The DOI matches its Crossref record; 71 of the 72 references it cites were found in a registry or an index.
Copper, iron and zinc in Alzheimer's disease senile plaques
Abstract
Concentrations of copper (Cu), iron (Fe) and zinc (Zn) were measured in the rims and cores of senile plaques (SP) and in the neuropil of the amygdala of nine Alzheimer's disease (AD) patients and in the neuropil of the amygdala of five neurologically normal control subjects using micro particle-induced X-ray emission (micro-PIXE). Comparison of SP rim and core values revealed no significant differences between levels of Cu, Fe or Zn. Zinc and Fe in SP rims and cores were significantly elevated in AD compared with AD neuropil (P<0.05). Copper was significantly elevated (P<0.05) in the rim of SP compared with AD neuropil. Comparison of AD and control neuropil revealed a significant (P<0.05) elevation of Zn in AD subjects. The elevation of these elements in SP in AD is of interest in light of the observation that Cu, Fe and particularly Zn, can accelerate aggregation of amyloid beta peptide.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Post-mortem examination of the brain suggested that bio-available metals (i.e., copper, zinc, and iron) are found in high concentration in the amyloid plaques.”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [12]
In the citing paper
“Thus, these metal ions have been shown to promote Aβ40 aggregation,23–27,29–32”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [23]
In the citing paper
“Remarkably high concentrations of Zn, Cu, and Fe have been found within the amyloid deposits in AD-affected brains,23,24”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [23]
In the citing paper
“This is in contrast with a large number of reports showing the aggregation-promoting effect of metal ions on the Aβ peptide.23–27,29–32,37,38”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [23]
In the citing paper
“unusually high concentrations of copper, iron, and zinc have been found within the amyloid deposits in AD-affected brains.11”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [11]
Citations
Cites
McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Consortium to Establish a Registry for Alzheimer's Disease (CERAD)
Fillenbaum, G., & Heyman, A. (2002) · doi:10.1002/0470846410.ch42(iii · Cited by 2,859
Diagnosis of Alzheimer's Disease
Khachaturian, Z. S. (1985) · Archives of Neurology · doi:10.1001/archneur.1985.04060100083029 · Cited by 2,499
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383
Self-citationEvans, D. A. (1989) · JAMA · doi:10.1001/jama.262.18.2551 · Cited by 1,627
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
Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296
Self-citationRelease of endogenous Zn2+ from brain tissue during activity
Assaf, S. Y., & Chung, S. (1984) · Nature · doi:10.1038/308734a0 · Cited by 1,113
Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A., & Butterfield, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3270 · Cited by 1,086
Research works printed but not linked: 3
- Ben-Shachar, 1987, Dopamine D2 receptor modulation by brain non-haem iron, Br J Pharmacol, 90, 2P
- Hess, 1974, Chronische Bleivergiftung. Praxis, 63, 177
- Markesbery WR, Ehmann WD. Brain trace elements in Alzheimer disease. In: Terry RD, Katzman R, Bick KL, editors. Alzheimer disease. New York: Raven Press, 1994:353–67.
