Accumulation of APP-CTF induces mitophagy dysfunction in the iNSCs model of Alzheimer’s disease

Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance

Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081 · see citing works

The Cellular Phase of Alzheimer’s Disease

De Strooper, B., & Karran, E. (2016) · Cell · doi:10.1016/j.cell.2015.12.056 · Cited by 1,990 · see citing works

Mitophagy inhibits amyloid-β and tau pathology and reverses cognitive deficits in models of Alzheimer’s disease

Fang, E. F., Hou, Y., Palikaras, K., Adriaanse, B. A., Kerr, J. S., Yang, B., Lautrup, S., Hasan-Olive, M. M., Caponio, D., Dan, X., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0332-9 · Cited by 1,740 · see citing works

Mitochondria dysfunction in the pathogenesis of Alzheimer’s disease: Recent advances.

Wang, W., Zhao, F., Ma, X., Perry, G., & Zhu, X. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00376-6 · Cited by 1,274 · see citing works

Autophagy and apoptosis dysfunction in neurodegenerative disorders

Ghavami, S., Shojaei, S., Yeganeh, B., Ande, S. R., Jangamreddy, J. R., Mehrpour, M., Christoffersson, J., Chaabane, W., Moghadam, A. R., Kashani, H. H., et al. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.10.004 · Cited by 1,039 · see citing works

Mitophagy and Alzheimer’s Disease: Cellular and Molecular Mechanisms

Kerr, J. S., Adriaanse, B. A., Greig, N. H., Mattson, M. P., Cader, M. Z., Bohr, V. A., & Fang, E. F. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.002 · Cited by 870 · see citing works

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 · see citing works

Ubiquitination and selective autophagy

Shaid, S., Brandts, C. H., Serve, H., & Dikic, I. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.72 · Cited by 800 · see citing works

Building and decoding ubiquitin chains for mitophagy

Harper, J. W., Ordureau, A., & Heo, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.129 · Cited by 668 · see citing works

Amyloid-β and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice

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

Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease

Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654 · see citing works

Upregulated function of mitochondria‐associated ER membranes in Alzheimer disease

Area‐Gomez, E., del Carmen Lara Castillo, M., Tambini, M. D., Guardia‐Laguarta, C., de Groof, A. J. C., Madra, M., Ikenouchi, J., Umeda, M., Bird, T. D., Sturley, S. L., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.202 · Cited by 638 · see citing works

APP, PSEN1, and PSEN2 mutations in early-onset Alzheimer disease: A genetic screening study of familial and sporadic cases

Lanoiselée, H.-M., Nicolas, G., Wallon, D., Rovelet-Lecrux, A., Lacour, M., Rousseau, S., Richard, A.-C., Pasquier, F., Rollin-Sillaire, A., Martinaud, O., et al. (2017) · PLOS Medicine · doi:10.1371/journal.pmed.1002270 · Cited by 616 · see citing works

Defining and measuring autophagosome flux—concept and reality

Loos, B., du Toit, A., & Hofmeyr, J. S. (2014) · Autophagy · doi:10.4161/15548627.2014.973338 · Cited by 317 · see citing works

Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer's disease patient brains

Ye, X., Sun, X., Starovoytov, V., & Cai, Q. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv056 · Cited by 274 · see citing works

Disease-associated tau impairs mitophagy by inhibiting Parkin translocation to mitochondria

Cummins, N., Tweedie, A., Zuryn, S., Bertran‐Gonzalez, J., & Götz, J. (2019) · The EMBO Journal · doi:10.15252/embj.201899360 · Cited by 267 · see citing works

Accumulation of amyloid precursor protein C-terminal fragments triggers mitochondrial structure, function, and mitophagy defects in Alzheimer’s disease models and human brains

Vaillant-Beuchot, L., Mary, A., Pardossi-Piquard, R., Bourgeois, A., Lauritzen, I., Eysert, F., Kinoshita, P. F., Cazareth, J., Badot, C., Fragaki, K., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02234-7 · Cited by 263 · see citing works

OXPHOS mutations and neurodegeneration

Koopman, W. J. H., Distelmaier, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.300 · Cited by 254 · see citing works

Intraneuronal aggregation of the β-CTF fragment of APP (C99) induces Aβ-independent lysosomal-autophagic pathology

