Cited by 186Alzheimer's disease research and treatmentsMitochondrial Function and PathologyCoenzyme Q10 studies and effects

The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.

Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a mouse model of Alzheimer's disease

Open access

Fukui, Hirokazu, Diaz, Francisca, Garcia, Sofia, Moraes, Carlos T.·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0705738104PMC PMC1955773

Open this paper in CoChat — free account

Abstract

Defects in the mitochondrial cytochrome c oxidase (COX) have been associated with Alzheimer's Disease, in which the age-dependent accumulation of beta-amyloid plays an important role in synaptic dysfunction and neurodegeneration. To test the possibility that age-dependent decline in the mitochondrial respiratory function, especially COX activity, may participate in the formation and accumulation of beta-amyloid, we generated mice expressing mutant amyloid precursor protein and mutant presenilin 1 in a neuron-specific COX-deficient background. A neuron-specific COX-deficient mouse was generated by the Cre-loxP system, in which the COX10 gene was deleted by a CamKIIalpha promoter-driven Cre-recombinase. COX10 is a farnesyltransferase involved in the biosynthesis of heme a, required for COX assembly and function. These KO mice showed an age-dependent COX deficiency in the cerebral cortex and hippocampus. Surprisingly, COX10 KO mice exhibited significantly fewer amyloid plaques in their brains compared with the COX-competent transgenic mice. This reduction in amyloid plaques in the KO mouse was accompanied by a reduction in Abeta42 level, beta-secretase activity, and oxidative damage. Likewise, production of reactive oxygen species from cells with partial COX activity was not elevated. Collectively, our results suggest that, contrary to previous models, a defect in neuronal COX does not increase oxidative damage nor predispose for the formation of amyloidgenic amyloid precursor protein fragments.

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 · 10.1073/pnas.0705738104

Cites

45 of 45 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.

Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
Kujoth, G. C., Hiona, A., Pugh, T. D., Someya, S., Panzer, K., Wohlgemuth, S. E., Hofer, T., Seo, A. Y., Sullivan, R., Jobling, W. A., et al. (2005) · Science · doi:10.1126/science.1112125 · Cited by 2,165
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease
Bender, A., Krishnan, K. J., Morris, C. M., Taylor, G. A., Reeve, A. K., Perry, R. H., Jaros, E., Hersheson, J. S., Betts, J., Klopstock, T., et al. (2006) · Nature Genetics · doi:10.1038/ng1769 · Cited by 1,570
The Curry Spice Curcumin Reduces Oxidative Damage and Amyloid Pathology in an Alzheimer Transgenic Mouse
Lim, G. P., Chu, T., Yang, F., Beech, W., Frautschy, S. A., & Cole, G. M. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-21-08370.2001 · Cited by 1,530
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507
Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins
Borchelt, 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
A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity
Lee, S. S., Lee, R. Y. N., Fraser, A. G., Kamath, R. S., Ahringer, J., & Ruvkun, G. (2003) · Nature Genetics · doi:10.1038/ng1056 · Cited by 969
Co-expression of multiple transgenes in mouse CNS: a comparison of strategies
Jankowsky, J. L., Slunt, H. H., Ratovitski, T., Jenkins, N. A., Copeland, N. G., & Borchelt, D. R. (2001) · Biomolecular Engineering · doi:10.1016/s1389-0344(01)00067-3 · Cited by 746
Elevated β-secretase expression and enzymatic activity detected in sporadic Alzheimer disease
Yang, L.-B., Lindholm, K., Yan, R., Citron, M., Xia, W., Yang, X.-L., Beach, T., Sue, L., Wong, P., Price, D., et al. (2003) · Nature Medicine · doi:10.1038/nm0103-3 · Cited by 729