Cited by
Sorted by citations
Items 801–900 of 1,007
Delivery of Curcumin and Medicinal Effects of the Copper(II)-Curcumin Complexes
Leung, M. H. M., Harada, T., & Kee, T. W. (2013) · Current Pharmaceutical Design · doi:10.2174/138161213805289237 · Cited by 51
Disturbed Copper Bioavailability in Alzheimer′s Disease
Kaden, D., Bush, A. I., Danzeisen, R., Bayer, T. A., & Multhaup, G. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/345614 · Cited by 51
Effects of aluminum on amyloid-beta aggregation in the context of Alzheimer’s disease
Zhang, Q., Zhang, F., Ni, Y., & Serge Kokot, A. (2015) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2015.06.019 · Cited by 51
Concepts for the treatment of Alzheimer's disease: molecular mechanisms and clinical application
Pietrzik, C. U., & Behl, C. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00435.x · Cited by 52
Ren, Y., Houghton, P. J., & Hider, R. C. (2006) · Journal of Pharmacy and Pharmacology · doi:10.1211/jpp.58.7.0015 · Cited by 51
Moreira, P. I., Honda, K., Zhu, X., Nunomura, A., Casadesús, G., Smith, M. A., & Perry, G. L. (2006) · Neurology · doi:10.1212/01.wnl.0000192307.15103.83 · Cited by 51
Elevated Zinc Transporter-6 in Mild Cognitive Impairment, Alzheimer Disease, and Pick Disease
Lovell, M. A., Smith, J. L., & Markesbery, W. R. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000229237.98124.91 · Cited by 51
Self-citationHouse, M. J., Pierre, T. G. S., & McLean, C. (2008) · Magnetic Resonance in Medicine · doi:10.1002/mrm.21586 · Cited by 51
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
Elevated glutathione as a therapeutic strategy in Alzheimer's disease
Butterfield, D. A., Pocernich, C. B., & Drake, J. (2002) · Drug Development Research · doi:10.1002/ddr.10095 · Cited by 51
Kowalik‐Jankowska, T., Ruta-Dolejsz, M., Wiśniewska, K., & Łankiewicz, L. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00495-6 · Cited by 51
Rossi, L. C., Squitti, R., Pasqualetti, P., Marchese, E., Cassetta, E., Forastiere, E., Rotilio, G., Rossini, P. M., & Finazzi‐Agrò, A. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00599-2 · Cited by 51
Braymer, J. J., DeToma, A. S., Choi, J.-S., Ko, K. S., & Lim, M. H. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/623051 · Cited by 50
“Elevated concentrations of Cu(II) and Zn(II) have been observed in senile plaques [1, 4, 13–15, 24, 25]; in particular, high concentrations of labile zinc are found in the regions of the brain most affected by AD, the cortex and hippocampus [4, 13–17, 19].”
BackgroundWhitmore, C. A., Haynes, J. R., Behof, W. J., Rosenberg, A. J., Tantawy, M. N., Hachey, B. C., Wadzinski, B. E., Spiller, B. W., Peterson, T. E., Paffenroth, K. C., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15060742 · Cited by 50
Longitudinal Analysis of Serum Copper and Ceruloplasmin in Alzheimer's Disease
Rembach, A., Doecke, J. D., Roberts, B. R., Watt, A. D., Faux, N. G., Volitakis, I., Pertile, K. K., Rumble, R. L., Trounson, B. O., Fowler, C. J., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121474 · Cited by 51
In vivo target bio-imaging of Alzheimer's disease by fluorescent zinc oxide nanoclusters
Lai, L., Zhao, C., Su, M., Li, X., Liu, X., Jiang, H., Amatore, C. A., & Wang, X. (2016) · Biomaterials Science · doi:10.1039/c6bm00233a · Cited by 50
Effects of Cu(II) on the aggregation of amyloid-β
Weibull, M. G. M., Simonsen, S., Oksbjerg, C. R., Tiwari, M. K., & Hemmingsen, L. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01727-5 · Cited by 52
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
Tangpong, J., Sompol, P. M., Vore, M. E., Clair, W. H. S., Butterfield, D. A., & Clair, D. K. S. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.046 · Cited by 50
Zheng, H., Youdim, M. B. H., & Fridkin, M. (2010) · ACS Chemical Neuroscience · doi:10.1021/cn100069c · Cited by 50
Pogocki, 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
Copper‐Binding Peptides Attenuate Microglia Inflammation through Suppression of NF‐kB Pathway
Caetano‐Silva, M. E., Rund, L. A., Vailati-Riboni, M., Pacheco, M. T. B., & Johnson, R. W. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202100153 · Cited by 49
Gómez, M., Esparza, J. L., Cabré, M., García, T. G., & Domingo, J. L. (2008) · Toxicology · doi:10.1016/j.tox.2008.05.004 · Cited by 49
Miura, T., Suzuki, K., & Takeuchi, H. (2001) · Journal of Molecular Structure · doi:10.1016/s0022-2860(01)00807-9 · Cited by 49
Increased expression of ferritin in cerebral cortex after human traumatic brain injury
Liu, H., Li, W., Chen, Z.-R., Zhou, M., Zhuang, Z., Zhang, D.-D., Zhu, L., & Hang, C. (2012) · Neurological Sciences · doi:10.1007/s10072-012-1214-7 · Cited by 49
Cerebral Amyloidosis: Postmortem Detection with Human 7.0-T MR Imaging System
