VDAC1, mitochondrial dysfunction, and Alzheimer’s disease

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Lipid Rafts: Linking Alzheimer′s Amyloid‐βProduction, Aggregation, and Toxicity at Neuronal Membranes

Rushworth, J. V., & Hooper, N. M. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/603052 · Cited by 218 · see citing works

lncRNA H19/miR-675 axis regulates cardiomyocyte apoptosis by targeting VDAC1 in diabetic cardiomyopathy

Li, X., Wang, H., Yao, B., Xu, W., Chen, J., & Zhou, X. (2016) · Scientific Reports · doi:10.1038/srep36340 · Cited by 213 · see citing works

Hierarchical involvement of Bak, VDAC1 and Bax in cisplatin-induced cell death

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Mitochondria in Neurodegeneration

Lezi, E., & Swerdlow, R. H. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_12 · Cited by 204 · see citing works

Mitochondria and Cell Bioenergetics: Increasingly Recognized Components and a Possible Etiologic Cause of Alzheimer's Disease

Swerdlow, R. H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4149 · Cited by 203 · see citing works

Early alterations in energy metabolism in the hippocampus of APPswe/PS1dE9 mouse model of Alzheimer's disease

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Mitochondrial Dysfunction: The First Domino in Brain Aging and Alzheimer's Disease?

Leuner, K., Hauptmann, S., Abdel-Kader, R. M., Scherping, I., Keil, U., Strosznajder, J. B., Eckert, A., & Müller, W. E. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1763 · Cited by 194 · see citing works

VDAC1: from structure to cancer therapy

Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 193 · see citing works

The involvement of lipid rafts in Alzheimer's disease (Review)

Cordy, J. M., Cordy, J. M., Hooper, N. M., & Turner, A. J. (2006) · Molecular Membrane Biology · doi:10.1080/09687860500496417 · Cited by 188 · see citing works

Intracellular Amyloid-β1–42, but Not Extracellular Soluble Amyloid-β Peptides, Induces Neuronal Apoptosis

Kienlen-Campard, P., Miolet, S., Tasiaux, B., & Octave, J.-N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200887200 · Cited by 187 · see citing works

Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model

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The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis.

Vyssokikh, M. Y., & Brdiczka, D. G. (2003) · Acta Biochimica Polonica · doi:10.18388/abp.2003_3693 · Cited by 185 · see citing works

Role of Mitochondrial Amyloid-β in Alzheimer's Disease

Chen, J. X., & Yan, S. S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100357 · Cited by 181 · see citing works

The Role of Mitochondrial Porins and the Permeability Transition Pore in Learning and Synaptic Plasticity

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Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein

Arbel, N., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.345918 · Cited by 179 · see citing works

Uncovering the role of VDAC in the regulation of cell life and death

Shoshan‐Barmatz, V., Keinan, N., & Zaid, H. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9147-9 · Cited by 179 · see citing works

Voltage-dependent Anion Channel-1 (VDAC-1) Contributes to ATP Release and Cell Volume Regulation in Murine Cells

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A brief overview of amyloids and Alzheimer's disease

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Voltage‐dependent anion‐selective channel (VDAC) in the plasma membrane

Pinto, V. D., Messina, A. A., Lane, D. J. R., & Lawen, A. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.049 · Cited by 174 · see citing works

The Supramolecular Assemblies of Voltage-dependent Anion Channels in the Native Membrane

Hoogenboom, B. W., Suda, K., Engel, A. H., & Fotiadis, D. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.073 · Cited by 174 · see citing works

A Greek Tragedy: The Growing Complexity of Alzheimer Amyloid Precursor Protein Proteolysis

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Voltage-dependent Anion Channel 1-based Peptides Interact with Hexokinase to Prevent Its Anti-apoptotic Activity

Arzoine, L., Zilberberg, N., Ben-Romano, R., & Shoshan‐Barmatz, V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803614200 · Cited by 173 · see citing works

Cancer and Neurodegeneration: Between the Devil and the Deep Blue Sea

Plun‐Favreau, H., Lewis, P. A., Hardy, J., Martins, L. M., & Wood, N. W. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001257 · Cited by 173 · see citing works

