Amyloid beta-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer's disease: Implications for synaptic dysfunction and neuronal damage

Alzheimer's Disease: Genes, Proteins, and Therapy

Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063 · see citing works

The phosphatidylinositol 3-Kinase–AKT pathway in human cancer

Vivanco, I., & Sawyers, C. L. (2002) · Nature reviews. Cancer · doi:10.1038/nrc839 · Cited by 6,041 · see citing works

2013 Alzheimer's disease facts and figures

Thies, W. H., & Bleiler, L. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.02.003 · Cited by 3,331 · see citing works

Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · see citing works

Pathways towards and Away from Alzheimer’s Disease

Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052 · see citing works

Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo

Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336 · see citing works

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

Shimizu, S., Narita, M., Tsujimoto, Y., & Tsujimoto, Y. (1999) · Nature · doi:10.1038/20959 · Cited by 2,178 · see citing works

Intracellular amyloid-β in Alzheimer's disease

LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942 · see citing works

Effect of oestrogen during menopause on risk and age at onset of Alzheimer's disease

Tang, M., Jacobs, D. M., Stern, Y., Marder, K. S., Schofield, P., Gurland, B. J., Andrews, H., & Mayeux, R. P. (1996) · The Lancet · doi:10.1016/s0140-6736(96)03356-9 · Cited by 1,647 · see citing works

The glamour and gloom of glycogen synthase kinase-3

Jope, R. S., & Johnson, G. V. W. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.12.004 · Cited by 1,522 · see citing works

Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease

Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,488 · see citing works

Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation

Hoeflich, K. P., Luo, J., Rubie, E. A., Tsao, M., Jin, O., & Woodgett, J. R. (2000) · Nature · doi:10.1038/35017574 · Cited by 1,394 · see citing works

Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease

DeMattos, R. B., Bales, K. R., Cummins, D. J., Dodart, J.-C., Paul, S. M., & Holtzman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261398 · Cited by 1,298 · see citing works

The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases

MCGEER, P., & MCGEER, E. (1995) · Brain Research Reviews · doi:10.1016/0165-0173(95)00011-9 · Cited by 1,287 · see citing works

Ten years of protein kinase B signalling: a hard Akt to follow

Brazil, D. P., & Hemmings, B. A. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01958-2 · Cited by 1,177 · see citing works

Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression

Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · see citing works

Role of Glycogen Synthase Kinase-3 in the Phosphatidylinositol 3-Kinase/Akt Cell Survival Pathway

Pap, M., & Cooper, G. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.19929 · Cited by 1,046 · see citing works

Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer’s disease

Reddy, P. H., & Beal, M. F. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.002 · Cited by 975 · see citing works

Mild cognitive impairment can be distinguished from Alzheimer disease and normal aging for clinical trials

Grundman, M. (2004) · Archives of Neurology · doi:10.1001/archneur.61.1.59 · Cited by 972 · see citing works

Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease

Yao, J., Irwin, R. W., Zhao, L., Nilsen, J., Hamilton, R. T., & Brinton, R. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903563106 · Cited by 940 · see citing works

Oxidative damage in Alzheimer's

Smith, M. A., Perry, G. L., Richey, P. L., Sayrec, L. M., Anderson, V. E., Beal, M. F., & Kowall, N. W. (1996) · Nature · doi:10.1038/382120b0 · Cited by 897 · see citing works

GSK3: a multifaceted kinase in Wnt signaling

Wu, D., & Pan, W. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.10.002 · Cited by 862 · see citing works

Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage

Mańczak, M., Calkins, M. J., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr139 · Cited by 830 · see citing works

Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction

Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792 · see citing works

Glycogen synthase kinase-3 (GSK3): Inflammation, diseases, and therapeutics

Jope, R. S., Yuskaitis, C. J., & Beurel, E. (2007) · Neurochemical Research · doi:10.1007/s11064-006-9128-5 · Cited by 774 · see citing works

Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer β-amyloid peptide in rodent

Greig, N. H., Utsuki, T., Ingram, D. K., Wang, Y., Pepeu, G., Scali, C., Yu, Q.-S., Mamczarz, J., Holloway, H. W., Giordano, T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508575102 · Cited by 745 · see citing works

Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease

Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738 · see citing works

Mitochondrial Binding of Hexokinase II Inhibits Bax-induced Cytochrome c Release and Apoptosis

Pastorino, J. G., Shulga, N., & Hoek, J. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109950200 · Cited by 714 · see citing works

The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae

Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V., Ito, A., Winblad, B., Glaser, E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806192105 · Cited by 693 · see citing works

Dietary Intake of Antioxidant Nutrients and the Risk of Incident Alzheimer Disease in a Biracial Community Study

Morris, M. C. (2002) · JAMA · doi:10.1001/jama.287.24.3230 · Cited by 678 · see citing works

Hexokinase-Mitochondria Interaction Mediated by Akt Is Required to Inhibit Apoptosis in the Presence or Absence of Bax and Bak

Majewski, N., Nogueira, V., Bhaskar, P. T., Coy, P. E., Skeen, J. E., Gottlob, K., Chandel, N. S., Thompson, C. B., Robey, R. B., & Hay, N. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.014 · Cited by 633 · see citing works

Emerging roles of Wnts in the adult nervous system

Inestrosa, N. C., & Arenas, E. (2009) · Nature reviews. Neuroscience · doi:10.1038/nrn2755 · Cited by 611 · see citing works

Cytochrome oxidase deficiency in Alzheimer’s disease

Parker, W. D., Filley, C. M., & Parks, J. K. (1990) · Neurology · doi:10.1212/wnl.40.8.1302 · Cited by 598 · see citing works

Oxidative stress in the brain: Novel cellular targets that govern survival during neurodegenerative disease

Chong, Z. Z., Li, F., & Maiese, K. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.02.004 · Cited by 536 · see citing works

Cholinesterase inhibitors for patients with Alzheimer's disease: systematic review of randomised clinical trials

Kaduszkiewicz, H., Zimmermann, T., Beck-Bornholdt, H.-P., & van den Bussche, H. (2005) · BMJ · doi:10.1136/bmj.331.7512.321 · Cited by 522 · see citing works

A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients

Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475 · see citing works

Mitochondria-targeted antioxidants protect against amyloid-β toxicity in Alzheimer's disease neurons

Manczak, M., Mao, P., Calkins, M. J., Cornea, A., Reddy, A. P., Murphy, M. P., Szeto, H. H., Park, B., & Reddy, P. H. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100564 · Cited by 469 · see citing works

Increased oxidative damage in nuclear and mitochondrial DNA in Alzheimer's disease

Wang, J., Xiong, S., Xie, C., Markesbery, W. R., & Lovell, M. A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03053.x · Cited by 452 · see citing works

Alzheimer's disease: the two-hit hypothesis.

