The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Cytochrome c oxidase is decreased in Alzheimer’s disease platelets
Abstract
Cytochrome c oxidase (COX) activity reportedly is reduced in Alzheimer's disease (AD) brain and platelets. The reasons for the defect in either tissue are unknown, but its presence in a non-degenerating tissue suggests it is not simply a consequence of neurodegeneration. We now offer confirmation of the AD platelet COX defect. Compared to age-matched controls, in mitochondria isolated from AD platelets there was a 15% decrease in COX activity despite the fact that COX subunits were present at normal levels. Platelet ATP levels were diminished in AD (from 11.33 +/- 0.52 to 9.11 +/- 0.72 nmol/mg), while reactive oxygen species (ROS) were increased (from 97.03 +/- 25.9 to 338.3 +/- 100 K/mg). Platelet membrane fluidity, Vitamin E, and cholesterol content were similar between groups. We conclude that COX catalytic activity is indeed diminished in AD platelet mitochondria, does not result from altered membrane fluidity, and is associated with ROS overproduction and ATP under-production.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“however, in mitochondria isolated from AD platelets, the activity of complex IV, or cytochrome c oxidase, is significantly decreased [109,110,111]”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [110]
Citations
Cites
Sequence and organization of the human mitochondrial genome
Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,740
A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250
SEDMAK, J. J., & Grossberg, S. E. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90428-6 · Cited by 3,019
Reactive Oxygen Species and the Central Nervous System
Halliwell, B. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10990.x · Cited by 2,947
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Oxidative damage and mitochondrial decay in aging.
Shigenaga, M. K., Hagen, T. M., & Ames, B. N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10771 · Cited by 2,055
Fluidity parameters of lipid regions determined by fluorescence polarization
Shinitzky, M., & Barenholz, Y. (1978) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(78)90010-2 · Cited by 1,885
Bass, D., Parce, J. W., DeChatelet, L. R., Szejda, P., Seeds, M. C., & Thomas, M. (1983) · The Journal of Immunology · doi:10.4049/jimmunol.130.4.1910 · Cited by 1,811
[45] Cytochrome oxidase from beef heart mitochondria
Wharton, D. C., & Tzagoloff, A. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(67)10048-7 · Cited by 1,264
Beal, M. F. (1992) · Annals of Neurology · doi:10.1002/ana.410310202 · Cited by 962
Lipid peroxidation damage to cell components.
Tappel, A. L. (1973) · PubMed · Cited by 902
Research works printed but not linked: 1
- Ragan CI, Wilson MT, Darley-Usmar VM, Lowe PN. Subfractionation of mitochondria, and isolation of the proteins of oxidative phosphorylation. In: Mitochondria, a practical approach. London: IRL Press; 1987. p. 79–112.
Cited by
Sorted by citations
Items 201–280 of 280
Burbaeva, G. S., Бокша, И. С., Turishcheva, M. S., Savushkina, O. K., Beniashvili, A. G., Rupchev, G., & Ma, M. (2011) · Health · doi:10.4236/health.2011.31003 · Cited by 11
Conjugated linoleic acid protects brain mitochondrial function in acrolein induced male rats
Aydın, B., Şahin, C. G., Şekeroğlu, V., & Şekeroğlu, Z. A. (2021) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2021.1952673 · Cited by 11
Granov, R., Vedad, S., Wang, S.-H., Durham, A., Shah, D., & Pasinetti, G. M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04339-6 · Cited by 12
Min, J.-H., Sarlus, H., & Harris, R. A. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1467333 · Cited by 11