Altered mitochondria, energy metabolism, voltage-dependent anion channel, and lipid rafts converge to exhaust neurons in Alzheimer’s disease

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Tauopathies with parkinsonism: clinical spectrum, neuropathologic basis, biological markers, and treatment options

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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

Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity

Arbel, N., & Shoshan-Barmatz, V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082990 · Cited by 168 · see citing works

NMR Structural Investigation of the Mitochondrial Outer Membrane Protein VDAC and Its Interaction with Antiapoptotic Bcl-xL

Malia, T., & Wagner, G. (2006) · Biochemistry · doi:10.1021/bi061577h · Cited by 164 · see citing works

Signaling pathway cross talk in Alzheimer’s disease

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VDAC is a conserved element of death pathways in plant and animal systems

Godbole, A., Varghese, J., Sarin, A., & Mathew, M. K. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(03)00102-2 · Cited by 162 · see citing works

Characterization of human VDAC isoforms: A peculiar function for VDAC3?

Pinto, V. D., Guarino, F., Guarnera, A., Messina, A. A., Reina, S., Tomasello, M. F., Palermo, V., & Mazzoni, C. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.031 · Cited by 159 · see citing works

The voltage-dependent anion channel

Shoshan-Barmatz, V., & Gincel, D. (2007) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:39:3:279 · Cited by 158 · see citing works

Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins

Shi, Y., Chen, J., Weng, C., Chen, R., Zheng, Y., Chen, Q., & Tang, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00871-4 · Cited by 158 · see citing works

Convergence of Amyloid-β and Tau Pathologies on Mitochondria In Vivo

Eckert, A., Schulz, K. L., Rhein, V. F., & Götz, J. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8109-5 · Cited by 158 · see citing works

VDAC1 Is a Transplasma Membrane NADH-Ferricyanide Reductase

Baker, M. A., Lane, D. J. R., Ly, J. D., Pinto, V. D., & Lawen, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311020200 · Cited by 158 · see citing works

Novel Compounds Targeting the Mitochondrial Protein VDAC1 Inhibit Apoptosis and Protect against Mitochondrial Dysfunction

Ben-Hail, D., Begas-Shvartz, R., Shalev, M., Shteinfer-Kuzmine, A., Gruzman, A., Reina, S., De Pinto, V., & Shoshan-Barmatz, V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744284 · Cited by 158 · see citing works

Supramolecular Assembly of VDAC in Native Mitochondrial Outer Membranes

Gonçalves, R. P., Buzhynskyy, N., Prima, V., Sturgis, J. N., & Simon Scheuring, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.063 · Cited by 157 · see citing works

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

Reddy, P. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.012 · Cited by 147 · see citing works

Apoptosis is regulated by the VDAC1 N-terminal region and by VDAC oligomerization: release of cytochrome c, AIF and Smac/Diablo

Shoshan‐Barmatz, V., Keinan, N., Abu‐Hamad, S., Tyomkin, D., & Aram, L. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.003 · Cited by 147 · see citing works

Brain-specific knockdown of miR-29 results in neuronal cell death and ataxia in mice

Roshan, R., Shridhar, S., Sarangdhar, M. A., Banik, A., Chawla, M., Garg, M., Singh, V. P., & Pillai, B. (2014) · RNA · doi:10.1261/rna.044008.113 · Cited by 146 · see citing works

Diagnosis and biomarkers of predementia in Alzheimer's disease

Forlenza, O. V., Diniz, B. S., & Gattaz, W. F. (2010) · BMC Medicine · doi:10.1186/1741-7015-8-89 · Cited by 145 · see citing works

Mitochondrial import and degradation of amyloid-β peptide

Pinho, C. M., Teixeira, P. F., & Glaser, E. G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.02.007 · Cited by 145 · 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

Mitochondria and Neurodegeneration

Petrozzi, L., Ricci, G., Giglioli, N. J., Siciliano, G., & Mancuso, M. (2007) · Bioscience Reports · doi:10.1007/s10540-007-9038-z · Cited by 140 · see citing works

Cytochrome c release from isolated rat liver mitochondria can occur independently of outer-membrane rupture: possible role of contact sites

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Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.

