019: 12 · 2018: 9 · 2017: 11 · 2016: 6 · 2015: 6 · 2014: 12 · 2013: 9 · 2012: 22
FWCI: 4.58
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7016 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: amyloid-beta, metal-induced aggregation, zinc, copper, amyloid cytotoxicity, oxidative stress, amyloid plaques, heparin, pH effect, Alzheimer's disease
MeSH terms: Animals, Cell Line, Cell Survival, Cells, Cultured, Circular Dichroism, Copper, Hippocampus, Humans, Neurons, Zinc, Amyloid beta-Peptides, Cell Death, Rats

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

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

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