The DOI matches its Crossref record; 258 of the 258 references it cites were found in a registry or an index.
The metal ion hypothesis of Alzheimer’s disease and the anti-neuroinflammatory effect of metal chelators
Abstract
Alzheimer's disease (AD), characterized by the β-amyloid protein (Aβ) deposition and tau hyperphosphorylation, is the most common dementia with uncertain etiology. The clinical trials of Aβ monoclonal antibody drugs have almost failed, giving rise to great attention on the other etiologic hypothesis regarding AD such as metal ions dysmetabolism and chronic neuroinflammation. Mounting evidence revealed that the metal ions (iron, copper, and zinc) were dysregulated in the susceptible brain regions of AD patients, which was highly associated with Aβ deposition, tau hyperphosphorylation, neuronal loss, as well as neuroinflammation. Further studies uncovered that iron, copper and zinc could not only enhance the production of Aβ but also directly bind to Aβ and tau to promote their aggregations. In addition, the accumulation of iron and copper could respectively promote ferroptosis and cuproptosis. Therefore, the metal ion chelators were recognized as promising agents for treating AD. This review comprehensively summarized the effects of metal ions on the Aβ dynamics and tau phosphorylation in the progression of AD. Furthermore, taking chronic neuroinflammation contributes to the progression of AD, we also provided a summary of the mechanisms concerning metal ions on neuroinflammation and highlighted the metal ion chelators may be potential agents to alleviate neuroinflammation under the condition of AD. Nevertheless, more investigations regarding metal ions on neuroinflammation should be taken into practice, and the effects of metal ion chelators on neuroinflammation should gain more attention. Running title: Metal chelators against neuroinflammation.
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
“This hypothesis suggests that metal dyshomeostasis can lead to oxidative stress, which is linked to various pathological events in AD, such as amyloidosis and tauopathy.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [21]
In the citing paper
“The metal ion hypothesis examines the dysregulation of metal ions, particularly copper, zinc, and iron, which plays a significant role in the pathogenesis of AD.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [21]
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedNIA‐AA Research Framework: Toward a biological definition of Alzheimer's disease
Jack, C. R., Bennett, D. A., Blennow, K., Carrillo, M. C., Dunn, B., Haeberlein, S. B., Holtzman, D. M., Jagust, W., Jessen, F., Karlawish, J., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.02.018 · Cited by 10,537
Neurotoxic reactive astrocytes are induced by activated microglia
Liddelow, S. A., Guttenplan, K. A., Clarke, L. E., Bennett, F. C., Bohlen, C. J., Schirmer, L., Bennett, M. L., Münch, A. E., Chung, W.-S., Peterson, T. C., et al. (2017) · Nature · doi:10.1038/nature21029 · Cited by 7,971
Neuroinflammation in Alzheimer's disease
Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226
Astrocyte-endothelial interactions at the blood-brain barrier
Abbott, N. J., Rönnbäck, L., & Hansson, E. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1824 · Cited by 5,595
A Unique Microglia Type Associated with Restricting Development of Alzheimer’s Disease
Keren-Shaul, H., Spinrad, A., Weiner, A., Matcovitch-Natan, O., Dvir-Szternfeld, R., Ulland, T. K., David, E., Baruch, K., Lara-Astaiso, D., Toth, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.018 · Cited by 5,493
Copper induces cell death by targeting lipoylated TCA cycle proteins
Tsvetkov, P., Coy, S., Petrova, B., Dreishpoon, M., Verma, A., Abdusamad, M., Rossen, J., Joesch-Cohen, L., Humeidi, R., Spangler, R. D., et al. (2022) · Science · doi:10.1126/science.abf0529 · Cited by 4,932
Phases of Aβ-deposition in the human brain and its relevance for the development of AD
Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490
FSP1 is a glutathione-independent ferroptosis suppressor
Doll, S., Freitas, F. P., Shah, R., Aldrovandi, M., da Silva, M. C., Ingold, I., Goya Grocin, A., Xavier da Silva, T. N., Panzilius, E., Scheel, C. H., et al. (2019) · Nature · doi:10.1038/s41586-019-1707-0 · Cited by 3,341
Neuroinflammation and microglial activation in Alzheimer disease: where do we go from here?