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Mitochondrial VDAC1: Function in Cell Life and Death and a Target for Cancer Therapy

Shoshan‐Barmatz, V., & Golan, M. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712798992110 · Cited by 139 · see citing works

Voltage‐dependent anion channel 1 is involved in endostatin‐induced endothelial cell apoptosis

Yuan, S., Fu, Y., Wang, X., Shi, H., Huang, Y., Song, X., Li, L., Song, N., & Luo, Y. (2008) · The FASEB Journal · doi:10.1096/fj.08-107417 · Cited by 137 · see citing works

Truncated tau and Aβ cooperatively impair mitochondria in primary neurons

Quintanilla, R. A., Dolan, P. J., Jin, Y. N., & Johnson, G. V. W. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.007 · Cited by 136 · 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

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

Altered Mitochondrial Sensitivity for ADP and Maintenance of Creatine-stimulated Respiration in Oxidative Striated Muscles from VDAC1-deficient Mice

Anflous, K., Armstrong, D. D., & Craigen, W. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006587200 · Cited by 132 · see citing works

Insights into Mitochondrial Dysfunction: Aging, Amyloid-β, and Tau–A Deleterious Trio

Schmitt, K., Grimm, A., Wilkaniec, A., Strosznajder, J. B., Götz, J., & Eckert, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4400 · Cited by 132 · see citing works

MicroRNA-7 Regulates the Function of Mitochondrial Permeability Transition Pore by Targeting VDAC1 Expression

Chaudhuri, A., Choi, D. C., Kabaria, S., Tran, A., & Junn, E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691352 · Cited by 132 · see citing works

Insulin dysfunction and Tau pathology

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Evidence for secretory pathway localization of a voltage-dependent anion channel isoform

Buettner, R., Papoutsoglou, G., Scemes, E., Spray, D. C., & Dermietzel, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3201 · Cited by 131 · see citing works

Nuclear but not mitochondrial‐encoded oxidative phosphorylation genes are altered in aging, mild cognitive impairment, and Alzheimer's disease

Mastroeni, D., Khdour, O. M., Delvaux, E., Nolz, J., Olsen, G., Berchtold, N. C., Cotman, C. W., Hecht, S. M., & Coleman, P. D. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.09.003 · Cited by 131 · see citing works

Connecting Alzheimer's disease to diabetes: Underlying mechanisms and potential therapeutic targets

Vieira, M. N. N., Lima‐Filho, R. A. S., & Felice, F. G. D. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.11.014 · Cited by 131 · see citing works

Metformin promotes tau aggregation and exacerbates abnormal behavior in a mouse model of tauopathy

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A Mitocentric View of Alzheimer's Disease Suggests Multi-Faceted Treatments

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Porin Is Present in the Plasma Membrane Where It Is Concentrated in Caveolae and Caveolae-related Domains

Báthori, G., Parolini, I., Tombola, F., Szabó, I., Messina, A. A., Oliva, M., Pinto, V. D., Lisanti, M. P., Sargiacomo, M., & Zoratti, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.29607 · Cited by 121 · see citing works

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

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New perspectives on the role of tau in Alzheimer's disease. Implications for therapy

Medina, M., & Ávila, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.013 · Cited by 118 · see citing works

The role of calcium in VDAC1 oligomerization and mitochondria-mediated apoptosis

Keinan, N., Pahima, H. T., Ben-Hail, D., & Shoshan‐Barmatz, V. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.017 · Cited by 116 · see citing works

Bidirectional interactions between diabetes and Alzheimer's disease

Shinohara, M., & Sato, N. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.04.020 · Cited by 115 · see citing works

The Role of Lipids in VDAC Oligomerization

Betaneli, V., Petrov, E. P., & Schwille, P. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.049 · Cited by 113 · see citing works

Mitochondrial Creatine Kinase in Contact Sites: Interaction with Porin and Adenine Nucleotide Translocase, Role in Permeability Transition and Sensitivity to Oxidative Damage

Dolder, M., Wendt, S., & Wallimann, T. (2001) · Neurosignals · doi:10.1159/000046878 · Cited by 113 · see citing works

Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium

Schlattner, U., Dolder, M., Wallimann, T., & Tokarska-Schlattner, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106524200 · Cited by 111 · see citing works

Ca2+-mediated regulation of VDAC1 expression levels is associated with cell death induction

