[1]
|
Barker, W.W., Luis, C.A., Kashuba, A., Luis, M., Harwood, D.G., Loewenstein, D., Waters, C., Jimison, P., Shepherd, E., Sevush, S., Graff-Radford, N., Newland, D., Todd, M., Miller, B., Gold, M., Heilman, K., Doty, L., Goodman, I., Robinson, B., Gary, P., Dennis, D. and Duara, R. (2002) Relative Frequencies of Alzheimer Disease, Lewy Body, Vascular and Frontotemporal Dementia, and Hippocampal Sclerosis in the State of Florida Brain Bank. Alzheimer Disease & Associated Disorders, 16, 203-212. https://doi.org/10.1097/00002093-200210000-00001
|
[2]
|
Rajan, K.B., Weuve, J., Barnes, L.L., Mcaninch, E.A., Wilson, R.S. and Evans, D.A. (2021) Population Estimate of People with Clinical Alzheimer’s Disease and Mild Cognitive Impairment in the United States (2020-2060). Alzheimer’s & Dementia, 17, 1966-1975. https://doi.org/10.1002/alz.12362
|
[3]
|
Nichols, E., Steinmetz, J.D., Vollset, S.E., Fukutaki, K., Chalek, J., Abd-Allah, F., Abdoli, A., Abualhasan, A., Abu-Gharbieh, E., Akram, T.T., Al Hamad, H., Alahdab, F., Alanezi, F.M., Alipour, V., Almustanyir, S., Amu, H., Ansari, I., Arabloo, J., Ashraf, T., Bezabih, Y.M., et al. (2022) Estimation of the Global Prevalence of Dementia in 2019 and Forecasted Prevalence in 2050: An Analysis for the Global Burden of Disease Study 2019. The Lancet Public Health, 7, e105-e125.
https://doi.org/10.1016/S2468-2667(21)00249-8
|
[4]
|
Schultz, C., Del Tredici, K. and Braak, H. (2004) Neuropathology of Alzheimer’s Disease. In: Richter, R.W., Richter, B.Z., Eds., Alzheimer’s Disease Current Clinical Neurology, Humana Press, Totowa, NJ.
|
[5]
|
Hippius, H. and Neundörfer, G. (2003) The Discovery of Alzheimer’s Disease. Dialogues in Clinical Neuroscience, 5, 101-108.
https://doi.org/10.31887/DCNS.2003.5.1/hhippius
|
[6]
|
Kametani, F. and Hasegawa, M. (2018) Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer’s Disease. Frontiers in Neuroscience, 12. Article 25.
https://doi.org/10.3389/fnins.2018.00025
|
[7]
|
Liu, P.-P., Xie, Y., Meng, X.-Y. and Kang, J.-S. (2019) History and Progress of Hypotheses and Clinical Trials for Alzheimer’s Disease. Signal Transduction and Targeted Therapy, 4, Article No. 29. https://doi.org/10.1038/s41392-019-0063-8
|
[8]
|
Barbier, P., Zejneli, O., Martinho, M., Lasorsa, A., Belle, V., Smet-Nocca, C., Tsvetkov, P.O., Devred, F. and Landrieu, I. (2019) Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects. Frontiers in Aging Neuroscience, 11, Article 204. https://doi.org/10.3389/fnagi.2019.00204
|
[9]
|
Demattos, R., Lu, J., Tang, Y., Racke, M., Delong, C., Tzaferis, J., Hole, J., Forster, B., Mcdonnell, P., Liu, F., Kinley, R., Jordan, W. and Hutton, M. (2012) A Plaque-Specific Antibody Clears Existing β-Amyloid Plaques in Alzheimer’s Disease Mice. Neuron, 76, 908-920. https://doi.org/10.1016/j.neuron.2012.10.029
|
[10]
|
Kiani Shabestari, S., Morabito, S., Danhash, E.P., Mcquade, A., Sanchez, J.R., Miyoshi, E., Chadarevian, J.P., Claes, C., Coburn, M.A., Hasselmann, J., Hidalgo, J., Tran, K.N., Martini, A.C., Chang Rothermich, W., Pascual, J., Head, E., Hume, D.A., Pridans, C., Davtyan, H., Swarup, V. and Blurton-Jones, M. (2022) Absence of Microglia Promotes Diverse Pathologies and Early Lethality in Alzheimer’s Disease Mice. Cell Reports, 39, Article ID: 110961. https://doi.org/10.1016/j.celrep.2022.110961