van Rooden, S., Maat–Schieman, M. L. C., Nabuurs, R. J. A., van der Weerd, L., van Duijn, S., van Duinen, S. G., Natté, R., van Buchem, M. A., & van der Grond, J. (2009) · Radiology · doi:10.1148/radiol.2533090490 · 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
Interaction of amyloid β peptides with redox active heme cofactor: Relevance to Alzheimer's disease
Pramanik, D., Ghosh, C., Mukherjee, S., & Dey, S. G. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.02.025 · Cited by 50
Ex vivo T2 relaxation: associations with age-related neuropathology and cognition
Dawe, R. J., Bennett, D. A., Schneider, J. A., Leurgans, S. E., Kotrotsou, A., Boyle, P. A., & Arfanakis, K. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.144 · Cited by 50
pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide
Ghalebani, L., Wahlström, A., Danielsson, J., Wärmländer, S. K. T. S., & Gräslund, A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.043 · Cited by 48
Interdisciplinary challenges and promising theranostic effects of nanoscience in Alzheimer's disease
Laurent, S., Ejtehadi, M. R., Rezaei, M., Kehoe, P. G., & Mahmoudi, M. (2012) · RSC Advances · doi:10.1039/c2ra01374f · Cited by 51
Hofer, T., & Perry, G. L. (2016) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.06.005 · Cited by 49
Tripeptide GGH as the Inhibitor of Copper-Amyloid-β-Mediated Redox Reaction and Toxicity
Hu, X., Zhang, Q., Wang, W., Yuan, Z., Zhu, X., Chen, B., & Chen, X.-Y. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00145 · Cited by 49
Köseoğlu, E., Köşeoğlu, R., Kendirci, M., Saraymen, R., & Saraymen, B. (2016) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.09.002 · Cited by 49
Yu, Y., Yu, C., Yin, T., Ou, S., Sun, X., Wen, X., Zhang, L., Tang, D., & Yin, X. (2016) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2016.08.066 · Cited by 49
A novel fluorescent sensor based on imidazole derivative for Fe3+ ions
Kuzu, B., Tan, M., Ekmekci, Z., & Mengeş, N. (2017) · Journal of Luminescence · doi:10.1016/j.jlumin.2017.08.057 · Cited by 49
Serum and brain natural copper stable isotopes in a mouse model of Alzheimer’s disease
Moynier, F., Creech, J., Dallas, J., & Borgne, M. L. (2019) · Scientific Reports · doi:10.1038/s41598-019-47790-5 · Cited by 50
Ciccone, L., Tonali, N., Nencetti, S., & Orlandini, E. (2020) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2020.1760262 · Cited by 49
Fonte, J., Miklossy, J., Atwood, C., & Martins, R. N. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3206 · Cited by 49
Modulation of Fibrillogenesis of Amyloid β(1−40) Peptide with Cationic Gemini Surfactant
Cao, M., Han, Y., Wang, J., & Wang, Y. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp075271b · Cited by 49
Amyloid β and neuromelanin—Toxic or protective molecules?The cellular context makes the difference
Rao, K. S. J., Hegde, M. L., Anitha, S., Musicco, M., Zucca, F. A., TURRO, N. J., & Zecca, L. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.03.004 · Cited by 49
Uranga, R. M., & Salvador, G. A. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2850341 · Cited by 48
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
Role of Nanomedicine-Based Therapeutics in the Treatment of CNS Disorders
Guo, Z.-H., Khattak, S., Rauf, M. A., Ansari, M. A., Alomary, M. N., Razak, S., Yang, C., Wu, D., & Ji, X. (2023) · Molecules · doi:10.3390/molecules28031283 · Cited by 49
The effect of iron in MRI and transverse relaxation of amyloid‐beta plaques in Alzheimer's disease
Meadowcroft, M. D., Peters, D. G., Dewal, R. P., Connor, J. R., & Yang, Q. X. (2014) · NMR in Biomedicine · doi:10.1002/nbm.3247 · Cited by 48
Advances in Nanomedicine for the Treatment of Alzheimer’s and Parkinson’s Diseases
Hernando, S., Gartziandia, O., Herrán, E., Pedraz, J. L., Igartúa, M., & Hernández, R. M. (2016) · Nanomedicine · doi:10.2217/nnm-2016-0019 · Cited by 48
Zn2+ Aggravates Tau Aggregation and Neurotoxicity
Li, X., Du, X., & Ni, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030487 · Cited by 48
Kenward, A. G., Bartolotti, L. J., & Burns, C. (2007) · Biochemistry · doi:10.1021/bi602473r · Cited by 48
Blat, D., Weiner, L. M., Youdim, M. B. H., & Fridkin, M. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070800l · Cited by 49
Chen, Y., Han, K.-Y., & Liu, Y. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.04.016 · Cited by 48
Vicente-Zurdo, D., Rosales-Conrado, N., León-González, M. E., Brunetti, L., Piemontese, L., Pereira-Santos, A. R., Cardoso, S. M., Madrid, Y., Chaves, S., & Santos, M. A. (2022) · Biomedicines · doi:10.3390/biomedicines10071510 · Cited by 47
“In fact, more than two decades ago several studies revealed the accumulation of metal ions, such as Fe(II), Cu(II) and Zn(II), in amyloid aggregates [14].”
