Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

Schägger, H., & von JAGOW, G. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90094-a · Cited by 2,267

The cholinergic hypothesis of Alzheimer’s disease: A review of progress

Francis, P. T., Palmer, A. M., Snape, M., & Wilcock, G. K. (1999) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.66.2.137 · Cited by 2,198 · cited 1×

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120

Editorial on Consensus Recommendations for the Postmortem Diagnosis of Alzheimer Disease from the National Institute on Aging and the Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer Disease

HYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447

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

Translating cell biology into therapeutic advances in Alzheimer's disease

Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,166

Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression

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

Consensus Recommendations for the Postmortem Diagnosis of Alzheimer’s Disease

(1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00057-2 · Cited by 981

Interactions between BIM Protein and Beta-Amyloid May Reveal a Crucial Missing Link between Alzheimer’s Disease and Neuronal Cell Death

Malishev, R., Nandi, S., Śmiłowicz, D., Bakavayev, S., Engel, S., Bujanover, N., Gazit, R., Metzler‐Nolte, N., & Jelinek, R. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00177 · Cited by 21

Mitochondrially-Targeted Therapeutic Strategies for Alzheimer’s Disease

Onyango, I. G., Bennett, J. P., & Stokin, G. B. (2021) · Current Alzheimer Research · doi:10.2174/1567205018666211208125855 · Cited by 22

Therapeutic approaches of nutraceuticals in the prevention of Alzheimer's disease

Pandey, S. N., Singh, G., Semwal, B. C., Gupta, G., Alharbi, K. S., Almalki, W. H., Albratty, M., Najmi, A., & Meraya, A. M. (2022) · Journal of Food Biochemistry · doi:10.1111/jfbc.14426 · Cited by 23

Proteomic Analysis of Lymphoblastoid Cells from Nasu-Hakola Patients: A Step Forward in Our Understanding of This Neurodegenerative Disorder

Giuliano, S., Agresta, A. M., Palma, A. D., Viglio, S., Mauri, P., Fumagalli, M., Iadarola, P., Montalbetti, L., Salvini, R., & Bardoni, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110073 · Cited by 21

Polymorphism in the TOMM40 gene modifies the risk of developing sporadic inclusion body myositis and the age of onset of symptoms

Mastaglia, F. L., Rojana-udomsart, A., JAMES, I. R., Needham, M., Day, T. J., Kiers, L., Corbett, J. A., Saunders, A. M., Lutz, M. W., & Roses, A. D. (2013) · Neuromuscular Disorders · doi:10.1016/j.nmd.2013.09.008 · Cited by 22

Mitochondria are devoid of amyloid β-protein (Aβ)-producing secretases: Evidence for unlikely occurrence within mitochondria of Aβ generation from amyloid precursor protein

Mamada, N., Tanokashira, D., Ishii, K., Tamaoka, A., & Araki, W. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.03.035 · Cited by 22

Elucidating Critical Proteinopathic Mechanisms and Potential Drug Targets in Neurodegeneration

Dar, K. B., Bhat, A. H., Amin, S., Reshi, B. A., Zargar, M. A., Masood, A., & Ganie, S. A. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00741-0 · Cited by 23

Synergistic effects of β-amyloid and ceramide-induced insulin resistance on mitochondrial metabolism in neuronal cells

Kwon, B., Gamache, T., Lee, H., & Querfurth, H. W. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.05.012 · Cited by 23

Mitochondrial bioenergetics is defective in presymptomatic Tg2576 AD Mice

Varghese, M., Zhao, W., Wang, J., Cheng, A., Qian, X., Chaudhry, A., Ho, L., & Pasinetti, G. M. (2011) · Translational Neuroscience · doi:10.2478/s13380-011-0011-8 · Cited by 22

BACE1 activity impairs neuronal glucose oxidation: rescue by beta-hydroxybutyrate and lipoic acid

Findlay, J. A., Hamilton, D. L., & Ashford, M. L. J. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00382 · Cited by 22

Alzheimer's Disease and Frontotemporal Dementia: A Review of Pathophysiology and Therapeutic Approaches

Kelliny, S., Zhou, X., & Bobrovskaya, L. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70046 · Cited by 27

Mitochondrial pathway polygenic risk scores are associated with Alzheimer's Disease

