The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Exposure of rat hippocampal neurons to amyloid β peptide (25–35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β
Abstract
Exposure of rat hippocampal neurons to the peptide amyloid beta (A beta) (25-35) as well as A beta (1-40) peptides enhances phosphorylation of tau to a paired helical filament (PHF)-state through activation of tau protein kinase I (TPK I)/glycogen synthase kinase-3 beta (GSK-3 beta) [Busciglio, J., Lorenzo, A., Yeh, J. and Yankner, B.A., Neuron, 14 (1995) 879-888; Takashima, A., Ishiguro, K., Noguchi, K., Michel, G., Hoshi, M., Sato, K., Takahashi, M., Hoshino, T., Uchida, T. and Imahori, K., Neurosci. Meeting Abstr., 671 (1995) 17]. In order to examine the effects of A beta treatment on intracellular signaling mechanism, we have investigated the role of phosphatidyl inositol-3 (PI-3) kinase in the phosphorylation of tau. A beta (25-35) exposure induced an inactivation of PI-3 kinase and an activation of TPK I/GSK-3 beta in rat hippocampal culture. Wortmannin, an inhibitor of PI-3 kinase, also activated TPK I/GSK-3 beta, leading to an enhancement of tau phosphorylation and neuronal death in hippocampal culture. These results suggest that A beta (25-35) inhibition of PI-3 kinase results in the activation of TPK I/GSK-3 beta, the phosphorylation of tau, and resultant neuronal death in rat hippocampal neurons.
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
“The GSK3β can orchestrate pathological tau-phosphorylation at over two-dozen disease-associated sites [181–184].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [183]
Citations
Cites
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975
Mattson, M. P., Cheng, B., Davis, D. G., Bryant, K., Lieberburg, I. M., & Rydel, R. E. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-02-00376.1992 · Cited by 1,633
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417
Requirement for Phosphatidylinositol-3 Kinase in the Prevention of Apoptosis by Nerve Growth Factor
Yao, R., & Cooper, G. M. (1995) · Science · doi:10.1126/science.7701324 · Cited by 1,393
Arcaro, A., & Wymann, M. P. (1993) · Biochemical Journal · doi:10.1042/bj2960297 · Cited by 1,138
Pike, C. J., Walencewicz‐Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., & Cotman, C. W. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010253.x · Cited by 699
β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding
Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595
Welsh, G. I., & Proud, C. G. (1993) · Biochemical Journal · doi:10.1042/bj2940625 · Cited by 397
Tau protein kinase I is essential for amyloid beta-protein-induced neurotoxicity.
Takashima, A., Noguchi, K., Sato, K., Hoshino, T., & Imahori, K. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7789 · Cited by 385
Self-citation
Cited by
Sorted by citations
Items 101–200 of 263
Xian, Y., Mao, Q., Wu, J. C., Su, Z., Chen, J., Lai, X., Ip, S., & Lin, Z. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131457 · Cited by 84
Sirerol‐Piquer, M., Gómez‐Ramos, P., Hernández, F., Pérez, M., Morán, M. A., Fuster-Matanzo, A., Lucas, J. J., Ávila, J., & García‐Verdugo, J. M. (2010) · Hippocampus · doi:10.1002/hipo.20805 · Cited by 83
Mishra, R., Barthwal, M. K., Sondarva, G. V., Rana, B., Wong, L., Chatterjee, M., Woodgett, J. R., & Rana, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705895200 · Cited by 78
Changes in the ageing brain in health and disease