Show all 45 references

Sorted by citations

Glycolytic oligodendrocytes maintain myelin and long-term axonal integrity
Fünfschilling, U., Supplie, L. M., Mahad, D., Boretius, S., Saab, A. S., Edgar, J., Brinkmann, B. G., Kassmann, C. M., Tzvetanova, I. D., Möbius, W., et al. (2012) · Nature · doi:10.1038/nature11007 · Cited by 1,523
Self-citation
Mitochondria in neuroplasticity and neurological disorders
Mattson, M. P., Gleichmann, M., & Cheng, A. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.010 · Cited by 1,081
Mitochondria and Mitochondrial Cascades in Alzheimer’s disease
Swerdlow, R. H. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170585 · Cited by 850
The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.010 · Cited by 786
The Alzheimer’s Disease Mitochondrial Cascade Hypothesis
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562
“nundrum using genetically altered mice [88].”
Reduced IGF-1 signaling delays age-associated proteotoxicity in mice
Cohen, E., Paulsson, J. F., Blinder, P., Burstyn-Cohen, T., Du, D., Estepa, G., Adame, A., Pham, H. M., Holzenberger, M., Kelly, J. W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.11.014 · Cited by 488
Mitochondrial DNA damage and reactive oxygen species in neurodegenerative disease
Nissanka, N., & Moraes, C. T. (2017) · FEBS Letters · doi:10.1002/1873-3468.12956 · Cited by 477
Pharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383
The Role of Mitochondria in Neurodegenerative Diseases: the Lesson from Alzheimer’s Disease and Parkinson’s Disease
Monzio Compagnoni, G., Di Fonzo, A., Corti, S., Comi, G. P., Bresolin, N., & Masliah, E. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01926-1 · Cited by 378
Mitochondrial Dysfunctions in Neurodegenerative Diseases: Relevance to Alzheimer’s Disease
Hroudová, J., Singh, N., & Fišar, Z. (2014) · BioMed Research International · doi:10.1155/2014/175062 · Cited by 319
Mitochondrion-derived reactive oxygen species lead to enhanced amyloid beta formation
Leuner, K., Schütt, T., Kurz, C., Eckert, S. H., Schiller, C., Occhipinti, A., Mai, S., Jendrach, M., Eckert, G. P., Kruse, S. E., et al. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4173 · Cited by 354
Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: Implications for early intervention and therapeutics
Mao, P., & Reddy, P. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.08.005 · Cited by 316
Antioxidant properties of natural polyphenols and their therapeutic potentials for Alzheimer's disease
Choi, D., Lee, Y., Hong, J. T., & Lee, H. (2011) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.11.014 · Cited by 311
Large-scale in silico modeling of metabolic interactions between cell types in the human brain
Lewis, N. E., Schramm, G., Bordbar, A., Schellenberger, J., Andersen, M. P., Cheng, J. K., Patel, N., Yee, A., Lewis, R. A., Eils, R., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1711 · Cited by 266
Multifunctional roles of gelsolin in health and diseases
Li, G. H., Arora, P. D., Chen, Y., McCulloch, C. A., & Liu, P. J. (2010) · Medicinal Research Reviews · doi:10.1002/med.20231 · Cited by 255
The mitochondrial impairment, oxidative stress and neurodegeneration connection: reality or just an attractive hypothesis?
Fukui, H., & Moraes, C. T. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.02.008 · Cited by 250
The Axon-Myelin Unit in Development and Degenerative Disease
Stassart, R. M., Möbius, W., Nave, K.-A., & Edgar, J. M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00467 · Cited by 246
Amyloid precursor protein processing and bioenergetics
Wilkins, H., & Swerdlow, R. H. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.009 · Cited by 228
Dysfunctional Mitochondria and Mitophagy as Drivers of Alzheimer’s Disease Pathogenesis
Chakravorty, A., Jetto, C. T., & Manjithaya, R. R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00311 · Cited by 225
The Alzheimer's disease mitochondrial cascade hypothesis: an update
Swerdlow, R. H., & Khan, S. M. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.01.011 · Cited by 206
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 206
The pathophysiology of mitochondrial disease as modeled in the mousePreprint
Wallace, D. C., & Fan, W. (2009) · Genes & Development · doi:10.1101/gad.1784909 · Cited by 204
Mitochondrial dysfunction in neurodegenerative disorders: Potential therapeutic application of mitochondrial transfer to central nervous system-residing cells
Bustamante-Barrientos, F. A., Luque‐Campos, N., Araya, M. J., Lara-Barba, E., Solminihac, J. D., Pradenas, C., Molina, L., Herrera-Luna, Y., Utreras‐Mendoza, Y., Elizondo-Vega, R. J., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04493-w · Cited by 204