|
[11]
|
Jennings, B.H. (2011) Drosophila—A Versatile Model in Biology & Medicine. Materials Today, 14, 190-195. https://doi.org/10.1016/S1369-7021(11)70113-4
|
[12]
|
Pandey, U.B. and Nichols, C.D. (2011) Human Disease Models in Drosophila melanogaster and the Role of the Fly in Therapeutic Drug Discovery. Pharmacological Reviews, 63, 411-436. https://doi.org/10.1124/pr.110.003293
|
[13]
|
Reiter, L.T., Potocki, L., Chien, S., Gribskov, M. and Bier, E. (2001) A Systematic Analysis of Human Disease-Associated Gene Sequences in Drosophila melanogaster. Genome Research, 11, 1114-1125. https://doi.org/10.1101/gr.169101
|
[14]
|
Bier, E. (2005) Drosophila, the Golden Bug, Emerges as a Tool for Human Genetics. Nature Reviews Genetics, 6, 9-23. https://doi.org/10.1038/nrg1503
|
[15]
|
Mcguire, S.E., Deshazer, M. and Davis, R.L. (2005) Thirty Years of Olfactory Learning and Memory Research in Drosophila melanogaster. Progress in Neurobiology, 76, 328-347. https://doi.org/10.1016/j.pneurobio.2005.09.003
|
[16]
|
Stocker, H. and Gallant, P. (2008) Getting Started. Methods in Molecular Biology, 420, 27-44. https://doi.org/10.1007/978-1-59745-583-1_2
|
[17]
|
Sun, Y., Yolitz, J., Wang, C., Spangler, E., Zhan, M. and Zou, S. (2013) Aging Studies in Drosophila melanogaster. Methods in Molecular Biology, 1048, 77-93.
https://doi.org/10.1007/978-1-62703-556-9_7
|
[18]
|
Fossgreen, A., Brückner, B., Czech, C., Masters, C.L., Beyreuther, K. and Paro, R. (1998) Transgenic Drosophila Expressing Human Amyloid Precursor Protein Show γ-Secretase Activity and a Blistered-Wing Phenotype. Proceedings of the National Academy of Sciences, 95, 13703-13708. https://doi.org/10.1073/pnas.95.23.13703
|
[19]
|
Sang, T.-K. and Jackson, G.R. (2005) Drosophila Models of Neurodegenerative Disease. NeuroRX, 2, 438-446. https://doi.org/10.1602/neurorx.2.3.438
|
[20]
|
Prüßing, K., Voigt, A. and Schulz, J.B. (2013) Drosophila Melanogaster as a Model Organism for Alzheimer’s Disease. Molecular Neurodegeneration, 8, Article No. 35.
https://doi.org/10.1186/1750-1326-8-35
|
[21]
|
O’brien, R.J. and Wong, P.C. (2011) Amyloid Precursor Protein Processing and Alzheimer’s Disease. Annual Review of Neuroscience, 34, 185-204.
https://doi.org/10.1146/annurev-neuro-061010-113613
|
[22]
|
Tyan, S.-H., Shih, A.Y.-J., Walsh, J.J., Maruyama, H., Sarsoza, F., Ku, L., Eggert, S., Hof, P.R., Koo, E.H. and Dickstein, D.L. (2012) Amyloid Precursor Protein (APP) Regulates Synaptic Structure and Function. Molecular and Cellular Neuroscience, 51, 43-52. https://doi.org/10.1016/j.mcn.2012.07.009
|
[23]
|
López-Toledano, M.A. and Shelanski, M.L. (2007) Increased Neurogenesis in Young Transgenic Mice Overexpressing Human APPSw,Ind. Journal of Alzheimer’s Disease, 12, 229-240. https://doi.org/10.3233/JAD-2007-12304
|
[24]
|
Zhou, Z.-D., Chan, C.H.-S., Ma, Q.-H., Xu, X.-H., Xiao, Z.-C. and Tan, E.-K. (2011) The Roles of Amyloid Precursor Protein (APP) in Neurogenesis. Cell Adhesion & Migration, 5, 280-292. https://doi.org/10.4161/cam.5.4.16986
|
[25]
|
Zheng, H. and Koo, E.H. (2011) Biology and Pathophysiology of the Amyloid Precursor Protein. Molecular Neurodegeneration, 6, Article No. 27.