Anderton, B. H. (1997) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1997.0162 · Cited by 82
Hellström‐Lindahl, E. (2000) · European Journal of Pharmacology · doi:10.1016/s0014-2999(00)00028-5 · Cited by 76
Farías, G. G., Godoy, J. A., Hernández, F., Avila, J., Fisher, A., & Inestrosa, N. C. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.07.016 · Cited by 59
Liu, G., Zhang, Y., Yao, X., Zhang, C., Fang, J., Wang, Q., & Wang, J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.03.012 · Cited by 72
A molecular cell biology of lithium
Williams, R. S. B., Ryves, W. J., Dalton, E. C., Eickholt, B. J., Shaltiel, G., Agam, G., & Harwood, A. J. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320799 · Cited by 71
Kanninen, K. M., White, A. R., Koıstınaho, J., & Malm, T. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/985085 · Cited by 70
Kumar, P., Jha, N. K., Jha, S. K., Ramani, K., & Ambasta, R. K. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140933 · Cited by 67
Su, J. H., Cummings, B. J., & Cotman, C. W. (1998) · Acta Neuropathologica · doi:10.1007/s004010050920 · Cited by 67
Effects of endogenous β‐amyloid overproduction on tau phosphorylation in cell culture
Wang, Z., Li, H., Li, X., Zhang, Q., Tian, Q., Wang, Q., Xu, H., & Wang, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03956.x · Cited by 65
Novel Anti-Alzheimer’s Therapeutic Molecules Targeting Amyloid Precursor Protein Processing
Uddin, M. S., Kabir, M. T., Jeandet, P., Mathew, B., Ashraf, G. M., Perveen, A., Bin-Jumah, M. N., Mousa, S. A., & Abdel‐Daim, M. M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7039138 · Cited by 67
Westmark, C. J. (2012) · Molecular Psychiatry · doi:10.1038/mp.2012.122 · Cited by 63
Liu, M., Paranjpe, M. D., Zhou, X., Duy, P. Q., Goyal, M. S., Benzinger, T. L. S., Lu, J., Wang, R., & Zhou, Y. (2019) · Theranostics · doi:10.7150/thno.35366 · Cited by 67
Khanfar, M. A., Hill, R. A., Kaddoumi, A., & Sayed, K. A. E. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100941j · Cited by 63
Qu, L., Li, S., Ji, L., Luo, S., Ding, M., Yin, F., Wang, C., Luo, H., Lu, D., Liu, X., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113889 · Cited by 61
Cheng, H., Gang, X., Liu, Y., Wang, G., Zhao, X., & Wang, G. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00179.2019 · Cited by 63
Glycogen Synthase Kinase-3 in Neurodegeneration and Neuroprotection:Lessons from Lithium
Aghdam, S. Y., & Barger, S. W. (2007) · Current Alzheimer Research · doi:10.2174/156720507779939832 · Cited by 61
Huang, H., Ou, H., & Hsieh, S. (2000) · Life Sciences · doi:10.1016/s0024-3205(00)00511-7 · Cited by 61
Okuda, M., Fujita, Y., Hijikuro, I., Wada, M., Uemura, T., Kobayashi, Y., Waku, T., Tanaka, N., Nishimoto, T., Izumi, Y., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161017 · Cited by 59
Protective effects of erythropoietin on tau phosphorylation induced by β‐amyloid
Sun, Z., Yang, H., Pan, J., Zhen, H., Wang, Z., Chen, S., & Ding, J. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21745 · Cited by 58
Modi, K. K., Jana, A., Ghosh, S., Watson, R. L., & Pahan, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103606 · Cited by 55
Muñoz-Montaño, J. R., Lim, F., Moreno, F. J., Ávila, J., & Díaz‐Nido, J. (1999) · Journal of Alzheimer s Disease · doi:10.3233/jad-1999-1602 · Cited by 55
Tau acts as a mediator forAlzheimer's disease‐related synaptic deficits
Liao, D., Miller, E. C., & Teravskis, P. J. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12504 · Cited by 53