Mechanisms of formation and accumulation of mitochondrial DNA deletions in aging neurons
Fukui, H., & Moraes, C. T. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn437 · Cited by 185
Melatonin treatment restores mitochondrial function in Alzheimer’s mice: a mitochondrial protective role of melatonin membrane receptor signaling
Dragicevic, N., Copes, N., O’Neal-Moffitt, G., Jin, J., Buzzeo, R. W., Mamcarz, M., Tan, J., Cao, C., Olcese, J., Arendash, G. W., et al. (2011) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2011.00864.x · Cited by 185
Deregulation of mitochondrial F1FO-ATP synthase via OSCP in Alzheimer’s disease
Beck, S. J., Guo, L., Phensy, A. J., Tian, J., Wang, L., Tandon, N., Gauba, E., Lu, L., Pascual, J. M., Kroener, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms11483 · Cited by 178
Role of mitochondrial homeostasis and dynamics in Alzheimer's disease
Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175
The mitochondria-targeted antioxidant MitoQ extends lifespan and improves healthspan of a transgenic Caenorhabditis elegans model of Alzheimer disease
Ng, L. F., Gruber, J., Cheah, I. K.-M., Goo, C. K., Cheong, W. F., Shui, G., Sit, K. P., Wenk, M. R., & Halliwell, B. B. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.003 · Cited by 173
A Synergistic Dysfunction of Mitochondrial Fission/Fusion Dynamics and Mitophagy in Alzheimer's Disease
Santos, R. X., Correia, S. C., Wang, X., Perry, G. L., Smith, M. A., Moreira, P. I., & Zhu, X. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100666 · Cited by 162
Alzheimer’s Disease Pathogenesis: Role of Autophagy and Mitophagy Focusing in Microglia
Eshraghi, M., Adlimoghaddam, A., Mahmoodzadeh, A., Sharifzad, F., Yasavoli-Sharahi, H., Lorzadeh, S., Albensi, B. C., & Ghavami, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073330 · Cited by 158
From Mitochondrial Dysfunction to Amyloid Beta Formation: Novel Insights into the Pathogenesis of Alzheimer’s Disease
Leuner, K., Müller, W. E., & Reichert, A. S. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8307-4 · Cited by 160
Respiration-Deficient Astrocytes Survive As Glycolytic Cells In Vivo
Supplie, L. M., Düking, T., Campbell, G., Diaz, F., Moraes, C. T., Götz, M., Hamprecht, B., Boretius, S., Mahad, D., & Nave, K.-A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0756-16.2017 · Cited by 153
Turn up the power - pharmacological activation of mitochondrial biogenesis in mouse models
Komen, J. C., & Thorburn, D. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12413 · Cited by 149
Deep undepleted human serum proteome profiling toward biomarker discovery for Alzheimer’s disease
Dey, K. K., Wang, H., Niu, M., Bai, B., Wang, X., Li, Y., Cho, J.-H., Tan, H., Mishra, A., High, A. A., et al. (2019) · Clinical Proteomics · doi:10.1186/s12014-019-9237-1 · Cited by 135
Enhanced Transcriptional Activity and Mitochondrial Localization of STAT3 Co-induce Axon Regrowth in the Adult Central Nervous System
Luo, X., Ribeiro, M., Bray, E. R., Lee, D.-H., Yungher, B. J., Mehta, S. T., Thakor, K., Díaz, F., Lee, J. K., Moraes, C. T., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.029 · Cited by 128
Cytochrome c oxidase deficiency: Patients and animal models
Diaz, F. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.013 · Cited by 127
Mitochondrial complex I as a therapeutic target for Alzheimer's disease
Trushina, E. V., Trushin, S., & Hasan, M. F. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.11.003 · Cited by 131
The Bioprotective Effects of Polyphenols on Metabolic Syndrome against Oxidative Stress: Evidences and Perspectives
Liu, K., Luo, M., & Wei, S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6713194 · Cited by 128
Genome instability in Alzheimer disease
Hou, Y., Song, H., Croteau, D. L., Akbari, M., & Bohr, V. A. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.04.005 · Cited by 120
Mitochondrial dysfunction and Alzheimer's disease
Maruszak, A., & Żekanowski, C. (2010) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2010.07.004 · Cited by 124
Mitochondria and reactive oxygen and nitrogen species in neurological disorders and stroke: Therapeutic implications☆
Bolaños, J. P., Moro, M. Á., Lizasoaín, I., & Almeida, Á. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.05.009 · Cited by 120
The role of the immune system in Alzheimer’s disease
Wu, K., Zhang, Y.-R., Huang, Y., Dong, Q., Tan, L., & Yu, J. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101409 · Cited by 119
Oxidative Stress, Mitochondrial Dysfunction and the Mitochondria Theory of Aging
Kong, Y., Trabucco, S. E., & Zhang, H. (2014) · Interdisciplinary topics in gerontology and geriatrics · doi:10.1159/000358901 · Cited by 117