Hong-liang, Y., Liu, X., & Liu, Y. (2015) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2014.15.23.10469 · Cited by 10
Mitochondrial Dysfunction and Alzheimer’s Disease
Albrekkan, F. M., & Kelly-Worden, M. L. (2013) · Open Journal of Endocrine and Metabolic Diseases · doi:10.4236/ojemd.2013.32a003 · Cited by 10
Hroudová, J., Fišar, Z., Korábečný, J., & Kuča, K. (2011) · PubMed · Cited by 10
Scholes, H. M., Cryar, A., Kerr, F., Sutherland, D., Gethings, L. A., Vissers, J. P. C., Lees, J., Orengo, C. A., Partridge, L., & Thalassinos, K. (2020) · Scientific Reports · doi:10.1038/s41598-020-74748-9 · Cited by 13
Targeting mitochondrial dysfunction in Alzheimer's disease: New findings and perspectives
Hroudová, J., & Fišar, Z. (2025) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2025.111491 · Cited by 9
Stavros, J. (2013) · InTech eBooks · doi:10.5772/56079 · Cited by 9
Argentati, C., Tortorella, I., Bazzucchi, M., Emiliani, C., Morena, F., & Martino, S. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030115 · Cited by 10
Huang, J., Song, Z., Wei, B., Li, Q., Lin, P., Li, H., & Dong, K. (2023) · BMC Psychiatry · doi:10.1186/s12888-023-04634-x · Cited by 9
Cortical Metabolic Deficits in a Rat Model of Cholinergic Basal Forebrain Degeneration
Gelfo, F., Petrosini, L., Graziano, A., Bartolo, P. D., Burello, L., Vitale, E., Polverino, A., Iuliano, A., Sorrentino, G., & Mandolesi, L. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1120-2 · Cited by 9
Dietary Phytochemicals in Neurodegenerative Disease
Jacquet, A. D. R., Tambe, M. A., & Rochet, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-802928-2.00018-7 · Cited by 8
Immunonutrition: future perspective in neurodegenerative disorders
Claro, C., Rivero‐Pino, F., Torrecillas-López, M., Jiménez-González, V., & la Paz, S. M. (2024) · Nutritional Neuroscience · doi:10.1080/1028415x.2024.2425565 · Cited by 10
Popov, V. M., Vlădăreanu, A. M., Bumbea, H., Kovács, E., Savopol, T., Iordache, M. M., & Moisescu, M. G. (2015) · Blood Coagulation & Fibrinolysis · doi:10.1097/mbc.0000000000000287 · Cited by 8
Mitochondria and Alzheimer’s Disease: An Electron Microscopy Study
Balogiannis, S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.84881 · Cited by 9
Trends of mitochondrial changes in AD: a bibliometric study
Song, R., Guo, Y., Fu, Y., Ren, H., Wang, H., Yan, H., & Ge, Y. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1136400 · Cited by 7
Metal Ions and Alzheimer's Disease
Adlard, P. A., & Bush, A. I. (2007) · Springer eBooks · doi:10.1007/978-0-387-70830-0_15 · Cited by 6
Loera‐Castañeda, V., Sandoval-Ramı́rez, L., Pacheco-Moisés, F. P., Macías-Islas, M. Á., Alatorre-Jiménez, M. A., González-Renovato, E. D., Cortés-Enríquez, F., de la Rosa, A. C., Velázquez-Brizuela, I. E., & Ortíz, G. G. (2014) · International Journal of Alzheimer s Disease · doi:10.1155/2014/794530 · Cited by 7
Wallace, D. C., Lott, M. T., & Procaccio, V. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00013-6 · Cited by 8
Platelets in Alzheimer’s Disease
Plagg, B., & Humpel, C. (2015) · InTech eBooks · doi:10.5772/60535 · Cited by 7
Howell, N., Dykens, J. A., & Moos, W. H. (2005) · Drug Development Research · doi:10.1002/ddr.20046 · Cited by 7
Isıyel, M., Ceylan, H., & Demir, Y. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05973-y · Cited by 6
Metabolomic Signatures of Brainstem in Mice following Acute and Subchronic Hydrogen Sulfide Exposure
Kim, D.-S., Maldonado, C. M. S., Giulivi, C., & Rumbeiha, W. K. (2024) · Metabolites · doi:10.3390/metabo14010053 · Cited by 6
ProMotE: an efficient algorithm for counting independent motifs in uncertain network topologies
Ren, Y., Sarkar, A., & Kahveci, T. (2018) · BMC Bioinformatics · doi:10.1186/s12859-018-2236-9 · Cited by 6
Mitochondria and Alzheimer’s Disease