Khanfar, M. A., Abuasal, B., Mudit, M., Kaddoumi, A., & Sayed, K. A. E. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.06.054 · Cited by 53
Zhao, R., Zhang, Z., Song, Y., Wang, D., Qi, J., & Wen, S. (2010) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2010.11.054 · Cited by 53
RetractedCytoskeletal mechanisms of neuronal degeneration
Brandt, R. (2001) · Cell and Tissue Research · doi:10.1007/s004410000334 · Cited by 52
Hypoxia-induced mitochondrial and nuclear DNA damage in the rat brain
Englander, E. W., Greeley, G. H., Wang, G., Perez-Polo, J. R., & Lee, H.-M. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19991015)58:2 · Cited by 51
Zhang, Z., Zhao, R., Qi, J., Wen, S., Tang, Y., & Wang, D. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22563 · Cited by 48
Jones, A., Kulozik, P., Ostertag, A., & Herzig, S. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0973 · Cited by 47
Yao, X., Zhang, X., Yin, Y., Liu, B., Luo, D., Liu, D., Chen, N., Ni, Z.-F., Wang, X., Wang, Q., et al. (2011) · Biochemical Journal · doi:10.1042/bj20110347 · Cited by 47
Dieckol Ameliorates Aβ Production via PI3K/Akt/GSK-3β Regulated APP Processing in SweAPP N2a Cell
Yoon, J.-H., Lee, N., Youn, K., Jo, M. R., Kim, H., Lee, D., Ho, C., & Jun, M. (2021) · Marine Drugs · doi:10.3390/md19030152 · Cited by 46
The multifaceted role of WNT signaling in Alzheimer’s disease onset and age-related progression.
Kostes, W. W., & Brafman, D. A. (2023) · Cells · doi:10.3390/cells12081204 · Cited by 43
Oxidative Stress-Induced Damage to the Developing Hippocampus Is Mediated by GSK3β
Abbah, J., Vacher, C., Goldstein, E. Z., Li, Z., Kundu, S., Talbot, B., Bhattacharya, S., Hashimoto‐Torii, K., Wang, L., Banerjee, P., et al. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.2389-21.2022 · Cited by 46
Aβ Influences Cytoskeletal Signaling Cascades with Consequences to Alzheimer’s Disease
Henriques, A. G., Oliveira, J. M., Carvalho, L., & Silva, O. A. B. D. C. E. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8913-4 · Cited by 45
Fan, L., Qiu, X., Zhu, Z., Lv, J., Lu, J., Mao, F., Zhu, J., Wang, J., Guan, X., Chen, J., et al. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0220-1 · Cited by 46
Pavı́a, J., CEBALLOS, M. L. D., & de la Cuesta, F. S. (1998) · Fundamental and Clinical Pharmacology · doi:10.1111/j.1472-8206.1998.tb00975.x · Cited by 44
Phosphatidylinositol-3-kinase activation blocks amyloid beta-induced neurotoxicity
Lee, K., Koh, S., Noh, M., Kim, S. H., & Lee, Y. J. (2007) · Toxicology · doi:10.1016/j.tox.2007.09.020 · Cited by 44
Arc Regulates Transcription of Genes for Plasticity, Excitability and Alzheimer’s Disease
Leung, H.-W., Foo, G., & VanDongen, A. M. J. (2022) · Biomedicines · doi:10.3390/biomedicines10081946 · Cited by 41
Liu, F., Gong, X., Zhang, G., Marquis, K. L., Reinhart, P. H., & Andree, T. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03474.x · Cited by 42
Kim, J., Yang, M., Kim, S.-H., Kim, J. C., Wang, H., Shin, T., & Moon, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070356 · Cited by 39
Modi, K. K., Jana, A., Ghosh, S., Watson, R. L., & Pahan, K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180602 · Cited by 39
Takashima, A. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00047 · Cited by 39
Self-citationModeling Alzheimer’s disease with human iPS cells: advancements, lessons, and applications
Essayan-Perez, S., Zhou, B., Nabet, A. M., Wernig, M., & Huang, Y. A. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104503 · Cited by 40