Leng, F., & Edison, P. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-020-00435-y · Cited by 3,179
The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease
Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059
Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis
Yang, W. S., Kim, K. J., Gaschler, M. M., Patel, M., Shchepinov, M. S., & Stockwell, B. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603244113 · Cited by 2,329
Bloom (2014) · doi:10.1001/jamaneurol.2013.5847 · Cited by 2,194
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
Alpha-lipoic acid as a biological antioxidant
Packer, L., Witt, E. H., & Tritschler, H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00017-r · Cited by 1,995
Neuroinflammation in Alzheimer's disease: current evidence and future directions
Calsolaro, V., & Edison, P. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.02.010 · Cited by 1,726
Microglia in neurodegeneration
Hickman, S., Izzy, S., Sen, P., Morsett, L., & El Khoury, J. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0242-x · Cited by 1,710
Role of GPX4 in ferroptosis and its pharmacological implication
Seibt, T. M., Proneth, B., & Conrad, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.014 · Cited by 1,520
NLRP3 inflammasome activation drives tau pathology
Ising, C., Venegas, C., Zhang, S., Scheiblich, H., Schmidt, S. V., Vieira-Saecker, A., Schwartz, S., Albasset, S., McManus, R. M., Tejera, D., et al. (2019) · Nature · doi:10.1038/s41586-019-1769-z · Cited by 1,487
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
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Two Randomized Phase 3 Studies of Aducanumab in Early Alzheimer's Disease
Budd Haeberlein, S., Aisen, P. S., Barkhof, F., Chalkias, S., Chen, T., Cohen, S., Dent, G., Hansson, O., Harrison, K., von Hehn, C., et al. (2022) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2022.30 · Cited by 1,367
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
Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188
EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
Bieschke, J., Russ, J., Friedrich, R. P., Ehrnhoefer, D. E., Wobst, H. J., Neugebauer, K., & Wanker, E. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910723107 · Cited by 1,044
Simpson, D. S. A., & Oliver, P. L. (2020) · Antioxidants · doi:10.3390/antiox9080743 · Cited by 1,044
Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988
Sala Frigerio, C., Wolfs, L., Fattorelli, N., Thrupp, N., Voytyuk, I., Schmidt, I., Mancuso, R., Chen, W.-T., Woodbury, M. E., Srivastava, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.099 · Cited by 926
Microglia-mediated neuroinflammation in neurodegenerative diseases
Subhramanyam, C. S., Wang, C., Hu, Q., & Dheen, S. T. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.004 · Cited by 897
López, J. A., González, H. M., & Léger, G. C. (2019) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804766-8.00013-3 · Cited by 887
Glutathione: new roles in redox signaling for an old antioxidant
Aquilano, K., Baldelli, S., & Ciriolo, M. R. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00196 · Cited by 869
Zinc in Infection and Inflammation
Gammoh, N. Z., & Rink, L. (2017) · Nutrients · doi:10.3390/nu9060624 · Cited by 861
The pathological process underlying Alzheimer’s disease in individuals under thirty
Braak, H., & Del Tredici, K. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0789-4 · Cited by 812
Intramuscular desferrioxamine in patients with Alzheimer's disease
MCLACHLAN, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)92978-b · Cited by 764
Lannfelt, L., Blennow, K., Zetterberg, H., Batsman, S., Ames, D., Harrison, J., Masters, C. L., Targum, S., Bush, A. I., Murdoch, R., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70167-4 · Cited by 725
Mechanism of intranasal drug delivery directly to the brain
Crowe, T. P., Greenlee, M. H. W., Kanthasamy, A. G., & Hsu, W. H. (2018) · Life Sciences · doi:10.1016/j.lfs.2017.12.025 · Cited by 721
Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686
Loss of ferroportin induces memory impairment by promoting ferroptosis in Alzheimer’s disease
Bao, W.-D., Pang, P., Zhou, X.-T., Hu, F., Xiong, W., Chen, K., Wang, J., Wang, F., Xie, D., Ya⁃zhuo, H. U., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00685-9 · Cited by 682
Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., Volitakis, I., Liu, X., Smith, J. P., Perez, K., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.018 · Cited by 672
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
Mogi, M., Harada, M., Narabayashi, H., Inagaki, H., Minami, M., & Nagatsu, T. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)12706-3 · Cited by 545
Chandran, B., & Goel, A. (2012) · Phytotherapy Research · doi:10.1002/ptr.4639 · Cited by 527
Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526
Zinc is an Antioxidant and Anti-Inflammatory Agent: Its Role in Human Health
Prasad, A. S. (2014) · Frontiers in Nutrition · doi:10.3389/fnut.2014.00014 · Cited by 523
Activation of microglia and astrocytes: a roadway to neuroinflammation and Alzheimer’s disease
Kaur, D., Sharma, V., & Deshmukh, R. R. (2019) · Inflammopharmacology · doi:10.1007/s10787-019-00580-x · Cited by 503
Metal Toxicity Links to Alzheimer's Disease and Neuroinflammation
Huat, T. J., Camats‐Perna, J., Newcombe, E. A., Valmas, N., Kitazawa, M., & Medeiros, R. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.01.018 · Cited by 501
Microglial activation and tau propagate jointly across Braak stages
Pascoal, T. A., Benedet, A. L., Ashton, N. J., Kang, M. S., Therriault, J., Chamoun, M., Savard, M., Lussier, F. Z., Tissot, C., Karikari, T. K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01456-w · Cited by 490
Zhang, J., Zheng, Y., Luo, Y., Du, Y., Zhang, X., & Fu, J. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.09.020 · Cited by 464
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
Current understanding of metal ions in the pathogenesis of Alzheimer’s disease
Wang, L., Yin, Y.-L., Liu, X.-Z., Shen, P., Zheng, Y.-G., Lan, X.-R., Lu, C.-B., & Wang, J.-Z. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00189-z · Cited by 454
TLR2 Is a Primary Receptor for Alzheimer’s Amyloid β Peptide To Trigger Neuroinflammatory Activation
Liu, S., Liu, Y., Hao, W., Wolf, L., Kiliaan, A. J., Penke, B., Rübe, C. E., Walter, J., Heneka, M. T., Hartmann, T., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1101121 · Cited by 439
Hepatotoxicity of high oral dose (−)-epigallocatechin-3-gallate in mice
Lambert, J. D., Kennett, M. J., Sang, S., Reuhl, K. R., Ju, J., & Yang, C. S. (2009) · Food and Chemical Toxicology · doi:10.1016/j.fct.2009.10.030 · Cited by 436
Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β
Nussbaum, J. M., Schilling, S., Cynis, H., Silva, A., Swanson, E., Wangsanut, T., Tayler, K., Wiltgen, B., Hatami, A., Rönicke, R., et al. (2012) · Nature · doi:10.1038/nature11060 · Cited by 427
PBT2 Rapidly Improves Cognition in Alzheimer's Disease: Additional Phase II Analyses
Faux, N. G., Ritchie, C. W., Gunn, A. P., Rembach, A., Tsatsanis, A., Bedő, J., Harrison, J., Lannfelt, L., Blennow, K., Zetterberg, H., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1390 · Cited by 406
Redox-active iron mediates amyloid-β toxicity
Rottkamp, C. A., Raina, A. K., Zhu, X., Gaier, E., Bush, A. I., Atwood, C., Chevion, M., Perry, G. L., & Smith, M. A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00494-9 · Cited by 379
Metal Ions in Alzheimer’s Disease: A Key Role or Not?
