Arsenic and Tau Phosphorylation: A Mechanistic Review
Abstract
Arsenic poisoning can affect the peripheral nervous system and cause peripheral neuropathy. Despite different studies on the mechanism of intoxication, the complete process is not explained yet, which can prevent further intoxication and produce effective treatment. In the following paper, we would like to consider the idea that arsenic might cause some diseases via inflammation induction, and tauopathy in neurons. Tau protein, one of the microtubule-associated proteins expressed in neurons, contributes to neuronal microtubules structure. Arsenic may be involved in cellular cascades involved in modulating tau function or hyperphosphorylation of tau protein, which ultimately leads to nerve destruction. For proof of this assumption, some investigations have been planned to measure the association between arsenic and quantities of phosphorylation of tau protein. Additionally, some researchers have investigated the association between microtubule trafficking in neurons and the levels of tau protein phosphorylation. It should be noticed that changing tau phosphorylation in arsenic toxicity may add a new feature to understanding the mechanism of poisonousness and aid in discovering novel therapeutic candidates such as tau phosphorylation inhibitors for drug development.
Integrity signals
Registry
Cites
Statistics
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?
Arsenic is involved in cellular signalling cascades that regulate tau protein function or hyperphosphorylation, ultimately leading to neurological damage.
“Arsenic is involved in cellular signalling cascades involved in regulating tau protein function or hyperphosphorylation, which ultimately leads to neurological damage [143].”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [143]
Cites
1 retracted
Li, L., McBride, D. W., Doycheva, D. M., Dixon, B. J., Krafft, P. R., Zhang, J. H., & Tang, J. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2014.12.020 · Cited by 109 · see citing works
RetractedMeijer, L., Nelson, D. J., Riazanski, V., Gabdoulkhakova, A. G., Héry-Arnaud, G., Berre, R. L., Loaëc, N., Oumata, N., Galons, H., Nowak, E., et al. (2016) · Journal of Innate Immunity · doi:10.1159/000444256 · Cited by 4,992 · see citing works
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089 · see citing works
Oxidative stress and the amyloid beta peptide in Alzheimer’s disease
Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185 · see citing works
Tau pathology and neurodegeneration
Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133 · see citing works
Neurotoxicity induces cleavage of p35 to p25 by calpain
Lee, M.-S., Kwon, Y. T., Li, M., Peng, J., Friedlander, R. M., & Tsai, L. (2000) · Nature · doi:10.1038/35012636 · Cited by 1,057 · see citing works
Stýblo, M., Razo, L. M. D., Vega, L., Germolec, D. R., LeCluyse, E. L., Hamilton, G. A., Reed, W., Wang, C., Cullen, W., & Thomas, D. J. (2000) · Archives of Toxicology · doi:10.1007/s002040000134 · Cited by 999 · see citing works
Embi, N., Rylatt, D. B., & Cohen, P. (1980) · PubMed · Cited by 911 · see citing works
Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878 · see citing works
Glycogen Synthase Kinase‐3 from Rabbit Skeletal Muscle
Noor, E. M. B. I., RYLATT, D. B., & Cohen, P. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb06059.x · Cited by 837 · see citing works
Frame, S., Cohen, P., & Biondi, R. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00253-2 · Cited by 703 · see citing works
Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Biomolecules · doi:10.3390/biom6010006 · Cited by 698 · see citing works
Arsenic: Health Effects, Mechanisms of Actions, and Research Issues
Abernathy, C. O., Liu, Y. P., Longfellow, D. G., Aposhian, H. V., Beck, B. D., Fowler, B. A., Goyer, R. A., Menzer, R. E., Rossman, T. G., Thompson, C. L., et al. (1999) · Environmental Health Perspectives · doi:10.1289/ehp.99107593 · Cited by 657 · see citing works
Tau protein kinases: Involvement in Alzheimer's disease
Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631 · see citing works
Tau phosphorylation in neuronal cell function and dysfunction
Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624 · see citing works
Arsenic geochemistry and health
Duker, A. A., Carranza, E. J. M., & Hale, M. (2004) · Environment International · doi:10.1016/j.envint.2004.10.020 · Cited by 583 · see citing works
Induction of oxyradicals by arsenic: Implication for mechanism of genotoxicity
Liu, S. X., Athar, M., Lippai, I., Waldren, C. A., & Hei, T. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1643 · Cited by 539 · see citing works
Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits
Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works
Cdk5 Is a Key Factor in Tau Aggregation and Tangle Formation In Vivo
Noble, W. J., Olm, V., Takata, K., Casey, E., Mary, O., Meyerson, J. L., Gaynor, K., LaFrancois, J. J., Wang, L., Kondo, T., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00259-9 · Cited by 511 · see citing works
Tyler, C. R., & Allan, A. (2014) · Current Environmental Health Reports · doi:10.1007/s40572-014-0012-1 · Cited by 507 · see citing works
Lovestone, S., Reynolds, C. H., Latimer, D. A., Davis, D. R., Anderton, B. H., Gallo, J., Hanger, D. P., Mulot, S., Marquardt, B., Stabel, S., et al. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00246-3 · Cited by 470 · see citing works
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 · see citing works
Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase
Zmijewski, J. W., Banerjee, S., Bae, H., Friggeri, A., Lazarowski, E. R., & Abraham, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143685 · Cited by 441 · see citing works
Zhu, X.-W., Raina, A., Rottkamp, C., Aliev, G., Perry, G., Boux, H., & Smith, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00046.x · Cited by 440 · see citing works
Tau phosphorylation: physiological and pathological consequences
Stoothoff, W. H., & Johnson, G. V. W. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.017 · Cited by 439 · see citing works
Regulation of Akt and glycogen synthase kinase-3β phosphorylation by sodium valproate and lithium
Sarno, P. D., Li, X., & Jope, R. S. (2002) · Neuropharmacology · doi:10.1016/s0028-3908(02)00215-0 · Cited by 433 · see citing works
Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction
Mietelska‐Porowska, A., Wasik, U., Goras, M., Filipek, A., & Niewiadomska, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034671 · Cited by 407 · see citing works
AMPK As a Metabolic Tumor Suppressor: Control of Metabolism and Cell Growth
Luo, Z., Zang, M., & Guo, W. (2010) · Future Oncology · doi:10.2217/fon.09.174 · Cited by 381 · see citing works
Arsenic: A Global Environmental Challenge
Chen, Q. Y., & Costa, M. (2021) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-030220-013418 · Cited by 358 · see citing works
Forlenza, O. V., de Paula, V. D. J. R., & Diniz, B. S. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn5000309 · Cited by 333 · see citing works
Schmitz, K. J., Wohlschlaeger, J., Lang, H., Sotiropoulos, G. C., Malagó, M., Steveling, K., Reis, H., Cicinnati, V. R., Schmid, K. W., & Baba, H. A. (2007) · Journal of Hepatology · doi:10.1016/j.jhep.2007.08.018 · Cited by 310 · see citing works
The effects of arsenic exposure on the nervous system
Rodríguez, V. M. (2003) · Toxicology Letters · doi:10.1016/s0378-4274(03)00262-5 · Cited by 305 · see citing works
Vingtdeux, V., Davies, P., Dickson, D. W., & Marambaud, P. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0759-x · Cited by 297 · see citing works
Perry, G., Roder, H., Nunomura, A., Takeda, A., Friedlich, A., Zhu, X.-W., Raina, A., Holbrook, N., Siedlak, S., Harris, P., et al. (1999) · NeuroReport · doi:10.1097/00001756-199908020-00035 · Cited by 296 · see citing works
A walk through tau therapeutic strategies
Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 286 · see citing works
Evidence for Irreversible Inhibition of Glycogen Synthase Kinase-3β by Tideglusib
Domı́nguez, J. M., Fuertes, A., Orozco, L., del Monte-Millán, M., Delgado, E., & Medina, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.306472 · Cited by 249 · see citing works
Fang, S., Wan, X. H., Zou, X., Sun, S. Y., Hao, X., Liang, C., Zhang, Z., Zhang, F., Sun, B., Li, H., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-020-03357-1 · Cited by 224 · see citing works
AMP‐activated protein kinase: a potential player in Alzheimer’s disease
Salminen, A., Kaarniranta, K., Haapasalo, A., Soininen, H. S., & Hiltunen, M. O. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07331.x · Cited by 221 · see citing works
Sanli, T., Steinberg, G. R., Singh, G., & Tsakiridis, T. (2014) · Cancer Biology & Therapy · doi:10.4161/cbt.26726 · Cited by 220 · see citing works
Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia
Ittner, L. M., Fath, T., Ke, Y. D., Bi, M., van Eersel, J., Li, K. M., Gunning, P. W., & Götz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808084105 · Cited by 219 · see citing works
Xia, Y., Prokop, S., & Giasson, B. I. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00460-5 · Cited by 218 · see citing works
Liu, Y., Guyton, K. Z., Gorospe, M., Xu, Q., Lee, J. C., & Holbrook, N. J. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)00176-1 · Cited by 213 · see citing works
Arsenic targets tubulins to induce apoptosis in myeloid leukemia cells.