Intranasal insulin and orexins to treat age-related cognitive decline
Erichsen, J. M., Calva, C. B., Reagan, L. P., & Fadel, J. R. (2021) · Physiology & Behavior · doi:10.1016/j.physbeh.2021.113370 · Cited by 38
Birajdar, S. V., Mazahir, F., Alam, M. I., Kumar, A., & Yadav, A. K. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176117 · Cited by 37
Yagishita, S., Murayama, M., Ebihara海老原朋江, T., Maruyama丸山敬, K., & 高島, 明. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.619668 · Cited by 35
NUB1 modulation of GSK3β reduces tau aggregation
Richet, E., Pooler, A. M., Rodriguez, T., Novoselov, S. S., Schmidtke, G., Groettrup, M., Hanger, D. P., Cheetham, M. E., & van der Spuy, J. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds376 · Cited by 35
Takashima, A. (2009) · Journal of Pharmacological Sciences · doi:10.1254/jphs.08r29fm · Cited by 34
Self-citationNeuroprotective effects of ginsenoside Rb1 on hippocampal neuronal injury and neurite outgrowth
Yuan, Q., Liu, J., He, J. H., Huang, L., Dou, L., & Wu, S. (2014) · Neural Regeneration Research · doi:10.4103/1673-5374.133137 · Cited by 34
Recruitment of active glycogen synthase kinase-3 into neuronal lipid rafts
Sui, Z., Kovács, A., & Maggirwar, S. B. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.087 · Cited by 35
Salemi, J., Obregon, D. F., Cobb, A., Reed, S., Sadic, E., Jin, J., Fernandez, F., Tan, J., & Giunta, B. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-3 · Cited by 28
Stress proteins in Alzheimer's disease
Smith, R. C., Rosen, K. M., Pola, R., & Magrané, J. (2005) · International Journal of Hyperthermia · doi:10.1080/02656730500133165 · Cited by 33
Advances in the development of kinase inhibitor therapeutics for Alzheimer's disease
Savage, M. J., & Gingrich, D. E. (2009) · Drug Development Research · doi:10.1002/ddr.20287 · Cited by 33
Bareiss, S. K., Kim, K., & Lu, Q. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22414 · Cited by 32
Huang, H.-J., Chen, S.-L., Chang, Y.-T., Chyuan, J., & Hsieh‐Li, H. M. (2018) · Nutrients · doi:10.3390/nu10121888 · Cited by 31
Sugano, T., Yanagita, T., Yokoo, H., Satoh, S., Kobayashi, H., & Wada, A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03846.x · Cited by 32
Rahman, S., Ayyagari, A., Jan, A. T., & Minakshi, R. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00030 · Cited by 33
Goodenough, S., Conrad, S., Skutella, T., & Behl, C. (2004) · Brain Research · doi:10.1016/j.brainres.2004.08.021 · Cited by 31
Aβ inhibits SREBP-2 activation through Akt inhibition
Mohamed, A., Viveiros, A., Williams, K., & Chaves, E. (2018) · Journal of Lipid Research · doi:10.1194/jlr.m076703 · Cited by 35
Mavroidi, B., Kaminari, A., Matiadis, D., Hadjipavlou‐Litina, D., Pelecanou, M., Tzinia, A. K., & Sagnou, M. (2022) · Brain Sciences · doi:10.3390/brainsci12060806 · Cited by 30
Growth factor treatment to overcome Alzheimer's dysfunctional signaling
Lauzon, M.-A., Daviau, A., Marcos, B., & Faucheux, N. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.02.018 · Cited by 30
Amyloid beta1-42 peptide regulates microtubule stability independently of tau
Pianu, B., Lefort, R., Thuiliere, L., Tabourier, E., & Bartolini, F. (2014) · Journal of Cell Science · doi:10.1242/jcs.143750 · Cited by 30
Li, B., Ryder, J. W., Yuan, S., Moore, S. A., Jr., Liu, F., Solenberg, P. J., Brune, K. A., Fox, N. W., Ni, B., Liu, R., et al. (2004) · Transgenic Research · doi:10.1023/b:trag.0000040039.44899.6f · Cited by 28
Bridging the Gap between Alzheimer’s Disease and Alzheimer’s-like Diseases in Animals