Zhu, X.-W., Raina, A., Perry, G., & Smith, M. A. (2004) · Lancet Neurology · doi:10.1016/s1474-4422(04)00707-0 · Cited by 449 · see citing works

Inhibition of GSK3β-mediated BACE1 expression reduces Alzheimer-associated phenotypes

Ly, P. T. T., Wu, Y., Zou, H., Wang, R., Zhou, W., Kinoshita, A., Zhang, M., Yang, Y., Cai, F., Woodgett, J., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64516 · Cited by 442 · see citing works

Role of Glycogen Synthase Kinase-3β in Neuronal Apoptosis Induced by Trophic Withdrawal

Hetman, M., Cavanaugh, J. E., Kimelman, D., & Xia, Z. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-07-02567.2000 · Cited by 440 · see citing works

Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease

Liu, F., Shi, J., Tanimukai, H., Gu, J., Gu, J., Grundke-Iqbal, I., Iqbal, K., & Gong, C.-X. (2009) · Brain · doi:10.1093/brain/awp099 · Cited by 439 · see citing works

Differential Expression of Oxidative Phosphorylation Genes in Patients With Alzheimer's Disease: Implications for Early Mitochondrial Dysfunction and Oxidative Damage

Mańczak, M., Park, B. S., Jung, Y., & Reddy, P. H. (2004) · NeuroMolecular Medicine · doi:10.1385/nmm:5:2:147 · Cited by 432 · see citing works

In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death

AZOULAY-ZOHAR, H., ISRAELSON, A., ABU-HAMAD, S., & SHOSHAN-BARMATZ, V. (2004) · Biochemical Journal · doi:10.1042/bj20031465 · Cited by 408 · see citing works

Activation of Glycogen Synthase Kinase 3β Disrupts the Binding of Hexokinase II to Mitochondria by Phosphorylating Voltage-Dependent Anion Channel and Potentiates Chemotherapy-Induced Cytotoxicity

Pastorino, J. G., Hoek, J. B., & Shulga, N. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1925 · Cited by 398 · see citing works

Abnormal mitochondrial dynamics and synaptic degeneration as early events in Alzheimer’s disease: Implications to mitochondria-targeted antioxidant therapeutics

Reddy, P. H., Tripathi, R., Troung, Q., Tirumala, K., Reddy, T. P., Anekonda, V., Shirendeb, U. P., Calkins, M. J., Reddy, A. P., Mao, P., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.011 · Cited by 394 · see citing works

Hexokinases

Wilson, J. E. (2006) · Springer eBooks · doi:10.1007/bfb0049776 · Cited by 366 · see citing works

Cholinesterase Inhibitors Used in the Treatment of Alzheimer???s Disease

Wilkinson, D. G., Francis, P. T., Schwam, E. M., & Payne-Parrish, J. (2004) · Drugs & Aging · doi:10.2165/00002512-200421070-00004 · Cited by 365 · see citing works

GSK3 and tau: Two convergence points in Alzheimer’s disease

Hernandez, F., Lucas, J. J., & Avila, J. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-129025 · Cited by 359 · see citing works

VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function

Rostovtseva, T. K., & Colombini, M. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78841-6 · Cited by 357 · see citing works

Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer’s disease

Manczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds360 · Cited by 348 · see citing works

Melatonin increases survival and inhibits oxidative and amyloid pathology in a transgenic model of Alzheimer's disease

Matsubara, E., Bryant‐Thomas, T., Pacheco Quinto, J., Henry, T. L., Poeggeler, B., Herbert, D., Cruz‐Sanchez, F., Chyan, Y., Smith, M. A., Perry, G., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01654.x · Cited by 332 · see citing works

Vitamin E and Vitamin C Supplement Use and Risk of Incident Alzheimer Disease

Morris, M. C., Beckett, L. A., Scherr, P. A., Hebert, L. E., Bennett, D. A., Field, T. S., & Evans, D. A. (1998) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-199809000-00001 · Cited by 332 · see citing works

Copper-Dependent Inhibition of Human Cytochrome<i>c</i>Oxidase by a Dimeric Conformer of Amyloid-β_1-42

Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327 · see citing works

Gene expression profiles of transcripts in amyloid precursor protein transgenic mice: up-regulation of mitochondrial metabolism and apoptotic genes is an early cellular change in Alzheimer's disease

Reddy, P. H., McWeeney, S. K., Park, B. S., Mańczak, M., Gutala, R. V., Partovi, D., Jung, Y., Yau, V., Searles, R. P., Mori, M., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh140 · Cited by 327 · see citing works

Brain aging, Alzheimer's disease, and mitochondria

Swerdlow, R. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.08.012 · Cited by 306 · see citing works

Aβ1-42 inhibition of LTP is mediated by a signaling pathway involving caspase-3, Akt1 and GSK-3β

Jo, J., Whitcomb, D. J., Olsen, K. M., Kerrigan, T. L., Lo, S.-C., Bru-Mercier, G., Dickinson, B., Scullion, S., Sheng, M., Collingridge, G., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2785 · Cited by 305 · see citing works

Glycogen Synthase Kinase-3β Facilitates Staurosporine- and Heat Shock-induced Apoptosis

Bijur, G. N., Sarno, P. D., & Jope, R. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7583 · Cited by 302 · see citing works

Relation of the tocopherol forms to incident Alzheimer disease and to cognitive change

Morris, M. C., Evans, D. A., Tangney, C. C., Bienias, J. L., Wilson, R. S., Aggarwal, N. T., & Scherr, P. A. (2005) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn.81.2.508 · Cited by 302 · see citing works

Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease

Reddy, P. H. (2011) · Brain Research · doi:10.1016/j.brainres.2011.07.052 · Cited by 300 · see citing works

The voltage-dependent anion channel-1 modulates apoptotic cell death

Zaid, H., Abu‐Hamad, S., Israelson, A., Nathan, I., & Shoshan‐Barmatz, V. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401599 · Cited by 299 · see citing works

Early Vitamin E supplementation in young but not aged mice reduces Aβ levels and amyloid deposition in a transgenic model of Alzheimer's disease

Sung, S., Yao, Y., Uryu, K., Yang, H., Lee, V. M. ‐., Trojanowski, J. Q., & Praticò, D. (2003) · The FASEB Journal · doi:10.1096/fj.03-0961fje · Cited by 298 · see citing works

Are mitochondria critical in the pathogenesis of Alzheimer's disease?

Reddy, P. H., & Beal, M. F. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.03.004 · Cited by 289 · see citing works

Divide and Die: Cell Cycle Events as Triggers of Nerve Cell Death

Herrup, K., Neve, R. L., Ackerman, S. L., & Copani, A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3347-04.2004 · Cited by 285 · see citing works

Regulation of Metabolite Flux through Voltage-Gating of VDAC Channels

Hodge, T., & Colombini, M. (1997) · The Journal of Membrane Biology · doi:10.1007/s002329900235 · Cited by 281 · see citing works

Hexokinase-I Protection against Apoptotic Cell Death Is Mediated via Interaction with the Voltage-dependent Anion Channel-1

Abu-Hamad, S., Zaid, H., Israelson, A., Nahon, E., & Shoshan-Barmatz, V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708216200 · Cited by 278 · see citing works

VDAC structure, selectivity, and dynamics

Colombini, M. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.12.026 · Cited by 274 · see citing works

Abnormal Mitochondrial Dynamics in the Pathogenesis of Alzheimer's Disease

Zhu, X., Perry, G., Smith, M. A., & Wang, X. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-129005 · Cited by 242 · see citing works

Amyloid-β and Mitochondria in Aging and Alzheimer's Disease: Implications for Synaptic Damage and Cognitive Decline

Reddy, P. H., Mańczak, M., Mao, P., Calkins, M. J., Reddy, A. P., & Shirendeb, U. P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100504 · Cited by 240 · see citing works

Maternal family history of Alzheimer's disease predisposes to reduced brain glucose metabolism

Mosconi, L., Brys, M., Switalski, R., Mistur, R., Glodzik, L., Pirraglia, E., Tsui, W., De Santi, S., & de Leon, M. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705036104 · Cited by 237 · see citing works

Inhibition of Glycogen Synthase Kinase-3 Ameliorates β-Amyloid Pathology and Restores Lysosomal Acidification and Mammalian Target of Rapamycin Activity in the Alzheimer Disease Mouse Model

Avrahami, L., Farfara, D., Shaham-Kol, M., Vassar, R. J., Frenkel, D., & Eldar-Finkelman, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.409250 · Cited by 232 · see citing works

Prevention of age-related spatial memory deficits in a transgenic mouse model of Alzheimer's disease by chronic Ginkgo biloba treatment

Stackman, R. W., Eckenstein, F., Frei, B., Kulhanek, D., Nowlin, J., & Quinn, J. F. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00399-6 · Cited by 230 · see citing works