Lauritzen, I., Pardossi-Piquard, R., Bourgeois, A., Pagnotta, S., Biferi, M.-G., Barkats, M., Lacor, P., Klein, W., Bauer, C., & Checler, F. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1577-6 · Cited by 219 · see citing works

Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's disease

Weggen, S., & Beher, D. (2012) · Alzheimer's Research & Therapy · doi:10.1186/alzrt107 · Cited by 192 · see citing works

Tau accumulation impairs mitophagy via increasing mitochondrial membrane potential and reducing mitochondrial Parkin

Hu, Y., Li, X., Wang, Z.-H., Luo, Y., Zhang, X., Liu, X., Feng, Q., Wang, Q., Yue, Z., Chen, Z., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7861 · Cited by 171 · see citing works

Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99)

Jiang, Y., Sato, Y., Im, E., Berg, M., Bordi, M., Darji, S., Kumar, A., Mohan, P. S., Bandyopadhyay, U., Diaz, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0578-19.2019 · Cited by 166 · see citing works

Defective Autophagy and Mitophagy in Aging and Alzheimer’s Disease

Tran, M., & Reddy, P. H. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.612757 · Cited by 166 · see citing works

The γ-secretase complex: from structure to function

Zhang, X., Li, Y., Xu, H., & Zhang, Y. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00427 · Cited by 164 · see citing works

Amyloid precursor protein-mediated endocytic pathway disruption induces axonal dysfunction and neurodegeneration.

Xu, W., Weissmiller, A. M., White, J. A., Fang, F., Wang, X., Wu, Y.-W., Pearn, M. L., Zhao, X.-B., Sawa, M., Chen, S.-D., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci82409 · Cited by 157 · see citing works

Contribution of Tau Pathology to Mitochondrial Impairment in Neurodegeneration

Maria Jose Perez, J., Jara, C., & Quintanilla, R. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00441 · Cited by 153 · see citing works

Mitophagy Failure in Fibroblasts and iPSC-Derived Neurons of Alzheimer’s Disease-Associated Presenilin 1 Mutation

Martín-Maestro, P., Gargini, R., Sproul, A. A., García, E., Antón, L. C., Noggle, S., Arancio, O., Ávila, J., & García‐Escudero, V. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00291 · Cited by 125 · see citing works

Dysfunction of mitochondria and oxidative stress in the pathogenesis of Alzheimer's disease: On defects in the cytochrome c oxidase complex and aldehyde detoxification

Ohta, S., & Ohsawa, I. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9208 · Cited by 121 · see citing works

Rapid and Efficient Direct Conversion of Human Adult Somatic Cells into Neural Stem Cells by HMGA2/let-7b

Yu, K., Shin, J., Kim, J.-J., Koog, M. G., Lee, J. Y., Choi, S. W., Kim, H.-S., Seo, Y., Lee, S., Shin, T., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.038 · Cited by 112 · see citing works

Impairments in learning and memory accompanied by neurodegeneration in mice transgenic for the carboxyl-terminus of the amyloid precursor protein

Berger-Sweeney, J. E., McPhie, D. L., Arters, J., Greenan, J., Oster‐Granite, M. L., & Neve, R. L. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00014-5 · Cited by 91 · see citing works

Lysosomal dysfunction in the brain of a mouse model with intraneuronal accumulation of carboxyl terminal fragments of the amyloid precursor protein

Kaur, G., Pawlik, M., Gandy, S., Ehrlich, M., Smiley, J., & Levy, E. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.189 · Cited by 53 · see citing works

Does Intraneuronal Accumulation of Carboxyl-terminal Fragments of the Amyloid Precursor Protein Trigger Early Neurotoxicity in Alzheimer's Disease?

Lauritzen, I., Pardossi-Piquard, R., Bourgeois, A., Bécot, A., & Checler, F. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190325092841 · Cited by 53 · see citing works

C-terminal fragments of the amyloid precursor protein in cerebrospinal fluid as potential biomarkers for Alzheimer disease

García‐Ayllón, M., López‐Font, I., Boix, C. P., Fortea, J., Sánchez‐Valle, R., Lleó, A., Molinuevo, J. L., Zetterberg, H., Blennow, K., & Sáez‐Valero, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-02841-7 · Cited by 52 · see citing works

Targeting γ-secretase triggers the selective enrichment of oligomeric APP-CTFs in brain extracellular vesicles from Alzheimer cell and mouse models

Lauritzen, I., Bécot, A., Bourgeois, A., Pardossi-Piquard, R., Biferi, M., Barkats, M., & Checler, F. (2019) · Translational Neurodegeneration · doi:10.1186/s40035-019-0176-6 · Cited by 37 · see citing works

Human iNSC-derived brain organoid model of lysosomal storage disorder in Niemann–Pick disease type C

Lee, S., Shin, N., Kook, M. G., Kong, D., Kim, N. G., Choi, S. W., & Kang, K. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03262-7 · Cited by 35 · see citing works

Accumulation of carboxy-terminal fragments of APP increases phosphodiesterase 8B.