Backgroundvan Rooden, S., Doan, N. T., Versluis, M. J., Goos, J. D. C., WEBB, A. G., Oleksik, A. M., van der Flier, W. M., Scheltens, P., Barkhof, F., Weverling‐Rynsburger, A. W. E., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.07.006 · Cited by 47
Abduljabbar, T. N., Sharp, B. L., Reid, H. J., Barzegar-Befroei, N., Pető, T., & Lengyel, I. (2019) · Talanta · doi:10.1016/j.talanta.2019.05.098 · Cited by 49
Induction of cyclooxygenase-2 expression by manganese in cultured astrocytes
LIAO, S., OU, Y., Chen, S., CHIANG, A., & Chen, C. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.09.016 · 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
Revisiting the Role of Vitamins and Minerals in Alzheimer’s Disease
Shah, H., Dehghani, F., Ramezan, M., Gannaban, R. B., Haque, Z. F., Rahimi, F. C., Abbasi, S., & Shin, A. C. (2023) · Antioxidants · doi:10.3390/antiox12020415 · Cited by 48
Zhong, G., Wang, X., Li, J., Xie, Z., Wu, Q., Chen, J., Wang, Y., Chen, Z., Cao, X., Li, T., et al. (2023) · Current Neuropharmacology · doi:10.2174/1570159x22666231103085859 · Cited by 49
Recent Advances in Targeting Transition Metals (Copper, Iron, and Zinc) in Alzheimer’s Disease
Singh, R., Panghal, A., Jadhav, K., Thakur, A., Verma, R. K., Singh, C., Goyal, M., Kumar, J., & Namdeo, A. G. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04256-8 · Cited by 50
Cu(II) enhances the effect of Alzheimer’s amyloid-β peptide on microglial activation
Yu, F., Gong, P., Hu, Z., Qiu, Y. L., Cui, Y., Gao, X., Chen, H., & Li, J. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0343-3 · Cited by 47
Alzheimer's Disease: Another Target for Heparin Therapy
Bergamaschini, L. C., Rossi, E., Vergani, C., & Simoni, M. G. D. (2009) · The Scientific World JOURNAL · doi:10.1100/tsw.2009.100 · Cited by 46
Thermal aggregation of β-lactoglobulin in presence of metal ions
Navarra, G., Leone, M., & Militello, V. (2007) · Biophysical Chemistry · doi:10.1016/j.bpc.2007.09.003 · Cited by 47
Streltsov, V. A., Epa, V. C., James, S., Churches, Q. I., Caine, J. M., Kenche, V. B., & Barnham, K. J. (2013) · Chemical Communications · doi:10.1039/c3cc47326k · Cited by 46
Decreased serum zinc is an effect of ageing and not Alzheimer's disease
Rembach, A., Hare, D. J., Doecke, J. D., Burnham, S. C., Volitakis, I., Fowler, C. J., Cherny, R. A., McLean, C., Grimm, R., Martins, R. N., et al. (2014) · Metallomics · doi:10.1039/c4mt00060a · Cited by 46
Proteomics of Alzheimer’s disease: understanding mechanisms and seeking biomarkers
Lovestone, S., Güntert, A., Hye, A., Lynham, S., Thambisetty, M., & Ward, M. A. (2007) · Expert Review of Proteomics · doi:10.1586/14789450.4.2.227 · Cited by 46
Minniti, A. N., Rebolledo, D. L., Grez, P. M., Fadić, R., Aldunate, R., Volitakis, I., Cherny, R. A., Opazo, C., Masters, C. L., Bush, A. I., et al. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-2 · Cited by 46
Liu, L., Zhang, L., Niu, L., Xu, M., Mao, X., Yang, Y., & Wang, C. (2011) · ACS Nano · doi:10.1021/nn201773x · Cited by 46
Iron in neurodegenerative disorders: being in the wrong place at the wrong time?
