Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer’s disease
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The purpose of our study was to determine the relationship between voltage-dependent anion channel 1 protein (VDAC1) and amyloid beta (Aβ) and phosphorylated tau in Alzheimer's disease (AD). Using brain specimens from AD patients, control subjects and 6-, 12- and 24-month-old Aβ precursor protein (APP) transgenic mice, we studied VDAC1 protein levels. Further, we also studied the interaction between VDAC1 and Aβ (monomers and oligomers) and phosphorylated tau, using cortical issues from AD patients, control subjects, APP, APP/PS1 and 3XTg.AD mice. We also studied age- and VDAC1-linked, mutant APP/Aβ-induced mitochondrial dysfunction in APP and non-transgenic wild-type (WT) mice. We found progressively increased levels of VDAC1 in the cortical tissues from the brains of patients with AD, relative to control subjects, and significantly increased levels of VDAC1 in the cerebral cortices of 6-, 12- and 24-month-old APP transgenic mice, relative to the age-matched control WT mice. Interestingly, we found VDAC1 interacted with Aβ and phosphorylated tau in the brains from AD patients and from APP, APP/PS1 and 3XTg.AD mice. We found progressively increased mitochondrial dysfunction in APP mice relative to WT mice. These observations led us to conclude that VDAC1 interacts with Aβ, and phosphorylated tau may in turn block mitochondrial pores, leading to mitochondrial dysfunction in AD pathogenesis. Based on current study observations, we propose that reduced levels of VDAC1, Aβ and phosphorylated tau may reduce the abnormal interaction between VDAC1 and APP, VDAC1 and Aβ, and VDAC1 and phosphorylated tau; and that reduced levels of VDAC1, Aβ and phosphorylated tau may maintain normal mitochondrial pore opening and pore closure, ultimately leading to normal mitochondrial function, mitochondria supplying ATP to nerve terminals and boosting synaptic and cognitive function in AD.
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VDAC1 overexpression, which favors oligomerization and promotes apoptosis, is present in AD brain and increases as the disease progresses.
“VDAC1 overexpression, which favors oligomerization and promotes apoptosis [103], is present in AD brain and increases as the disease progresses [104].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [104]
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Cites
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
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210 · see citing works
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · 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
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
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367 · see citing works
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303 · see citing works
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224 · see citing works
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
Self-citationBorchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., Copeland, N. G., Price, D. L., & Sisodia, S. S. (1997) · Neuron · doi:10.1016/s0896-6273(00)80974-5 · Cited by 1,023 · see citing works
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
Self-citationYao, 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
Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 935 · 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
Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885 · see citing works
Wang, X., Su, B., Siedlak, S. L., Moreira, P. I., Fujioka, H., Wang, Y., Casadesus, G., & Zhu, X. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804871105 · Cited by 835 · see citing works
Mańczak, M., Calkins, M. J., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr139 · Cited by 830 · see citing works
Self-citationEbneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., Mandelkow, E.-M., & Mandelkow, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.3.777 · Cited by 820 · see citing works
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
Praticò, D., Uryu, K., Leight, S., Trojanoswki, J. Q., & Lee, V. M.-Y. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-12-04183.2001 · Cited by 777 · see citing works
A “mitochondrial cascade hypothesis” for sporadic Alzheimer’s disease
Swerdlow, R. H., & Khan, S. M. (2004) · Medical Hypotheses · doi:10.1016/j.mehy.2003.12.045 · Cited by 758 · 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
Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model
Du, H., Guo, L., Yan, S., Sosunov, A. A., McKhann, G. M., & ShiDu Yan, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006586107 · Cited by 704 · see citing works
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
Rhein, V., Song, X., Wiesner, A., Ittner, L. M., Baysang, G., Meier, F., Ozmen, L., Bluethmann, H., Dröse, S., Brandt, U., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905529106 · Cited by 655 · see citing works
Calkins, M. J., Manczak, M., Mao, P., Shirendeb, U., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr381 · Cited by 646 · see citing works
Self-citationCytochrome 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
Demonstration of amyloid deposits and neurofibrillary changes in whole brain sections
Braak, H., & Braak, E. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00661.x · Cited by 598 · see citing works
Choo, Y. S. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh162 · Cited by 515 · see citing works
Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport
Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L. (2010) · Science · doi:10.1126/science.1194653 · Cited by 486 · 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
Self-citationMańczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds072 · Cited by 453 · see citing works
Self-citationIncreased 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
Proteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice
David, D. C., Hauptmann, S., Scherping, I., Schuessel, K., Keil, U., Rizzu, P., Ravid, R., Dröse, S., Brandt, U., Müller, W. E., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500356200 · Cited by 447 · see citing works
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
Self-citationClogging of axons by tau, inhibition of axonal traffic and starvation of synapses.