Paliwal, D., McInerney, T. W., Pa, J., Swerdlow, R. H., Easteal, S., Andrews, S. J., & Initiative, F. T. A. D. N. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.08.005 · Cited by 21

Peripheral Pathways to Neurovascular Unit Dysfunction, Cognitive Impairment, and Alzheimer’s Disease

Nelson, A. R. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.858429 · Cited by 24

Chlamydia pneumoniae in Alzheimer's disease pathology

Subedi, L., Gaire, B. P., Koronyo, Y., Koronyo‐Hamaoui, M., & Crother, T. R. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1393293 · Cited by 24

Combined age- and trauma-related proteomic changes in rat neocortex: a basis for brain vulnerability

Mehan, N. D., & Strauss, K. I. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.029 · Cited by 20

Mitochondrial therapeutics in Alzheimer's disease and Parkinson's disease

Hoekstra, J. G., Montine, K. S., Zhang, J., & Montine, T. J. (2011) · Alzheimer s Research & Therapy · doi:10.1186/alzrt83 · Cited by 21

Down-regulation of aminolevulinate synthase, the rate-limiting enzyme for heme biosynthesis in Alzheimer's disease

Dwyer, B. E., Smith, M. A., Richardson, S. L., Perry, G. L., & Zhu, X. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.05.058 · Cited by 22

Proteasome regulates turnover of toxic human amylin in pancreatic cells

Singh, S., Trikha, S., Sarkar, A. A., & Jeremic, A. M. (2016) · Biochemical Journal · doi:10.1042/bcj20160026 · Cited by 21

Amyloid precursor protein, heat-shock proteins, and Bcl-2 form a complex in mitochondria and modulate mitochondria function and apoptosis in N2a cells

Yang, T.-T., Hsu, C.-T., & Kuo, Y. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.07.002 · Cited by 21

SuperAgers and centenarians, dynamics of healthy ageing with cognitive resilience

Islam, M. A., Sehar, U., Sultana, O. F., Mukherjee, U., Brownell, M., Kshirsagar, S., & Reddy, P. H. (2024) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2024.111936 · Cited by 21

Decoding Cancer through Silencing the Mitochondrial Gatekeeper VDAC1

Arif, T., Shteinfer‐Kuzmine, A., & Shoshan‐Barmatz, V. (2024) · Biomolecules · doi:10.3390/biom14101304 · Cited by 23

A Levee to the Flood: Pre-injury Neuroinflammation and Immune Stress Influence Traumatic Brain Injury Outcome

Houle, S., & Kokiko‐Cochran, O. N. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.788055 · Cited by 22

Therapeutic Potential of Heterocyclic Compounds Targeting Mitochondrial Calcium Homeostasis and Signaling in Alzheimer’s Disease and Parkinson’s Disease

Tapias, V., González-Andrés, P., Fernández-Peña, L., Barbero, A., Núñez, L., & Villalobos, C. (2023) · Antioxidants · doi:10.3390/antiox12061282 · Cited by 21

Exploring the role of mitochondrial proteins as molecular target in Alzheimer’s disease

Chadha, S., Behl, T., Sehgal, A., Kumar, A., & BUNGAU, S. G. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.11.008 · Cited by 20

Metabotyping of Docosahexaenoic Acid - Treated Alzheimer’s Disease Cell Model

Bahety, P., Tan, Y. M., Hong, Y., Zhang, L., Chan, E. C. Y., & Ee, P. L. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090123 · Cited by 20

Age-Dependent Decrease of Mitochondrial Complex II Activity in a Familial Mouse Model for Alzheimer’s Disease

Emmerzaal, T. L., Rodenburg, R. J., Tanila, H., Verweij, V., Kiliaan, A. J., & Kozicz, T. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180337 · Cited by 21

Mitochondrial vulnerability to oxidation in human brain organoids modelling Alzheimer's disease

Holubiec, M. I., Alloatti, M., Bianchelli, J., Greloni, F., Arnaiz, C., Gonzalez Prinz, M., Fernandez Bessone, I., Pozo Devoto, V., & Falzone, T. L. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.08.028 · Cited by 20

Resveratrol in Neurodegeneration, in Neurodegenerative Diseases, and in the Redox Biology of the Mitochondria

Danışman, B., Kelek, S. E., & Aslan, M. (2023) · Psychiatry and Clinical Psychopharmacology · doi:10.5152/pcp.2023.23633 · Cited by 23