https://doi.org/10.1186/1750-1326-6-27
|
[26]
|
Coronel, R., Bernabeu-Zornoza, A., Palmer, C., Muñiz-Moreno, M., Zambrano, A., Cano, E. and Liste, I. (2018) Role of Amyloid Precursor Protein (APP) and Its Derivatives in the Biology and Cell Fate Specification of Neural Stem Cells. Molecular Neurobiology, 55, 7107-7117. https://doi.org/10.1007/s12035-018-0914-2
|
[27]
|
Pirooznia, S.K., Sarthi, J., Johnson, A.A., Toth, M.S., Chiu, K., Koduri, S. and Elefant, F. (2012) Tip60 HAT Activity Mediates APP Induced Lethality and Apoptotic Cell Death in the CNS of a Drosophila Alzheimer’s Disease Model. PLOS ONE, 7, e41776. https://doi.org/10.1371/journal.pone.0041776
|
[28]
|
Utley, R.T. and Côté, J. (2003) The MYST Family of Histone Acetyltransferases. Current Topics in Microbiology and Immunology, 274, 203-236.
https://doi.org/10.1007/978-3-642-55747-7_8
|
[29]
|
Ikura, T., Ogryzko, V.V., Grigoriev, M., Groisman, R., Wang, J., Horikoshi, M., Scully, R., Qin, J. and Nakatani, Y. (2000) Involvement of the TIP60 Histone Acetylase Complex in DNA Repair and Apoptosis. Cell, 102, 463-473.
https://doi.org/10.1016/S0092-8674(00)00051-9
|
[30]
|
Li, Z. and Rasmussen, L.J. (2020) TIP60 in Aging and Neurodegeneration. Ageing Research Reviews, 64, Article ID: 101195. https://doi.org/10.1016/j.arr.2020.101195
|
[31]
|
Wang, X., Wang, Z., Chen, Y., Huang, X., Hu, Y., Zhang, R., Ho, M.S. and Xue, L. (2014) FoxO Mediates App-Induced AICD-Dependent Cell Death. Cell Death & Disease, 5, e1233. https://doi.org/10.1038/cddis.2014.196
|
[32]
|
Webb, A.E. and Brunet, A. (2014) FOXO Transcription Factors: Key Regulators of Cellular Quality Control. Trends in Biochemical Sciences, 39, 159-169.
https://doi.org/10.1016/j.tibs.2014.02.003
|
[33]
|
Zhang, X., Tang, N., Hadden, T.J. and Rishi, A.K. (2011) Akt, Foxo and Regulation of Apoptosis. Biochimica Et Biophysica Acta (BBA)-Molecular Cell Research, 1813, 1978-1986. https://doi.org/10.1016/j.bbamcr.2011.03.010
|
[34]
|
O’connor, L. (1998) Bim: A Novel Member of the Bcl-2 Family That Promotes Apoptosis. The EMBO Journal, 17, 384-395. https://doi.org/10.1093/emboj/17.2.384
|
[35]
|
Peng, F., Zhao, Y., Huang, X., Chen, C., Sun, L., Zhuang, L. and Xue, L. (2015) Loss of Polo Ameliorates App-Induced Alzheimer’s Disease-Like Symptoms in Drosophila. Scientific Reports, 5, Article ID: 16816. https://doi.org/10.1038/srep16816
|
[36]
|
Zitouni, S., Nabais, C., Jana, S.C., Guerrero, A. and Bettencourt-Dias, M. (2014) Polo-Like Kinases: Structural Variations Lead to Multiple Functions. Nature Reviews Molecular Cell Biology, 15, 433-452. https://doi.org/10.1038/nrm3819
|
[37]
|
Archambault, V., Lépine, G. and Kachaner, D. (2015) Understanding the Polo Kinase Machine. Oncogene, 34, 4799-4807. https://doi.org/10.1038/onc.2014.451
|
[38]
|
Song, B., Davis, K., Liu, X.S., Lee, H.-G., Smith, M. and Liu, X. (2011) Inhibition of Polo-Like Kinase 1 Reduces Beta-Amyloid-Induced Neuronal Cell Death in Alzheimer’s Disease. Aging, 3, 846-851. https://doi.org/10.18632/aging.100382
|
[39]
|
Lee, J.S., Lee, Y., André, E.A., Lee, K.J., Nguyen, T., Feng, Y., Jia, N., Harris, B.T., Burns, M.P. and Pak, D.T.S. (2019) Inhibition of Polo-Like Kinase 2 Ameliorates Pathogenesis in Alzheimer’s Disease Model Mice. PLOS ONE, 14, e0219691.