Mandelkow, E., Stamer, K., Vogel, R., Thies, E., & Mandelkow, E. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.007 · Cited by 422 · see citing works
Shirendeb, U. P., Calkins, M. J., Mańczak, M., Anekonda, V., Dufour, B. D., McBride, J. L., Mao, P., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr475 · Cited by 383 · see citing works
Self-citationRostovtseva, T. K., & Colombini, M. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78841-6 · Cited by 357 · see citing works
Abnormalities of mitochondrial enzymes in Alzheimer disease
Gibson, G. E., Sheu, K.-F. R., & Blass, J. P. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050099 · Cited by 345 · see citing works
Brain oxidative stress in a triple-transgenic mouse model of Alzheimer disease
Resende, R., Moreira, P. I., Proença, T., Deshpande, A., Busciglio, J., Pereira, C., & Oliveira, C. R. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.012 · Cited by 343 · see citing works
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
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
Self-citationMisfolded Mutant SOD1 Directly Inhibits VDAC1 Conductance in a Mouse Model of Inherited ALS
Israelson, A., Arbel, N., Cruz, S. D., Ilieva, H. S., Yamanaka, K., Shoshan‐Barmatz, V., & Cleveland, D. W. (2010) · Neuron · doi:10.1016/j.neuron.2010.07.019 · Cited by 313 · see citing works
Reddy, P. H. (2011) · Brain Research · doi:10.1016/j.brainres.2011.07.052 · Cited by 300 · see citing works
Self-citationRegulation 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
Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice
Li, F., Calingasan, N. Y., Yu, F., Mauck, W. M., Toidze, M., Almeida, C. G., Takahashi, R. H., Carlson, G. A., Beal, M. F., Lin, M. T. S., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02455.x · Cited by 276 · 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
Calkins, M. J., & Reddy, P. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.01.007 · Cited by 244 · see citing works
Self-citationReddy, 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
Self-citationProteomics Analysis of the Alzheimer's Disease Hippocampal Proteome
Rukhsana Sultana, A., Debra Boyd-kimball, A., Cai, J., Pierce, W. M. J., Klein, J. B., Merchant, M. L., & Butterfield, D. A. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11203 · Cited by 231 · see citing works
Zheng, Y., Shi, Y., Tian, C., Jiang, C., Jin, H., Chen, J., Almasan, A., Tang, H., & Chen, Q. (2003) · Oncogene · doi:10.1038/sj.onc.1207205 · Cited by 202 · 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
Self-citationEckert, A., Hauptmann, S., Scherping, I., Rhein, V. F., Müller-Spahn, F., Götz, J., & Müller, W. E. (2008) · Neurodegenerative Diseases · doi:10.1159/000113689 · Cited by 153 · 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
Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N. N., Yang, L., Starkov, A. A., & Beal, F. M. (2011) · The FASEB Journal · doi:10.1096/fj.11-186650 · Cited by 139 · see citing works
Schmidt, C., Lepsverdize, E., L, S., Das, A. M., Pizzo, S. V., Dityatev, A. E., & Schachner, M. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4002077 · Cited by 136 · see citing works
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
Amyloid-β-Derived Diffusible Ligands Cause Impaired Axonal Transport of Mitochondria in Neurons
Wang, X., Perry, G. L., Smith, M. A., & Zhu, X. (2010) · Neurodegenerative Diseases · doi:10.1159/000283484 · Cited by 126 · see citing works
Early dysregulation of the mitochondrial proteome in a mouse model of Alzheimer's disease
Chou, J. L., Shenoy, D. V., Thomas, N., Choudhary, P. K., LaFerla, F. M., Goodman, S. R., & Breen, G. A. M. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2010.12.012 · Cited by 123 · see citing works
Devi, L., & Ohno, M. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.09.001 · Cited by 121 · 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
Dubey, M., Chaudhury, P., Kabiru, H., & Shea, T. B. (2007) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20243 · Cited by 91 · see citing works
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
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
Sampson, M. J., Lovell, R. S., & Craigen, W. J. (1996) · Genomics · doi:10.1006/geno.1996.0193 · Cited by 69 · see citing works
Mańczak, M., Sesaki, H., Kageyama, Y., & Reddy, P. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.02.017 · Cited by 69 · see citing works
Self-citationA Novel Mouse Mitochondrial Voltage-Dependent Anion Channel Gene Localizes to Chromosome 8
Sampson, M. J., Lovell, R. S., Davison, D. B., et al. (1996) · Genomics · doi:10.1006/geno.1996.0445 · Cited by 60 · see citing works
Sampson, M. J., Ross, L. O., Decker, W. K., & Craigen, W. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30482 · Cited by 55 · see citing works
Positive effects of pollution?
Friebe, A., Malkewitz, J., Schultz, G., et al. (1996) · Nature · doi:10.1038/382120a0 · Cited by 52 · see citing works
Sensi, S. L., Rapposelli, I. G., Frazzini, V., & Mascetra, N. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.10.018 · Cited by 49 · see citing works
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
Matsumoto, K., Akao, Y., Yi, H. L., Shamoto‐Nagai, M., Maruyama, W., & Naoi, M. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-005-0318-0 · Cited by 33 · see citing works
THINNES, F. P. (2011) · Wiener Medizinische Wochenschrift · doi:10.1007/s10354-011-0887-5 · Cited by 31 · see citing works
Mitochondria morphology and DNA content upon sublethal exposure to beta-amyloid(1-42) peptide.