Li, Y. M., & Broome, J. D. (1999) · PubMed · Cited by 211 · see citing works
Liu, Z., Li, T., Li, P., Wei, N., Zhao, Z., Liang, H., Ji, X., Chen, W., Xue, M., & Wei, J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/352723 · Cited by 208 · see citing works
Alzheimer-like Changes in Microtubule-associated Protein Tau Induced by Sulfated Glycosaminoglycans
Hasegawa, M., Crowther, R. A., Jakes, R., & Goedert, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.33118 · Cited by 205 · see citing works
Mechanism of CDK5/p25 Binding by CDK Inhibitors
Mapelli, M., Massimiliano, L., Crovace, C., Seeliger, M. A., Tsai, L., Meijer, L., & Musacchio, A. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049323m · Cited by 202 · see citing works
Tau-Centric targets and drugs in clinical development for the treatment of alzheimer's disease
Panza, F., Solfrizzi, V., Seripa, D., Imbimbo, B. P., Lozupone, M., Santamato, A., Zecca, C., Barulli, M. R., Bellomo, A., Pilotto, A., et al. (2016) · BioMed Research International · doi:10.1155/2016/3245935 · Cited by 195 · see citing works
Endoplasmic reticulum stress: an arising target for metal-based anticancer agents
King, A. P., & Wilson, J. J. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00259c · Cited by 189 · see citing works
Silencing of CDK5 Reduces Neurofibrillary Tangles in Transgenic Alzheimer's Mice
Piedrahita, D., Hernández, I., Tobon, A., Fedorov, D., Obara, B., Manjunath, B. S., Boudreau, R. L., Davidson, B. L., LaFerla, F. M., Gallego-Gómez, J. C., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3637-10.2010 · Cited by 184 · see citing works
Thornton, C., Bright, N. J., Sastre, M., Muckett, P. J., & Carling, D. (2011) · Biochemical Journal · doi:10.1042/bj20101485 · Cited by 183 · see citing works
Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells
Su, B., Wang, X., Lee, H., Tabaton, M., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.010 · Cited by 178 · see citing works
Tumor necrosis factor induces GSK3 kinase–mediated cross-tolerance to endotoxin in macrophages
Park, S. H., Park‐Min, K., Chen, J., Hu, X., & Ivashkiv, L. B. (2011) · Nature Immunology · doi:10.1038/ni.2043 · Cited by 176 · see citing works
Atzori, C., Ghetti, B. F., Piva, R., Srinivasan, A., Zolo, P., Delisle, M. B., Mirra, S. S., & Migheli, A. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.12.1190 · Cited by 175 · see citing works
Winneke, G. (2011) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2011.05.020 · Cited by 173 · see citing works
Arsenic Induces Apoptosis in Rat Cerebellar Neurons via Activation of JNK3 and p38 MAP Kinases
Namgung, U., & Xia, Z. (2001) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2001.9200 · Cited by 172 · see citing works
Corcoran, N. M., Martin, D., Hutter‐Paier, B., Windisch, M., Nguyen, T. T., Nheu, L., Sundström, L., Costello, A. J., & Hovens, C. M. (2010) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2010.04.020 · Cited by 168 · see citing works
Reactivating Kinase/p38 Phosphorylates τ Protein In Vitro
Reynolds, C. H., Nebreda, A. R., Gibb, G. M., Utton, M. A., & Anderton, B. H. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69010191.x · Cited by 161 · see citing works
Mondragón‐Rodríguez, S., Perry, G. L., Zhu, X., Moreira, P. I., Acevedo, M., & Williams, S. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/940603 · Cited by 155 · see citing works
Peripheral Neuropathy Caused by Arsenical Intoxication
Heyman, A., Pfeiffer, J. B., Willett, R. W., & Taylor, H. M. (1956) · New England Journal of Medicine · doi:10.1056/nejm195603012540901 · Cited by 153 · see citing works
Rajasekhar, K., & Govindaraju, T. (2018) · RSC Advances · doi:10.1039/c8ra03620a · Cited by 150 · see citing works
Health effects of arsenic exposure in Latin America: An overview of the past eight years of research