Neuroprotective Efficacy of Apple Cider Vinegar on Zinc-High Fat Diet-Induced Mono Amine Oxidase Alteration in Murine Model of AD

Tripathi, S., & Mazumder, P. M. (2021) · Journal of the American Nutrition Association · doi:10.1080/07315724.2021.1948933 · Cited by 19

Alteration of mitochondrial homeostasis is an early event in a C. elegans model of human tauopathy

Palikaras, K., Achanta, K., Choi, S., Akbari, M., & Bohr, V. A. (2021) · Aging · doi:10.18632/aging.203683 · Cited by 18

Cytosolic Quality Control of Mitochondrial Protein Precursors—The Early Stages of the Organelle Biogenesis

Lenkiewicz, A. M., Krakowczyk, M., & Brągoszewski, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010007 · Cited by 18

Mitochondrial proteotoxicity: implications and ubiquitin-dependent quality control mechanisms

Karbowski, M., Oshima, Y., & Verhoeven, N. A. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04604-8 · Cited by 21

Simple model systems reveal conserved mechanisms of Alzheimer’s disease and related tauopathies

Jiang, Y., & MacNeil, L. T. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00664-x · Cited by 22

Amyloid Beta Oligomers Activate Death Receptors and Mitochondria-Mediated Apoptotic Pathways in Cerebral Vascular Smooth Muscle Cells; Protective Effects of Carbonic Anhydrase Inhibitors

Anzovino, A., Canepa, E., Alves, M., Lemon, N. L., Carare, R. O., & Fossati, S. (2023) · Cells · doi:10.3390/cells12242840 · Cited by 19

Rescue of mitochondrial import failure by intercellular organellar transfer

Needs, H. I., Glover, E., Pereira, G. C., Witt, A., Hübner, W., Dodding, M. P., Henley, J. M., & Collinson, I. R. (2024) · Nature Communications · doi:10.1038/s41467-024-45283-2 · Cited by 23

Mitochondrial Proteome Changes Correlating with β-Amyloid Accumulation

Völgyi, K., Háden, K., Kis, V., Gulyássy, P., Badics, K., Györffy, B. A., Simor, A., Szabó, Z., Janáky, T., Drahos, L., et al. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9682-4 · Cited by 20

Association Analysis of Polymorphisms in TOMM40, CR1, PVRL2, SORL1, PICALM, and 14q32.13 Regions in Colombian Alzheimer Disease Patients

Ortega-Rojas, J., Morales, L. C., Guerrero, E., Bustos, C., Mejía, A., Forero, D. A., López, L., Pardo, R., Arboleda, G., Yunis, J. J., et al. (2016) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0000000000000142 · Cited by 19

Targeted Lipidomics of Mitochondria in a Cellular Alzheimer’s Disease Model

Kurokin, I., Lauer, A. A., Janitschke, D., Winkler, J., Theiss, E. L., Griebsch, L. V., Pilz, S. M., Matschke, V., van der Laan, M., Grimm, H. S., et al. (2021) · Biomedicines · doi:10.3390/biomedicines9081062 · Cited by 20

The Rationale for Insulin Therapy in Alzheimer’s Disease

Ribarič, S. (2016) · Molecules · doi:10.3390/molecules21060689 · Cited by 20

Novel DNA methylation marker discovery by assumption‐free genome‐wide association analysis of cognitive function in twins

Mohammadnejad, A., Soerensen, M., Baumbach, J., Mengel‐From, J., Li, W., Lund, J., Li, S., Christiansen, L., Christensen, K., Hjelmborg, J., et al. (2021) · Aging Cell · doi:10.1111/acel.13293 · Cited by 18

Two hit mitochondrial-driven model of synapse loss in neurodegeneration

Баранов, В. С., Jauhari, A., Carlisle, D. L., & Friedlander, R. M. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105451 · Cited by 19

Natural Bioactive Products and Alzheimer’s Disease Pathology: Lessons from Caenorhabditis elegans Transgenic Models

Navarro‐Hortal, M. D., Romero‐Márquez, J. M., Osta, S., Jiménez-Trigo, V., Muñoz-Ollero, P., & Varela‐López, A. (2022) · Diseases · doi:10.3390/diseases10020028 · Cited by 18

Mitochondrial dysfunction rapidly modulates the abundance and thermal stability of cellular proteins