https://doi.org/10.1371/journal.pone.0219691
|
[40]
|
Rockenstein, E., Mante, M., Alford, M., Adame, A., Crews, L., Hashimoto, M., Esposito, L., Mucke, L. and Masliah, E. (2005) High β-Secretase Activity Elicits Neurodegeneration in Transgenic Mice despite Reductions in Amyloid-β Levels. Journal of Biological Chemistry, 280, 32957-32967. https://doi.org/10.1074/jbc.M507016200
|
[41]
|
Cavanagh, C., Colby-Milley, J., Bouvier, D., Farso, M., Chabot, J.-G., Quirion, R. and Krantic, S. (2013) βCTF-Correlated Burst of Hippocampal TNFα Occurs at a Very Early, Pre-Plaque Stage in the TgCRND8 Mouse Model of Alzheimer’s Disease. Journal of Alzheimer’s Disease, 36, 233-238.
https://doi.org/10.3233/JAD-122131
|
[42]
|
Mondragón-Rodríguez, S., Gu, N., Manseau, F. and Williams, S. (2018) Alzheimer’s Transgenic Model Is Characterized by Very Early Brain Network Alterations and β-CTF Fragment Accumulation: Reversal by β-Secretase Inhibition. Frontiers in Cellular Neuroscience, 12, Article 121. https://doi.org/10.3389/fncel.2018.00121
|
[43]
|
Cai, Y., Xiong, K., Zhang, X.-M., Cai, H., Luo, X.-G., Feng, J.-C., Clough, R.W., Struble, R.G., Patrylo, P.R., Chu, Y., Kordower, J.H. and Yan, X.-X. (2010) β-Secretase-1 Elevation in Aged Monkey and Alzheimer’s Disease Human Cerebral Cortex Occurs around the Vasculature in Partnership with Multisystem Axon Terminal Pathogenesis and β-Amyloid Accumulation. European Journal of Neuroscience, 32, 1223-1238. https://doi.org/10.1111/j.1460-9568.2010.07376.x
|
[44]
|
Pera, M., Larrea, D., Guardia-Laguarta, C., Montesinos, J., Velasco, K.R., Agrawal, R. R., Xu, Y., Chan, R.B., Di Paolo, G., Mehler, M.F., Perumal, G.S., Macaluso, F.P., Freyberg, Z.Z., Acin-Perez, R., Enriquez, J.A., Schon, E.A. and Area-Gomez, E. (2017) Increased Localization of App-C99 in Mitochondria-Associated ER Membranes Causes Mitochondrial Dysfunction in Alzheimer Disease. The EMBO Journal, 36, 3356-3371. https://doi.org/10.15252/embj.201796797
|
[45]
|
Bourgeois, A., Lauritzen, I., Lorivel, T., Bauer, C., Checler, F. and Pardossi-Piquard, R. (2018) Intraneuronal Accumulation of c99 Contributes to Synaptic Alterations, Apathy-Like Behavior, and Spatial Learning Deficits in 3×TgAD and 2×TgAD Mice. Neurobiology of Aging, 71, 21-31.
https://doi.org/10.1016/j.neurobiolaging.2018.06.038
|
[46]
|
Rimal, S., Li, Y., Vartak, R., Geng, J., Tantray, I., Li, S., Huh, S., Vogel, H., Glabe, C., Grinberg, L.T., Spina, S., Seeley, W.W., Guo, S. and Lu, B. (2021) Inefficient Quality Control of Ribosome Stalling during APP Synthesis Generates Cat-Tailed Species That Precipitate Hallmarks of Alzheimer’s Disease. Acta Neuropathologica Communications, 9, Article No. 169. https://doi.org/10.1186/s40478-021-01268-6
|
[47]
|
Udagawa, T., Seki, M., Okuyama, T., Adachi, S., Natsume, T., Noguchi, T., Matsuzawa, A. and Inada, T. (2021) Failure to Degrade Cat-Tailed Proteins Disrupts Neuronal Morphogenesis and Cell Survival. Cell Reports, 34, Article ID: 108599.
