Cited by 149Alzheimer's disease research and treatmentsMitochondrial Function and PathologyNeuroscience and Neuropharmacology Research

The DOI matches its Crossref record; 131 of the 133 references it cites were found in a registry or an index.

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

Open access

Reddy, P. Hemachandra·2013·Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease

DOI 10.1016/j.bbadis.2013.06.012PMC PMC3825775

Open this paper in CoChat — free account Open PDF

Abstract

Glycogen synthase kinase 3 (GSK3) is a serine/threonine protein kinase that is involved in the multiple signaling processes of a cell. Increasing evidence suggests that GSK3β plays a key role in multiple cellular processes in the progression of diabetes, obesity, Alzheimer's disease (AD), Parkinson's disease (PD), inflammatory diseases, schizophrenia, bipolar and several mood disorders, and mitochondrial diseases. Recent research has found that increased GSK3β activity is linked to the pathogenesis of AD through amyloid beta (Aβ), phosphorylated tau and mitochondrial dysfunction. Recent research has also revealed that GSK3β is elevated in AD-affected tissues and is critically involved in dissociating the voltage-dependent anion channel 1 (VDAC1) protein from hexokinases, and causing disrupted glucose metabolism, mitochondrial dysfunction and activating apoptotic cell death. The purpose of this article is to review recent research that is elucidating the role of GSK3β in AD pathogenesis. We discuss the involvement of GSK3β in the phosphorylation of VDAC1 and dissociation of VADC1 with hexokinases in AD neurons.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.bbadis.2013.06.012

Cites

131 of 131 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The phosphatidylinositol 3-Kinase–AKT pathway in human cancer
Vivanco, I., & Sawyers, C. L. (2002) · Nature reviews. Cancer · doi:10.1038/nrc839 · Cited by 6,155
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
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 3,372
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
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
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
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
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
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
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 1,535

Flagged first, then by citations

Show all 133 references

2 of the 133 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

Jimenez, 2011, J. Biol. Chem., 286, 18414-1825

Sorted by citations

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 378
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 297
“…to contribute to Aβ accumulation, tau phosphorylation, and neuronal damage in models of AD (DaRocha-Souto et al., 2012; Hernandez et al., 2013; Hurtado et al., 2012; Reddy, 2013), SYK-related modulation of the GSK3β pathway may contribute to the exacerbation of disease seen in 5xFAD SykΔMG mice.”
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 331
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
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
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
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 280
Self-citation
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 226
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 230
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 208
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
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
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 170
Self-citation
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 165
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 148
Self-citation
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
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 135
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
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
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 109
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 96
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 96
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 91
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 86
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 89
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 80
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 84
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
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 79
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
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 76
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
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 72
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 70
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
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
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 64
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 60
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
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
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 65
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 57
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 50
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 52
Self-citation
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
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
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 54
Mitochondrial calcium signalling and neurodegenerative diseases
Britti, E., Delaspre, F., Tamarit, J., & Ros, J. (2018) · Neuronal Signaling · doi:10.1042/ns20180061 · Cited by 47
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
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 48
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
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 44
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
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 41
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
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
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 34
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
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 41
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 35
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
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 32
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 31
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
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 34
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 32
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 31
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 29
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
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
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 27
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 27
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
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 26
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 28
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
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
Self-citation
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 25
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
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
Alzheimer Disease: The Role of Aβ in the Glutamatergic System
Campos‐Peña, V., & Antônio, M. (2014) · InTech eBooks · doi:10.5772/57367 · Cited by 24
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
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 18
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 20
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
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
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., Seixas, F., Collares, T., Alves, D., Praticò, D., & Savegnago, L. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00661 · Cited by 17
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
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 20
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
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 16
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
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
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 13
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
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 10
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
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 14
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
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

Authors: Reddy, P. H.
Affiliations: Oregon National Primate Research Center (US)
Corresponding author: Reddy, P. Hemachandra
ORCID: Reddy, P. Hemachandra
Venue: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Publisher: Elsevier BV
Published: 2013-12
Volume: 1832
Issue: 12
Pages: 1913-1921
ISSN: 0925-4439 (ISSN-L)
DOI: 10.1016/j.bbadis.2013.06.012
PMC: PMC3825775
OpenAlex: W2077701948
Cited by: 147
References: 133
Citations by year: 2026: 9 · 2025: 13 · 2024: 12 · 2023: 12 · 2022: 16 · 2021: 15 · 2020: 10 · 2019: 12 · 2018: 13 · 2017: 9 · 2016: 5 · 2015: 11 · 2014: 10
FWCI: 0.96
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 365 d)
Locations: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: NIH (AG028072, AG042178, RR000163)
Medical Research Foundation of Oregon
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: Alzheimer's disease, glycogen synthase kinase-3β, VDAC1, amyloid-beta, hexokinase, mitochondrial dysfunction, glucose metabolism, synaptic dysfunction, neuronal injury, apoptosis
MeSH terms: Glycogen Synthase Kinase 3 beta, Alzheimer Disease, Animals, Humans, Neurons, Phosphorylation, Synapses, Amyloid beta-Peptides, Glycogen Synthase Kinase 3, Voltage-Dependent Anion Channel 1

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks