The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity
Open accessAbstract
Oxidative stress markers as well as high concentrations of copper are found in the vicinity of Abeta amyloid deposits in Alzheimer's disease. The neurotoxicity of Abeta in cell culture has been linked to H(2)O(2) generation by an unknown mechanism. We now report that Cu(II) markedly potentiates the neurotoxicity exhibited by Abeta in cell culture. The potentiation of toxicity is greatest for Abeta1-42 > Abeta1-40 >> mouse/rat Abeta1-40, corresponding to their relative capacities to reduce Cu(II) to Cu(I), form H(2)O(2) in cell-free assays and to exhibit amyloid pathology. The copper complex of Abeta1-42 has a highly positive formal reduction potential ( approximately +500-550 mV versus Ag/AgCl) characteristic of strongly reducing cuproproteins. These findings suggest that certain redox active metal ions may be important in exacerbating and perhaps facilitating Abeta-mediated oxidative damage in Alzheimer's disease.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The cited source says what the claim attributes to it.
In the citing paper
“Since metal-Aβ species have been shown to be neurotoxic,25,51,92”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [92]
The cited source says what the claim attributes to it.
In the citing paper
“Because Cu2+–Aβ species have been shown to be neurotoxic,20,21,31,51,52”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [52]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Oxygen toxicity, oxygen radicals, transition metals and disease
Halliwell, B., & Gutteridge, J. M. C. (1984) · Biochemical Journal · doi:10.1042/bj2190001 · Cited by 5,330
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
Self-citationScheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Self-citationCopper, 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
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074
Rae, T., Schmidt, P. J., Pufahl, R. A., Culotta, V., & O’Halloran, T. V. (1999) · Science · doi:10.1126/science.284.5415.805 · Cited by 1,640
Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1
Duff, K., Eckman, C., Zehr, C., Yu, X., Prada, C.-M., Pérez‐Tur, J., Hutton, M., Buée, L., Harigaya, Y., Yager, D., et al. (1996) · Nature · doi:10.1038/383710a0 · Cited by 1,486
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
The cellular prion protein binds copper in vivo
Brown, D. R., Qin, K., Herms, J., Madlung, A., Manson, J., Strome, R., Fraser, P., Kruck, T., von Bohlen, A., Schulz-Schaeffer, W., et al. (1997) · Nature · doi:10.1038/37783 · Cited by 1,300
The biological chemistry of the elements
(1993) · The Science of The Total Environment · doi:10.1016/0048-9697(93)90224-t · Cited by 1,173
Flagged first, then by citations
Research works printed but not linked: 1
- Basun, 1991, J. Neural Transm. Park. Dis. Dement. Sect., 3, 231
Cited by
Sorted by citations
Items 301–400 of 769
ASS234, As a New Multi-Target Directed Propargylamine for Alzheimer's Disease Therapy
Marco, J. L., Unzeta, M., Bolea, I., Esteban, G., Ramsay, R. R., Romero, A., Martínez‐Murillo, R., Carreiras, M. C., & Ismaïli, L. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00294 · Cited by 75
Oxidative stress in Alzheimer's disease: Primary villain or physiological by-product?
Sutherland, G. T., Chami, B., Youssef, P., & Witting, P. K. (2013) · Redox Report · doi:10.1179/1351000213y.0000000052 · Cited by 80
Hong, L., Carducci, T. M., Bush, W. D., Dudzik, C. G., Millhauser, G. L., & Simon, J. D. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp103272v · Cited by 73
Chen, Z., Digiacomo, M., Tu, Y., Gu, Q., Wang, S., Yang, X., Chu, J., Chen, Q., Han, Y., Chen, J., et al. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.09.052 · Cited by 75
Jalili‐Baleh, L., Forootanfar, H., Küçükkılınç, T. T., Nadri, H., Abdolahi, Z., Ameri, A., Jafari, M., Ayazgök, B., Baeeri, M., Rahimifard, M., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.04.058 · Cited by 73
Melatonin: A potential nighttime guardian against Alzheimer’s
Zhang, Z., Xue, P., Bendlin, B. B., Zetterberg, H., Felice, F. G. D., Tan, X. W., & Benedict, C. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02691-6 · Cited by 76
Brain proteins that mind metals: a neurodegenerative perspective
Brown, D. R. (2009) · Dalton Transactions · doi:10.1039/b822135a · Cited by 72
Teo, E., Ravi, S., Barardo, D., Kim, H.-S., Fong, S., Cazenave-Gassiot, A., Tan, T. Y., Ching, J., Kovalik, J.-P., Wenk, M. R., et al. (2019) · eLife · doi:10.7554/elife.50069 · Cited by 72
White, A. R., Guirguis, R., Brazier, M. W., Jobling, M. F., Hill, A. F., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Collins, S. J., & Cappai, R. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0386 · Cited by 70
Self-citationInteraction of neurons and astrocytes underlies the mechanism of Aβ-induced neurotoxicity
Angelova, P. R., & Abramov, A. Y. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140153 · Cited by 71
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
Mechanism of Hydrogen Peroxide Production by Copper-Bound Amyloid Beta Peptide: A Theoretical Study
Hewitt, N., & Rauk, A. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp807327a · Cited by 69
Trace Element Levels and Cognitive Function in Rural Elderly Chinese
Gao, S., Jin, Y., Unverzagt, F. W., Ma, F., Hall, K. S., Murrell, J. R., Cheng, Y., Shen, J., Ying, B., Ji, R., et al. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.6.635 · Cited by 69
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
Antioxidant protection and neurodegenerative disease: The role of amyloid-β and tau
Castellani, R. J., Lee, H., Perry, G. L., & Smith, M. A. (2006) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/153331750602100213 · Cited by 72
Nicotine attenuates the β‐amyloid neurotoxicity through regulating metal homeostasis
Zhang, J., Liu, Q., Chen, Q., Liu, N.-Q., Li, F., Lu, Z., Qin, C., Zhu, H., Huang, Y., He, W., et al. (2006) · The FASEB Journal · doi:10.1096/fj.05-5214fje · Cited by 70
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
Self-citationNovel therapeutic strategies provide the real test for the amyloid hypothesis of Alzheimer's disease
Dominguez, D. I., & Strooper, B. D. (2002) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(02)02038-2 · Cited by 68
Neurotoxicity from glutathione depletion is dependent on extracellular trace copper
White, A. R., & Cappai, R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10537 · Cited by 66
Exploring the Formation of Alzheimer's Disease Senile Plaques in Silico
Edelstein‐Keshet, L., & Spiros, Ä. (2002) · Journal of Theoretical Biology · doi:10.1006/jtbi.2002.2540 · Cited by 66
Murine Aβ over-production produces diffuse and compact Alzheimer-type amyloid deposits
Xu, G., Ran, Y., Fromholt, S. E., Fu, C., Yachnis, A. T., Golde, T. E., & Borchelt, D. R. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0252-9 · Cited by 65
Copper(II) complexation by human and mouse fragments (11–16) of β-amyloid peptide
Kowalik‐Jankowska, T., Ruta-Dolejsz, M., Wiśniewska, K., Łankiewicz, L., & Kozłowski, H. (2000) · Journal of the Chemical Society Dalton Transactions · doi:10.1039/b006125p · Cited by 65
Jiang, D., Zhang, L., Grant, G. P. G., Dudzik, C. G., Chen, S., Patel, S., Hao, Y., Millhauser, G. L., & Zhou, F. (2012) · Biochemistry · doi:10.1021/bi301053h · Cited by 64
Geriatric Medicine and Gerontology