https://doi.org/10.1016/j.celrep.2020.108599
|
[48]
|
Masters, C.L., Simms, G., Weinman, N.A., Multhaup, G., McDonald, B.L. and Beyreuther, K. (1985) Amyloid Plaque Core Protein in Alzheimer Disease and Down Syndrome. Proceedings of the National Academy of Sciences, 82, 4245-4249.
https://doi.org/10.1073/pnas.82.12.4245
|
[49]
|
Selkoe, D.J. and Hardy, J. (2016) The Amyloid Hypothesis of Alzheimer’s Disease at 25 Years. EMBO Molecular Medicine, 8, 595-608.
https://doi.org/10.15252/emmm.201606210
|
[50]
|
Woloshin, S. and Kesselheim, A.S. (2022) What to Know About the Alzheimer Drug Aducanumab (Aduhelm). JAMA Internal Medicine, 182, Article No. 892.
https://doi.org/10.1001/jamainternmed.2022.1039
|
[51]
|
Iijima-Ando, K. and Iijima, K. (2009) Transgenic Drosophila Models of Alzheimer’s Disease and Tauopathies. Brain Structure and Function, 214, 245-262.
https://doi.org/10.1007/s00429-009-0234-4
|
[52]
|
Singh, A. and Irvine, K.D. (2011) Drosophila as a Model for Understanding Development and Disease. Developmental Dynamics, 241, 1-2.
https://doi.org/10.1002/dvdy.23712
|
[53]
|
Kumar, J.P. (2017) The Fly Eye: Through the Looking Glass. Developmental Dynamics, 247, 111-123. https://doi.org/10.1002/dvdy.24585
|
[54]
|
Hua, H., Münter, L., Harmeier, A., Georgiev, O., Multhaup, G. and Schaffner, W. (2011) Toxicity of Alzheimer’s Disease-Associated Aβ Peptide Is Ameliorated in a Drosophila Model by Tight Control of Zinc and Copper Availability. Biological Chemistry, 392, 919-926. https://doi.org/10.1515/BC.2011.084
|
[55]
|
Sarkar, A., Gogia, N., Glenn, N., Singh, A., Jones, G., Powers, N., Srivastava, A., Kango-Singh, M. and Singh, A. (2018) A Soy Protein Lunasin Can Ameliorate Amyloid-Beta 42 Mediated Neurodegeneration in Drosophila Eye. Scientific Reports, 8, Article No. 13545. https://doi.org/10.1038/s41598-018-31787-7
|
[56]
|
De lumen, B.O. (2005) Lunasin: A Cancer-Preventive Soy Peptide. Nutrition Reviews, 63, 16-21. https://doi.org/10.1111/j.1753-4887.2005.tb00106.x
|
[57]
|
Jiang, Q., Pan, Y., Cheng, Y., Li, H., Liu, D. and Li, H. (2016) Lunasin Suppresses the Migration and Invasion of Breast Cancer Cells by Inhibiting Matrix Metalloproteinase-2/-9 via the FAK/Akt/ERK and NF-κB Signaling Pathways. Oncology Reports, 36, 253-262. https://doi.org/10.3892/or.2016.4798
|
[58]
|
Wan, X., Liu, H., Sun, Y., Zhang, J., Chen, X., and Chen, N. (2017) Lunasin: A Promising Polypeptide for the Prevention and Treatment of Cancer. Oncology Letters, 13, 3997-4001. https://doi.org/10.3892/ol.2017.6017
|
[59]
|
Davis, R.L. (1993) Mushroom Bodies and Drosophila Learning. Neuron, 11, 1-14.