Khan, K. M., Chakraborty, R., Bundschuh, J., Bhattacharya, P., & Parvez, F. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.136071 · Cited by 145 · see citing works
Discovery of MK-8719, a Potent O-GlcNAcase Inhibitor as a Potential Treatment for Tauopathies
Selnick, H. G., Hess, J. F., Tang, C., Liu, K., Schachter, J. B., Ballard, J. E., Marcus, J., Klein, D. J., Wang, X., Pearson, M. S., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01090 · Cited by 144 · see citing works
Tau-Based Treatment Strategies in Neurodegenerative Diseases
Schneider, A., & Mandelkow�, E. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.006 · Cited by 142 · see citing works
PD98059 Prevents Neurite Degeneration Induced by Fibrillar β‐Amyloid in Mature Hippocampal Neurons
Rapoport, M., & Ferreira, A. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740125.x · Cited by 139 · see citing works
Sugiyama, M. G., Fairn, G. D., & Antonescu, C. N. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00070 · Cited by 134 · see citing works
Cyclin‐dependent kinase 5 in synaptic plasticity, learning and memory
Angelo, M., Plattner, F., & Giese, K.-P. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04040.x · Cited by 133 · see citing works
Alzheimer's Disease: The Role of Microglia in Brain Homeostasis and Proteopathy
Clayton, K. A., Enoo, A. A. V., & Ikezu, T. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00680 · Cited by 132 · see citing works
Aberrant Stress-induced Phosphorylation of Perikaryal Neurofilaments
Giasson, B. I., & Mushynski, W. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30404 · Cited by 131 · see citing works
The Role of CDK5/P25 Formation/Inhibition in Neurodegeneration
Camins, A., Verdaguer, E., Folch, J., Canudas, A. M., & Pallàs, M. (2006) · Drug News & Perspectives · doi:10.1358/dnp.2006.19.8.1043961 · Cited by 124 · see citing works
Xiong, Y., Jing, X.-P., Zhou, X.-W., Wang, X.-L., Yang, Y., Sun, X.-Y., Qiu, M., Cao, F.-Y., Lu, Y.-M., Liu, R., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.07.003 · Cited by 122 · see citing works
Moya‐Alvarado, G., Gershoni‐Emek, N., Perlson, E., & Bronfman, F. C. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r115.053330 · Cited by 119 · see citing works
Vega, L., Gonsebatt, M. E., & Ostrosky‐Wegman, P. (1995) · Mutation Research/Environmental Mutagenesis and Related Subjects · doi:10.1016/0165-1161(95)90074-8 · Cited by 118 · see citing works
The Arsenic Exposure Hypothesis for Alzheimer Disease
Gong, G., & O’Bryant, S. E. (2010) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0b013e3181d71bc7 · Cited by 117 · see citing works
The role of caspases in Alzheimer’s disease; potential novel therapeutic opportunities
Rohn, T. T. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0463-2 · Cited by 112 · see citing works
Yeung, A. W. K., Tzvetkov, N. T., Georgieva, M. G., Ognyanov, I., Kordos, K., Jóźwik, A., Kühl, T., Perry, G. L., Petralia, M. C., Mazzon, E., et al. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7952 · Cited by 110 · see citing works
SCHOOLMEESTER, W. L., & WHITE, D. R. (1980) · Southern Medical Journal · doi:10.1097/00007611-198002000-00021 · Cited by 109 · see citing works
Jin, N., Yin, X., Yu, D., Cao, M., Gong, C., Iqbal, K., Ding, F., Gu, X., & Liu, F. (2015) · Scientific Reports · doi:10.1038/srep08187 · Cited by 107 · see citing works
Polyneuropathy Due to Acute Arsenic Intoxication: Biopsy Studies
Goebel, H. H., Schmidt, P. F., Böhl, J., Tettenborn, B., Krämer, G., & Gutmann, L. (1990) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199003000-00006 · Cited by 93 · see citing works
Florea, A.-M., Splettstoesser, F., & Büsselberg, D. (2007) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2007.01.022 · Cited by 91 · see citing works
Amalfitano, A., & Chamberlain, J. S. (1996) · Muscle & Nerve · doi:10.1002/(sici)1097-4598(199612)19:12 · Cited by 88 · see citing works
Encephalopathy: An uncommon manifestation of workplace arsenic poisoning?