Liu, Y., Nguyen, M., Robert, A., & Meunier, B. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.9b00248 · Cited by 353
The clinical promise of biomarkers of synapse damage or loss in Alzheimer’s disease
the Synaptic Health Endpoints Working Group, Colom-Cadena, M., Spires-Jones, T., Zetterberg, H., Blennow, K., Caggiano, A., DeKosky, S. T., Fillit, H., Harrison, J. E., Schneider, L. S., et al. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00588-4 · Cited by 328
Astrocytic interleukin-3 programs microglia and limits Alzheimer’s disease
McAlpine, C. S., Park, J., Griciuc, A., Kim, E., Choi, S. H., Iwamoto, Y., Kiss, M. G., Christie, K. A., Vinegoni, C., Poller, W. C., et al. (2021) · Nature · doi:10.1038/s41586-021-03734-6 · Cited by 322
Role of metal dyshomeostasis in Alzheimer's disease
Bonda, D., Lee, H., Blair, J. A., Zhu, X., Perry, G. L., & Smith, M. A. (2011) · Metallomics · doi:10.1039/c0mt00074d · Cited by 316
Tau Protein Is Required for Amyloid β-Induced Impairment of Hippocampal Long-Term Potentiation
Shipton, O. A., Leitz, J. R., Dworzak, J., Acton, C. E. J., Tunbridge, E. M., Denk, F., Dawson, H. N., Vitek, M. P., Wade-Martins, R., Paulsen, O., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2610-10.2011 · Cited by 315
Zhang, Y., Wang, D., Xu, S., Zhang, S., Fan, Y., Yang, Y., Guo, S., Wang, S., Guo, T., Wang, Z., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.001 · Cited by 312
Self-citationMechanisms of Brain Iron Transport: Insight into Neurodegeneration and CNS Disorders
Mills, E., Dong, X.-P., Wang, F., & Xu, H. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.09.140 · Cited by 309
Dhillon, S. (2021) · Drugs · doi:10.1007/s40265-021-01569-z · Cited by 293
Shinto, L., Quinn, J., Montine, T., Dodge, H. H., Woodward, W., Baldauf-Wagner, S., Waichunas, D., Bumgarner, L., Bourdette, D., Silbert, L., et al. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-130722 · Cited by 288
“Is dopamine involved in Alzheimer's disease?”
Martorana, A., & Koch, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00252 · Cited by 276
Elevated cortical zinc in Alzheimer disease
Religa, D., Strozyk, D., Cherny, R. A., Volitakis, I., Haroutunian, V., Winblad, B. G., Näslund, J., & Bush, A. I. (2006) · Neurology · doi:10.1212/01.wnl.0000223644.08653.b5 · Cited by 273
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
Rajan, K. B., Weuve, J., Barnes, L. L., Wilson, R. S., & Evans, D. A. (2019) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.07.216 · Cited by 245
Zhou, Z., & Tan, E. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0218-4 · Cited by 241
Davis, M. R., O`Connell, T., Johnson, S., Cline, S. K., Merikle, E. P., Martényi, F., & Simpson, K. N. (2018) · Current Alzheimer Research · doi:10.2174/1567205015666180119092427 · Cited by 241
Immune hyperreactivity of Aβ plaque-associated microglia in Alzheimer's disease
Yin, Z., Raj, D., Saiepour, N., Van Dam, D., Brouwer, N., Holtman, I. R., Eggen, B. J. L., Möller, T., Tamm, J. A., Abdourahman, A., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.03.021 · Cited by 238
Wang, C., Zhang, X., Teng, Z., Zhang, T., & Li, Y. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.06.051 · Cited by 233
Trinder, D., Oates, P. S., Thomas, C., Sadleir, J., & Morgan, E. H. (2000) · Gut · doi:10.1136/gut.46.2.270 · Cited by 231
Yu, H., Yang, C., Lei, J., Guo, S., Chen, R., Li, K., Qu, F., Tao, K. X., Fu, Y., Luo, F., et al. (2019) · Oncology Reports · doi:10.3892/or.2019.7189 · Cited by 225
Robert, A., Liu, Y., Nguyen, M., & Meunier, B. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00119 · Cited by 212
Microglia: Multitasking Specialists of the Brain
Casano, A. M., & Peri, F. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.018 · Cited by 209
Protective role of microglial HO-1 blockade in aging: Implication of iron metabolism
Fernández‐Mendívil, C., Luengo, E., Trigo-Alonso, P., García‐Magro, N., Negredo, P., & López, M. G. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101789 · Cited by 202
Guo, C., Wang, T., Zheng, W. H., Shan, Z., Teng, W., & Wang, Z. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.05.009 · Cited by 200
Self-citationSarell, C. J., Wilkinson, S. R., & Viles, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.171355 · Cited by 199
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
Inflammation-induced iron transport and metabolism by brain microglia
McCarthy, R. C., Sosa, J. C., Gardeck, A. M., Baez, A. S., Lee, C., & Wessling‐Resnick, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001949 · Cited by 193
Shearer, J., & Szalai, V. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805940m · Cited by 191
Three Histidine Residues of Amyloid-β Peptide Control the Redox Activity of Copper and Iron
Nakamura, M., Shishido, N., Nunomura, A., Smith, M. A., Perry, G. L., Hayashi, Y., Nakayama, K., & Hayashi, T. (2007) · Biochemistry · doi:10.1021/bi701079z · Cited by 184
Iron loading is a prominent feature of activated microglia in Alzheimer’s disease patients
Kenkhuis, B., Somarakis, A., de Haan, L., Dzyubachyk, O., IJsselsteijn, M. E., de Miranda, N. F. C. C., Lelieveldt, B. P. F., Dijkstra, J., van Roon-Mom, W. M. C., Höllt, T., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01126-5 · Cited by 184
Phase II trial of tetrathiomolybdate in patients with advanced kidney cancer.