A defect in the mitochondrial complex III, but not complex IV, triggers early ROS-dependent damage in defined brain regions
Díaz, F., García, S., Padgett, K. R., & Moraes, C. T. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds350 · Cited by 110
Systematic Dissection of the Metabolic-Apoptotic Interface in AML Reveals Heme Biosynthesis to Be a Regulator of Drug Sensitivity
Lin, K., Xie, A., Rutter, J. C., Ahn, Y.-R., Lloyd-Cowden, J. M., Nichols, A., Soderquist, R. S., Koves, T. R., Muoio, D. M., MacIver, N. J., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.011 · Cited by 110
Mitochondria, Cybrids, Aging, and Alzheimer's Disease
Swerdlow, R. H., Koppel, S., Weidling, I., Hayley, C., Ji, Y., & Wilkins, H. M. (2017) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2016.12.017 · Cited by 106
Vascular and metabolic dysfunction in Alzheimer’s disease: a review
Murray, I. V. J., Proza, J. F., Sohrabji, F., & Lawler, J. M. (2011) · Experimental Biology and Medicine · doi:10.1258/ebm.2011.010355 · Cited by 104
Constitutive SIRT1 overexpression impairs mitochondria and reduces cardiac function in mice
Kawashima, T., Inuzuka, Y., Okuda, J., Kato, T., Niizuma, S., Tamaki, Y., Iwanaga, Y., Kawamoto, A., Narazaki, M., Matsuda, T., et al. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.09.013 · Cited by 93
Amyloid-β Peptide Binds to Cytochrome C Oxidase Subunit 1
Hernández-Zimbrón, L. F., Luna‐Muñoz, J., Mena, R., Vázquez‐Ramírez, R., Kubli‐Garfias, C., Cribbs, D. H., Manoutcharian, K., & Gevorkian, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042344 · Cited by 93
Aβ accumulation in choroid plexus is associated with mitochondrial-induced apoptosis
Vargas, T., Ugalde, C., Spuch, C., Antequera, D., Morán, M., Martín, M. A., Ferrer, I., Bermejo‐Pareja, F., & Carro, E. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.08.017 · Cited by 93
CD45 Deficiency Drives Amyloid-β Peptide Oligomers and Neuronal Loss in Alzheimer's Disease Mice
Zhu, Y., Hou, H., Rezai-Zadeh, K. P., Giunta, B. N., Ruscin, A., Gemma, C., Jin, J., Dragicevic, N., Bradshaw, P. C., Rasool, S., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3268-10.2011 · Cited by 90
Dopaminergic midbrain neurons are the prime target for mitochondrial DNA deletions
Bender, A., Schwarzkopf, R.-M., McMillan, A., Krishnan, K. J., Rieder, G., Neumann, M., Elstner, M., Turnbull, D. M., & Klopstock, T. (2008) · Journal of Neurology · doi:10.1007/s00415-008-0892-9 · Cited by 87
Mitochondrial dysfunctions trigger the calcium signaling-dependent fungal multidrug resistance
Li, Y., Zhang, Y., Zhang, C., Wang, H., Wei, X., Chen, P., & Lü, L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911560116 · Cited by 87
Integrating Gene and Protein Expression Reveals Perturbed Functional Networks in Alzheimer’s Disease
Canchi, S., Raao, B., Masliah, D., Rosenthal, S. B., Šášik, R., Fisch, K. M., Jager, P. L. D., Bennett, D. A., & Rissman, R. A. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.073 · Cited by 82
Preclinical Alzheimer disease: Brain oxidative stress, Aβ peptide and proteomics
Aluise, C. D., Sowell, R. A., Beckett, T. L., Murphy, M. P., Cai, J., Pierce, W. M. J., Markesbery, W. R., & Butterfield, D. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.04.011 · Cited by 83
Proteinopathies and OXPHOS dysfunction in neurodegenerative diseases
Kawamata, H., & Manfredi, G. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201709172 · Cited by 86
The Alzheimer’s Disease Mitochondrial Cascade Hypothesis: A Current Overview
Swerdlow, R. H. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221286 · Cited by 88
Age-Related Neuronal Degeneration: Complementary Roles of Nucleotide Excision Repair and Transcription-Coupled Repair in Preventing Neuropathology
Jaarsma, D., van der Pluijm, I., de Waard, M. C., Haasdijk, E. D., Brandt, R. M. C., Vermeij, M., Rijksen, Y., Maas, A., STEEG, H. V., Hoeijmakers, J. H. J., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002405 · Cited by 80
Mitochondrial genome changes and neurodegenerative diseases
Pinto, M., & Moraes, C. T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.012 · Cited by 75
Clinical Features and Pathogenesis of Alzheimer’s Disease: Involvement of Mitochondria and Mitochondrial DNA
Mancuso, M., Orsucci, D., LoGerfo, A., Calsolaro, V., & Siciliano, G. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6448-9_4 · Cited by 69
The GRACILE mutation introduced into Bcs1l causes postnatal complex III deficiency: A viable mouse model for mitochondrial hepatopathy
Levéen, P., Kotarsky, H., Mörgelin, M., Karikoski, R., Elmér, E., & Fellman, V. (2010) · Hepatology · doi:10.1002/hep.24031 · Cited by 68
Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets
Han, S.-H., Park, J.-C., & Mook-Jung, I. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.12.004 · Cited by 67
Mitophagy and the Brain
Swerdlow, N., & Wilkins, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249661 · Cited by 66
Emerging perspectives on mitochondrial dysfunction and inflammation in Alzheimer’s disease
Yoo, S., Park, J., Kim, S., & Jung, Y. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.1.274 · Cited by 65
RETRACTED: Cytoplasmic gelsolin increases mitochondrial activity and reduces Aβ burden in a mouse model of Alzheimer's disease
Antequera, D., Vargas, T., Ugalde, C., Spuch, C., Molina, J. A., Ferrer, I., Bermejo‐Pareja, F., & Carro, E. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.06.018 · Cited by 64
Retracted
Catalytic Antioxidants and Neurodegeneration
Golden, T. R., & Patel, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2256 · Cited by 62
Mitochondrial Dysfunction and Stress Responses in Alzheimer’s Disease
Weidling, I. W., & Swerdlow, R. H. (2019) · Biology · doi:10.3390/biology8020039 · Cited by 59
Loss of the mitochondrial i‐AAA protease YME1L leads to ocular dysfunction and spinal axonopathy
Sprenger, H., Wani, G. A., Hesseling, A., König, T., Patrón, M., MacVicar, T., Ahola, S., Wai, T., Barth, E., Rugarli, E. I., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201809288 · Cited by 59
Bilobalide: A review of its pharmacology, pharmacokinetics, toxicity, and safety
Lu, J., Xie, L., Liu, K., Zhang, X., Wang, X., Dai, X., Liang, Y., Cao, Y. L., & Li, X. (2021) · Phytotherapy Research · doi:10.1002/ptr.7220 · Cited by 59
Engineering the alternative oxidase gene to better understand and counteract mitochondrial defects: state of the art and perspectives
El‐Khoury, R., Kemppainen, K. K., Dufour, E., Szibor, M., Jacobs, H. T., & Rustin, P. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12570 · Cited by 56
Genetic association of the cytochrome c oxidase-related genes with Alzheimer’s disease in Han Chinese
Bi, R., Zhang, W., Zhang, D., Xu, M., Fan, Y., Hu, Q.-X., Jiang, H., Tan, L., Li, T., Fang, Y., et al. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0144-3 · Cited by 54
Mitochondrial function and Aβ in Alzheimer's disease postmortem brain
Troutwine, B. R., Strope, T. A., Franczak, E., Lysaker, C. R., Hamid, L., Mansel, C., Stopperan, J. A., Gouvion, C. M., Haeri, M., Swerdlow, R. H., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105781 · Cited by 51
4-O-Methylhonokiol attenuates memory impairment in presenilin 2 mutant mice through reduction of oxidative damage and inactivation of astrocytes and the ERK pathway
Lee, Y. J., Choi, I. S., Park, M. H., Lee, Y.-M., Song, J. K., Kim, Y. H., Kim, K. H., Hwang, D. Y., Jeong, J. H., Yun, Y. P., et al. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.10.698 · Cited by 52
Meclizine is neuroprotective in models of Huntington's disease
Gohil, V. M., Offner, N., Walker, J. A., Sheth, S. A., Fossale, E., Gusella, J. F., MacDonald, M. E., Néri, C., & Mootha, V. K. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq464 · Cited by 48
Temporal progression of Alzheimer's disease in brains and intestines of transgenic mice
Manocha, G. D., Floden, A. M., Miller, N., Smith, A. J., Nagamoto‐Combs, K., Saito, T., Saido, T. C., & Combs, C. K. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.05.025 · Cited by 51
Mitochondrial DNA damage in a mouse model of Alzheimer's disease decreases amyloid beta plaque formation
Pinto, M., Pickrell, A. M., Fukui, H., & Moraes, C. T. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.04.014 · Cited by 47
The role of cytochrome c oxidase deficiency in ROS and amyloid plaque formation
Pickrell, A. M., Fukui, H., & Moraes, C. T. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9245-3 · Cited by 47
RETRACTED: Bezafibrate improves mitochondrial function in the CNS of a mouse model of mitochondrial encephalopathy
Noe, N., Dillon, L. M., Lellek, V., Díaz, F., Hida, A., Moraes, C. T., & Wenz, T. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.12.003 · Cited by 49
Retracted
Amyloid precursor protein‐mediated mitochondrial regulation and Alzheimer's disease
Lopez Sanchez, M. I. G., van Wijngaarden, P., & Trounce, I. A. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14554 · Cited by 45
The Role of Bioenergetics in Neurodegeneration
Strope, T. A., Birky, C. J., & Wilkins, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169212 · Cited by 44
Schwann cell mitochondria as key regulators in the development and maintenance of peripheral nerve axons
Ino, D., & Iino, M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2364-1 · Cited by 43
Partial complex I deficiency due to the CNS conditional ablation of Ndufa5 results in a mild chronic encephalopathy but no increase in oxidative damage