Zawada, E. T. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.77654 · Cited by 64
Luo, Y., Zhang, J., Liu, N., Luo, Y., & Zhao, B. (2011) · Science China Life Sciences · doi:10.1007/s11427-011-4180-z · Cited by 63
Role of antioxidants and a nutrient rich diet in Alzheimer's disease
Veurink, G., Perry, G. L., & Singh, S. K. (2020) · Open Biology · doi:10.1098/rsob.200084 · Cited by 69
Mishra, P., Mittal, A. K., Kalonia, H., Madan, S., Ghosh, S., Sinha, J. K., & Rajput, S. K. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200729111744 · Cited by 70
The Amyloid Paradox: Amyloid‐β‐Metal Complexes can be Neurotoxic and Neuroprotective
Bishop, G. M., & Robinson, S. R. (2004) · Brain Pathology · doi:10.1111/j.1750-3639.2004.tb00089.x · Cited by 65
Zatta, P. F., Tognon, G., & Carampin, P. (2003) · Journal of Pineal Research · doi:10.1034/j.1600-079x.2003.00058.x · Cited by 64
Cofactors of mitochondrial enzymes attenuate copper‐induced death in vitro and in vivo
Sheline, C. T., Choi, E. H., Kim‐Han, J. S., Dugan, L. L., & Choi, D. W. (2002) · Annals of Neurology · doi:10.1002/ana.10276 · Cited by 63
Paramagnetic Metal Ions in Pulsed ESR Distance Distribution Measurements
Ji, M., Ruthstein, S., & Saxena, S. (2013) · Accounts of Chemical Research · doi:10.1021/ar400245z · Cited by 65
Metal-protein attenuating compounds and Alzheimer’s disease
Ritchie, C. W., Bush, A. I., & Masters, C. L. (2004) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.13.12.1585 · Cited by 62
Self-citationForet, M. K., Orciani, C., Welikovitch, L. A., Huang, C., Cuello, A. C., & Carmo, S. D. (2024) · Communications Biology · doi:10.1038/s42003-024-06552-4 · Cited by 63
Zheng, H., Amit, T., Bar‐Am, O., Fridkin, M., Youdim, M. B. H., & Mandel, S. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120013 · Cited by 62
Twenty years of metallo-neurobiology: where to now?
Bush, A. I., & Curtain, C. C. (2007) · European Biophysics Journal · doi:10.1007/s00249-007-0228-1 · Cited by 62
Self-citationProbing copper/tau protein interactions electrochemically
Martic, S., Rains, M. K., & Kraatz, H.-B. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.07.015 · Cited by 60
Dual-function triazole–pyridine derivatives as inhibitors of metal-induced amyloid-β aggregation
Jones, M. R., Service, E. L., Thompson, J. R., Wang, M. C. P., Kimsey, I. J., DeToma, A. S., Ramamoorthy, A., Lim, M. H., & Storr, T. (2012) · Metallomics · doi:10.1039/c2mt20113e · Cited by 60
Three Dimensional Models of Cu 2+ -Aβ(1–16) Complexes from Computational Approaches
Alí‐Torres, J., Maréchal, J., Rodrı́guez-Santiago, L., & Sodupe, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203407v · Cited by 60
Agricultural Use of Copper and Its Link to Alzheimer’s Disease
Coelho, F. C., Squitti, R., Ventriglia, M., Cerchiaro, G., Daher, J. P. L., da Rocha, J. G., Rongioletti, M. C. A., & Moonen, A. (2020) · Biomolecules · doi:10.3390/biom10060897 · Cited by 60
Red wine micronutrients as protective agents in Alzheimer-like induced insult
Russo, A., Palumbo, M., Aliano, C., Lempereur, L., Scoto, G. M., & Renis, M. (2003) · Life Sciences · doi:10.1016/s0024-3205(03)00123-1 · Cited by 60
Physiological Role of Amyloid Beta in Neural Cells: The Cellular Trophic Activity
Cárdenas‐Aguayo, M. D. C., Silva‐Lucero, M., Cortés-Ortiz, M., Jimnez-Ramos, B., Gomez‐Virgilio, L., Ramrez-Rodrguez, G., Arroyo, E. V., Fiorentino-Prez, R., Garca, U., Luna-Muoz, J., et al. (2014) · InTech eBooks · doi:10.5772/57398 · Cited by 67
Neighboring Amide Participation in Thioether Oxidation: Relevance to Biological Oxidation
Glass, R. S., Hug, G. L., Schöneich, C., Wilson, G. S., Kuznetsova, L., Lee, T.-M., Ammam, M., Lorance, E. D., Nauser, T., Nichol, G. S., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904895u · Cited by 61
Jiménez-Del-Río, M., & Velez‐Pardo, C. (2004) · Archives of Medical Research · doi:10.1016/j.arcmed.2004.01.001 · Cited by 59
Jiang, H., Wu, Y.-C., Nakamura, M., Liang, Y., Tanaka, Y., Holmes, S., Dawson, V. L., Dawson, T. M., Ross, C. A., & Smith, W. W. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.07.017 · Cited by 62
What has fluorescent sensing told us about copper and brain malfunction?