Balogiannis, S. (2014) · Journal of Neurology & Stroke · doi:10.15406/jnsk.2014.01.00028 · Cited by 4
Genetic, Biochemical and Histopathological Aspects of Familiar Alzheimer's Disease
Ortíz, G. G., Pacheco-Moisés, F. P., González-Renovato, E. D., Figuera, L. E., Macías-Islas, M. Á., Mireles-Ramírez, M. A., Flores-Alvarado, L. J., Sánchez-López, A. L., Nuño-Penilla, D. G., Velázquez-Brizuela, I. E., et al. (2015) · InTech eBooks · doi:10.5772/59809 · Cited by 5
Tissue-specific implications of mitochondrial alterations in aging
Liu, D. (2012) · Frontiers in Bioscience-Elite · doi:10.2741/e654 · Cited by 5
Hroudová, J., Nováková, T., Korábečný, J., Maliňák, D., Górecki, L., & Fišar, Z. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02172-1 · Cited by 5
Targeting cellular batteries for the therapy of neurological diseases
Arora, A., Behl, T., Sehgal, A., Singh, S., Sharma, N., Mathew, B., & BUNGAU, S. G. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-14665-0 · Cited by 5
Nervonic acid and 15-epi-PGA1 mediate systemic mitochondrial dysfunction in AD dementia
Heimler, S., Amick, K. A., Bergstrom, J., Moliné, M., Mahapatra, G., Craft, S., & Molina, A. J. A. (2025) · GeroScience · doi:10.1007/s11357-025-01776-6 · Cited by 4
Mitotherapy in Alzheimer’s and Parkinson’s diseases: A systematic review of preclinical studies
Modiri, A., Hosseini, L., Abolhasanpour, N., Azizi, H., & Sadeh, R. N. (2025) · BMC Neurology · doi:10.1186/s12883-025-04241-1 · Cited by 4
Mitochondrial Dysfunction and Molecular Bases of Neurodegenerative Diseases
Kolesnikova, E. E. (2013) · Neurophysiology · doi:10.1007/s11062-013-9341-1 · Cited by 4
Hugo, M. M., & Banerjee, I. A. (2018) · Soft Materials · doi:10.1080/1539445x.2018.1548357 · Cited by 4
Khyzhnyak, S. V., Sorokina, L. V., Stepanova, L. I., & Kaplia, A. A. (2014) · The Ukrainian Biochemical Journal · doi:10.15407/ubj86.06.106 · Cited by 4
Mitochondria at the Base of Neuronal Innate Immunity in Alzheimer’s and Parkinson’s Diseases
Esteves, A. R., Silva, D. F., Santos, D., Candeias, E., Filipe, F., & Cardoso, S. M. (2018) · InTech eBooks · doi:10.5772/intechopen.72612 · Cited by 4
Self-citationEditorial: Systemic implications of Alzheimer's disease
Cortés, C. J., Thyfault, J. P., & Wilkins, H. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1219987 · Cited by 4
Energy deprivation in youth and old age
Stern, M. (2025) · Journal of Cell Science · doi:10.1242/jcs.264018 · Cited by 3
A blood based mitochondrial functional index biomarker for Alzheimer's disease
Hauger, B. M., Kemna, R. E., Kueck, P. J., Strope, T. A., John, C. S., Smith, K. P., Mayfield, H. D., Herrold, E., Cox, K., Bothwell, R. J., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.71061 · Cited by 3
Seong, M., Oh, Y., Park, H. J., Choi, W.-S., & Kim, J. G. (2022) · Biosensors · doi:10.3390/bios12111019 · Cited by 3
Alzheimer Disease and Metabolism: Role of Cholesterol and Membrane Fluidity
Genaro, G., Fermin, P., Luis, J., Miguel, A., Irma, E., Anguiano, A., Torres-Sánchez, E. D., Eddic, W., Jose, A., Genaro, E., et al. (2013) · InTech eBooks · doi:10.5772/54091 · Cited by 3
New Targets for Diagnosis and Treatment Against Alzheimer’s Disease: The Mitochondrial Approach
Maria Jose Perez, J., Jara, C., Muñoz-Urrutia, E., & Quintanilla, R. A. (2016) · InTech eBooks · doi:10.5772/64327 · Cited by 3
Biochemical Platelet Markers of Cognitive Impairments in Alzheimer’s Disease
Кодинцев, А. Н., Izmozherova, N. V., Aa, P., Volkova, L. I., Петровна, А. И., & Ryabinina, A. V. (2023) · Neurochemical Journal · doi:10.1134/s1819712423010105 · Cited by 3
Heme metabolism, mitochondria, and complex I in neuropsychiatric disorders
Ifhar, L. S., & Ben‐Shachar, D. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814037-6.00008-2 · Cited by 3