Algor, S. W., Keinan, N., Ben-Hail, D., Arif, T., & Shoshan‐Barmatz, V. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.021 · Cited by 106 · see citing works

Tau-Based Therapeutic Approaches for Alzheimer's Disease - A Mini-Review

Boutajangout, A., & Wısnıewskı, T. (2014) · Gerontology · doi:10.1159/000358875 · Cited by 105 · 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

Structure-based Analysis of VDAC1 Protein

Geula, S., Naveed, H., Liang, J., & Shoshan-Barmatz, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.268920 · Cited by 97 · see citing works

Interaction between NH2-tau fragment and Aβ in Alzheimer's disease mitochondria contributes to the synaptic deterioration

Amadoro, G., Corsetti, V., Atlante, A., Florenzano, F., Capsoni, S., Bussani, R., Mercanti, D., & Calissano, P. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.08.001 · Cited by 94 · see citing works

Molecular correlates of axonal and synaptic pathology in mouse models of Batten disease

Kielar, C., Wishart, T. M., Palmer, A., Dihanich, S., Wong, A. M., Macauley, S. L., Chan, C.-H., Sands, M. S., Pearce, D. A., Cooper, J. D., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp355 · Cited by 93 · see citing works

Pin1: A New Genetic Link between Alzheimers Disease, Cancer and Aging

Driver, J. A., & Lu, K. P. (2010) · Current Aging Science · doi:10.2174/1874609811003030158 · Cited by 92 · see citing works

A NH2 Tau Fragment Targets Neuronal Mitochondria at AD Synapses: Possible Implications for Neurodegeneration

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VDAC and ERα interaction in caveolae from human cortex is altered in Alzheimer's disease

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The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins

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The formation of prostaglandins in the postmortem cerebral cortex of Alzheimer-type dementia patients

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Oligomerization of the Mitochondrial Protein VDAC1

Shoshan‐Barmatz, V., Mizrachi, D., & Keinan, N. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-386931-9.00011-8 · Cited by 87 · see citing works

Is the mitochondrial outermembrane protein VDAC1 therapeutic target for Alzheimer's disease?

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Voltage-dependent anion channel (VDAC) participates in amyloid beta-induced toxicity and interacts with plasma membrane estrogen receptor α in septal and hippocampal neurons

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Mitochondrial Abnormalities in Alzheimer’s Disease

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Modes of Aβ toxicity in Alzheimer’s disease

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Each mammalian mitochondrial outer membrane porin protein is dispensable: effects on cellular respiration

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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

Impaired peripheral glucose homeostasis and Alzheimer's disease

Wijesekara, N., Gonçalves, R. A., Felice, F. G. D., & Fraser, P. E. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.11.027 · Cited by 80 · see citing works

VDAC1-based peptides: novel pro-apoptotic agents and potential therapeutics for B-cell chronic lymphocytic leukemia

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C-IGF1R encoded by cIGF1R acts as a molecular switch to restrict mitophagy of drug-tolerant persister tumour cells in non-small cell lung cancer

Wang, H., Liang, Y., Zhang, T., Yu, X., Song, X., Chen, Y., Mao, Q., Xia, W., Chen, B., Xu, L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01222-0 · Cited by 28 · see citing works

Bioenergetic failure and oxidative stress: mitochondrial contributions to Alzheimer’s disease

Wasim, R. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01916-6 · Cited by 30 · see citing works

Mitochondrial Calcium Signaling as a Therapeutic Target for Alzheimer’s Disease

Wu, A. J., Tong, B. C., Huang, S., Li, M., & Cheung, K. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191210091302 · Cited by 29 · see citing works

Alzheimer and Purinergic Signaling: Just a Matter of Inflammation?