Gołaszewska, A., Bik, W., Motyl, T., & Orzechowski, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071664 · Cited by 31
RETRACTED: Characterising the spatial and temporal brain metal profile in a mouse model of tauopathy
Rao, S. S., Lago, L., de Vega, R. G., Bray, L., Hare, D. J., Clases, D., Doble, P., & Adlard, P. A. (2019) · Metallomics · doi:10.1039/c9mt00267g · Cited by 27
RetractedMukherjee, S., & Karati, D. (2023) · Pharmacological Research - Modern Chinese Medicine · doi:10.1016/j.prmcm.2023.100226 · Cited by 27
Lanzillotta, A., Sarnico, I., Benarese, M., Branca, C., Baiguera, C., Hutter‐Paier, B., Windisch, M., Spano, P., Imbimbo, B. P., & Pizzi, M. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9482-2 · Cited by 27
The contribution of C. elegans neurogenetics to understanding neurodegenerative diseases
Liang, J., McKinnon, I. A., & Rankin, C. H. (2020) · Journal of Neurogenetics · doi:10.1080/01677063.2020.1803302 · Cited by 28
Noël, A., Barrier, L., & Ingrand, S. S. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.06.020 · Cited by 24
Diabetes, Insulin and Alzheimer's Disease
Craft, S., & Christen, Y. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0 · Cited by 24
Zhang, Y., Ma, R.-H., Li, X., Zhang, J.-Y., Shi, H.-R., Wei, W., Luo, D., Wang, Q., Wang, J., & Liu, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00123 · Cited by 23
Lin, Y., Lee, C.-C., Chan, W.-L., Chang, W., Wu, Y., & Chang, J. (2011) · Toxicology · doi:10.1016/j.tox.2011.04.004 · Cited by 23
Serotonin Receptors as a Potential Target in the Treatment of Alzheimer’s Disease
Eremin, D. V., Kondaurova, E. M., Rodnyy, A. Y., Molobekova, C. A., Kudlay, D. A., & Naumenko, V. S. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923120064 · Cited by 23
Huang, H., Ou, H., & Hsieh, S. (2000) · Neurochemical Research · doi:10.1023/a:1007592007956 · Cited by 21
Untold New Beginnings: Adult Hippocampal Neurogenesis and Alzheimer’s Disease
Teixeira, C. M., Pallas‐Bazarra, N., Bolós, M., Terreros‐Roncal, J., Ávila, J., & Llorens-Martı́n, M. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179918 · Cited by 20
Wu, B., Kitagawa, K., Zhang, N., Liu, B., & Inagaki, C. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02805.x · Cited by 20
Asl, F. S. S., Malverdi, N., Mojahedian, F., Baziyar, P., & Nabi‐Afjadi, M. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141273 · Cited by 19
Zou, Y., Gan, C., Xin, Z., Zhang, H., Zhang, Q., Lee, T. H., Pan, X., & Chen, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.769229 · Cited by 19
Spears, W. E., Furgerson, M., Sweetnam, J. M. C., Evans, P. T., Gearing, M., Fechheimer, M., & Furukawa, R. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-74 · Cited by 19
Corbett, N. J., Gabbott, P. L. A., Klementiev, B., Davies, H. A., Colyer, F. M., Novikova, T., & Stewart, M. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071479 · Cited by 19
Aβ Deposition Does Not Cause the Aggregation of Endogenous Tau in Transgenic Mice
Xu, G. M., Gonzales, V., & Borchelt, D. (2002) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-200207000-00011 · Cited by 19
Huang, H., Ou, H., & Hsueh, S.-J. (1998) · Life Sciences · doi:10.1016/s0024-3205(98)00260-4 · Cited by 19
Blom, E. S., Wang, Y., Skoglund, L., Hansson, A. C., Ubaldi, M., Lourdusamy, A., Sommer, W. H., Mielke, M. L., Hyman, B. T., Heilig, M. A., et al. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/936580 · Cited by 18
Modulating Metals As A Therapeutic Strategy For Alzheimer’s Disease