Editorial: Metabolism in Alzheimer's Disease
Morris, J. K., Wood, L. B., & Wilkins, H. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.824145 · Cited by 3
Mitochondrial Function and Neurodegenerative Diseases
Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2
Li, Q., & Masters, C. L. (2007) · Elsevier eBooks · doi:10.1016/b978-012369367-9/50805-3 · Cited by 2
Tackling Alzheimer’s Disease by Targeting Oxidative Stress and Mitochondria
Castellani, R. J., Correia, S. C., Moreira, P. I., & Perry, G. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00018-6 · Cited by 2
Bcl-2-Homology-Only Proapoptotic Peptides Modulate β-Amyloid Aggregation and Toxicity
Ben-Zichri, S., Malishev, R., Oren, O., Bloch, D. N., Taube, R., Papo, N., & Jelinek, R. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00611 · Cited by 2
Mitochondria in Alzheimer disease : regulatory mechanisms and cell death
Hedskog, L. (2012) · Figshare · Cited by 2
Strope, T. A., Troutwine, B., Hauger, B. M., Smith, K. P., Swerdlow, R. H., & Wilkins, H. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251360243 · Cited by 2
Eysert, F., Deportes, G., Delaquaize, E., & Chami, M. (2026) · Current Opinion in Neurology · doi:10.1097/wco.0000000000001457 · Cited by 1
Niño, S. A., Barrios-Camus, O., Silva-Pavez, E. E., Cárdenas, J. C., & González-Billault, C. E. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168211 · Cited by 1
Maiese, K. (2026) · Medical Gas Research · doi:10.4103/mgr.medgasres-d-26-00073 · Cited by 2
Baloyannis, S. J. (2014) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608058709114020003 · Cited by 1
Mavroudis, I. A., PETRIDIS, F., KAZIS, D., Njau, S. N., Costa, V., & Balogiannis, S. (2020) · Annals of the Academy of Romanian Scientists Series on Biological Sciences · doi:10.56082/annalsarscibio.2020.2.43 · Cited by 1
Translational bioenergetics: blood cells based laboratory diagnostics
Черепнев, Г. В., Novozhilova, A. A., Ягудина, Л. А., Antzilevich, L. M., & Prokopiev, Y. V. (2022) · Laboratory Service · doi:10.17116/labs20221103134 · Cited by 1
Bhatnagar, D., Ladhe, S., & Kumar, D. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815136142123010012 · Cited by 1
The role of mitochondrial dysfunction in the stabilization of the glaucomatous process
Власова, А. С., Malishevskaya, Т. N., Sa, P., Gubin, D. G., Petrov, S. Y., & Filippova, Y. E. (2024) · Russian Annals of Ophthalmology · doi:10.17116/oftalma202414004149 · Cited by 1
Widyarti, S., Wibowo, S., Sabarudin, A., Abhirama, I., & Sumitro, S. B. (2023) · Preprints.org · doi:10.20944/preprints202301.0220.v1 · Cited by 1
Deregulation of oxidative phosphorylation system and energy homeostasis in Alzheimer's disease
Rhein, V. F. (2009) · edoc (University of Basel) · doi:10.5451/unibas-005042311
Role of Mitochondria in Alzheimer ́s Disease
Ortiz, G. G., Pacheco-Moisés, F. P., García-Trejo, J. D. J., Rocio, E., Miguel, A., Jose, A., Irma, E., Arias‐Merino, E. D., & de la Ros, A. C. (2011) · InTech eBooks · doi:10.5772/16713
Aβ in Mitochondria—One Piece in the Alzheimer’s Disease Puzzle
Ankarcrona, M. (2013) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-1-62703-598-9_5
Peng, J., Zeng, F., He, Y.-H., Tang, Y., Yin, H.-Y., & Yu, S.-G. (2014) · Journal of Acupuncture and Tuina Science · doi:10.1007/s11726-014-0773-y
The Potential Application of Antioxidant Agents in Alzheimer Disease Therapeutics
Moreira, P. I., Smith, M. A., Zhu, X., Nunomura, A., & Perry, G. L. (2007) · Springer eBooks · doi:10.1007/978-0-387-71522-3_12
dos Santos, A. C. F., & dos Santos (2012)
Verri, M. (2019) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2019.13.002449
THE INFLUENCE OF MITOCHONDRIA IN ALZHEIMER DISEASE AND POSSIBLE ALTERNATIVE THERAPIES