Kametani, F., & Haga, S. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.09.029 · Cited by 23 · see citing works

Generation of patient specific human neural stem cells from Niemann-Pick disease type C patient-derived fibroblasts

Sung, E., Yu, K., Shin, J., Seo, Y., Kim, H., Koog, M. G., Kang, I., Kim, J.-J., Lee, B., Shin, T., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.19976 · Cited by 23 · see citing works

Mitophagy in Alzheimer’s disease: Molecular defects and therapeutic approaches

Mary, A., Eysert, F., Checler, F., & Chami, M. (2023) · Molecular Psychiatry · doi:10.1038/s41380-022-01631-6 · Cited by 244 · see citing works

Neuropathogenesis-on-chips for neurodegenerative diseases

Amartumur, S., Nguyen, H. M., Huynh, T., Kim, T. S., Woo, R., Oh, E., Kim, K. K., Lee, L. P., & Heo, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46554-8 · Cited by 120 · see citing works

Treadmill Exercise Improves PINK1/Parkin-Mediated Mitophagy Activity Against Alzheimer’s Disease Pathologies by Upregulated SIRT1-FOXO1/3 Axis in APP/PS1 Mice

Zhao, N., Zhang, X., Li, B., Wang, J., Zhang, C., & Xu, B. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03035-7 · Cited by 69 · see citing works

Promoting Alzheimer’s disease research and therapy with stem cell technology

Cao, Z., Kong, F., Ding, J., Chen, C., He, F., & Deng, W. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-03737-w · Cited by 59 · see citing works

Accumulation of APP C-terminal fragments causes endolysosomal dysfunction through the dysregulation of late endosome to lysosome-ER contact sites

Bretou, M., Sannerud, R., Escamilla‐Ayala, A., Leroy, T., Vrancx, C., Acker, Z. P. V., Perdok, A., Vermeire, W., Vorsters, I., Keymolen, S. V., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.03.030 · Cited by 43 · see citing works

Therapeutic Potential of Targeting Mitochondria for Alzheimer’s Disease Treatment

Atlante, A., Amadoro, G., Latina, V., & Valenti, D. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11226742 · Cited by 39 · see citing works

Mitophagy: A potential therapeutic target for insulin resistance

Ning, P., Jiang, X., Yang, J., Zhang, J., Yang, F., & Cao, H. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.957968 · Cited by 35 · see citing works

The Impact of the Cellular Environment and Aging on Modeling Alzheimer's Disease in 3D Cell Culture Models

Hebisch, M., Klostermeier, S., Wolf, K., Boccaccini, A. R., Wolf, S. E., Tanzi, R. E., & Kim, D. Y. (2023) · Advanced Science · doi:10.1002/advs.202205037 · Cited by 29 · see citing works

The amyloid precursor protein and its derived fragments concomitantly contribute to the alterations of mitochondrial transport machinery in Alzheimer’s disease

Vaillant-Beuchot, L., Eysert, F., Duval, B., Kinoshita, P.-F., Pardossi-Piquard, R., Bauer, C., Eddarkaoui, S., Buée, L., Checler, F., & Chami, M. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06742-2 · Cited by 24 · see citing works

How the gut microbiota impacts neurodegenerative diseases by modulating CNS immune cells

Schaible, P., Henschel, J., & Erny, D. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03371-0 · Cited by 31 · see citing works

Unraveling mitochondrial dysfunction: comprehensive perspectives on its impact on neurodegenerative diseases

Yusoff, A. A. M., & Khair, S. Z. N. M. (2024) · Reviews in the Neurosciences · doi:10.1515/revneuro-2024-0080 · Cited by 22 · see citing works

Parkin as a Molecular Bridge Linking Alzheimer’s and Parkinson’s Diseases?