Non‐steroidal anti‐inflammatory drugs (NSAIDs) in Alzheimer's disease: old and new mechanisms of action

Gasparini, L., Ongini, E., & Wenk, G. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02743.x · Cited by 226 · see citing works

Glycogen synthase kinase 3: A point of convergence for the host inflammatory response

Wang, H., Brown, J. R., & Martin, M. (2010) · Cytokine · doi:10.1016/j.cyto.2010.10.009 · Cited by 215 · see citing works

Proapoptotic Stimuli Induce Nuclear Accumulation of Glycogen Synthase Kinase-3β

Bijur, G. N., & Jope, R. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105725200 · Cited by 204 · see citing works

Age-dependent Accumulation of Soluble Amyloid β (Aβ) Oligomers Reverses the Neuroprotective Effect of Soluble Amyloid Precursor Protein-α (sAPPα) by Modulating Phosphatidylinositol 3-Kinase (PI3K)/Akt-GSK-3β Pathway in Alzheimer Mouse Model

Jiménez, S., Torres, M., Vizuete, M., Sanchez-Varo, R. M., Sánchez‐Mejías, E., Trujillo‐Estrada, L., Carmona‐Cuenca, I., Caballero, C., Ruano, D., Gutiérrez, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209718 · Cited by 190 · see citing works

Glycogen synthase kinase 3 beta: can it be a target for oral cancer

Mishra, R. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-144 · Cited by 188 · see citing works

Mitochondrial Dysfunction in Aging and Alzheimer's Disease: Strategies to Protect Neurons

Reddy, P. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1754 · Cited by 187 · see citing works

Activation of glycogen synthase kinase-3 beta mediates β-amyloid induced neuritic damage in Alzheimer's disease

DaRocha-Souto, B., Coma, M., Pérez-Nievas, B. G., Scotton, T. C., Siao, M., Sánchez-Ferrer, P., Hashimoto, T., Fan, Z., Hudry, E., Barroeta, I., et al. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.09.002 · Cited by 180 · see citing works

Signal transduction to the permeability transition pore

Rasola, A., Sciacovelli, M., Pantic, B., & Bernardi, P. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.022 · Cited by 178 · see citing works

Inhibition of GSK-3 Ameliorates Aβ Pathology in an Adult-Onset Drosophila Model of Alzheimer's Disease

Sofola, O., Kerr, F., Rogers, I., Killick, R., Augustin, H., Gandy, C., Allen, M. J., Hardy, J., Lovestone, S., & Partridge, L. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001087 · Cited by 174 · see citing works

Why size matters – balancing mitochondrial dynamics in Alzheimer's disease

DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 164 · see citing works

Vitamin E reduces amyloidosis and improves cognitive function in Tg2576 mice following repetitive concussive brain injury

Conte, V., Uryu, K., Fujimoto, S., Yao, Y., Rokach, J., Longhi, L., Trojanowski, J. Q., Lee, V. M., McIntosh, T. K., & Praticò, D. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02560.x · Cited by 164 · see citing works

GSK3: a key target for the development of novel treatments for type 2 diabetes mellitus and Alzheimer disease

Gao, C., Hölscher, C., Liu, Y., & Li, L. (2012) · revneuro · doi:10.1515/rns.2011.061 · Cited by 164 · see citing works

HIV‐1 Tat‐Mediated Activation of Glycogen Synthase Kinase‐3β Contributes to Tat‐Mediated Neurotoxicity

Maggirwar, S. B., Tong, N., Ramirez, S. H., Gelbard, H. A., & Dewhurst, S. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730578.x · Cited by 164 · see citing works

Cholinesterase inhibitors in the treatment of dementia.

Ellis, J. M. (2005) · PubMed · Cited by 159 · see citing works

GSK3 and Alzheimer’s disease: facts and fiction…

Kremer, A. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00017 · Cited by 155 · see citing works

Synaptic Mitochondrial Pathology in Alzheimer's Disease

Du, H., Guo, L., & Yan, S. S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4277 · Cited by 150 · see citing works

Reduced cerebral glucose metabolism in patients at risk for Alzheimer's disease

Hunt, A., Schönknecht, P., Henze, M., Seidl, U., Haberkorn, U., & Schröder, J. (2007) · Psychiatry Research: Neuroimaging · doi:10.1016/j.pscychresns.2006.12.003 · Cited by 146 · cited 6× · see citing works

VDAC inhibition by tubulin and its physiological implications

Rostovtseva, T. K., & Bezrukov, S. M. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.004 · Cited by 142 · see citing works

Effect of the Alzheimer amyloid fragment Aβ(25–35) on Akt/PKB kinase and survival of PC12 cells

Martı́n, D., Salinas, M., López‐Valdaliso, R., Serrano, E., Recuero, M., & Cuadrado, A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00472.x · Cited by 140 · see citing works

Enhanced Expression of the Voltage-Dependent Anion Channel 1 (VDAC1) in Alzheimer's Disease Transgenic Mice: An Insight into the Pathogenic Effects of Amyloid-β

Cuadrado‐Tejedor, M., Vilariño, M., Cabodevilla, F., Río, J. D., Frechilla, D., & Pérez‐Mediavilla, A. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100966 · Cited by 134 · see citing works

Changes of voltage-dependent anion-selective channel proteins VDAC1 and VDAC2 brain levels in patients with Alzheimer's disease and Down Syndrome

Yoo, B. C., Fountoulakis, M., Cairns, N. J., & Lübec, G. (2001) · Electrophoresis · doi:10.1002/1522-2683(200101)22:1 · Cited by 129 · see citing works

Redox Proteomics Identification of Oxidatively Modified Brain Proteins in Alzheimer's Disease and Mild Cognitive Impairment: Insights into the Progression of this Dementing Disorder

Butterfield, D. A., & Rukhsana Sultana, A. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12107 · Cited by 126 · see citing works

Selectively silencing GSK-3 isoforms reduces plaques and tangles in mouse models of Alzheimer's disease

Hurtado, D. E., Molina-Porcel, L., Carroll, J. C., MacDonald, C., Aboagye, A. K., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0889-12.2012 · Cited by 126 · see citing works

GSK-3 Inhibitors: A Ray of Hope for the Treatment of Alzheimer's Disease?

Martı́nez, A., & Pérez, D. I. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-15204 · Cited by 125 · see citing works

Mitochondrial dysfunction and accumulation of the β-secretase-cleaved C-terminal fragment of APP in Alzheimer’s disease transgenic mice

Devi, L., & Ohno, M. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.09.001 · Cited by 121 · see citing works

Hyperphosphorylation of Tau Induced by Naturally Secreted Amyloid-β at Nanomolar Concentrations Is Modulated by Insulin-dependent Akt-GSK3β Signaling Pathway

Tokutake, T., Kasuga, K., Yajima, R., Sekine, Y., Tezuka, T., Nishizawa, M., & Ikeuchi, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.348300 · Cited by 117 · see citing works

Purification and characterization of a bindable form of mitochondrial bound hexokinase from the highly glycolytic AS-30D rat hepatoma cell line.