Hung, L. W., & Barnham, K. J. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.32 · Cited by 18
Effect of arctigenin on neurological diseases: A review
Li, M., Jiang, H., Wang, Y., Xu, Z., Xu, H., Chen, Y., Zhu, J., Lin, Z., & Zhang, M. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116642 · Cited by 17
Parkin Attenuates Wild-Type τ Modification in the Presence of β-Amyloid and α-Synuclein
Moussa, C. (2008) · Journal of Molecular Neuroscience · doi:10.1007/s12031-008-9099-x · Cited by 17
Wu, X., Kosaraju, J., Zhou, W., & Tam, K. Y. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.01.003 · Cited by 16
Varshavskaya, K. B., Mitkevich, V. A., Makarov, A. А., & Barykin, E. P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315036 · Cited by 18
Gene expression profile in β-amyloid-treated SH-SY5Y neuroblastoma cells
Martínez, T., & Pascual, A. (2007) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2007.01.010 · Cited by 15
Kubo, T., Nishimura, S., & Oda, T. (2002) · Molecular Brain Research · doi:10.1016/s0169-328x(02)00416-3 · Cited by 14
Khan, R. I., Nirzhor, S. S. R., & Rashid, B. (2018) · Brain Sciences · doi:10.3390/brainsci8090162 · Cited by 12
Oat Extract Avenanthramide-C Reverses Hippocampal Long-Term Potentiation Decline in Tg2576 Mice
Lee, Y., Wang, M., Son, Y., Yang, E. J., Kang, M.-S., Kim, H., Kim, H., & Jo, J. (2021) · Molecules · doi:10.3390/molecules26206105 · Cited by 12
Multifunctional Role of Fas-Associated Death Domain Protein in Apoptosis
Kim, K. (2002) · BMB Reports · doi:10.5483/bmbrep.2002.35.1.001 · Cited by 13
Parkin Attenuates Wild-Type τ Modification in the Presence of β-Amyloid and α-Synuclein
Moussa, C. (2009) · Journal of Molecular Neuroscience · doi:10.1007/s12031-008-9167-2 · Cited by 11
GSK-3β orchestrates the inhibitory innervation of adult-born dentate granule cells in vivo
Moreno-Jiménez, E. P., Flor-García, M., Hernández-Vivanco, A., Terreros-Roncal, J., Rodríguez-Moreno, C. B., Toni, N., Mendez, P., & Llorens-Martín, M. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04874-w · Cited by 10
Wongjaikam, S., Nopparat, C., Boontem, P., Panmanee, J., Thasana, N., Shukla, M., & Govitrapong, P. (2024) · Biology · doi:10.3390/biology13070518 · Cited by 10
Engel, T., Goñi‐Oliver, P., Gómez‐Ramos, P., Morán, M. A., Lucas, J. J., Ávila, J., & Hernández, F. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.09.047 · Cited by 10
Metadata
- Authors
- Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K., & Imahori, K.
- Corresponding author
- Takashima, Akihiko
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 1996-01
- Volume
- 203
- Issue
- 1
- Pages
- 33-36
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W1986537744
- Cited by
- 260
- References
- 18
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 5 · 2023: 9 · 2022: 4 · 2021: 9 · 2020: 5 · 2019: 11 · 2018: 12 · 2017: 3 · 2016: 3 · 2015: 7 · 2014: 15 · 2013: 13 · 2012: 13
- FWCI
- 3.21
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid beta 25-35, Aβ40, phosphatidylinositol 3-kinase, glycogen synthase kinase-3β, tau phosphorylation, paired helical filaments, hippocampal neurons, neuronal cell death, wortmannin, Alzheimer's disease
- MeSH terms
- Wortmannin, Alzheimer Disease, Androstadienes, Animals, Cells, Cultured, Dose-Response Relationship, Drug, Enzyme Inhibitors, Glycogen Synthase, Hippocampus, Phosphotransferases, Amyloid beta-Protein Precursor, tau Proteins, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review