Diana, A., Šimić, G., Sinforiani, E., Orrù, N., Pichiri, G., & Bono, G. G. (2008) · PubMed · Cited by 28 · see citing works
Xu, X., & Colombini, M. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78855-6 · Cited by 21 · see citing works
Flagged first, then by citations
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Busche, M. A., & Hyman, B. T. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0687-6 · Cited by 1,242 · see citing works
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870 · 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
Tau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272 · see citing works
Mitochondria and Calcium in Alzheimer’s Disease: From Cell Signaling to Neuronal Cell Death
Calvo-Rodriguez, M., & Bacskai, B. J. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2020.10.004 · Cited by 254 · see citing works
The Association of Tau With Mitochondrial Dysfunction in Alzheimer’s Disease
Cheng, Y., & Bai, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00163 · Cited by 239 · see citing works
Mitochondrial Dysfunction and Synaptic Transmission Failure in Alzheimer’s Disease
Guo, L., Tian, J., & Du, H. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160702 · Cited by 211 · see citing works
Towards a Better Understanding of GABAergic Remodeling in Alzheimer’s Disease
Govindpani, K., Calvo-Flores Guzmán, B., Vinnakota, C., Waldvogel, H., Faull, R., & Kwakowsky, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081813 · Cited by 208 · 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
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
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
Self-citationSmilansky, 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
Corsetti, V., Florenzano, F., Atlante, A., Bobba, A., Ciotti, M. T., Natale, F., Della Valle, F., Borreca, A., Manca, A., Meli, G., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv059 · Cited by 129 · see citing works
Mitochondrial cholesterol: mechanisms of import and effects on mitochondrial function
Martin, L. A., Kennedy, B. E., & Karten, B. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9592-6 · Cited by 128 · 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
Differential S-nitrosylation of proteins in Alzheimer’s disease
Zahid, S., Khan, R., Oellerich, M., Ahmed, N., & Asif, A. R. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2013.10.026 · Cited by 91 · see citing works
Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease
Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85 · see citing works
“VDAC1 overexpression, which favors oligomerization and promotes apoptosis [103], is present in AD brain and increases as the disease progresses [104].”
BackgroundVDAC1-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
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
Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67 · see citing works
(2020) · International Review of Neurobiology · doi:10.1016/bs.irn.2020.02.010 · Cited by 58 · see citing works
Vijayan, M., Alvir, R. V., Alvir, R. V., Bunquin, L. E., Pradeepkiran, J. A., & Reddy, P. H. (2022) · Aging Cell · doi:10.1111/acel.13663 · Cited by 40 · see citing works
Self-citationBotchway, B. O., Okoye, F. C., Chen, Y., Arthur, W. E., & Fang, M. (2022) · Aging and disease · doi:10.14336/ad.2021.0616 · Cited by 32 · see citing works
Zhu, Q., Niu, Y., Gundry, M., & Zong, C. (2021) · Science Advances · doi:10.1126/sciadv.abf3329 · Cited by 18 · see citing works
Molecular mechanisms of Alzheimer’s disease: From therapeutic targets to promising drugs
Alan, E., Kerry, Z., & Sevin, G. (2023) · Fundamental & Clinical Pharmacology · doi:10.1111/fcp.12861 · Cited by 17 · see citing works
- Authors
- Manczak, M., & Reddy, P. H.
- Affiliations
- Oregon National Primate Research Center (US)
- Corresponding author
- Reddy, P. H.
- ORCID
- Reddy, P. H.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2012-08-27
- Volume
- 21
- Issue
- 23
- Pages
- 5131-5146
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC3490521
- OpenAlex
- W2144956444
- Cited by
- 348
- References
- 78
- Citations by year
- 2026: 22 · 2025: 35 · 2024: 33 · 2023: 37 · 2022: 33 · 2021: 38 · 2020: 36 · 2019: 15 · 2018: 17 · 2017: 18 · 2016: 15 · 2015: 18 · 2014: 14 · 2013: 15 · 2012: 1
- FWCI
- 10.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Human Molecular Genetics (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Oregon Health and Science University
- National Institutes of Health (RR000163)
- Oregon National Primate Research Center (RR000163)
- National Institute on Aging (R01AG042178, R01AG028072, AG028072, AG042178)
- National Institute of Neurological Disorders and Stroke (P30NS061800)
- National Center for Research Resources (RR000163)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- VDAC1, amyloid-beta, phosphorylated tau, Alzheimer's disease, mitochondrial dysfunction, APP transgenic mice, APP/PS1 mice, 3xTg-AD mice, protein-protein interaction, cortical tissue
- MeSH terms
- Age Factors, Alzheimer Disease, Animals, Brain, Disease Models, Animal, Humans, Mice, Transgenic, Mitochondria, Phosphorylation, Protein Binding, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, tau Proteins, Voltage-Dependent Anion Channel 1, Mice
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