Nakashima, R. A., Paggi, M. G., Scott, L. J., & Pedersen, P. L. (1988) · PubMed · Cited by 114 · see citing works

Role of GSK3 Signaling in Neuronal Morphogenesis

Kim, Y. T., Hur, E., Snider, W. D., & Zhou, F. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00048 · Cited by 109 · see citing works

Structure-based analysis of VDAC1: N-terminus location, translocation, channel gating and association with anti-apoptotic proteins

Geula, S., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Biochemical Journal · doi:10.1042/bj20112079 · Cited by 105 · see citing works

Effects of α-tocopherol on an animal model of tauopathies

Nakashima, H., Ishihara, T., Yokota, O., Terada, S., Trojanowski, J. Q., Lee, V. M. ‐., & Kuroda, S. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.037 · Cited by 99 · see citing works

Apolipoprotein E and β‐amyloid (1–42) regulation of glycogen synthase kinase‐3β

Cedazo-Mı́nguez, Á., Popescu, B. O., Blanco‐Millán, J. M., Akterin, S., Pei, J. ‐., Winblad, B. G., & Cowburn, R. F. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02088.x · Cited by 97 · see citing works

The cell cycle as a therapeutic target for Alzheimer's disease

Neve, R. L., & McPhie, D. L. (2006) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2005.09.005 · Cited by 92 · see citing works

Voltage-dependant anion channels: novel insights into isoform function through genetic models

Raghavan, A., Sheiko, T., Graham, B. H., & Craigen, W. J. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.10.019 · Cited by 92 · see citing works

VDAC1, Having a Shorter N-Terminus Than VDAC2 but Showing the Same Migration in an SDS−Polyacrylamide Gel, Is the Predominant Form Expressed in Mitochondria of Various Tissues

Yamamoto, T., Yamada, A., Watanabe, M., Yoshimura, Y., Yamazaki, N., Yoshimura, Y., Yamauchi, T., Kataoka, M., Nagata, T., Terada, H., et al. (2006) · Journal of Proteome Research · doi:10.1021/pr060291w · Cited by 90 · see citing works

Akt/GSK3β serine/threonine kinases: evidence for a signalling pathway mediated by familial Alzheimer's disease mutations

Ryder, J. W., Yuan, S., & Ni, B. (2003) · Cellular Signalling · doi:10.1016/j.cellsig.2003.07.004 · Cited by 89 · see citing works

Spectroscopic Studies of GSK3β Phosphorylation of the Neuronal Tau Protein and Its Interaction with the N-Terminal Domain of Apolipoprotein E

Leroy, A., Landrieu, I., Huvent, I., Legrand, D., Codeville, B., Wieruszeski, J.-M., & Lippens, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149419 · Cited by 86 · see citing works

Oestrogen Receptors and Signalling Pathways: Implications for Neuroprotective Effects of Sex Steroids in Parkinson’s Disease

Al-Sweidi, S., Sánchez, M. G., Bourque, M., Morissette, M., Dluzen, D. E., & Paolo, T. D. (2011) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2011.02193.x · Cited by 82 · see citing works

Glycogen synthase kinase 3 in the world of cell migration

Sun, T., Rodriguez, M., & Kim, L. (2009) · Development Growth & Differentiation · doi:10.1111/j.1440-169x.2009.01141.x · Cited by 80 · see citing works

DNA damage–induced cell-cycle arrest of hematopoietic cells is overridden by activation of the PI-3 kinase/Akt signaling pathway

Henry, M. K., Lynch, J. T., Eapen, A. K., & Quelle, F. W. (2001) · Blood · doi:10.1182/blood.v98.3.834 · Cited by 80 · see citing works

Rationale for the Development of Cholinesterase Inhibitors as Anti- Alzheimer Agents

Lahiri, D. K., Rogers, J. T., Greig, N. H., & Sambamurti, K. (2004) · Current Pharmaceutical Design · doi:10.2174/1381612043383331 · Cited by 76 · see citing works

Protective Effects of Hesperidin Against Amyloid-β (Aβ) Induced Neurotoxicity Through the Voltage Dependent Anion Channel 1 (VDAC1)-Mediated Mitochondrial Apoptotic Pathway in PC12 Cells

Wang, D., Li, S., Zhu, X., Wang, Y., Wu, W., & Zhang, X. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1013-4 · Cited by 75 · see citing works

VDAC proteomics: Post-translation modifications

Kerner, J., Lee, K., Tandler, B., & Hoppel, C. L. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.013 · Cited by 74 · see citing works

Determination of the Conformation of the Human VDAC1 N‐Terminal Peptide, a Protein Moiety Essential for the Functional Properties of the Pore

Pinto, V. D., Tomasello, M. F., Messina, A. A., Guarino, F., Benz, R., Mendola, D. L., Magrì, A. L., Milardi, D., & Pappalardo, G. (2007) · ChemBioChem · doi:10.1002/cbic.200700009 · Cited by 72 · see citing works

Activity of flurbiprofen and chemically related anti-inflammatory drugs in models of Alzheimer's disease

Gasparini, L., Ongini, E., Wilcock, D. M., & Morgan, D. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.12.029 · Cited by 68 · see citing works

Cholinesterase inhibitors influence APP metabolism in Alzheimer disease patients

Zimmermann, M., Borroni, B., Cattabeni, F., Padovani, A., & Luca, M. D. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.01.002 · Cited by 67 · see citing works

Emerging Roles of Glycogen Synthase Kinase 3 in the Treatment of Brain Tumors

Mills, C. N., Nowsheen, S., Bonner, J. A., & Yang, E. S.-H. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00047 · Cited by 65 · see citing works

Wild-Type But Not FAD Mutant Presenilin-1 Prevents Neuronal Degeneration by Promoting Phosphatidylinositol 3-Kinase Neuroprotective Signaling

Baki, L., Neve, R. L., Shao, Z., Shioi, J., Georgakopoulos, A., & Robakis, N. K. R. K. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4067-07.2008 · Cited by 62 · see citing works

Reduced Risk of Alzheimer Disease in Users of Antioxidant Vitamin Supplements: The Cache County Study

Zandi, P. P. (2004) · Archives of Neurology · doi:10.1001/archneur.61.1.82 · Cited by 47 · see citing works

Regulation of mitochondrial function by voltage dependent anion channels in ethanol metabolism and the Warburg effect

Lemasters, J. J., Holmuhamedov, E., Czerny, C., Zhong, Z., & Maldonado, E. N. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.11.034 · Cited by 46 · see citing works

Genetic strategies for dissecting mammalian and Drosophila voltage-dependent anion channel functions

Craigen, W. J., & Graham, B. H. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9146-x · Cited by 43 · see citing works

Therapeutic Opportunities in Alzheimer Disease: One for all or all for One?

Marlatt, M. W., Webber, K., Moreira, P. I., Lee, H., Casadesús, G., Honda, K., Zhu, X., Perry, G. L., & Smith, M. A. (2005) · Current Medicinal Chemistry · doi:10.2174/0929867053764644 · Cited by 43 · see citing works

Roles of GSK3 in metabolic shift toward abnormal anabolism in cell senescence

Kim, Y., Seo, Y., Park, C., Yoon, S., & Yoon, G. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05617.x · Cited by 41 · see citing works

Nonsteroidal anti-inflammatory drugs and Alzheimer disease: what's next?

Launer, L. (2003) · Journal of the American Medical Association (JAMA) · doi:10.1001/jama.289.21.2865 · Cited by 37 · see citing works

Sleep and biorythm disturbances in schizophrenia, mood and anxiety disorders: a review

Bersani, F. S., Iannitelli, A., Pacitti, F., & Bersani, G. (2012) · Rivista di psichiatria · doi:10.1708/1175.13027 · Cited by 37 · see citing works

Beyond Estrogen: Targeting Gonadotropin Hormones in the Treatment of Alzheimers Disease

Casadesús, G., Zhu, X., Atwood, C., Webber, K., Perry, G. L., Bowen, R. L., & Smith, M. A. (2004) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1568007043337265 · Cited by 35 · see citing works

Apoptogenic interactions of plasmalemmal type-1 VDAC and Aβ peptides via GxxxG motifs induce Alzheimer's disease – a basic model of apoptosis?*

THINNES, F. P. (2011) · Wiener Medizinische Wochenschrift · doi:10.1007/s10354-011-0887-5 · Cited by 31 · see citing works

Selective treatment of mixed-lineage leukemia leukemic stem cells through targeting glycogen synthase kinase 3 and the canonical Wnt/β-catenin pathway