https://doi.org/10.1016/0896-6273(93)90266-T
|
[60]
|
Heisenberg, M. (2003) Mushroom Body Memoir: From Maps to Models. Nature Reviews Neuroscience, 4, 266-275. https://doi.org/10.1038/nrn1074
|
[61]
|
Pech, U., Dipt, S., Barth, J., Singh, P., Jauch, M., Thum, A.S., Fiala, A. and Riemensperger, T. (2013) Mushroom Body Miscellanea: Transgenic Drosophila Strains Expressing Anatomical and Physiological Sensor Proteins in Kenyon Cells. Frontiers in Neural Circuits, 7, Article 147. https://doi.org/10.3389/fncir.2013.00147
|
[62]
|
Iijima-Ando, K., Hearn, S.A., Granger, L., Shenton, C., Gatt, A., Chiang, H.-C., Hakker, I., Zhong, Y. and Iijima, K. (2008) Overexpression of Neprilysin Reduces Alzheimer Amyloid-β42 (Aβ42)-Induced Neuron Loss and Intraneuronal Aβ42 Deposits but Causes a Reduction in cAMP-Responsive Element-Binding Protein-Mediated Transcription, Age-Dependent Axon Pathology, and Premature Death in Drosophila. Journal of Biological Chemistry, 283, 19066-19076.
https://doi.org/10.1074/jbc.M710509200
|
[63]
|
Nalivaeva, N., Zhuravin, I. and Turner, A. (2020) Neprilysin Expression and Functions in Development, Ageing and Disease. Mechanisms of Ageing and Development, 192, Article ID: 111363. https://doi.org/10.1016/j.mad.2020.111363
|
[64]
|
El-Amouri, S.S., Zhu, H., Yu, J., Marr, R., Verma, I.M. and Kindy, M.S. (2008) Neprilysin: An Enzyme Candidate to Slow the Progression of Alzheimer’s Disease. The American Journal of Pathology, 172, 1342-1354.
https://doi.org/10.2353/ajpath.2008.070620
|
[65]
|
Iijima-Ando, K., Hearn, S.A., Shenton, C., Gatt, A., Zhao, L. and Iijima, K. (2009) Mitochondrial Mislocalization Underlies Aβ42-Induced Neuronal Dysfunction in a Drosophila Model of Alzheimer’s Disease. PLOS ONE, 4, e8310.
https://doi.org/10.1371/journal.pone.0008310
|
[66]
|
Wang, X. and Davis, R.L. (2020) Early Mitochondrial Fragmentation and Dysfunction in a Drosophila Model for Alzheimer’s Disease. Molecular Neurobiology, 58, 143-155. https://doi.org/10.1007/s12035-020-02107-w
|
[67]
|
Brand, M.D., Orr, A.L., Perevoshchikova, I.V. and Quinlan, C.L. (2013) The Role of Mitochondrial Function and Cellular Bioenergetics in Ageing and Disease. British Journal of Dermatology, 169, 1-8. https://doi.org/10.1111/bjd.12208
|
[68]
|
Mandelkow, E. (1998) Tau in Alzheimer’s Disease. Trends in Cell Biology, 8, 425-427. https://doi.org/10.1016/S0962-8924(98)01368-3
|
[69]
|
Iqbal, K., Liu, F., Gong, C.-X. and Grundke-Iqbal, I. (2010) Tau in Alzheimer Disease and Related Tauopathies. Current Alzheimer Research, 7, 656-664.
https://doi.org/10.2174/156720510793611592
|
[70]
|
Mandelkow, E.-M., Biernat, J., Drewes, G., Gustke, N., Trinczek, B. and Mandelkow, E. (1995) Tau Domains, Phosphorylation, and Interactions with Microtubules. Neurobiology of Aging, 16, 355-362. https://doi.org/10.1016/0197-4580(95)00025-A
|
[71]
|
Alonso, A.C., Zaidi, T., Grundke-Iqbal, I. and Iqbal, K. (1994) Role of Abnormally Phosphorylated Tau in the Breakdown of Microtubules in Alzheimer Disease. Proceedings of the National Academy of Sciences, 91, 5562-5566.
https://doi.org/10.1073/pnas.91.12.5562
|
[72]
|
Li, B., Chohan, M.O., Grundke-Iqbal, I. and Iqbal, K. (2007) Disruption of Microtubule Network by Alzheimer Abnormally Hyperphosphorylated Tau. Acta Neuropathologica, 113, 501-511. https://doi.org/10.1007/s00401-007-0207-8
|
[73]
|
Medeiros, R., Baglietto-vargas, D. and Laferla, F.M. (2010) The Role of Tau in Alzheimer’s Disease and Related Disorders. CNS Neuroscience & Therapeutics, 17, 514-524. https://doi.org/10.1111/j.1755-5949.2010.00177.x
|
[74]
|
Beharry, C., Alaniz, M.E. and Alonso, A.D.C. (2013) Expression of Alzheimer-Like Pathological Human Tau Induces a Behavioral Motor and Olfactory Learning Deficit in Drosophila Melanogaster. Journal of Alzheimer’s Disease, 37, 539-550.