Shen, C., & New, E. J. (2014) · Metallomics · doi:10.1039/c4mt00288a · Cited by 58
Kański, J., Aksenova, M. V., & Butterfield, D. A. (2002) · Neurotoxicity Research · doi:10.1080/10298420290023945 · Cited by 58
The neuroprotective role of melatonin against amyloidβpeptide injected mice
Masilamoni, J. G., Jesudason, E. P., Dhandayuthapani, S., Ashok, B. S., Vignesh, S., Walter, C. E. J., Paul, S. F. D., & Rajadas, J. (2008) · Free Radical Research · doi:10.1080/10715760802277388 · Cited by 60
Pharmacotherapeutic targets in Alzheimer's disease
Biran, Y., Masters, C. L., Barnham, K. J., Bush, A. I., & Adlard, P. A. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00595.x · Cited by 59
Self-citationPenna, G. L., Hureau, C., Andreussi, O., & Faller, P. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp410046w · Cited by 57
Toni, M., Massimino, M. L., Mario, A. D., Angiulli, E., & Spisni, E. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00003 · Cited by 56
Gomes, L. M., Mahammed, A., Prosser, K. E., Smith, J. R., Silverman, M. A., Walsby, C. J., Gross, Z., & Storr, T. (2018) · Chemical Science · doi:10.1039/c8sc04660c · Cited by 56
Sodium pyruvate protects against H2O2 mediated apoptosis in human neuroblastoma cell line-SK-N-MC
Jagtap, J. C., Chandele, A., Chopde, B. A., & Shastry, P. (2003) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(03)00037-1 · Cited by 56
Bahadi, R., Farrelly, P. V., Kenna, B. L., Kourie, J. I., Tagliavini, F., Forloni, G., & Salmona, M. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00077.2003 · Cited by 56
Marques, S. S., Magalhães, L. M., Tóth, I. V., & Segundo, M. A. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150711387 · Cited by 56
Sheline, C. T., & Wei, L. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.02.019 · Cited by 56
α-Synuclein enhances secretion and toxicity of amyloid beta peptides in PC12 cells
Wilkaniec, A., Strosznajder, J. B., & Adamczyk, A. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.08.004 · Cited by 59
Metallothioneins and copper metabolism are candidate therapeutic targets in Huntington's disease
Hands, S. L., Mason, R. P., Sajjad, M. U., Giorgini, F., & Wyttenbach, A. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380552 · Cited by 55
Capturing a Reactive State of Amyloid Aggregates
Parthasarathy, S., Yoo, B., McElheny, D., Tay, W. M., & Ishii, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.511345 · Cited by 55
Tabner, B. J., Mayes, J., & Allsop, D. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/546380 · Cited by 56
Sublethal Doses of β-Amyloid Peptide Abrogate DNA-dependent Protein Kinase Activity
Cardinale, A., Racaniello, M., Saladini, S., Chiara, G. D., Mollinari, C., de Stefano, M. C., Pocchiari, M., Garaci, E., & Merlo, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.276550 · Cited by 54
Turnbull, S., Tabner, B. J., El‐Agnaf, O. M. A., Twyman, L. J., & Allsop, D. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00510-x · Cited by 54
Tajes, M., Eraso‐Pichot, A., Rubio-Moscardó, F., Guivernau, B., Bosch-Morató, M., Valls-Comamala, V., & Muñoz, F. J. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.07.047 · Cited by 53
CuII Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function
Stefaniak, E., & Bal, W. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b01399 · Cited by 56
Metal ion interactions with mAbs: Part 1
Glover, Z. K., Basa, L. J., Moore, B. N., Laurence, J. S., & Sreedhara, A. (2015) · mAbs · doi:10.1080/19420862.2015.1062193 · Cited by 52
Single Nanoskived Nanowires for Electrochemical Applications
Dawson, K., Strutwolf, J., Rodgers, K., Herzog, G., Arrigan, D. W. M., Quinn, A. J., & O'Riordan, A. J. (2011) · Analytical Chemistry · doi:10.1021/ac2004086 · Cited by 52
Notch-1 activation by familial Alzheimer's disease (FAD)-linked mutant forms of presenilin-1
Nakajima, M., Shimizu, T., & Shirasawa, T. (2000) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20001015)62:2 · Cited by 27
Self-citationStereospecific interactions are necessary for Alzheimer disease amyloid-β toxicity.