Fung, T. K., Gandillet, A., & So, C. W. E. (2012) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3283545615 · Cited by 26 · see citing works

Cholinergic and glutamatergic drugs in Alzheimer’s disease therapy

Clarke, N. A., & Francis, P. T. (2005) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.5.5.671 · Cited by 16 · see citing works

Role of acetylcholinesterase inhibitors in the regulation of amyloid β precursor protein (AβPP) metabolism

Racchi, M., Mazzucchelli, M., Lenzken, S. C., Porrello, E., Lanni, C., & Govoni, S. M. (2005) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.10.099 · Cited by 16 · see citing works

Mitochondrial VDAC1: A Key Gatekeeper as Potential Therapeutic Target

Camara, A. K. S., Zhou, Y., Wen, P., Tajkhorshid, E., & Kwok, W.-M. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00460 · Cited by 357 · see citing works

SYK coordinates neuroprotective microglial responses in neurodegenerative disease

Ennerfelt, H., Frost, E. L., Shapiro, D. A., Holliday, C., Zengeler, K. E., Voithofer, G., Bolte, A. C., Lammert, C. R., Kulas, J. A., Ulland, T. K., et al. (2022) · Cell · doi:10.1016/j.cell.2022.09.030 · Cited by 329 · see citing works

The Akt pathway in oncology therapy and beyond (Review)

Nițulescu, G. M., van de Venter, M., Nițulescu, G., Ungurianu, A., Juzenas, P., Peng, Q., Olaru, O. T., Grădinaru, D., Tsatsakis, A. M., Tsoukalas, D., et al. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4597 · Cited by 329 · see citing works

VDAC1, mitochondrial dysfunction, and Alzheimer’s disease

Shoshan-Barmatz, V., Nahon-Crystal, E., Shteinfer-Kuzmine, A., & Gupta, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.03.010 · Cited by 286 · see citing works

Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer's disease patient brains

Ye, X., Sun, X., Starovoytov, V., & Cai, Q. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv056 · Cited by 274 · see citing works

Alzheimer's disease and type 2 diabetes: a critical assessment of the shared pathological traits

Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270 · see citing works

Dynamics of diabetes and obesity: Epidemiological perspective

Boles, A. N., Kandimalla, R. J. L., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.01.016 · Cited by 266 · see citing works

Alterations in Mitochondrial Quality Control in Alzheimer’s Disease

Cai, Q., & Tammineni, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00024 · Cited by 215 · see citing works

Metabolic Dysregulation Contributes to the Progression of Alzheimer’s Disease

Yan, X., Hu, Y., Wang, B., Wang, S., & Zhang, X. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.530219 · Cited by 217 · see citing works

Implications of Phosphoinositide 3-Kinase-Akt (PI3K-Akt) Pathway in the Pathogenesis of Alzheimer’s Disease

Kumar, M., & Bansal, N. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02611-7 · Cited by 204 · see citing works

Alzheimer’s Disease: Exploring the Landscape of Cognitive Decline

Tenchov, R., Sasso, J. M., & Zhou, Q. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00339 · Cited by 170 · see citing works

VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress

Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170 · see citing works

Deregulated mitochondrial microRNAs in Alzheimer's disease: Focus on synapse and mitochondria

Gowda, P., Reddy, P. H., & Kumar, S. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101529 · Cited by 166 · see citing works

VDAC1 functions in Ca2+ homeostasis and cell life and death in health and disease

Shoshan‐Barmatz, V., Krelin, Y., & Shteinfer‐Kuzmine, A. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.06.007 · Cited by 162 · see citing works

Multiple faces of dynamin-related protein 1 and its role in Alzheimer's disease pathogenesis

Kandimalla, R. J. L., & Reddy, P. H. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.018 · Cited by 144 · see citing works

The voltage-dependent anion channel 1 mediates amyloid β toxicity and represents a potential target for Alzheimer disease therapy

Smilansky, A., Dangoor, L., Nakdimon, I., Ben-Hail, D., Mizrachi, D., & Shoshan-Barmatz, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691493 · Cited by 143 · see citing works

Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics

Shoshan‐Barmatz, V., Krelin, Y., Shteinfer‐Kuzmine, A., & Arif, T. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00154 · Cited by 134 · see citing works

Insulin Resistance as Common Molecular Denominator Linking Obesity to Alzheimer‘s Disease

Nuzzo, D., Picone, P., Baldassano, S., Caruana, L., Messina, E., Gammazza, A., Cappello, F., Mulè, F., & Carlo, M. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150710115506 · Cited by 119 · see citing works

Nuclear Factor-Erythroid 2-Related Factor 2 (Nrf2) and Mitochondrial Dynamics/Mitophagy in Neurological Diseases

Kang, T. (2020) · Antioxidants · doi:10.3390/antiox9070617 · Cited by 120 · see citing works

Targeting the overexpressed mitochondrial protein VDAC1 in a mouse model of Alzheimer’s disease protects against mitochondrial dysfunction and mitigates brain pathology

Verma, A., Shteinfer‐Kuzmine, A., Kamenetsky, N., Pittala, S., Paul, A., Crystal, E. N., Ouro, A., Caspi, V. C., Pandey, S. K., Monsonego, A., et al. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00329-7 · Cited by 106 · see citing works

Disrupted‐in‐schizophrenia‐1 protects synaptic plasticity in a transgenic mouse model of Alzheimer’s disease as a mitophagy receptor

Wang, Z., Lu, M., Zhang, Y., Ji, W., Lei, L., Wang, W., Fang, L., Wang, L., Fan, Y., Wang, J., et al. (2018) · Aging Cell · doi:10.1111/acel.12860 · Cited by 95 · see citing works

Therapeutic Potential of Vital Transcription Factors in Alzheimer’s and Parkinson’s Disease With Particular Emphasis on Transcription Factor EB Mediated Autophagy

Nand, S., Tiwari, N. K., Singh, P., Mishra, D., Singh, A. K., Hooshmandi, E., Vamanu, E., & Singh, M. P. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.777347 · Cited by 95 · see citing works

Cell-based Models To Investigate Tau Aggregation

Lim, S., Haque, M. M., Kim, D., Kim, D. J., & Kim, Y. K. (2014) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2014.09.011 · Cited by 84 · see citing works

Protective Effect of Caffeic Acid against Alzheimer’s Disease Pathogenesis via Modulating Cerebral Insulin Signaling, β-Amyloid Accumulation, and Synaptic Plasticity in Hyperinsulinemic Rats

Chang, W., Huang, D., Lo, Y.-M. M., Tee, Q., Kuo, P., Wu, J. S., Huang, W., & Shen, S. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b02078 · Cited by 85 · see citing works

Inside the diabetic brain: Insulin resistance and molecular mechanism associated with cognitive impairment and its possible therapeutic strategies

Dutta, B. J., Singh, S., Seksaria, S., Gupta, G. D., & Singh, A. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106358 · Cited by 87 · see citing works

How the Wnt signaling pathway protects from neurodegeneration: the mitochondrial scenario

Arrázola, M. S., Silva-Álvarez, C., & Inestrosa, N. C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00166 · Cited by 82 · see citing works

Early Life Stress and Epigenetics in Late-onset Alzheimer’s Dementia: A Systematic Review

Lemche, E. (2018) · Current Genomics · doi:10.2174/1389202919666171229145156 · Cited by 82 · see citing works

VDAC1-interacting anion transport inhibitors inhibit VDAC1 oligomerization and apoptosis

Ben-Hail, D., & Shoshan-Barmatz, V. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.002 · Cited by 80 · see citing works

GSK3β Regulates Brain Energy Metabolism

Martin, S. A., Souder, D. C., Miller, K. N., Clark, J. P., Sagar, M. A. K., Eliceiri, K. W., Puglielli, L., Beasley, T. M., & Anderson, R. M. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.045 · Cited by 78 · see citing works