Redman, B. G., Esper, P., Pan, Q., Dunn, R. L., Hussain, H. K., Chenevert, T. L., Brewer, G. J., & Merajver, S. D. (2003) · PubMed · Cited by 178
Meadowcroft, M. D., Connor, J. R., Smith, M. B., & Yang, Q. X. (2009) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.21731 · Cited by 176
Atrián‐Blasco, E., Gonzalez, P., Santoro, A., Aliès, B., Faller, P., & Hureau, C. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.007 · Cited by 175
Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains
Danscher, G., Jensen, K. B., Frederickson, C. J., Kemp, K., Andreasen, A., Juhl, S., Stoltenberg, M., & Ravid, R. (1997) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(97)00079-4 · Cited by 174
Zinc Triggers Microglial Activation
Kauppinen, T. M., Higashi, Y., Suh, S. W., Escartin, C., Nagasawa, K., & Swanson, R. A. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.1236-08.2008 · Cited by 174
The Zinc Dyshomeostasis Hypothesis of Alzheimer's Disease
Craddock, T. J. A., Tuszyński, J. A., Chopra, D., Casey, N. F., Goldstein, L. E., Hameroff, S. R., & Tanzi, R. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033552 · Cited by 172
Weiss, K. H., Askari, F. K., Członkowska, A., Ferenci, P., Bronstein, J. M., Bega, D., Ala, A., Nicholl, D. J., Flint, S., Olsson, L., et al. (2017) · The Lancet. Gastroenterology & hepatology · doi:10.1016/s2468-1253(17)30293-5 · Cited by 172
Cortical iron reflects severity of Alzheimer's disease
van Duijn, S., Bulk, M., van Duinen, S. G., Nabuurs, R. J. A., van Buchem, M. A., van der Weerd, L., & Natté, R. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161143 · Cited by 172
Copper induces microglia-mediated neuroinflammation through ROS/NF-κB pathway and mitophagy disorder
Zhou, Q., Zhang, Y., Lu, L., Zhang, H., Zhao, C., Pu, Y., & Yin, L. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113369 · Cited by 172
Wan, W., Cao, L., Liu, L., Zhang, C., Kalionis, B., Tai, X., Li, Y., & Xia, S. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13122 · Cited by 170
Li, L., Li, W., Zheng, X., Liu, Q., Du, Q., Lai, Y., & Liu, S. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00442-3 · Cited by 164
Fasae, K. D., Abolaji, A. O., Faloye, T. R., Odunsi, A., Oyetayo, B. O., Enya, J. I., Rotimi, J. A., Akinyemi, R., Whitworth, A. J., & Aschner, M. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126779 · Cited by 161
Cellular iron status influences the functional relationship between microglia and oligodendrocytes
Zhang, X., Surguladze, N., Slagle‐Webb, B., Cozzi, A., & Connor, J. R. (2006) · Glia · doi:10.1002/glia.20416 · Cited by 160
Serrano-Pozo, A., William, C. M., Ferrer, I., Uro-Coste, E., Delisle, M.-B., Maurage, C.-A., Hock, C., Nitsch, R. M., Masliah, E., Growdon, J. H., et al. (2010) · Brain · doi:10.1093/brain/awq056 · Cited by 159
Wang, Z., Jackson, R. J., Hong, W., Taylor, W. M., Corbett, G. T., Moreno, A. J., Liu, W., Li, S., Frosch, M. P., Slutsky, I., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2009-17.2017 · Cited by 157
Self-citationZeineh, M. M., Chen, Y., Kitzler, H. H., Hammond, R., Vogel, H., & Rutt, B. K. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.05.022 · Cited by 151
Collingwood, J. F., Chong, R. K. K., Kasama, T., Cervera-Gontard, L., Dunin-Borkowski, R. E., Perry, G., Pósfai, M., Siedlak, S. L., Simpson, E. T., Smith, M. A., et al. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-14211 · Cited by 147
Cellular, Synaptic and Network Effects of Acetylcholine in the Neocortex
Colangelo, C., Shichkova, P., Keller, D. X., Markram, H., & Ramaswamy, S. (2019) · Frontiers in Neural Circuits · doi:10.3389/fncir.2019.00024 · Cited by 143
Lee, M., Yu, W., Shih, Y., Chen, C., Guo, Z., Huang, S., Chan, J. C. C., & Chen, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-23122-x · Cited by 141
Janocko, N. J., Brodersen, K. A., Soto-Ortolaza, A., Ross, O., Liesinger, A. M., Duara, R., Graff-Radford, N., Dickson, D., & Murray, M. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1044-y · Cited by 138
James, S., Churches, Q. I., de Jonge, M. D., Birchall, I. E., Streltsov, V. A., McColl, G., Adlard, P. A., & Hare, D. J. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00362 · Cited by 136
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
Mitchell, C. J., Shawki, A., Ganz, T., Nemeth, E., & Mackenzie, B. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00348.2013 · Cited by 132
Iron homeostasis in astrocytes and microglia is differentially regulated by TNF‐α and TGF‐β1
Rathore, K. I., Redensek, A., & David, S. (2012) · Glia · doi:10.1002/glia.22303 · Cited by 130