Apostolakis, S., & Kypraiou, A.-M. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0020 · Cited by 47
β-Synuclein: An Enigmatic Protein with Diverse Functionality
Hayashi, J., & Carver, J. A. (2022) · Biomolecules · doi:10.3390/biom12010142 · Cited by 50
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
Compensatory responses induced by oxidative stress in Alzheimer disease
Moreira, P. I., Zhu, X., Liu, Q., Honda, K., Siedlak, S. L., Harris, P. L. R., Smith, M. A., & Perry, G. L. (2006) · Biological Research · doi:10.4067/s0716-97602006000100002 · Cited by 45
Lau, T., Gehman, J. D., Wade, J. D., Perez, K. A., Masters, C. L., Barnham, K. J., & Separovic, F. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.05.004 · Cited by 46
Lakatos, A., Zsigó, É., Hollender, D., May, N. V., Fülöp, L., Simon, D., Bozsó, Z., & Kiss, T. (2009) · Dalton Transactions · doi:10.1039/b916366b · Cited by 46
Iron in Alzheimer’s Disease: From Physiology to Disease Disabilities
Pal, A., Cerchiaro, G., Rani, I., Ventriglia, M., Rongioletti, M. C. A., Longobardi, A., & Squitti, R. (2022) · Biomolecules · doi:10.3390/biom12091248 · Cited by 49
The secret life of extracellular vesicles in metal homeostasis and neurodegeneration
Bellingham, S. A., Guo, B. B., & Hill, A. F. (2015) · Biology of the Cell · doi:10.1111/boc.201500030 · Cited by 45
Metallo-pathways to Alzheimer's disease: lessons from genetic disorders of copper trafficking
Greenough, M. A., Muñoz, A. R., Bush, A. I., & Opazo, C. (2016) · Metallomics · doi:10.1039/c6mt00095a · Cited by 45
Aggregation of Microtubule Binding Repeats of Tau Protein is Promoted by Cu2+
Ahmadi, S., Zhu, S., Sharma, R., Wu, B. H., Soong, R., Majumdar, R. D., Wilson, D. J., Simpson, A. J., & Kraatz, H. (2019) · ACS Omega · doi:10.1021/acsomega.8b03595 · Cited by 45
Teng, Y., Zhao, J., Ding, L., Ding, Y., & Zhou, P. (2019) · Molecules · doi:10.3390/molecules24162940 · Cited by 47
Zinc Binding to Tau Influences Aggregation Kinetics and Oligomer Distribution
Moreira, G. G., Cristóvão, J. S., Torres, V. M., Carapeto, A. P., Rodrigues, M. S., Landrieu, I., CORDEIRO, C. A., & Gomes, C. M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20235979 · Cited by 44
Sun, L., Sharma, A. K., Han, B.-H., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00376 · Cited by 46
Cheng, S. (2003) · Toxicology Letters · doi:10.1016/j.toxlet.2003.09.009 · Cited by 45
Glycosylated tetrahydrosalens as multifunctional molecules for Alzheimer's therapy
Storr, T., Scott, L. E., Bowen, M. L., Green, D. E., Thompson, K. H., Schugar, H. J., & Orvig, C. (2009) · Dalton Transactions · doi:10.1039/b902545f · Cited by 44
Differential alterations in antioxidant capacity in cells from Alzheimer patients
Gibson, G. E., Zhang, H., Sheu, K.-F. R., & Park, L. C. H. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00057-0 · Cited by 44
Shearer, J., Callan, P. E., Tran, T., & Szalai, V. A. (2010) · Chemical Communications · doi:10.1039/c0cc02446e · Cited by 44
Jiang, T., Wang, L., Zhang, S., Sun, P., Ding, C., Chu, Y., & Zhou, P. (2011) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2011.07.059 · 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
Aliès, B., Bijani, C., Sayen, S., Guillon, E., Faller, P., & Hureau, C. (2012) · Inorganic Chemistry · doi:10.1021/ic302097d · Cited by 44