Association of Aβ with ceramide-enriched astrosomes mediates Aβ neurotoxicity

Elsherbini, A., Kirov, A. S., Dinkins, M. B., Wang, G., Qin, H., Zhu, Z., Tripathi, P., Crivelli, S. M., & Bieberich, E. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00931-8 · Cited by 72 · see citing works

Direct pharmacological Akt activation rescues Alzheimer's disease like memory impairments and aberrant synaptic plasticity

Yi, J. H., Baek, S. J., Heo, S., Park, H. J., Kwon, H., Lee, S., Jung, J.-W., Park, S. J., Kim, B. C., Lee, Y. C., et al. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.10.028 · Cited by 73 · see citing works

Role of GSK-3β Inhibitors: New Promises and Opportunities for Alzheimer’s Disease

Shri, S. R., Manandhar, S., Nayak, Y., & Pai, K. S. R. (2023) · Advanced Pharmaceutical Bulletin · doi:10.34172/apb.2023.071 · Cited by 71 · see citing works

VDAC phosphorylation, a lipid sensor influencing the cell fate

Martel, C., Wang, Z., & Brenner, C. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.07.009 · Cited by 69 · see citing works

TCMBank: bridges between the largest herbal medicines, chemical ingredients, target proteins, and associated diseases with intelligence text mining

Lv, Q., Chen, G., He, H., Yang, Z., Zhao, L., Chen, H., & Chen, C. Y. (2023) · Chemical Science · doi:10.1039/d3sc02139d · Cited by 68 · see citing works

S-Nitrosylation in Alzheimer's disease

Zhao, Q., Yu, J., & Tan, L. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8672-2 · Cited by 63 · see citing works

Molecular dynamics and structure-based virtual screening and identification of natural compounds as Wnt signaling modulators: possible therapeutics for Alzheimer’s disease

Manandhar, S., Sankhe, R., Priya, K., Hari, G., Kumar, H., Mehta, C. H., Nayak, U. Y., & Pai, K. S. R. (2022) · Molecular Diversity · doi:10.1007/s11030-022-10395-8 · Cited by 63 · see citing works

Akt signaling pathway: a potential therapy for Alzheimer’s disease through glycogen synthase kinase 3 beta inhibition

Limantoro, J., de Liyis, B. G., & Sutedja, J. C. (2023) · The Egyptian Journal of Neurology Psychiatry and Neurosurgery · doi:10.1186/s41983-023-00751-2 · Cited by 59 · see citing works

Mitochondrial dysfunction as a therapeutic strategy for neurodegenerative diseases: Current insights and future directions

Gu, Y., Zhao, X., Zhang, N., Yang, Y., Yi, Y., Shao, Q.-H., Liu, M.-X., & Zhang, X.-L. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102577 · Cited by 58 · see citing works

A Mitocentric View of Alzheimer’s Disease

Hu, H., Tan, C., Tan, L., & Yu, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0117-7 · Cited by 58 · see citing works

Glycogen Synthase Kinase 3β Involvement in Neuroinflammation and Neurodegenerative Diseases

Gianferrara, T., Cescon, E., Grieco, I., Spalluto, G., & Federico, S. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220216113517 · Cited by 58 · see citing works

Molecular Mechanisms Associated with Neurodegeneration of Neurotropic Viral Infection

Wongchitrat, P., Chanmee, T., & Govitrapong, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03761-6 · Cited by 62 · see citing works

Resveratrol and Alzheimer's disease. From molecular pathophysiology to clinical trials

Drygalski, K., Fereniec, E., Koryciński, K., Chomentowski, A., Kiełczewska, A., Odrzygóźdź, C., & Modzelewska, B. (2018) · Experimental Gerontology · doi:10.1016/j.exger.2018.09.019 · Cited by 56 · see citing works

Novel function of ceramide for regulation of mitochondrial ATP release in astrocytes

Kong, J.-N., Zhu, Z., Itokazu, Y., Wang, G., Dinkins, M. B., Zhong, L., Lin, H.-P., Elsherbini, A. M., Leanhart, S., Jiang, X., et al. (2018) · Journal of Lipid Research · doi:10.1194/jlr.m081877 · Cited by 51 · see citing works

Amyloid beta modulators and neuroprotection in Alzheimer's disease: a critical appraisal

Kuruva, C. S., & Reddy, P. H. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.10.010 · Cited by 49 · see citing works

Wnt Signaling Prevents the Aβ Oligomer-Induced Mitochondrial Permeability Transition Pore Opening Preserving Mitochondrial Structure in Hippocampal Neurons

Arrázola, M. S., Ramos‐Fernández, E., Cisternas, P., Ordenes, D., & Inestrosa, N. C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0168840 · Cited by 49 · see citing works

Deep Learning and Random Forest Approach for Finding the Optimal Traditional Chinese Medicine Formula for Treatment of Alzheimer’s Disease

Chen, H., Chen, J., Li, J., Huang, H.-J., Chen, X., Zhang, H.-Y., & Chen, C. Y. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00041 · Cited by 49 · see citing works

Diabetes: Risk factor and translational therapeutic implications for Alzheimer's disease

Cummings, J. L., Ortiz, A. A., Castellino, J., & Kinney, J. W. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15619 · Cited by 50 · see citing works

Mitochondrial calcium signalling and neurodegenerative diseases

Britti, E., Delaspre, F., Tamarit, J., & Ros, J. (2018) · Neuronal Signaling · doi:10.1042/ns20180061 · Cited by 47 · see citing works

Synthesis and biological evaluation of 3-substituted 2-oxindole derivatives as new glycogen synthase kinase 3β inhibitors

Lozinskaya, N. A., Babkov, D. A., Zaryanova, E. V., Николаевна, Б. Е., Efremov, A. M., Tsymliakov, M. D., Аникина, Л. В., Zakharyascheva, O. Y., Borisov, A. V., Perfilova, V. N., et al. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.03.028 · Cited by 46 · see citing works

AMPK: Potential Therapeutic Target for Alzheimer's Disease

Yang, L., Jiang, Y., Shi, L., Zhong, D., Li, Y., Li, J., & Jin, R. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190819142746 · Cited by 46 · see citing works

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 · see citing works

Dysfunction of Mitochondria in Alzheimer’s Disease: ANT and VDAC Interact with Toxic Proteins and Aid to Determine the Fate of Brain Cells

Atlante, A., Valenti, D., Latina, V., & Amadoro, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147722 · Cited by 43 · see citing works

Guanosine monophosphate reductase 1 is a potential therapeutic target for Alzheimer’s disease

Liu, H., Luo, K., & Luo, D. (2018) · Scientific Reports · doi:10.1038/s41598-018-21256-6 · Cited by 42 · see citing works

BRCA1 and p53 Tumor Suppressor Molecules in Alzheimer’s Disease

Nakanishi, A., Minami, A., Kitagishi, Y., Ogura, Y., & Matsuda, S. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16022879 · Cited by 40 · see citing works

GSK3β is a key regulator of the ROS-dependent necrotic death induced by the quinone DMNQ

Ciotti, S., Iuliano, L., Cefalù, S., Comelli, M., Mavelli, I., Giorgio, E. D., & Brancolini, C. (2020) · Cell Death and Disease · doi:10.1038/s41419-019-2202-0 · Cited by 39 · see citing works

Naphthalene Monoimide Derivative Ameliorates Amyloid Burden and Cognitive Decline in a Transgenic Mouse Model of Alzheimer's Disease

Samanta, S., Rajasekhar, K., Ramesh, M., Murugan, N. A., Alam, S., Shah, D., Clement, J. P., & Govindaraju, T. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202000225 · Cited by 36 · see citing works

Amyloid β Induces Early Changes in the Ribosomal Machinery, Cytoskeletal Organization and Oxidative Phosphorylation in Retinal Photoreceptor Cells