https://doi.org/10.3233/JAD-130617
|
[75]
|
Mershin, A., Pavlopoulos, E., Fitch, O., Braden, B.C., Nanopoulos, D.V. and Skoulakis, E.M.C. (2004) Learning and Memory Deficits upon TAU Accumulation in Drosophila Mushroom Body Neurons. Learning & Memory, 11, 277-287.
https://doi.org/10.1101/lm.70804
|
[76]
|
Nishimura, I., Yang, Y. and Lu, B. (2004) PAR-1 Kinase Plays an Initiator Role in a Temporally Ordered Phosphorylation Process That Confers Tau Toxicity in Drosophila. Cell, 116, 671-682. https://doi.org/10.1016/S0092-8674(04)00170-9
|
[77]
|
Zhang, B., Li, Q., Chu, X., Sun, S. and Chen, S. (2016) Salidroside Reduces Tau Hyperphosphorylation via Up-Regulating Gsk-3β Phosphorylation in a Tau Transgenic Drosophila Model of Alzheimer’s Disease. Translational Neurodegeneration, 5, Article No. 21. https://doi.org/10.1186/s40035-016-0068-y
|
[78]
|
Shi, K., Wang, X., Zhu, J., Cao, G., Zhang, K. and Su, Z. (2015) Salidroside Protects Retinal Endothelial Cells against Hydrogen Peroxide-Induced Injury via Modulating Oxidative Status and Apoptosis. Bioscience, Biotechnology, and Biochemistry, 79, 1406-1413. https://doi.org/10.1080/09168451.2015.1038212
|
[79]
|
Liu, S., Yu, X., Hu, B., Zou, Y., Li, J., Bo, L. and Deng, X. (2015) Salidroside Rescued Mice from Experimental Sepsis through Anti-Inflammatory and Anti-Apoptosis Effects. Journal of Surgical Research, 195, 277-283.
https://doi.org/10.1016/j.jss.2015.01.021
|
[80]
|
Darshit, B.S. and Ramanathan, M. (2015) Activation of AKT1/GSK-3β/β-Catenin-TRIM11/Survivin Pathway by Novel GSK-3β Inhibitor Promotes Neuron Cell Survival: Study in Differentiated SH-SY5Y Cells in OGD Model. Molecular Neurobiology, 53, 6716-6729. https://doi.org/10.1007/s12035-015-9598-z
|
[81]
|
Ma, T. (2014) GSK3 in Alzheimer’s Disease: Mind the Isoforms. Journal of Alzheimer’s Disease, 39, 707-710. https://doi.org/10.3233/JAD-131661
|
[82]
|
Anupama, K.P., Antony, A., Shilpa, O., Raghu, S.V. and Gurushankara, H.P. (2022) Jatamansinol from Nardostachys jatamansi Ameliorates Tau-Induced Neurotoxicity in Drosophila Alzheimer’s Disease Model. Molecular Neurobiology, 59, 6091-6106.
https://doi.org/10.1007/s12035-022-02964-7
|
[83]
|
Liu, Q.F., Jeon, Y., Sung, Y.-W., Lee, J.H., Jeong, H., Kim, Y.-M., Yun, H.S., Chin, Y.-W., Jeon, S., Cho, K.S. and Koo, B.-S. (2018) Nardostachys jatamansi Ethanol Extract Ameliorates Aβ42 Cytotoxicity. Biological and Pharmaceutical Bulletin, 41, 470-477. https://doi.org/10.1248/bpb.b17-00750
|
[84]
|
Reinikainen, K.J., Soininen, H. and Riekkinen, P.J. (1990) Neurotransmitter Changes in Alzheimer’s Disease: Implications to Diagnostics and Therapy. Journal of Neuroscience Research, 27, 576-586. https://doi.org/10.1002/jnr.490270419
|