Merighi, S., Poloni, T. E., Terrazzan, A., Moretti, E., Gessi, S., & Ferrari, D. (2021) · Cells · doi:10.3390/cells10051267 · Cited by 29 · see citing works

Mitochondria Have Made a Long Evolutionary Path from Ancient Bacteria Immigrants within Eukaryotic Cells to Essential Cellular Hosts and Key Players in Human Health and Disease

Atlante, A., & Valenti, D. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45050283 · Cited by 30 · see citing works

Role of Mitochondrial Dysfunction in the Pathology of Amyloid-β

Huang, Z., Yan, Q., Wang, Y., Zou, Q., Li, J., Liu, Z., & Cai, Z. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200519 · Cited by 28 · see citing works

Latest assessment methods for mitochondrial homeostasis in cognitive diseases

You, W., Li, Y., Liu, K., Mi, X., Li, Y., Guo, X., & Li, Z. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382222 · Cited by 27 · see citing works

The role of hydrogen therapy in Alzheimer's disease management: Insights into mechanisms, administration routes, and future challenges

He, J., Liu, F., Xu, T., Ma, J., Yu, H., Zhao, J., Xie, Y., Luo, L., Yang, Q., Lou, T., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115807 · Cited by 28 · see citing works

L-Carnitine in the Treatment of Psychiatric and Neurological Manifestations: A Systematic Review

Wang, W., Pan, D., Liu, Q., Chen, X., & Wang, S. (2024) · Nutrients · doi:10.3390/nu16081232 · Cited by 27 · see citing works

Baicalin attenuates amyloid β oligomers induced memory deficits and mitochondria fragmentation through regulation of PDE-PKA-Drp1 signalling

Yu, H., Zhu, Y., Zhang, X.-L., Wang, L., Yan-meng, Z., Zhang, F.-F., Zhang, H., & Zhao, X. (2022) · Psychopharmacology · doi:10.1007/s00213-022-06076-x · Cited by 26 · see citing works

Structural basis of apoptosis induction by the mitochondrial voltage-dependent anion channel

Daniilidis, M., Günsel, U., Broutzakis, G., Leitl, K. D., Janowski, R., Fredriksson, K., Niessing, D., Gatsogiannis, C., & Hagn, F. (2025) · Nature Communications · doi:10.1038/s41467-025-65363-1 · Cited by 25 · see citing works

Loss of mitochondrial fatty acid β‐oxidation protein short‐chain Enoyl‐CoA hydratase disrupts oxidative phosphorylation protein complex stability and function

Burgin, H. J., Sharpe, A. J., Nie, S., Ziemann, M., Crameri, J. J., Stojanovski, D., Pitt, J. J., Ohtake, A., Murayama, K., & McKenzie, M. (2022) · FEBS Journal · doi:10.1111/febs.16595 · Cited by 25 · see citing works

VDAC1, as a downstream molecule of MLKL, participates in OGD/R-induced necroptosis by inducing mitochondrial damage

Wan, H., Yang, Y., Zhāng, Q., Chen, Y., Hu, X., Huang, Y., Shang, L., & Xiong, K. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e23426 · Cited by 25 · see citing works

Inhibition of the Nrf2/HO-1 Axis Suppresses the Mitochondria-Related Protection Promoted by Gastrodin in Human Neuroblastoma Cells Exposed to Paraquat

de Oliveira, M. R., Brasil, F. B., & Fürstenau, C. R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1222-6 · Cited by 25 · see citing works

Calcium signaling hypothesis: A non-negligible pathogenesis in Alzheimer’s disease

Wang, M., Zhang, H., Liang, J., Huang, J., Wu, T., & Chen, N. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.01.007 · Cited by 25 · see citing works

Mitochondriomics reveals the underlying neuroprotective mechanism of TrkB receptor agonist R13 in the 5×FAD mice

Li, T., Li, X., Huang, X., Yu, H., Li, S., Zhang, Z., Xie, Y., Song, X., Liu, J., Yang, X., et al. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108899 · Cited by 24 · see citing works

Myricetin Restores Aβ-Induced Mitochondrial Impairments in N2a-SW Cells

Yao, X., Zhang, J., Lu, Y.-F., Deng, Y., Zhao, R., & Xiao, S. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00591 · Cited by 23 · see citing works

Construction and evaluation of Alzheimer’s disease diagnostic prediction model based on genes involved in mitophagy

Pei, Y., Chen, S., Zhou, F., Xie, T., & Cao, H. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1146660 · Cited by 23 · see citing works

Effects of luteolin on canine osteosarcoma: Suppression of cell proliferation and synergy with cisplatin