Ciccotosto, G., Tew, D., Drew, S., Smith, D. G., Johanssen, T., Lal, V., Lau, T., Perez, K., Curtain, C., Wade, J., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.018 · Cited by 48
Self-citationRózga, M., & Bal, W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900358j · Cited by 54
Bandyopadhyay, S., Huang, X., Cho, H. K., Greig, N. H., Youdim, M. B. H., & Rogers, J. T. (2006) · Springer eBooks · doi:10.1007/978-3-211-33328-0_25 · Cited by 51
Self-citationSquitti, R. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.06.018 · Cited by 52
Celsi, F. (2003) · Neurochemistry International · doi:10.1016/s0197-0186(03)00101-3 · Cited by 50
Salahuddin, P., Khan, R. H., Furkan, M., Uversky, V. N., Islam, Z., & Fatima, M. T. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.07.056 · Cited by 50
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
Imaginem oblivionis: the prospects of neuroimaging for early detection of Alzheimer's disease
Villemagne, V. L., Rowe, C. C., Macfarlane, S., Novakovic, K. E., & Masters, C. L. (2005) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2004.03.011 · Cited by 50
Self-citationPogocki, D. (2003) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2003-1463 · Cited by 50
Sources and mechanisms of cytoplasmic oxidative damage in Alzheimer's disease
Marlatt, M. W., Lee, H., Perry, G. L., Smith, M. A., & Zhu, X. (2004) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2004-1493 · Cited by 49
Lang, M., Fan, Q., Wang, L., Zheng, Y., Xiao, G., Wang, X., Wang, W., Zhong, Y., & Zhou, B. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.029 · Cited by 51
A time-course analysis of changes in cerebral metal levels following a controlled cortical impact
Portbury, S. D., Hare, D. J., Sgambelloni, C., Finkelstein, D. I., & Adlard, P. A. (2015) · Metallomics · doi:10.1039/c5mt00234f · Cited by 49
Sharma, A. K., Kim, J., Prior, J. T., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2014) · Inorganic Chemistry · doi:10.1021/ic500926c · Cited by 48
Oxidative Stress in Alzheimer’s Disease: Molecular Hallmarks of Underlying Vulnerability
Uddin, M. S., & Kabir, M. T. (2019) · Springer eBooks · doi:10.1007/978-981-13-9636-6_5 · Cited by 50
Pal, A., Rani, I., Pawar, A. T., Picozza, M., Rongioletti, M. C. A., & Squitti, R. (2021) · Biomolecules · doi:10.3390/biom11111598 · Cited by 48
Yi, X., Feng, C., Hu, S., Li, H., & Wang, J. (2015) · The Analyst · doi:10.1039/c5an01864a · Cited by 52
Nagano, S., Huang, X., Moir, R. D., Payton, S. M., Tanzi, R. E., & Bush, A. I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313003200 · Cited by 48
Self-citationFree Radicals and Antioxidants in Human Disease
Lawson, M. K., Jomová, K., Poprac, P., Kuča, K., Musílek, K., & Valko, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-67625-8_12 · Cited by 47
Xu, W., Huang, H., Lin, C., & Jiang, Z.-F. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.03.105 · Cited by 47
Cai, Y., Xiao, R., Zhang, Y., Xu, D., Wang, N., Han, M., Zhang, Y., Zhang, L., & Zhou, W. (2022) · Antioxidants · doi:10.3390/antiox11091794 · Cited by 46
Chaudhari, V., Bagwe‐Parab, S., Buttar, H. S., Gupta, S., Vora, A., & Kaur, G. (2023) · Neurotoxicity Research · doi:10.1007/s12640-023-00634-7 · Cited by 47
Crouch, P. J., Barnham, K. J., Duce, J. A., Blake, R. E., Masters, C. L., & Trounce, I. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04050.x · Cited by 46
Self-citationInoue, K., Garner, C. O., Ackermann, B. L., Oe, T., & Blair, I. A. (2006) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2395 · Cited by 46