Deng, L., Pushpitha, K., Joseph, C., Gupta, V. B., Rajput, R., Chitranshi, N., Dheer, Y., Amirkhani, A., Kamath, K. S., Pascovici, D., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00024 · Cited by 35 · see citing works

Neuroprotective effects of honokiol against beta-amyloid-induced neurotoxicity via GSK-3β and β-catenin signaling pathway in PC12 cells

Xian, Y., Ip, S., Mao, Q., & Lin, Z. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.04.014 · Cited by 35 · see citing works

Exploring the Mechanisms and Therapeutic Approaches of Mitochondrial Dysfunction in Alzheimer’s Disease: An Educational Literature Review

Moawad, M. H. E. D., Serag, I., Alkhawaldeh, I. M., Abbas, A., Sharaf, A., Alsalah, S., Sadeq, M. A., Shalaby, M. M. M., Hefnawy, M. T., Abouzid, M., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04468-y · Cited by 34 · see citing works

Increasing hexokinase 1 expression improves mitochondrial and glycolytic functional deficits seen in sporadic Alzheimer’s disease astrocytes

Bell, S., Wareing, H. E., Capriglia, F., Hughes, R. M., Barnes, K., Hamshaw, A., Adair, L. D., Shaw, A. C., Olejnik, A., De, S., et al. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02746-8 · Cited by 34 · see citing works

Current biomarkers and treatment strategies in Alzheimer disease: An overview and future perspectives

Bhole, R. P., Chikhale, R. V., & Rathi, K. M. (2023) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2023.11.003 · Cited by 34 · see citing works

Treadmill Exercise Reduces Neuroinflammation, Glial Cell Activation and Improves Synaptic Transmission in the Prefrontal Cortex in 3 × Tg-AD Mice

Mu, L., Xia, D., Cai, J., Gu, B., Liu, X., Friedman, V., Liu, Q.-S., & Zhao, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012655 · Cited by 31 · see citing works

Hyperphosphorylated Human Tau Accumulates at the Synapse, Localizing on Synaptic Mitochondrial Outer Membranes and Disrupting Respiration in a Mouse Model of Tauopathy

Trease, A. J., George, J. W., Roland, N. J., Lichter, E. Z., Emanuel, K. M., Totusek, S., Fox, H. S., & Stauch, K. L. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.852368 · Cited by 30 · see citing works

Vinpocetine mitigates aluminum-induced cognitive impairment in socially isolated rats

Ali, A. A., Ahmed, H. I., Khaleel, S. A., & Abu‐Elfotuh, K. (2019) · Physiology & Behavior · doi:10.1016/j.physbeh.2019.112571 · Cited by 31 · see citing works

GSK-3β dysregulation in aging: Implications for tau pathology and Alzheimer's disease progression

Rekha, A., Afzal, M., Babu, M. A., Menon, S. V., Nathiya, D., Supriya, S., Mishra, S. B., Gupta, S., Goyal, K., Rana, M., et al. (2025) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2025.104005 · Cited by 33 · see citing works

Renal Contributions in the Pathophysiology and Neuropathological Substrates Shared by Chronic Kidney Disease and Alzheimer’s Disease

Stanciu, G. D., Ababei, D. C., Bild, V., Bild, W., Păduraru, L., Guţu, M. M., & Tamba, B.-I. (2020) · Brain Sciences · doi:10.3390/brainsci10080563 · Cited by 31 · see citing works

Natural products as pharmacological modulators of mitochondrial dysfunctions for the treatments of Alzheimer’s disease: A comprehensive review

Jin, X., Guo, J., Wang, L., Zhong, X., Yao, W., Gao, H., & Liu, M. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113401 · Cited by 29 · see citing works

Derivatives of the β-Crinane Amaryllidaceae Alkaloid Haemanthamine as Multi-Target Directed Ligands for Alzheimer’s Disease

Kohelová, E., Peřinová, R., Maafi, N., Korábečný, J., Hulcová, D., Maříková, J., Kučera, T., Martínez‐González, L., Hrabinová, M., Vorčáková, K., et al. (2019) · Molecules · doi:10.3390/molecules24071307 · Cited by 28 · see citing works

Exercise Rehabilitation and/or Astragaloside Attenuate Amyloid-beta Pathology by Reversing BDNF/TrkB Signaling Deficits and Mitochondrial Dysfunction

Wang, Y., Chio, C., Kuo, S., Yeh, C., Ma, J., Liu, W., Lin, M.-T., Lin, K., & Chang, C. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02728-3 · Cited by 26 · see citing works

Signaling Pathways Involved in the Neuroprotective Effect of Osthole: Evidence and Mechanisms

Singh, L., & Bhatti, R. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03580-9 · Cited by 27 · see citing works

The Ca 2+channel inhibitor 2‐ APB reverses β ‐amyloid‐induced LTP deficit in hippocampus by blocking BAX and caspase‐3 hyperactivation

Hu, W., He, Z., Yang, L., Zhang, M., Xing, D., & Xiao, Z. (2014) · British Journal of Pharmacology · doi:10.1111/bph.13048 · Cited by 26 · see citing works

β-Amyrin Ameliorates Alzheimer's Disease-Like Aberrant Synaptic Plasticity in the Mouse Hippocampus

Park, H. J., Kwon, H., Lee, J., Cho, E., Lee, Y. C., Moon, M., Jun, M., Kim, D. H., & Jung, J. W. (2019) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2019.024 · Cited by 26 · see citing works

Activation of Wnt/β-catenin/GSK3β signaling during the development of diabetic cardiomyopathy

Xi, X.-H., Wang, Y., Li, J., Fu-wen, W., Tian, G.-H., Yin, M.-S., Mu, Y.-L., & Chong, Z.-Z. (2014) · Cardiovascular Pathology · doi:10.1016/j.carpath.2014.12.002 · Cited by 26 · see citing works

Effects of exercise on brain-derived neurotrophic factor in Alzheimer's disease models: A systematic review and meta-analysis

Zhang, S., Gu, B., Zhen, K., Du, L., Lv, Y., & Yu, L. (2024) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2024.105538 · Cited by 25 · see citing works

The Role of Acupuncture Improving Cognitive Deficits due to Alzheimer’s Disease or Vascular Diseases through Regulating Neuroplasticity

Ji, S., Duan, J., Hou, X., Zhou, L., Qin, W., Niu, H., Luo, S., Zhang, Y., Chan, P., & Jin, X. (2021) · Neural Plasticity · doi:10.1155/2021/8868447 · Cited by 27 · see citing works

Cellular Interactome of Mitochondrial Voltage-Dependent Anion Channels: Oligomerization and Channel (Mis)Regulation

Khan, A., Kuriachan, G., & Mahalakshmi, R. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00429 · Cited by 25 · see citing works

Protective effects of BACE1 inhibitory ligand molecules against amyloid beta-induced synaptic and mitochondrial toxicities in Alzheimer’s disease

Pradeepkiran, J. A., Reddy, A. P., Yin, X., Mańczak, M., & Reddy, P. H. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz227 · Cited by 25 · see citing works

Minocycline attenuates ethanol-induced cell death and microglial activation in the developing spinal cord

Ren, Z., Wang, X., Xu, M., Frank, J. A., & Luo, J. (2018) · Alcohol · doi:10.1016/j.alcohol.2018.12.002 · Cited by 24 · see citing works

Vitamin K2 Modulates Organelle Damage and Tauopathy Induced by Streptozotocin and Menadione in SH-SY5Y Cells

Shandilya, S., Kesari, K. K., & Ruokolainen, J. (2021) · Antioxidants · doi:10.3390/antiox10060983 · Cited by 23 · see citing works

Correlation between abnormal GSK3β, β Amyloid, total Tau, p-Tau 181 levels and neuropsychological assessment total scores in CKD patients with cognitive dysfunction: Impact of rHuEPO therapy