Morton, W. E., & Caron, G. A. (1989) · American Journal of Industrial Medicine · doi:10.1002/ajim.4700150102 · Cited by 88 · see citing works
Shimada, K., Motoi, Y., Ishiguro, K., Kambe, T., Matsumoto, S., Itaya, M., Kunichika, M., Mori, H., Shinohara, A., Chiba, M., et al. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.050 · Cited by 87 · see citing works
Wang, R., Xia, L., Gabrilove, J., Waxman, S., & Jing, Y. (2013) · Leukemia · doi:10.1038/leu.2012.180 · Cited by 85 · see citing works
Götz, J., Xia, D., Leinenga, G., Chew, Y. L., & Nicholas, H. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00072 · Cited by 85 · see citing works
Matsuda, S., Nakagawa, Y., Tsuji, A., Kitagishi, Y., Nakanishi, A., & Murai, T. (2018) · Diseases · doi:10.3390/diseases6020028 · Cited by 85 · see citing works
Effects of As(III) Binding on α-Helical Structure
Cline, D. J., Thorpe, C., & Schneider, J. P. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0282644 · Cited by 80 · see citing works
Rahman, M. A., Hannan, M. A., Uddin, M. J., Rahman, M. S., Rashid, M., & Kim, B. (2021) · Toxics · doi:10.3390/toxics9080188 · Cited by 77 · see citing works
Xu, M., Wang, S. L., Zhu, L., Wu, P., Dai, W., & Rakesh, K. P. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.12.073 · Cited by 71 · see citing works
You, B. R., & Park, W. H. (2012) · Oncology Reports · doi:10.3892/or.2012.1852 · Cited by 70 · see citing works
Arsenic Methyltransferase and Methylation of Inorganic Arsenic
Roy, N. K., Murphy, A., & Costa, M. (2020) · Biomolecules · doi:10.3390/biom10091351 · Cited by 69 · see citing works
Role of Post‐translational Modifications in Alzheimer's Disease
Ramesh, M., Gopinath, P., & Govindaraju, T. (2019) · ChemBioChem · doi:10.1002/cbic.201900573 · Cited by 68 · see citing works
The Environmental Toxin Arsenite Induces Tau Hyperphosphorylation
Giasson, B. I., Sampathu, D. M., Wilson, C., Vogelsberg-Ragaglia, V., Mushynski, W. E., & Lee, V. M. ‐. (2002) · Biochemistry · doi:10.1021/bi026813c · Cited by 66 · see citing works
Arsenic Exposure Contributes to the Bioenergetic Damage in an Alzheimer’s Disease Model
Niño, S. A., Morales-Martínez, A., Chi-Ahumada, É., Carrizales, L., Salgado‐Delgado, R., Pérez‐Severiano, F., Díaz-Cintra, S. Y., Jiménez-Capdeville, M. E., & Zarazúa, S. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00278 · Cited by 64 · see citing works
Sarwar, T., Khan, S. A., Muhammad, S., & Amin, S. (2021) · Environmental Technology & Innovation · doi:10.1016/j.eti.2021.101392 · Cited by 58 · see citing works
Mitochondrial Dysfunction and Stress Responses in Alzheimer’s Disease
Weidling, I. W., & Swerdlow, R. H. (2019) · Biology · doi:10.3390/biology8020039 · Cited by 56 · see citing works
Chiu, H., Tseng, Y.-C., Hsu, Y., Lin, Y., Foo, N., Guo, H., & Wang, Y. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.10.025 · Cited by 53 · see citing works
Niño, S. A., Martel‐Gallegos, G., Castro‐Zavala, A., Ortega-Berlanga, B., Delgado, J. M., Hernández‐Mendoza, H., Romero-Guzmán, E. T., Ríos-Lugo, M. J., Rosales‐Mendoza, S., Jiménez-Capdeville, M. E., et al. (2017) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.7b00215 · Cited by 49 · see citing works