Squitti, R., Ventriglia, M., Gennarelli, M., Colabufo, N. A., Idrissi, I. G. E., Bucossi, S., Mariani, S., Rongioletti, M. C. A., Zanetti, O. O., Congiu, C., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9664-6 · Cited by 46
Yako, N., Young, T. R., Cottam, J. M., Hutton, C. A., Wedd, A. G., & Xiao, Z. (2017) · Metallomics · doi:10.1039/c6mt00299d · Cited by 46
Meleleo, D., Notarachille, G., Mangini, V., & Arnesano, F. (2019) · European Biophysics Journal · doi:10.1007/s00249-018-1344-9 · Cited by 47
Iron inhibits neurotoxicity induced by trace copper and biological reductants
White, A. R., Barnham, K. J., Huang, X., Volitakis, I., Beyreuther, K. T., Masters, C. L., Cherny, R. A., Bush, A. I., & Cappai, R. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0521-8 · Cited by 46
Self-citationA Concise Review on Oxidative Stress-Mediated Ferroptosis and Cuproptosis in Alzheimer’s Disease
Huang, X. (2023) · Cells · doi:10.3390/cells12101369 · Cited by 47
Self-citationFerrera, P., Mercado-Gómez, O. F., Silva-Aguilar, M., Valverde, M., & Arias, C. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9623-y · Cited by 46
One-electron oxidation of β-amyloid peptide: sequence modulation of reactivity
Kadlcik, V., Sicard‐Roselli, C., Mattioli, T. A., Kodı́ček, M., & Houée‐Levin, C. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.06.015 · Cited by 45
Williams, T. L., Serpell, L. C., & Urbanc, B. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.12.001 · Cited by 45
de la Monte, S. M., Ganju, N., Feroz, N., Luong, T., Banerjee, K., Cannon, J., & Wands, J. R. (2000) · Journal of Alzheimer s Disease · doi:10.3233/jad-2000-23-406 · Cited by 44
Links between copper and cholesterol in Alzheimer's disease
Hung, Y. H., Bush, A. I., & Fontaine, S. L. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00111 · Cited by 44
Self-citationBaruch-Suchodolsky, R., & Fischer, B. (2008) · Biochemistry · doi:10.1021/bi800114g · Cited by 44
Metadata
- Authors
- 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., Scarpa, R. C., Saunders, A. J., Lim, J., Moir, R. D., Glabe, C., Bowden, E. F., Masters, C. L., Fairlie, D. P., Tanzi, R. E., & Bush, A. I.
- Affiliations
- Harvard University (US)
- The University of Queensland (AU)
- North Carolina State University (US)
- Heidelberg University (DE)
- University of California, Irvine (US)
- Mental Health Research Institute (AU)
- Corresponding author
- Bush, Ashley I.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-12
- Volume
- 274
- Issue
- 52
- Pages
- 37111-37116
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2131633241
- Cited by
- 762
- References
- 40
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 13 · 2023: 14 · 2022: 14 · 2021: 10 · 2020: 15 · 2019: 30 · 2018: 16 · 2017: 19 · 2016: 26 · 2015: 27 · 2014: 33 · 2013: 28 · 2012: 42
- FWCI
- 14.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Massachusetts General Hospital
- Commonwealth of Massachusetts
- National Institutes of Health
- Medical Research Council
- Australian Research Council
- National Health and Medical Research Council
- National Institute on Aging
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid-beta, copper(II), neurotoxicity, oxidative stress, hydrogen peroxide production, amyloid-beta 42, Aβ40, copper proteins, metal ions, redox-active metals, oxidative damage
- MeSH terms
- Animals, Brain, Cells, Cultured, Computer Simulation, Copper, Electron Spin Resonance Spectroscopy, Hydrogen Peroxide, Oxidation-Reduction, Amyloid beta-Peptides, 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