Checler, F., & da Costa, C. A. (2022) · Biomolecules · doi:10.3390/biom12040559 · Cited by 19 · see citing works

The emerging role of exercise in Alzheimer’s disease: Focus on mitochondrial function

Feng, L., Li, B., Yong, S. S., Xu, W., & Tian, Z. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102486 · Cited by 17 · see citing works

SARS-CoV-2 Invasion and Pathological Links to Prion Disease

Lukiw, W. J., Jaber, V. R., Pogue, A. I., & Zhao, Y. (2022) · Biomolecules · doi:10.3390/biom12091253 · Cited by 15 · see citing works

Induced Pluripotent Stem Cells-Based Regenerative Therapies in Treating Human Aging-Related Functional Decline and Diseases

Yu, P., Liu, B., Dong, C., & Chang, Y. (2025) · Cells · doi:10.3390/cells14080619 · Cited by 17 · see citing works

Towards a Unitary Hypothesis of Alzheimer’s Disease Pathogenesis

Area-Gómez, E., & Schon, E. (2024) · Journal of Alzheimer's Disease · doi:10.3233/jad-231318 · Cited by 16 · see citing works

Mitochondrial alterations in fibroblasts from sporadic Alzheimer's disease (AD) patients correlate with AD-related clinical hallmarks

Eysert, F., Kinoshita, P. F., Lagarde, J., Lacas‐Gervais, S., Xicota, L., Dorothée, G., Bottlaender, M., Checler, F., Potier, M., Sarazin, M., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01807-x · Cited by 14 · see citing works

Gastrodin ameliorates synaptic impairment, mitochondrial dysfunction and oxidative stress in N2a/APP cells

Tang, Z., Peng, Y., Jiang, Y., Wang, L., Guo, M., Chen, Z., Luo, C., Zhang, T., Xiao, Y. C., Ni, R., et al. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150127 · Cited by 11 · see citing works

Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity

Kassir, M. F., Lee, H. G., Oleinik, N. V., Wofford, W., Walton, C., Atilgan, F. C., Janneh, A. H., Chakraborty, P., Calisir, K., Percin, E., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-4740 · Cited by 10 · see citing works

The AICD fragment of APP initiates a FoxO3a mediated response via FANCD2

Greenwood, E. K., Angelova, D. M., Büchner, H. M. I., & Brown, D. R. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103760 · Cited by 8 · see citing works

Developing Dynamic Structure‐Based Pharmacophore and ML‐Trained QSAR Models for the Discovery of Novel Resistance‐Free RET Tyrosine Kinase Inhibitors Through Extensive MD Trajectories and NRI Analysis

Sayyah, E., Oktay, L., Tunç, H., & Durdağı, S. (2024) · ChemMedChem · doi:10.1002/cmdc.202300644 · Cited by 6 · see citing works

Investigating Connectivity Deficits in Alzheimer’s Disease Using a Novel 3D Bioprinted Model Designed to Quantify Neurite Outgrowth

Whitehouse, C. A., Bravington, E., Patir, A., Wei, W., Brownlees, J., He, Y., & Corbett, N. J. (2025) · Bioengineering · doi:10.3390/bioengineering12030245 · Cited by 5 · see citing works

The Role of Mitochondrial Dysfunction in Alzheimer’s: Molecular Defects and Mitophagy-Enhancing Approaches

Farsi, R. M. (2023) · Life · doi:10.3390/life13040970 · Cited by 5 · see citing works

Pharmacological inhibition of PLK2 kinase activity mitigates cognitive decline but aggravates APP pathology in a sex-dependent manner in APP/PS1 mouse model of Alzheimer's disease

Martínez-Drudis, L., Bérard, M., Musiol, D., Rivest, S., & Oueslati, A. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e39571 · Cited by 6 · see citing works

APP β-CTF triggers cell-autonomous synaptic toxicity independent of AβPreprint

Luo, M., Zhou, J., Sun, C., Chen, W., Fu, C., Si, C., Zhang, Y., Geng, Y., & Chen, Y. (2024) · eLife · doi:10.7554/elife.100968 · Cited by 5 · see citing works

Mitophagy in neurodegeneration: crosstalk between PRKN/parkin-dependent and PRKN-independent pathways

Rasmussen, L. K., Moreira, D. G., Okarmus, J., Simonsen, A., & Meyer, M. (2026) · Autophagy · doi:10.1080/15548627.2026.2711596 · Cited by 4 · see citing works