Golgi fragmentation in Alzheimer's disease
Joshi, G. S., Bekier, M. E., & Wang, Y. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00340 · Cited by 129
Copper Exposure Perturbs Brain Inflammatory Responses and Impairs Clearance of Amyloid-Beta
Kitazawa, M., Hsu, H.-W., & Medeiros, R. (2016) · Toxicological Sciences · doi:10.1093/toxsci/kfw081 · Cited by 129
LRP1 modulates the microglial immune response via regulation of JNK and NF‐ΚB signaling pathways
Yang, L., Liu, C.-C., Zheng, H., Kanekiyo, T., Atagi, Y., Jia, L., Wang, D., N’songo, A., Can, D., Xu, H., et al. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0772-7 · Cited by 129
Zhong, X., Liu, M., Yao, W., Du, K., He, M., Jin, X., Jiao, L., Ma, G., Wei, B., & Wei, M. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201801230 · Cited by 129
Developing Effective Alzheimer’s Disease Therapies: Clinical Experience and Future Directions
Elmaleh, D. R., Farlow, M. R., Conti, P. S., Tompkins, R. G., Kundakovic, L., & Tanzi, R. E. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190507 · Cited by 129
Metal protein attenuating compounds for the treatment of Alzheimer's dementia
Sampson, E. L., Jenagaratnam, L., & McShane, R. H. (2014) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd005380.pub5 · Cited by 128
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
Up-regulation of divalent metal transporter 1 in 6-hydroxydopamine intoxication is IRE/IRP dependent
Jiang, H. F., Song, N., Xu, H., Zhang, S., Wang, J., & Xie, J. (2010) · Cell Research · doi:10.1038/cr.2010.20 · Cited by 121
Li, Y., Pan, K., Chen, L. V., Ning, J.-L., Li, X., Yang, T., Terrando, N., Gu, J., & Tao, G. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0740-2 · Cited by 116
Self-citationMaloney, B., & Lahiri, D. K. (2011) · Gene · doi:10.1016/j.gene.2011.06.004 · Cited by 112
Cu2+ Affects Amyloid-β (1–42) Aggregation by Increasing Peptide-Peptide Binding Forces
Hane, F. T., Tran, G., Attwood, S. J., & Leonenko, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059005 · Cited by 111
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
Nair, N. G., Perry, G. L., Smith, M. A., & Reddy, V. P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1346 · Cited by 109
Chiou, B., Neal, E. H., Bowman, A. B., Lippmann, E. S., Simpson, I. A., & Connor, J. R. (2018) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x18783372 · Cited by 108
Untangling Tau and Iron: Exploring the Interaction Between Iron and Tau in Neurodegeneration
Rao, S. S., & Adlard, P. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00276 · Cited by 108
Benchekroun, M., Romero, A., Egea, J., Leon, R. M., Michalska, P., Buendía, I., Jimeno, M. L., Jun, D., Janočková, J., Šepsová, V., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01178 · Cited by 107
Hughes, C., Choi, M. L., Yi, J.-H., Kim, S.-C., Drews, A., George-Hyslop, P. S., Bryant, C., Gandhi, S., Cho, K., & Klenerman, D. (2020) · Communications Biology · doi:10.1038/s42003-020-0792-9 · Cited by 107
Rong, S., Wan, D., Fan, Y., Liu, S., Sun, K., Huo, J., Zhang, P., Li, X., Xie, X., Wang, F., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00856 · Cited by 106
Self-citationTransport and diffusion of Tau protein in neurons
Scholz, T., & Mandelkow�, E. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1610-7 · Cited by 105
Protection against amyloid beta peptide toxicity by zinc
Lovell, M. A., Xie, C., & Markesbery, W. R. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01114-2 · Cited by 104
Brain uptake of trace metals, zinc and manganese, in rats
Takeda, A., Akiyama, T. H., Sawashita, J., & Okada, S. (1994) · Brain Research · doi:10.1016/0006-8993(94)91891-0 · Cited by 101
Antioxidant Berberine-Derivative Inhibits Multifaceted Amyloid Toxicity
Rajasekhar, K., Samanta, S., Bagoband, V., Murugan, N. A., & Govindaraju, T. (2020) · iScience · doi:10.1016/j.isci.2020.101005 · Cited by 100
Zheng, K.-M., Dai, X., Xiao, N., Wu, X., Wei, Z., Fang, W., Zhu, Y., Zhang, J., & Chen, X. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9802-9 · Cited by 96
He, Y., Cui, J., Lee, J. C., Ding, S., Chalimoniuk, M., Simonyi, Á., Sun, A. Y., Gu, Z., Weisman, G. A., Wood, W. G., et al. (2011) · ASN NEURO · doi:10.1042/an20100025 · Cited by 95
Szabo, S. T., Harry, G. J., Hayden, K. M., Szabo, D. T., & Birnbaum, L. S. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv325 · Cited by 94
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
Self-citationFilamentous recombinant human Tau activates primary astrocytes via an integrin receptor complex