Groh, C., Haberkant, P., Stein, F., Filbeck, S., Pfeffer, S., Savitski, M. M., Boos, F., & Herrmann, J. M. (2023) · Life Science Alliance · doi:10.26508/lsa.202201805 · Cited by 22

Plasticity of TOM complex assembly in skeletal muscle mitochondria in response to chronic contractile activity

Joseph, A.-M., & Hood, D. A. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.11.005 · Cited by 18

Bivalent Compound 17MN Exerts Neuroprotection through Interaction at Multiple Sites in a Cellular Model of Alzheimer’s Disease

Liu, K., Chojnacki, J. E., Wade, E. E., Saathoff, J. M., Lesnefsky, E. J., Chen, Q., & Zhang, S. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150242 · Cited by 18

The Dictyostelium model for mitochondrial biology and disease

Pearce, X. G., Annesley, S. J., & Fisher, P. R. (2019) · The International Journal of Developmental Biology · doi:10.1387/ijdb.190233pf · Cited by 18

Modulation of Reactive Oxygen Species Homeostasis as a Pleiotropic Effect of Commonly Used Drugs

Thomas, C., Wurzer, L., Malle, E., Ristow, M., & Madreiter‐Sokolowski, C. T. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.905261 · Cited by 18

The paradigm of amyloid precursor protein in amyotrophic lateral sclerosis: The potential role of the 682 YENPTY 687 motif

Matrone, C. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.01.008 · Cited by 17

Aggregation-prone Tau impairs mitochondrial import, which affects organelle morphology and neuronal complexity

Needs, H. I., Wilkinson, K. A., Henley, J. M., & Collinson, I. R. (2023) · Journal of Cell Science · doi:10.1242/jcs.260993 · Cited by 19

Diabetes mellitus and Alzheimer's disease: Understanding disease mechanisms, their correlation, and promising dual activity of selected herbs

Pramanik, R., Dey, A., Chakrabarty, A. K., Banerjee, D., Narwaria, A., Sharma, S. K., Rai, R. K., Katiyar, C. K., & Dubey, S. K. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118402 · Cited by 18

Multi-Target Effects of the Cannabinoid CP55940 on Familial Alzheimer’s Disease PSEN1 E280A Cholinergic-Like Neurons: Role of CB1 Receptor

Soto‐Mercado, V., Mendivil‐Perez, M., Jiménez-Del-Río, M., & Velez‐Pardo, C. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201045 · Cited by 19

In vivo brain imaging of mitochondrial Ca2+ in neurodegenerative diseases with multiphoton microscopy

Calvo-Rodríguez, M., Kharitonova, E. K., & Bacskai, B. J. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118998 · Cited by 17

Clinical Insights into Mitochondrial Neurodevelopmental and Neurodegenerative Disorders: Their Biosignatures from Mass Spectrometry-Based Metabolomics

Li, H., Uittenbogaard, M. N., Hao, L., & Chiaramello, A. (2021) · Metabolites · doi:10.3390/metabo11040233 · Cited by 18

Role of Mitochondrial Protein Import in Age-Related Neurodegenerative and Cardiovascular Diseases

Bogorodskiy, A. O., Okhrimenko, I. S., Burkatovskii, D., Jakobs, P., Maslov, I., Gordeliy, V., Dencher, N. A., Gensch, T., Voos, W., Altschmied, J., et al. (2021) · Cells · doi:10.3390/cells10123528 · Cited by 19

The Genetics of Alzheimer’s Disease and Parkinson’s Disease

Bekris, L. M., Yu, C., Bird, T. D., & Tsuang, D. W. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-7104-3_21 · Cited by 16

TSPO regulation in reactive gliotic diseases

McNeela, A. M., Bernick, C. B., Hines, R. M., & Hines, D. J. (2018) · Journal of Neuroscience Research · doi:10.1002/jnr.24212 · Cited by 22

Mitochondrial Complex I Inhibition Accelerates Amyloid Toxicity

Joh, Y., & Choi, W. (2017) · Development & Reproduction · doi:10.12717/dr.2017.21.4.417 · Cited by 16

The Emerging Role of Proteolysis in Mitochondrial Quality Control and the Etiology of Parkinson’s Disease