(2021) · International Journal of Neuroscience Research · doi:10.28933/ijnr-2021-04-0606
Mitochondrial Membrane Potential Influences Aβ Production and Amyloid Precursor Protein localizationPreprint
Wilkins, H., Troutwine, B., Menta, B. W., Manley, S., Strope, T. A., Lysaker, C. R., & Swerdlow, R. H. (2021) · Research Square · doi:10.21203/rs.3.rs-622670/v1
Blood Bioenergetic Biomarkers in Alzheimer’s Disease APOE ε4-CarriersPreprint
Wilkins, H., Manley, S., Wang, X., Menta, B. W., Koppel, S. J., Bothwell, R. J., Becker, A. M., Anderson, H., Schwartz, E., Burns, J. M., et al. (2020) · doi:10.21203/rs.3.rs-37441/v1
Biochemical Platelet Markers of Cognitive Impairment in Alzheimer’s Disease
Kodintcev, A. N., Izmozherova, N. V., Aa, P., Volkova, L. I., Петровна, А. И., & Ryabinina, A. V. (2023) · Нейрохимия · doi:10.31857/s1027813323010107
Mitochondrial Genomics and Their Clinical Significance
Mishra, S., Tiwari, B. S., & Tiwari, A. K. (2024) · Springer eBooks · doi:10.1007/978-981-97-3169-5_14
Zafar, S., Noor, A., Younas, N., Shafiq, M., Dittmar, K., Yagensky, O., Schmitz, M., Ferrer, I., Hermann, P., & Zerr, I. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05327-0 · Cited by 1
Plasma Proteomic Networks Reveal Shared Biology with Brain Linked to Alzheimer’s Disease PathologyPreprint
GUO, Q., Ping, L., Rathore, S., Duong, D. M., Shantaraman, A., Fox, E. J., Johnson, E. C. B., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2026) · medRxiv · doi:10.64898/2026.05.26.26353866
Bioactive Food Ingredients in the Treatment of Neuroinflmammatory Disorders
Sehar, N., & Sehar, S. (2026) · Food bioactive ingredients · doi:10.1007/978-3-032-23814-6_11
Mapping Alzheimer’s disease heterogeneity through exploratory unsupervised learning
Xavier, C., Correia, A. P., Lopes, J., Fernandes, J., Laranjinha, I., & Pinto, N. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1869804
Amyloid-β peptide and mitochondrial dysfunction
Yang, A. J. T., & Wilkins, H. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45078-5.00022-1
Mitochondrial dysfunction in neurology: biomarkers and clinical implications
Rossini, E., Garibaldi, M., Hanna, M. G., Pitceathly, R. D. S., & Pizzamiglio, C. (2026) · Nature Reviews Neurology · doi:10.1038/s41582-026-01274-z
Mosconi, L., Murray, J., McHugh, P. F., & de Leon, M. J. (2013) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-1-62703-598-9_10
Metadata
- Authors
- Cardoso, S. M., Proença, M. T., Santos, S., Santana, I., & Oliveira, C. R.
- Affiliations
- University of Coimbra (PT)
- Unidade Local de Saúde de Coimbra (PT)
- Corresponding author
- Oliveira, Catarina R
- Venue
- Neurobiology of Aging
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 25
- Issue
- 1
- Pages
- 105-110
- ISSN
- 0197-4580 (ISSN-L)
- OpenAlex
- W2072453593
- Cited by
- 281
- References
- 38
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 9 · 2023: 15 · 2022: 13 · 2021: 16 · 2020: 14 · 2019: 16 · 2018: 7 · 2017: 9 · 2016: 14 · 2015: 10 · 2014: 13 · 2013: 22 · 2012: 17
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neurobiology of Aging (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Keywords
- cytochrome c oxidase, Alzheimer's disease, platelets, mitochondrial dysfunction, ATP production, reactive oxygen species, platelet mitochondria, platelet membrane fluidity, vitamin E, cholesterol
- MeSH terms
- Adenine Nucleotides, Adenosine Triphosphate, Aged, Alzheimer Disease, Blood Platelets, Cholesterol, Chromatography, High Pressure Liquid, Citrate (si)-Synthase, Electron Transport Complex IV, Free Radicals, Humans, Middle Aged, Mitochondria, NADP, Succinate Cytochrome c Oxidoreductase, Vitamin E, Electrophoresis, Gel, Two-Dimensional, Case-Control Studies, Age of Onset, Electron Transport Complex I
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