Latimer, D. A., Gallo, J.-M., Lovestone, S., Miller, C. C. J., Hugh Reynolds, C., Marquardt, B., Stabel, S., Woodgett, J. R., & Anderton, B. H. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00434-b · Cited by 48 · see citing works
Chayapong, J., Madhyastha, H., Madhyastha, R., Nurrahmah, Q. I., Nakajima, Y., Choijookhuu, N., Hishikawa, Y., & Maruyama, M. (2016) · Environmental Science and Pollution Research · doi:10.1007/s11356-016-8215-7 · Cited by 47 · see citing works
Wisessaowapak, C., Visitnonthachai, D., Watcharasit, P., & Satayavivad, J. (2021) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2021.103626 · Cited by 47 · see citing works
Tripathi, M. K., Kartawy, M., Ginzburg, S., & Amal, H. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-01890-5 · Cited by 47 · see citing works
DeFuria, J., & SHEA, T. B. (2007) · Brain Research · doi:10.1016/j.brainres.2007.04.019 · Cited by 42 · see citing works
Kanno, T., Tsuchiya, A., Tanaka, A., & Nishizaki, T. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9405-x · Cited by 40 · see citing works
Patel, E. U., & Reynolds, M. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2013.08.002 · Cited by 40 · see citing works
Shen, X., Luo, T., Li, S., Ting, O., He, F., Xu, J., & Wang, H. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3281 · Cited by 40 · see citing works
Fu, S.-C., Lin, J.-W., Liu, J., Liu, S., Fang, K., Su, C., Hsu, R., Wu, C.-C., Huang, C.-F., Lee, K.-I., et al. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.05.008 · Cited by 39 · see citing works
Vahidnia, A., van der Straaten, R. J. H. M., Romijn, F. P. H. T. M., PELT, J. V., van der Voet, G. B., & de Wolff, F. A. (2007) · Toxicology in Vitro · doi:10.1016/j.tiv.2007.04.007 · Cited by 38 · see citing works
Curtis, D., & Bandyopadhyay, S. (2020) · Annals of Human Genetics · doi:10.1111/ahg.12410 · Cited by 38 · see citing works
ATF4 regulates arsenic trioxide-mediated NADPH oxidase, ER-mitochondrial crosstalk and apoptosis
Srivastava, R. K., Li, C., Ahmad, A. M., Abrams, O., Gorbatyuk, M. S., Harrod, K. S., Wek, R. C., Afaq, F., & Athar, M. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.09.003 · Cited by 36 · see citing works
GSK3 promotes arsenite‐induced apoptosis via facilitation of mitochondria disruption
Watcharasit, P., Thiantanawat, A., & Satayavivad, J. (2007) · Journal of Applied Toxicology · doi:10.1002/jat.1296 · Cited by 35 · see citing works
Pakzad, D., Akbari, V., Sepand, M. R., & Aliomrani, M. (2021) · Toxicology Research · doi:10.1093/toxres/tfab011 · Cited by 30 · see citing works
Beauchamp, E. M., Kościuczuk, E. M., Serrano, R. M. T., Nanavati, D. M., Swindell, E. P., Viollet, B., O’Halloran, T. V., Altman, J. K., & Platanias, L. C. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0665-t · Cited by 28 · see citing works
Effects of Deferasirox in Alzheimer’s Disease and Tauopathy Animal Models
Kwan, P., Ho, A. S.-W., & Baum, L. (2022) · Biomolecules · doi:10.3390/biom12030365 · Cited by 28 · see citing works
Jenkins, S. M., & Johnson, G. V. W. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741463.x · Cited by 27 · see citing works
Vahidnia, A., van der Straaten, R. J. H. M., Romijn, F. P. H. T. M., PELT, J. V., van der Voet, G. B., & de Wolff, F. A. (2008) · Toxicology in Vitro · doi:10.1016/j.tiv.2007.12.010 · Cited by 21 · see citing works