Shanbhag, R., Shi, G., Rujiviphat, J., & McQuibban, G. A. (2012) · Parkinson s Disease · doi:10.1155/2012/382175 · Cited by 17

The Kunitz-protease inhibitor domain in amyloid precursor protein reduces cellular mitochondrial enzymes expression and function

Chua, L. M., Lim, M., & Wong, B. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.07.022 · Cited by 17

Bridging pathway dysfunction and therapy: novel compounds for neuroprotection

Patel, S., Prajapati, C., Nand, S., & Singh, S. K. (2026) · 3 Biotech · doi:10.1007/s13205-026-04697-z · Cited by 16

Adapentpronitrile, a New Dipeptidyl Peptidase-IV Inhibitor, Ameliorates Diabetic Neuronal Injury Through Inhibiting Mitochondria-Related Oxidative Stress and Apoptosis

Lü, Y., Han, W., Luo, Y., Hu, X., Xu, Y. D., Li, H., Hu, C., Huang, D. Y., Ma, J., Yang, Y., et al. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00214 · Cited by 16

Quantitative interaction proteomics reveals differences in the interactomes of amyloid precursor protein isoforms

Andrew, R. J., Fisher, K., Heesom, K. J., Kellett, K. A. B., & Hooper, N. M. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14666 · Cited by 16

Current Perspective of Hydrogen Sulfide as a Novel Gaseous Modulator of Oxidative Stress in Glaucoma

Feng, Y., Prokosch, V., & Liu, H. (2021) · Antioxidants · doi:10.3390/antiox10050671 · Cited by 21

Potential for Ketotherapies as Amyloid-Regulating Treatment in Individuals at Risk for Alzheimer’s Disease

Taylor, M., Sullivan, D. K., Keller, J. E., Burns, J. M., & Swerdlow, R. H. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.899612 · Cited by 17

The 40-Hz White Light-Emitting Diode (LED) Improves the Structure–Function of the Brain Mitochondrial KATP Channel and Respiratory Chain Activities in Amyloid Beta Toxicity

Nazari, M., Vajed-Samiei, T., Torabi, N., Fahanik‐Babaei, J., Saghiri, R., Khodagholi, F., & Eliassi, A. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02681-7 · Cited by 15

A CHCHD6–APP axis connects amyloid and mitochondrial pathology in Alzheimer’s disease

Shang, Y., Sun, X., Chen, X., Wang, Q., Wang, E. J., Miller, E., Xu, R., Pieper, A. A., & Qi, X. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02499-0 · Cited by 15

The mitochondrial function was impaired in APP knockout mouse embryo fibroblast cells

Sheng, B., Niu, Y., Zhou, H. R., Yan, J., Zhao, N., Zhang, X., & Gong, Y. (2009) · 中国科学通报：英文版 · doi:10.1007/s11434-009-0239-7 · Cited by 15

Assembly of 809 whole mitochondrial genomes with clinical, imaging, and fluid biomarker phenotyping

Ridge, P. G., Wadsworth, M. E., Miller, J. B., Saykin, A. J., Green, R. C., Initiative, T. A. D. N., & Kauwe, J. S. K. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.11.013 · Cited by 15

Mitochondrial degradation of amyloidogenic proteins — A new perspective for neurodegenerative diseases

Lautenschläger, J., & Schierle, G. S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101660 · Cited by 16

Altered Mitochondrial Protein Homeostasis and Proteinopathies

Jishi, A., & Qi, X. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.867935 · Cited by 17

Targeting the alternative oxidase (AOX) for human health and food security, a pharmaceutical and agrochemical target or a rescue mechanism?

Szibor, M., Schenkl, C., Barsottini, M. R. D. O., Young, L., & Moore, A. L. (2022) · Biochemical Journal · doi:10.1042/bcj20180192 · Cited by 15

PI3K–ERK1/2 activation contributes to extracellular H2O2 generation in amyloid β toxicity

Ha, J. S., Sung, H. Y., Lim, H. M., Kwon, K., & Park, S. S. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.08.023 · Cited by 15

Protein Truncation as a Common Denominator of Human Neurodegenerative Foldopathies

Jadhav, S., Žilka, N., & Novák, M. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8440-8 · Cited by 15

Classifying Alzheimer’s disease and normal subjects using machine learning techniques and genetic-environmental features