Wang, Z., Zhang, Y., Zhang, W., Gao, H., Zhong, M., Huang, T., Guo, R., Liu, N., Li, D., Li, Y., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12502 · Cited by 44
The Molecular Dance of Fibronectin: Conformational Flexibility Leads to Functional Versatility
Mezzenga, R., & Mitsi, M. (2018) · Biomacromolecules · doi:10.1021/acs.biomac.8b01258 · Cited by 44
Wall, B. J., Will, M. F., Yawson, G. K., Bothwell, P. J., Platt, D. C., Apuzzo, C. F., Jones, M. A., Ferrence, G. M., & Webb, M. I. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00360 · Cited by 44
Huang, H., Hong, L., Chang, P., Zhang, J., Lu, S., Zheng, B.-W., & Jiang, Z.-F. (2014) · Neurotoxicity Research · doi:10.1007/s12640-014-9512-x · Cited by 44
Gene-Environment Interaction Research and Transgenic Mouse Models of Alzheimer's Disease (Erratum)
Chouliaras, L., Sierksma, A. S. R., Kenis, G., Prickaerts, J., Lemmens, M. A. M., Brasnjevic, I., van Donkelaar, E. L., Martínez‐Martínez, P., Losen, M. H., Baets, M. H. D., et al. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/356862 · Cited by 44
Differential profiles of copper-induced ROS generation in human neuroblastoma and astrocytoma cells
Qian, Y., Zheng, Y., Abraham, L., Ramos, K. S., & Tiffany‐Castiglioni, E. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.11.004 · Cited by 43
Molecular targeting of Alzheimer's amyloid plaques for contrast‐enhanced magnetic resonance imaging
Poduslo, J. F., Wengenack, T. M., Curran, G. L., Wısnıewskı, T., Sigurdsson, E. M., Macura, S. I., Borowski, B., & Jack, C. R. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.81.s1.20_5.x · Cited by 43
Sacco, C., Skowronsky, R. A., Gade, S., Kenney, J. M., & Spuches, A. M. (2012) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-012-0874-3 · Cited by 42
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
Baruch-Suchodolsky, R., & Fischer, B. (2008) · Biochemistry · doi:10.1021/bi800114g · Cited by 44
Rebolledo, D. L., Aldunate, R., Kohn, R., Neira, I., Minniti, A. N., & Inestrosa, N. C. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0336-11.2011 · Cited by 42
Metadata
- Authors
- Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R.
- Affiliations
- University of Kentucky (US)
- University of Guelph (CA)
- Venue
- Journal of the Neurological Sciences
- Publisher
- Elsevier BV
- Published
- 1998-06
- Volume
- 158
- Issue
- 1
- Pages
- 47-52
- ISSN
- 0022-510X (ISSN-L)
- OpenAlex
- W2083500052
- Cited by
- 2,120
- References
- 72
- Citations by year
- 2026: 38 · 2025: 52 · 2024: 69 · 2023: 82 · 2022: 100 · 2021: 92 · 2020: 95 · 2019: 103 · 2018: 80 · 2017: 94 · 2016: 87 · 2015: 82 · 2014: 89 · 2013: 96 · 2012: 116
- FWCI
- 18.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the Neurological Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (2-PO1-AG05119, P01AG005119, 5-P50 AG0514)
- 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 plaques, copper, iron, zinc, trace elements, amygdala, amyloid-beta aggregation, neuropil
- MeSH terms
- Alzheimer Disease, Amygdala, Copper, Humans, Iron, Spectrometry, X-Ray Emission, Zinc, Neuropil, Biotinylation, Plaque, Amyloid
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