Role of pigment epithelium-derived factor (PEDF) on arsenic-induced neuronal apoptosis
Zhang, W., Cui, X., Gao, Y., Sun, L., Wang, J., Yang, Y., Liu, X., Li, Y., Guo, X., & Sun, D. (2018) · Chemosphere · doi:10.1016/j.chemosphere.2018.10.100 · Cited by 21 · see citing works
Kesici, G. G. (2016) · Journal of Otology · doi:10.1016/j.joto.2016.03.001 · Cited by 21 · see citing works
Alizadeh‐Ghodsi, M., Zavvari, A., Kalan, A. E., Shiri‐Shahsavar, M. R., & Yousefi, B. (2016) · Nutritional Neuroscience · doi:10.1080/1028415x.2016.1239399 · Cited by 20 · see citing works
Hu, W.-C., Teo, W., Huang, T.-F., Lee, T.-C., & Lo, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00463 · Cited by 20 · see citing works
Nichols, T. (2014) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000159 · Cited by 19 · see citing works
Li, J., Tang, G., Qin, W., Yang, R., Ma, R., Ma, B., Wei, J., Lv, H., & Jiang, Y. (2018) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmy041 · Cited by 18 · see citing works
Involvement of Glycogen Synthase Kinase-3β in Arsenic Trioxide–Induced p21 Expression
Huang, H., Liu, Z., & Cheng, Y.-L. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr023 · Cited by 16 · see citing works
Srivastava, R. K., Li, C., Wang, Y., Weng, Z., Elmets, C. A., Harrod, K. S., Deshane, J. S., & Athar, M. (2016) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2016.07.015 · Cited by 15 · see citing works
Menka, N., Root, R. A., & Chorover, J. (2014) · Reviews on Environmental Health · doi:10.1515/reveh-2014-0009 · Cited by 9 · see citing works
Arsenic-Induced Developmental Neurotoxicity
Luo, J., & Shu, W. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-418688-0.00015-0 · Cited by 7 · see citing works
Hayes, W. P., Yangco, N., Chin, H. R., Mill, J. F., Pu, L. P., Taira, M., Dawid, I. B., & Gallo, V. (2001) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20010201)63:3 · Cited by 7 · see citing works
Zhao, W., Xiang, Y.-G., Zhang, Z., Liu, X., Jiang, M.-L., Jiang, B., Song, Y., & Hu, J.-Y. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106447 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
MicroRNAs: pioneering regulators in Alzheimer’s disease pathogenesis, diagnosis, and therapy
Li, Y.-B., Fu, Q., Guo, M., Du, Y., Chen, Y., & Cheng, Y. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03075-8 · Cited by 123 · see citing works
“In AD, however, tau undergoes abnormal phosphorylation and aggregation, resulting in the formation of NFTs [25, 26].”
Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63 · see citing works
“Arsenic is involved in cellular signalling cascades involved in regulating tau protein function or hyperphosphorylation, which ultimately leads to neurological damage [143].”
BackgroundAlzheimer's disease: The role of proteins in formation, mechanisms, and new therapeutic approaches
Gholami, A. (2023) · Neuroscience Letters · doi:10.1016/j.neulet.2023.137532 · Cited by 51 · see citing works
Functions of Intrinsically Disordered Regions
Xiao, L., & Xia, K. (2025) · Biology · doi:10.3390/biology14070810 · Cited by 17 · see citing works
“The modification of multiple phosphorylation sites (such as Ser262, Thr231) can alter the global conformation of TAU protein [43,44].”