Huang, Y.-H., Chen, Y., Ho, W.-M., Lee, R.-G., Chung, R., Liu, Y., Chang, P.-Y., Chang, S., Wang, C.-W., Chung, W., et al. (2023) · Journal of the Formosan Medical Association · doi:10.1016/j.jfma.2023.10.021 · Cited by 14

Translocator protein (TSPO) ligands attenuate mitophagy deficits in the SH-SY5Y cellular model of Alzheimer's disease via the autophagy adaptor P62

Fairley, L. H., Grimm, A., Herff, S. A., & Eckert, A. (2024) · Biochimie · doi:10.1016/j.biochi.2024.01.012 · Cited by 13

Interplay of mitochondria-associated membrane proteins and autophagy: Implications in neurodegeneration

Kulkarni, P. G., Mohire, V. M., Waghmare, P. P., & Banerjee, T. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101874 · Cited by 16

Altering Mitochondrial Dysfunction as an Approach to Treating Alzheimer’s Disease

Colca, J. R., & Feinstein, D. L. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-394816-8.00005-2 · Cited by 14

Endoplasmic reticulum-unfolded protein response pathway modulates the cellular response to mitochondrial proteotoxic stress

Sarkar, R., Rao, K. B. N., Jha, M. P., & Mapa, K. (2022) · Cell Stress and Chaperones · doi:10.1007/s12192-022-01264-2 · Cited by 14

The MitoLuc Assay System for Accurate Real-Time Monitoring of Mitochondrial Protein Import Within Mammalian Cells

Needs, H. I., Lorriman, J., Pereira, G. C., Henley, J. M., & Collinson, I. R. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168129 · Cited by 12

Reactive Oxygen Species in the Induction of Toxicity

Lenaz, G., & Strocchi, P. (2009) · Wiley eBooks · doi:10.1002/9780470744307.gat024 · Cited by 15

Mitophagy in Alzheimer's disease and its potential as a therapeutic target

Wei, J., Xiao, T., Lyu, J., Zhao, Y., Zhang, Y., Du, X., He, Y., Zhao, M., Yang, X., Yao, Y., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107162 · Cited by 13

Amyloid-beta glycation induces neuronal mitochondrial dysfunction and Alzheimer’s pathogenesis via VDAC1-dependent mtDNA efflux

Akhter, F., Akhter, A., Zhu, X., Schiff, H. C., Maffei, A., Douglas, J. T., Zhou, Q., Zhao, Z., & Zhu, D. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2505046122 · Cited by 16

Amyloid Beta Peptide-Mediated Alterations in Mitochondrial Dynamics and its Implications for Alzheimer’s Disease

Monsalvo-Maraver, L. Á., Maya-López, M., Rangel‐López, E., Túnez, I., Tinkov, A. A., Skalny, A. V., Ferrer, B., Aschner, M., & Santamaría, A. (2022) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527321666220616094036 · Cited by 14

The reciprocal relationship between amyloid precursor protein and mitochondrial function

Strope, T. A., & Wilkins, H. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16183 · Cited by 15

The H63D HFE gene variant promotes activation of the intrinsic apoptotic pathway via mitochondria dysfunction following β‐amyloid peptide exposure

Mairuae, N., Hall, E. C., II, Cheepsunthorn, P., Lee, S. Y., & Connor, J. R. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22466 · Cited by 13

Cognition in Vascular Aging and Mild Cognitive Impairment

Tsentidou, G., Μoraitou, D., & Tsolaki, M. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190638 · Cited by 13

Alterations in inter-organelle crosstalk and Ca2+ signaling through mitochondria during proteotoxic stresses

Ali, M., Rao, K. B. N., Majumder, P., Sarkar, R., & Mapa, K. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.12.003 · Cited by 13

Combined Genome-Wide CSF Aβ-42’s Associations and Simple Network Properties Highlight New Risk Factors for Alzheimer’s Disease

Initiative, A. D. N., de Souza, M. B. R., de Araújo, G. S., Costa, I. G., & de Oliveira, J. R. M. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0667-6 · Cited by 12

The Role of Caspases in Alzheimer’s Disease: Pathophysiology Implications and Pharmacologic Modulation

Khezri, M. R., & Ghasemnejad-Berenji, M. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220873 · Cited by 12

Alzheimer's disease approaches - Focusing on pathology, biomarkers and clinical trial candidates