Peralta, S., Torraco, A., Wenz, T., Garcia, S., Diaz, F., & Moraes, C. T. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt526 · Cited by 42
Metabolite Profiles Reveal Energy Failure and Impaired Beta-Oxidation in Liver of Mice with Complex III Deficiency Due to a BCS1L Mutation
Kotarsky, H., Keller, M., Davoudi, M., Levéen, P., Karikoski, R., Enot, D. P., & Fellman, V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041156 · Cited by 42
Regional brain metabolism with cytochrome c oxidase histochemistry in a PS1/A246E mouse model of autosomal dominant Alzheimer's disease: Correlations with behavior and oxidative stress
Strazielle, C., Jazi, R., Verdier, Y., Qian, S., & Lalonde, R. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.08.005 · Cited by 43
DARS2 protects against neuroinflammation and apoptotic neuronal loss, but is dispensable for myelin producing cells
Croon, M., Doğan, Ş. A., Lotter, S., Wang, S., Hermans, S., Wibom, R., Rugarli, E. I., & Trifunović, A. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx307 · Cited by 38
Signalling, Metabolic Pathways and Iron Homeostasis in Endothelial Cells in Health, Atherosclerosis and Alzheimer’s Disease
Bosseboeuf, E., & Raimondi, C. (2020) · Cells · doi:10.3390/cells9092055 · Cited by 38
Interactions between amyloid, amyloid precursor protein, and mitochondria
Wilkins, H. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220518 · Cited by 37
Mouse models of oxidative phosphorylation defects: Powerful tools to study the pathobiology of mitochondrial diseases
Torraco, A., Díaz, F., Vempati, U. D., & Moraes, C. T. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.06.003 · Cited by 38
Biomedical applications of cell- and tissue-specific metabolic network models
Fouladiha, H., & Marashi, S. (2017) · Journal of Biomedical Informatics · doi:10.1016/j.jbi.2017.02.014 · Cited by 37
The application of multifunctional nanomaterials in Alzheimer’s disease: A potential theranostics strategy
Xu, Y., Zhao, M.-N., Zhou, D., Zheng, T., & Zhang, H. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111360 · Cited by 38
Mitochondrial Membrane Potential Influences Amyloid-β Protein Precursor Localization and Amyloid-β Secretion
Wilkins, H., Troutwine, B., Menta, B. W., Manley, S., Strope, T., Lysaker, C., & Swerdlow, R. H. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215280 · Cited by 38
Xanthoceraside Ameliorates Mitochondrial Dysfunction Contributing to the Improvement of Learning and Memory Impairment in Mice with Intracerebroventricular Injection of Aβ1‐42
Ji, X., Chi, T., Xu, Q., He, X., Xiao-yu, Z., Zhang, R., & Zou, L. (2014) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2014/969342 · Cited by 34
Amyloid precursor protein and mitochondria
Strope, T. A., & Wilkins, H. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2022.102651 · Cited by 37
Mouse models of oxidative phosphorylation dysfunction and disease
Vempati, U. D., Torraco, A., & Moraes, C. T. (2008) · Methods · doi:10.1016/j.ymeth.2008.09.008 · Cited by 33
Serial protein labeling with infrared maleimide dyes to identify cysteine modifications
Riederer, I. M., Moreno-Herero, R., Leuba, G., & Riederer, B. M. (2008) · Journal of Proteomics · doi:10.1016/j.jprot.2008.04.006 · Cited by 33
Mitochondrial ubiquitin ligase alleviates Alzheimer’s disease pathology via blocking the toxic amyloid-β oligomer generation
Takeda, K., Uda, A., Mitsubori, M., Nagashima, S., Iwasaki, H., Ito, N., Shiiba, I., Ishido, S., Matsuoka, M., Inatome, R., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01720-2 · Cited by 32
Mitochondrial Complex I and β-Amyloid Peptide Interplay in Alzheimer’s Disease: A Critical Review of New and Old Little Regarded Findings
Atlante, A., & Valenti, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115951 · Cited by 33
Astrocytic GLUT1 deletion in adult mice enhances glucose metabolism and resilience to stroke
Thieren, L., Zanker, H. S., Droux, J., Dalvi, U., Wyss, M. T., Waag, R., Germain, P., von Ziegler, L., Looser, Z. J., Hösli, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59400-2 · Cited by 38
Placental Genome and Maternal-Placental Genetic Interactions: A Genome-Wide and Candidate Gene Association Study of Placental Abruption
Denis, M., Enquobahrie, D. A., Tadesse, M. G., Gelaye, B., Sánchez, S. E., Salazar, M., Ananth, C. V., & Williams, M. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0116346 · Cited by 32
Impaired mitochondrial energy production and ABC transporter function—A crucial interconnection in dementing proteopathies of the brain
Pahnke, J., Fröhlich, C., Krohn, M., Schumacher, T., & Paarmann, K. (2013) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2013.08.007 · Cited by 35