Wang, P., & Ye, Y. (2021) · Nature Communications · doi:10.1038/s41467-020-20322-w · Cited by 93
Khan, A., Dobson, J., & Exley, C. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.013 · Cited by 91
Activation of the NLRP3 inflammasome by cellular labile iron
Nakamura, K., Kawakami, T., Yamamoto, N., Tomizawa, M., Fujiwara, T., Ishii, T., Harigae, H., & Ogasawara, K. (2015) · Experimental Hematology · doi:10.1016/j.exphem.2015.11.002 · Cited by 89
Gerber, H., Wu, F., Dimitrov, M. I., Osuna, G. M. G., & Fraering, P. C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.754101 · Cited by 89
Squitti, R., Ventriglia, M., Simonelli, I., Bonvicini, C., Costa, A. C., Perini, G., Binetti, G. G., Benussi, L., Ghidoni, R., Koch, G., et al. (2021) · Biomolecules · doi:10.3390/biom11070960 · Cited by 84
Copper reduction by copper binding proteins and its relation to neurodegenerative diseases
Opazo, C., Barría, M. I., Ruiz, F. H., & Inestrosa, N. C. (2003) · BioMetals · doi:10.1023/a:1020795422185 · Cited by 83
Dias, K. S. T., de Paula, C. T., dos Santos, T., Souza, I. N. D. O., Boni, M. S., Guimarães, M. J. R., da Silva, F. M. R., Castro, N. G., Neves, G. A., Veloso, C. C., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.02.043 · Cited by 83
Cheignon, C., Faller, P., Testemale, D., Hureau, C., & Collin, F. (2016) · Metallomics · doi:10.1039/c6mt00150e · Cited by 81
Hu, Z., Yu, F., Gong, P., Qiu, Y. L., Zhou, W., Cui, Y., Li, J., & Chen, H. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.01.020 · Cited by 79
SFRP1 modulates astrocyte-to-microglia crosstalk in acute and chronic neuroinflammation
Rueda‐Carrasco, J., Martín‐Bermejo, M. J., Pereyra, G., Mateo, M. I., Borroto, A., Brosseron, F., Kummer, M. P., Schwartz, S., López‐Atalaya, J. P., Alarcón, B., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051696 · Cited by 79
Lan, J., Xie, S., Li, S., Pan, L.-F., Wang, X., & Kong, L. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.08.035 · Cited by 77
Lu, J. L., Wu, D., Zheng, Y., Sun, D., Hu, B., Shan, Q., Zhang, Z.-F., & Fan, S. (2008) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2008.09.003 · Cited by 77
Fe2+binding on amyloid β-peptide promotes aggregation
Boopathi, S., & Kolandaivel, P. (2016) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25075 · Cited by 75
Young, T. R., Kirchner, A., Wedd, A. G., & Xiao, Z. (2014) · Metallomics · doi:10.1039/c4mt00001c · Cited by 74
CSF soluble TREM2 as a measure of immune response along the Alzheimer's disease continuum
Rauchmann, B., Schneider-Axmann, T., Alexopoulos, P., & Perneczky, R. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.10.022 · Cited by 74
Zhang, Y., & He, M. (2017) · Brain Research · doi:10.1016/j.brainres.2017.09.019 · Cited by 71
Hybrid Multifunctional Modulators Inhibit Multifaceted Aβ Toxicity and Prevent Mitochondrial Damage
Rajasekhar, K., Mehta, K., & Govindaraju, T. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00033 · Cited by 69
Prasanthi, J. R. P., Schrag, M., Dasari, B., Marwarha, G., Dickson, A., Kirsch, W. M., & Ghribi, O. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111346 · Cited by 68
Copper deficiency elicits glial and neuronal response typical of neurodegenerative disorders
Zucconi, G. G., Cipriani, S., Scattoni, R., Balgkouranidou, I., Hawkins, D. P., & Ragnarsdottir, K. V. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00793.x · Cited by 67
Sakakibara, Y., Sekiya, M., Saito, T., Saido, T. C., & Iijima, K. M. (2019) · BMC Neuroscience · doi:10.1186/s12868-019-0496-6 · Cited by 65
Huy, P. D. Q., Vuong, V., Penna, G. L., Faller, P., & Li, M. S. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00109 · Cited by 64
Influence of extracellular zinc on M1 microglial activation
Higashi, Y., Aratake, T., Shimizu, S., Shimizu, T., Nakamura, K., Tsuda, M., Yawata, T., Ueba, T., & Saito, M. (2017) · Scientific Reports · doi:10.1038/srep43778 · Cited by 64
Wärmländer, S. K. T. S., Österlund, N., Wallin, C., Wu, J., Luo, J., Tiiman, A., Jarvet, J., & Gräslund, A. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01723-9 · Cited by 64
Role of Neuron and Glia in Alzheimer’s Disease and Associated Vascular Dysfunction
Bandyopadhyay, S. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.653334 · Cited by 64
Li, X., Lei, P., Tuo, Q., Ayton, S., Li, Q., Moon, S., Volitakis, I., Liu, R., Masters, C. L., Finkelstein, D. I., et al. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0378-2 · Cited by 63
Kleven, M. D., Dlakić, M., & Lawrence, C. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664565 · Cited by 63
A20 deficiency causes spontaneous neuroinflammation in mice
Guedes, R. P., Csizmadia, E., Moll, H. P., Ma, A. I., Ferran, C. J., & da Silva, C. G. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-122 · Cited by 63
Mild Cognitive Impairment and Alzheimer Patients Display Different Levels of Redox-Active CSF Iron
Manuel Lavados, M., Guillón, M., Mujica, M. C., Rojo, L. E., Fuentes, P., & Maccioni, R. B. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13211 · Cited by 61
Patel, T., Carnwath, T., Wang, X., Allen, M., Lincoln, S., Lewis‐Tuffin, L. J., Quicksall, Z., Lin, S., Tutor‐New, F. Q., Ho, C. C. G., et al. (2022) · Aging Cell · doi:10.1111/acel.13606 · Cited by 61
Wang, T., Wang, C., Shan, Z., Teng, W., & Wang, Z. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111874 · Cited by 60
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
Time-Dependent DNA Condensation Induced by Amyloid β-Peptide
Yu, H., Ren, J., & Qu, X. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.093559 · Cited by 60
Cornejo, F., Vruwink, M., Metz, C., Muñoz, P., Salgado, N., Poblete, J., Andrés, M. E., Eugenín, J., & von Bernhardi, R. (2018) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2017.12.007 · Cited by 59
Samanta, S., Rajasekhar, K., Babagond, V., & Govindaraju, T. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00216 · Cited by 59
Hongxia, L., Yuxiao, T., Zhilei, S., Yan, S., Qu, Y., Jiamin, S., Xin, X., Yang, J., Mo, F., & Shen, H. (2019) · Journal of Affective Disorders · doi:10.1016/j.jad.2019.02.041 · Cited by 56
Ji, S., Medvedeva, Y. V., & Weiss, J. H. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.113161 · Cited by 56
Iron potentiates microglial interleukin‐1β secretion induced by amyloid‐β
Nnah, I. C., Lee, C., & Wessling‐Resnick, M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14906 · Cited by 54
Takeda, A., Tamano, H., Tempaku, M., Sasaki, M., Uematsu, C., Sato, S., Kanazawa, H., Datki, Z., Adlard, P. A., & Bush, A. I. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.0954-17.2017 · Cited by 53
Squitti, R. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.06.018 · Cited by 52
Banerjee, P., Sahoo, A., Anand, S., Ganguly, A., Righi, G., Bovicelli, P., Saso, L., & Chakrabarti, S. (2014) · NeuroMolecular Medicine · doi:10.1007/s12017-014-8328-4 · Cited by 52
Kou, J., Wang, M., Shi, J., Zhang, H., Pu, X., Song, S., Yang, C., Yan, Y., Döring, Y., Xie, X., et al. (2021) · ACS Omega · doi:10.1021/acsomega.0c04810 · Cited by 52
Meadowcroft, M. D., Connor, J. R., & Yang, Q. X. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00255 · Cited by 51
Regulatory mechanisms for iron transport across the blood-brain barrier
Duck, K. A., Simpson, I. A., & Connor, J. R. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.10.083 · Cited by 51
Binding and Reactivity of Copper to R1 and R3 Fragments of tau Protein
Bacchella, C., Gentili, S., Bellotti, D., Quartieri, E., Draghi, S., Baratto, M. C., Remelli, M., Valensin, D., Monzani, E., Nicolis, S., et al. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b02266 · Cited by 51
Dinicola, S., Proietti, S., Cucina, A., Bizzarri, M., & Fuso, A. (2017) · Antioxidants · doi:10.3390/antiox6040074 · Cited by 50
Zinc Exacerbates Tau Pathology in a Tau Mouse Model
Craven, K. M., Kochen, W. R., Hernández, C. M., & Flinn, J. M. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180151 · Cited by 50
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
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
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
Calvaruso, G., Vitrano, A., Maggio, R. D., Lai, E., Colletta, G., Quota, A., Gerardi, C., Rigoli, L. C., Sacco, M., Pitrolo, L., et al. (2015) · American Journal of Hematology · doi:10.1002/ajh.24024 · Cited by 48
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
Ferritin light chain interacts with PEN-2 and affects γ-secretase activity
Li, X., Liu, Y., Zheng, Q., Yao, G., Peng, C., Bu, G., Xu, H., & Zhang, Y. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.05.018 · Cited by 47
He, Y., Ruganzu, J. B., Jin, H., Peng, X., Ji, S., Ma, Y., Zheng, L., & Yang, W. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112166 · Cited by 46
Sun, L., Sharma, A. K., Han, B.-H., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00376 · Cited by 46
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
Behar, A. E., Sabater, L., Baskin, M., Hureau, C., & Maayan, G. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202109758 · Cited by 45
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
Self-citationImpact of N‐Truncated Aβ Peptides on Cu‐ and Cu(Aβ)‐Generated ROS: CuI Matters!