Hroudová, J., & Fišar, Z. (2024) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2024.111069 · Cited by 13

Development of GMP ‐1 a molecular chaperone network modulator protecting mitochondrial function and its assessment in fly and mice models of Alzheimer's disease

Pavlov, P. F., Hutter‐Paier, B., Havas, D., Windisch, M., & Winblad, B. G. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13624 · Cited by 11

Mitochondrial Targeting of Amyloid-β Protein Precursor Intracellular Domain Induces Hippocampal Cell Death via a Mechanism Distinct from Amyloid-β

Sandberg, A. A., Manning, E., Wilkins, H., Mazzarino, R. C., Minckley, T. F., Swerdlow, R. H., Patterson, D., Qin, Y., & Linseman, D. A. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215108 · Cited by 12

Verteporfin is a substrate-selective γ-secretase inhibitor that binds the amyloid precursor protein transmembrane domain

Castro, M. A., Parson, K. F., Beg, I., Wilkinson, M. C., Nurmakova, K., Levesque, I., Voehler, M., Wolfe, M. S., Ruotolo, B. T., & Sanders, C. R. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101792 · Cited by 13

Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases

Reed, A. L., Mitchell, W., Alexandrescu, A. T., & Alder, N. N. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1263420 · Cited by 13

Quantitative Cytochrome Oxidase Histochemistry: Applications in Human Alzheimer's Disease and Animal Models

Valla, J., Schneider, L. E., Small, A. M., & Gonzalez-Lima, F. (2007) · Journal of Histotechnology · doi:10.1179/his.2007.30.4.235 · Cited by 11

Western and ketogenic diets in neurological disorders: can you tell the difference?

Habashy, K. J., Ahmad, F. A., Ibeh, S., Mantash, S., Kobeissy, F., Issa, H., Habis, R., Tfaily, A., Nabha, S. M., Harati, H., et al. (2022) · Nutrition Reviews · doi:10.1093/nutrit/nuac008 · Cited by 12

Analysis of cognitive performance and polymorphisms of SORL1, PVRL2, CR1, TOMM40, APOE, PICALM, GWAS_14q, CLU, and BIN1 in patients with mild cognitive impairment and cognitively healthy controls

Sanabria, F. C., Bonilla-Vargas, K. J., Estrada, K., Páez, O. M., Vega, E., Guerrero, E., Ortega-Rojas, J., María, F. M., Romero, A., Montañés, P., et al. (2020) · Neurología (English Edition) · doi:10.1016/j.nrleng.2018.07.012 · Cited by 12

Mitochondrial homeostasis dysregulation: Potential mechanisms of Alzheimer's disease mediated by TDP-43

Huang, W., Huang, J., Kuang, N., Wu, J., Feng, F., Luo, Y., & Huang, N. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103290 · Cited by 12

The interplay between glucose and ketone bodies in neural stem cell metabolism

Molloy, J. W., & Barry, D. (2024) · Journal of Neuroscience Research · doi:10.1002/jnr.25342 · Cited by 11

Mitochondrial genetic variation in human bioenergetics, adaptation, and adult disease

Friedrich, V. K., Rubel, M., & Schurr, T. G. (2021) · American Journal of Human Biology · doi:10.1002/ajhb.23629 · Cited by 11

Amyloid precursor protein and mitochondrial dysfunction in Alzheimer's disease

Anandatheerthavarada, H. K., & Devi, L. (2007) · The Neuroscientist · doi:10.1177/1073858407303536 · Cited by 95

Mitochondrial Translocation of Amyloid Precursor Protein and its Cleaved Products: Relevance to Mitochondrial Dysfunction in Alzheimer's Disease

Anandatheerthavarada, H. K., & Devi, L. (2007) · Reviews in the Neurosciences · doi:10.1515/revneuro.2007.18.5.343 · Cited by 28

P2‐291: Metabolism of mitochondria‐associated amyloid precursor protein (APP)

Pavlov, P. F. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.1169

P3–373: Role of mitochondrial Abeta in neuronal stress of Alzheimer disease

Yan, S. D., Yao, J., Xu, H. W., Caspersen, C. S., & Chen, X. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1643

Mitochondrial accumulation of APP and Aβ: significance for Alzheimer disease pathogenesis

Pavlov, P. F., Petersen, C. H., Glaser, E. G., & Ankarcrona, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00892.x · Cited by 84