Authors: Fukui, H., Diaz, F., Garcia, S., & Moraes, C. T.
Affiliations: University of Miami (US)
Departments of †Neurology and
ORCID: Fukui, Hirokazu
Moraes, Carlos T.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2007-08-28
Volume: 104
Issue: 35
Pages: 14163-14168
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0705738104
PMC: PMC1955773
OpenAlex: W2023378584
Cited by: 185
References: 45
Citations by year: 2026: 4 · 2025: 8 · 2024: 13 · 2023: 11 · 2022: 9 · 2021: 9 · 2020: 7 · 2019: 8 · 2018: 9 · 2017: 10 · 2016: 8 · 2015: 5 · 2014: 8 · 2013: 8 · 2012: 13
FWCI: 8.94
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Eye Institute (R01EY010804)
National Cancer Institute (R01CA085700)
National Institute of Neurological Disorders and Stroke (R01-NS41777, R01NS041777)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Keywords: cytochrome c oxidase deficiency, Alzheimer's disease, amyloid-beta, amyloid plaques, COX10, mitochondrial respiratory function, oxidative stress, reactive oxygen species, amyloid precursor protein, presenilin 1, beta-secretase, mouse model
MeSH terms: Alzheimer Disease, Amyloid, Animals, Citrate (si)-Synthase, Electron Transport Complex IV, Disease Models, Animal, Mitochondria, Neurons, Oxygen Consumption, Peroxides, Mice, Knockout, Oxidative Stress, Mice

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

Cytochrome c oxidase deficiency in neurons decreases both oxidative stress and amyloid formation in a mouse model of Alzheimer's disease

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