Ryu, S., Park, S., Lim, W., & Song, G. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27638 · Cited by 23 · see citing works

A review of the pathogenesis of mitochondria in breast cancer and progress of targeting mitochondria for breast cancer treatment

Huang, A., Xue, H., Xie, T., Xiang, L., Chen, Z., Ma, A., Yan, H., & Yuan, J. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06077-2 · Cited by 22 · see citing works

MicroRNA‐7a‐5p ameliorates diabetic peripheral neuropathy by regulating VDAC1/JNK/c‐JUN pathway

Jiao, Y., Zhang, Y., Wang, C., Yu, Y., Li, Y., Cui, W., Li, Q., & Yu, Y. (2022) · Diabetic Medicine · doi:10.1111/dme.14890 · Cited by 22 · see citing works

Critical appraisal on mitochondrial dysfunction in Alzheimer’s disease

Ahmad, F., & Sachdeva, P. (2022) · Aging Medicine · doi:10.1002/agm2.12217 · Cited by 22 · see citing works

Icariin protects against sodium azide—induced neurotoxicity by activating the PI3K/Akt/GSK-3β signaling pathway

Zhang, Y., Huang, N., Lu, H., Huang, J., Jin, H. D., Shi, J., & Jin, F. J. (2020) · PeerJ · doi:10.7717/peerj.8955 · Cited by 22 · see citing works

The Advancements of Marine Natural Products in the Treatment of Alzheimer’s Disease: A Study Based on Cell and Animal Experiments

Jia, C., Chai, J., Zhang, S., Sun, Y., He, L., Sang, Z., Chen, D., & Zheng, X. (2025) · Marine Drugs · doi:10.3390/md23030091 · Cited by 21 · see citing works

VDAC1 regulates neuronal cell loss after retinal trauma injury by a mitochondria-independent pathway

de Sousa, É., Móvio, M. I., de Lima-Vasconcellos, T. H., dos Santos, G. B., Gomes, T. D. S., Walter, L. T., da Silva, D. A., Rodrigues, T., Cerchiaro, G., & Kihara, A. H. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04755-3 · Cited by 21 · see citing works

Targeting VDAC: A potential therapeutic approach for mitochondrial dysfunction in Alzheimer's disease

Yang, Y., Jia, X.-T., Yang, X., Wang, J., Fang, Y., Ying, X., Zhang, M., Wei, J., & Pan, Y. (2024) · Brain Research · doi:10.1016/j.brainres.2024.148920 · Cited by 21 · see citing works

Mitochondrial Alterations in Alzheimer’s Disease: Insight from the 5xFAD Mouse Model

Keskinöz, E. N., Çelik, M., Toklucu, E. S., Birisik, K., Erişir, A., & Arslan, D. Ö. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04632-4 · Cited by 20 · see citing works

Effects of New Galantamine Derivatives in a Scopolamine Model of Dementia in Mice

Lazarova, M. I., Tancheva, L. P., Alexandrova, A., Tsvetanova, E. R., Georgieva, A. P., Stefanova, M. O., Tsekova, D. S., Vezenkov, L. T., Kalfin, R. E., Uzunova, D. N., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215165 · Cited by 20 · see citing works

Systematic Review of the Therapeutic Role of Apoptotic Inhibitors in Neurodegeneration and Their Potential Use in Schizophrenia

Morén, C., Treder, N., Martínez-Pinteño, A., Rodríguez, N., Arbelo, N., Madero, S., Gómez, M., Mas, S., Gassó, P., & Parellada, E. (2022) · Antioxidants · doi:10.3390/antiox11112275 · Cited by 20 · see citing works

Exploring lipid-dependent conformations of membrane-bound α-synuclein with the VDAC nanopore

Hoogerheide, D. P., Rostovtseva, T. K., & Bezrukov, S. M. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183643 · Cited by 20 · see citing works

Is the mitochondrial outermembrane protein VDAC1 therapeutic target for Alzheimer's disease?

Reddy, P. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.09.003 · Cited by 87 · 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

P1‐102: THE NEUROPROTECTIVE ROLE OF VDAC1 IN ALZHEIMER'S DISEASE

Anderson, A. J., Itaman, S., Davis, S. A., & Gitcho, M. A. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.06.105

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

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