Metal Toxicity and Dementia Including Frontotemporal Dementia: Current State of Knowledge
Gorini, F., & Tonacci, A. (2024) · Antioxidants · doi:10.3390/antiox13080938 · Cited by 17 · see citing works
“As is a well-known environmental toxicant, and, although a growing body of evidence has reported that even low concentrations of As impair neurological and cognitive functions [119], the exact mechanism of action of As remains to be elucidated (see [105,120–122] for more details).”
BackgroundMetabolome informs about the chemical exposome and links to brain health
Orešič, M., Karu, N., Zhao, H. N., Moseley, M. A., Hankemeier, T., Wishart, D. S., Dorrestein, P. C., Fiehn, O., Hyötyläinen, T., & Kaddurah‐Daouk, R. (2025) · Environment International · doi:10.1016/j.envint.2025.109741 · Cited by 15 · see citing works
“…and neuronal apoptosis (Gauvrit et al., 2022; Babić Leko et al., 2023; Huat et al., 2019; Yu et al., 2024; Paglia et al., 2016; Breijyeh and Karaman, 2020; Colomina and Peris-Sampedro, 2017; Ariafar et al., 2023; Deng et al., 2023; Mutter et al., 2004; Rahman et al., 2020; Zheng et al., 2003).”
Wang, R., Li, J., Li, X., Guo, Y., Chen, P., & Tian, P. (2025) · Reviews in the Neurosciences · doi:10.1515/revneuro-2025-0013 · Cited by 7 · see citing works
Oxidative stress – Alzheimer’s disease – DNA methylation: the role of arsenic
Antinori, D., Lucarelli, M., & Fuso, A. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253019 · Cited by 5 · see citing works
“Wisessaowapak et al. [40] exposed differentiated SH-SY5Y neuroblastoma cells to 1–10 μM of sodium arsenate, inducing increased tau hyperphosphorylation.”
Dutta, A., Phukan, B. C., Roy, R., Bhattacharya, P., Kumar, D., & Borah, A. (2025) · Current Alzheimer Research · doi:10.2174/0115672050390649250904100840 · Cited by 2 · see citing works
Gu, D., Chen, X., He, H.-L., Xia, M., Huang, J., He, G., Wang, X., Chen, Y.-Y., Kang, W.-R., Sun, B., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-04735-5 · Cited by 1 · see citing works
“Arsenic-containing compounds, such as NaAsO 2 and As 2 O 3 , can disrupt normal neural function by interfering with neurotransmitter synthesis and nerve signal transduction 27 .”
He, H.-Y., & Hsiao, H. (2024) · Microchemical Journal · doi:10.1016/j.microc.2024.112179 · Cited by 1 · see citing works
Decoding the Involvement of miRNAs in Alzheimer’s Disease: Focus on Neuroinflammation
Yadav, S., & Wojda, U. (2025) · RNA technologies · doi:10.1007/978-3-031-91072-2_14
Najm, M. S., Hammadi, N. I., Musleh, A. H., & Shalal, M. S. (2026) · Medical Journal of Babylon · doi:10.4103/mjbl.mjbl_1750_23
- Authors
- Ariafar, S., Makhdoomi, S., & Mohammadi, M.
- Affiliations
- Hamedan University of Medical Sciences (IR)
- Corresponding author
- Mohammadi, Mojdeh
- Venue
- Biological Trace Element Research
- Published
- 2023-05-22
- Volume
- 201
- Issue
- 12
- Pages
- 5708-5720
- ISSN
- 0163-4984 (ISSN-L)
- 1559-0720
- OpenAlex
- W4377193315
- Cited by
- 13
- References
- 127
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 4 · 2023: 1
- FWCI
- 0.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Biological Trace Element Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Heavy Metal Exposure and Toxicity
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Environmental Science › Environmental Chemistry › Arsenic contamination and mitigation
- Keywords
- arsenic toxicity, tau phosphorylation, peripheral neuropathy, tauopathy, neuroinflammation, microtubule-associated proteins, neuronal injury
- MeSH terms
- Arsenic, Microtubules, Neurons, Phosphorylation, tau Proteins
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