Esmieu, C., Ferrand, G., Borghesani, V., & Hureau, C. (2021) · Chemistry – A European Journal · doi:10.1002/chem.202003949 · Cited by 43
Lv, Z., Condron, M. M., Teplow, D. B., & Lyubchenko, Y. L. (2012) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-012-9416-6 · Cited by 40
Change of zinc distribution in rat brain with increasing age
Sawashita, J., Takeda, A., & Okada, S. (1997) · Developmental Brain Research · doi:10.1016/s0165-3806(97)00107-7 · Cited by 40
The Emerging Roles and Therapeutic Potential of Soluble TREM2 in Alzheimer’s Disease
Zhong, L., & Chen, X. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00328 · Cited by 40
Wang, S., Jiang, Y. X., Liu, Y., Liu, Q., Sun, H., Mei, M., & Liao, X. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02731-8 · Cited by 40
Alterations in human tau transcripts correlate with those of neurofilament in sporadic tauopathies
Umeda, Y., Taniguchi, S., Arima, K., Piao, Y.-S., Takahashi, H., Iwatsubo, T., Mann, D., & Hasegawa, M. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.01.060 · Cited by 39
Kim, S. M., Ha, J. S., Han, A. R., Cho, S., & Yang, S.-J. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.10.026 · Cited by 39
Salami, A., Papenberg, G., Sitnikov, R., Laukka, E. J., Persson, J., & Kalpouzos, G. (2021) · NeuroImage · doi:10.1016/j.neuroimage.2021.117792 · Cited by 39
Research works printed but not linked: 10
- Petersen, 2018, Practice Guideline Update Summary: Mild Cognitive Impairment: Report of the Guideline Development, Dissemination, and Implementation Subcommittee of the American Academy of Neurology, Neurology, 90, 126
- Rajasekhar, 2018, Current Progress, Challenges and Future Prospects of Diagnostic and Therapeutic Interventions in Alzheimer's Disease, RSC Adv, 8, 23780
- Schrag, 2011, Iron, Zinc and Copper in the Alzheimer's Disease Brain: A Quantitative Meta-Analysis, Some Insight on the Influence of Citation Bias on Scientific Opinion, Prog Neurobiol, 94, 296
- Feng, 2020, Transferrin Receptor Is a Specific Ferroptosis Marker, Cell Rep, 30, 3411
- Syme, 2006, Solution 1h Nmr Investigation of Zn2+ and Cd2+ Binding to Amyloid-Beta Peptide (Abeta) of Alzheimer's Disease, BBA, 1764, 246
- Yang, 2005, Curcumin Inhibits Formation of Amyloid Beta Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo, J Biol Chem, 280, 5892
- Liu, 2010, Neuronal Lrp1 Knockout in Adult Mice Leads to Impaired Brain Lipid Metabolism and Progressive, Age-Dependent Synapse Loss and Neurodegeneration, J Neurosci, 30, 17068
- Jalili-Baleh, 2021, Chromone-Lipoic Acid Conjugate: Neuroprotective Agent Having Acceptable Butyrylcholinesterase Inhibition, Antioxidant and Copper-Chelation Activities, Daru, 29, 23
- Zhang, 2015, Amentoflavone Protects Hippocampal Neurons: Anti-Inflammatory, Antioxidative, and Antiapoptotic Effects, Neural Regen Res, 10, 1125
- Tian, 2020, Flurbiprofen-Chalcone Hybrid Mannich Base Derivatives as Balanced Multifunctional Agents against Alzheimer's Disease: Design, Synthesis and Biological Evaluation, Bioorg Chem, 94
Cited by
Sorted by citations
Zhang, J., Zhang, Y., Wang, J., Xia, Y., Zhang, J., & Chen, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01911-3 · Cited by 1,138
Self-citationHomeostasis and metabolism of iron and other metal ions in neurodegenerative diseases
Chen, L., Shen, Q., Liu, Y., Zhang, Y., Sun, L., Ma, X., Song, N., & Xie, J. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02071-0 · Cited by 279
Self-citationCopper homeostasis and cuproptosis in health and disease
Yang, Y., Wu, J., Wang, L., Ji, G., & Dang, Y. (2024) · MedComm · doi:10.1002/mco2.724 · Cited by 103
“103,104 Copper metabolism disorders have also been linked to the progression of AD.”
BackgroundBrain Iron Metabolism, Redox Balance and Neurological Diseases
Gao, G., You, L., Zhang, J. J., Chang, Y., & Yu, P. (2023) · Antioxidants · doi:10.3390/antiox12061289 · Cited by 95
Influence of Physicochemical Properties of Iron Oxide Nanoparticles on Their Antibacterial Activity
Shoudho, K. N., Uddin, S., Rumon, M. M. H., & Shakil, M. S. (2024) · ACS Omega · doi:10.1021/acsomega.4c02822 · Cited by 97
Metadata
- Authors
- Chen, L.-L., Fan, Y.-G., Zhao, L.-X., Zhang, Q., & Wang, Z.-Y.
- Affiliations
- China Medical University (CN)
- Corresponding author
- Wang, Zhan-You
- Venue
- Bioorganic Chemistry
- Publisher
- Elsevier BV
- Published
- 2023-02
- Volume
- 131
- Pages
- 106301
- ISSN
- 0045-2068 (ISSN-L)
- OpenAlex
- W4310077403
- Cited by
- 200
- References
- 258
- Citations by year
- 2026: 45 · 2025: 65 · 2024: 60 · 2023: 30
- FWCI
- 5.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Bioorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (82001162, 92049106)
- Natural Science Foundation of Liaoning Province (LJKZ0736)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, iron, copper, zinc, metal chelators, neuroinflammation, amyloid-beta, tau hyperphosphorylation, ferroptosis, cuproptosis, amyloid fibril formation
- MeSH terms
- Neuroinflammatory Diseases, Alzheimer Disease, Chelating Agents, Copper, Humans, Ions, Iron, Metals, Zinc, 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