Vinothkumar, G., Krishnakumar, S., Riya, R., & Venkataraman, P. (2019) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2019.08.073 · Cited by 22 · see citing works

Alzheimer Disease: The Role of Aβ in the Glutamatergic System

Campos‐Peña, V., & Antônio, M. (2014) · InTech eBooks · doi:10.5772/57367 · Cited by 18 · see citing works

Chemoproteomic Approach to Explore the Target Profile of GPCR ligands: Application to 5‐HT1A and 5‐HT6 Receptors

Gamo, A. M., Gonzalez‐Vera, J. A., Rueda‐Zubiaurre, A., Alonso, D., Vázquez‐Villa, H., Martín‐Couce, L., Palomares, Ó., López, J. A., Martín‐Fontecha, M., Benhamú, B., et al. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201503101 · Cited by 18 · see citing works

Neuroprotective potential of hispidulin and diosmin: a review of molecular mechanisms

Singh, A., Singh, L., & Dalal, D. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01615-9 · Cited by 17 · see citing works

Antioxidant strategies against cellular senescence: unveiling the power of synthetic versus natural antioxidants in a systematic review

Ebrahimirad, F., Mirmahdizade, S. E., Mahmoodieh, B., Najafi, S., Banihashemian, S. A., Nikakhtar, S., Mobaraki, H., Sadeghi, A., Kossari, N., SadatRafiei, S. K., et al. (2025) · Frontiers in Aging · doi:10.3389/fragi.2025.1543360 · Cited by 17 · see citing works

The dual role of glycogen synthase kinase-3 beta (GSK3β) in neurodegenerative pathologies: interplay between autophagy and disease progression

Alhassan, H. H., Janiyani, K., Surti, M., Adnan, M., & Patel, M. B. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1693805 · Cited by 17 · see citing works

Contribution of hyperglycemia-induced changes in microglia to Alzheimer’s disease pathology

Rodríguez, M. H., Flores‐Clemente, C., Macías-Pérez, M. E., Rodríguez-Fonseca, R. A., Nicolás‐Vázquez, M. I., Martínez, J. O., Miranda, R., Rosas, M., & Jiménez, E. M. (2022) · Pharmacological Reports · doi:10.1007/s43440-022-00405-9 · Cited by 17 · see citing works

QTC-4-MeOBnE Rescues Scopolamine-Induced Memory Deficits in Mice by Targeting Oxidative Stress, Neuronal Plasticity, and Apoptosis

Fronza, M. G., Baldinotti, R., Fetter, J., Sacramento, M., Sousa, F. S. S., Seixas, F. K., Collares, T. V., Alves, D. A. C., Praticò, D., & Savegnago, L. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00661 · Cited by 17 · see citing works

Recent insights into viral infections as a trigger and accelerator in alzheimer's disease

Vlieger, L. D., Vandenbroucke, R. E., & Hoecke, L. V. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.103340 · Cited by 16 · see citing works

In Silico Investigation of Novel Compounds as Inhibitors of Acetylcholinesterase Enzyme for the Treatment of Alzheimer’s Diseases

Adebambo, K. F., & Ojoh, O. (2024) · International Journal of Alzheimer s Disease · doi:10.1155/2024/2988685 · Cited by 16 · see citing works

Reduction in Aβ‐induced cell death in the hippocampus of 17β‐estradiol‐treated female rats is associated with an increase in IGF‐I signaling and somatostatinergic tone

Perianes‐Cachero, A., Canelles, S., Aguado‐Llera, D., Frago, L. M., Toledo-Lobo, M. V., Carrera, I., Cacabelos, R., Chowen, J. A., Argente, J., Arilla, E., et al. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13381 · Cited by 16 · see citing works

Molecular docking based screening analysis of GSK3B

Joseph, O. A., Afees, O. J., Michael, A., & Omotuyi, O. I. (2019) · Bioinformation · doi:10.6026/97320630015201 · Cited by 15 · see citing works

Protective effect of maternal exercise against amyloid-β neurotoxicity in the male rat offspring’s cerebellum

Klein, C. P., Hoppe, J. B., Saccomori, A. B., dos Santos, B. G., August, P. M., Klein, I. P., Crestani, M. S., Bifi, F., Hözer, R. M., Navas, P., et al. (2020) · Journal of Developmental Origins of Health and Disease · doi:10.1017/s2040174420000562 · Cited by 13 · see citing works

Melatonin Attenuates High Glucose-Induced Changes in Beta Amyloid Precursor Protein Processing in Human Neuroblastoma Cells

Nopparat, C., Chaopae, W., Boontem, P., Sopha, P., Wongchitrat, P., & Govitrapong, P. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03290-5 · Cited by 17 · see citing works

Neuronal α‐amylase is important for neuronal activity and glycogenolysis and reduces in presence of amyloid beta pathology

Byman, E., Martinsson, I., Haukedal, H., Bank, T. N. B., Gouras, G. K., Freude, K., & Wennström, M. (2021) · Aging Cell · doi:10.1111/acel.13433 · Cited by 14 · see citing works

α‐Glyceryl‐phosphoryl‐ethanolamine protects human hippocampal neurons from ageing‐induced cellular alterations

Zappelli, E., Daniele, S., Ceccarelli, L., Vergassola, M., Ragni, L., Mangano, G., & Martini, C. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15783 · Cited by 12 · see citing works

Thiadiazolidinone (TDZD) Analogs Inhibit Aggregation-Mediated Pathology in Diverse Neurodegeneration Models, and Extend C. elegans Life- and Healthspan

Kakraba, S., Ayyadevara, S., Mainali, N., Balasubramaniam, M., Bowroju, S., Penthala, N. R., Atluri, R., Barger, S. W., Griffin, S. T., Crooks, P. A., et al. (2023) · Pharmaceuticals · doi:10.3390/ph16101498 · Cited by 13 · see citing works

Tau phosphorylation and OPA1 proteolysis are unrelated events: Implications for Alzheimer's Disease

Alavi, M. V. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119116 · Cited by 12 · see citing works

VDAC electronics: 5. Mechanism and computational model of hexokinase-dependent generation of the outer membrane potential in brain mitochondria

Lemeshko, V. V. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.10.004 · Cited by 12 · see citing works

Systemic Treatment with siRNA Targeting Gamma-Secretase Activating Protein Inhibits Amyloid-β Accumulation in Alzheimer’s Disease

Kim, S., Ullah, I., Beloor, J., Chung, K., Kim, J.-K., Yi, Y., Kang, E., Yun, G., Heo, S., Pyun, S.-H., et al. (2024) · Biomaterials Research · doi:10.34133/bmr.0027 · Cited by 11 · see citing works

Mitochondria-targeting by small molecules against Alzheimer's disease: A mechanistic perspective

Pal, C. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167617 · Cited by 12 · see citing works

Role of Glycogen Synthase Kinase 3 in Molecular Pathology of Alzheimer’s Disease

Gupta, A. (2022) · International Journal of Health Sciences and Pharmacy · doi:10.47992/ijhsp.2581.6411.0093 · Cited by 1 · see citing works

Role of glycogen synthase kinase-3 in the pathogenesis of Alzheimer's disease

Li, S. (2011)

Glycogen synthase kinase-3 signaling in Alzheimer's disease

Lauretti, E., Dincer, O., & Praticò, D. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118664 · Cited by 624 · see citing works

Role of glycogen synthase kinase 3 in Alzheimer's disease

Xiaomei, L. (2010) · International Journal of Pathology and Clinical Medicine

Glycogen synthase kinase 3β and Alzheimer’s disease: pathophysiological and therapeutic significance

Balaraman, Y., Limaye, A. R., Levey, A. I., & Srinivasan, S. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5597-y · Cited by 167 · see citing works