MAMs and Mitochondrial Quality Control: Overview and Their Role in Alzheimer’s Disease

Luo, J.-S., Zhai, W.-H., Ding, L.-L., Zhang, X.-J., Han, J., Ning, J., Chen, X.-M., Jiang, W., Yan, R., & Chen, M. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04205-w · Cited by 4 · see citing works

Mitochondrial quality control disorder in neurodegenerative disorders: Potential and advantages of traditional Chinese medicines

Xu, L., Zhang, T., Zhu, B., Tao, H., Liu, Y., Liu, X., Zhang, Y., & Meng, X. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2024.101146 · Cited by 4 · see citing works

Amyloidogenic proteolysis of APP regulates glutamatergic presynaptic functionPreprint

Kapadia, A., Schuhmann, F., Daşkın, E., Walter, J., Lindahl, I., Rahmani, N., Pezeshkian, W., & Hafner, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.01.667924 · Cited by 4 · see citing works

Unravelling the Parkinson’s puzzle, from medications and surgery to stem cells and genes: a comprehensive review of current and future management strategies

Chandrababu, K., Radhakrishnan, V., Anjana, A. S., Rajan, R. S., Sivan, U., Krishnan, S., & Chakrapani, P. S. B. (2023) · Experimental Brain Research · doi:10.1007/s00221-023-06735-1 · Cited by 3 · see citing works

APP β-CTF triggers cell-autonomous synaptic toxicity independent of AβPreprint

Luo, M., Zhou, J., Sun, C., Chen, W., Fu, C., Si, C., Zhang, Y., Geng, Y., & Chen, Y. (2024) · eLife · doi:10.7554/elife.100968.1 · Cited by 3 · see citing works

APP β-CTF triggers cell-autonomous synaptic toxicity independent of Aβ

Luo, M., Zhou, J., Sun, C., Chen, W., Fu, C., Si, C., Zhang, Y., Geng, Y., & Chen, Y. (2025) · eLife · doi:10.7554/elife.100968.3 · Cited by 2 · see citing works

Functional relationships linking C99/APP-βCTF dimerization, proteostasis disruption, and organelle dysfunction

Badot, C., Bini, A., Duplan, E., Checler, F., & Lauritzen, I. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02928-7 · Cited by 1 · see citing works

Production of Amyloid-β in the Aβ-Protein-Precursor Proteolytic Pathway Is Discontinued or Severely Suppressed in Alzheimer’s Disease-Affected Neurons: Contesting the ‘Obvious’

Volloch, V., & Rits‐Volloch, S. (2025) · Genes · doi:10.3390/genes16010046 · Cited by 2 · see citing works

Gastrodin ameliorates synaptic impairment, reestablishes mitochondrial membrane potential and reduces oxidative stress in N2a/APP cells through ERK1/2 and GSK-3β pathwaysPreprint

Tang, Z., Peng, Y., Wang, L., Guo, M., Chen, Z., Zhang, T., Xiao, Y. C., Ni, R., & Qi, X. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.15.524095 · Cited by 2 · see citing works

Cogs in the autophagic machine—equipped to combat dementia-prone neurodegenerative diseases

de Wet, S., Theart, R. P., & Loos, B. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1225227 · Cited by 1 · see citing works

N-tert-Butylhydroxylamine promotes melanin production in oxidative stress conditions through the MITF signaling pathway

Kim, G. H., & Kim, M.-M. (2025) · Archives of Dermatological Research · doi:10.1007/s00403-025-04054-9 · Cited by 1 · see citing works

Alzheimer’s Is a Multiform Disease of Sustained Neuronal Integrated Stress Response Driven by the C99 Fragment Generated Independently of AβPP; Proteolytic Production of Aβ Is Suppressed in AD-Affected Neurons: Evolution of a Theory

Volloch, V., & Rits‐Volloch, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094252 · Cited by 1 · see citing works

Presynaptic accumulation of APP-CTFβ may contribute to synaptic dysfunction in Alzheimer’s disease

Kapadia, A., Schuhmann, F., Daşkın, E., Walter, J., Lindahl, I., Rahmani, N., Morrema, T. H. J., Rozemüller, A. J. M., Boon, B. D. C., Pezeshkian, W., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00899-6 · Cited by 1 · see citing works

miR-204-5p Inhibits the Proliferation and Differentiation of Fetal Neural Stem Cells by Targeting Wingless-Related MMTV Integration Site 2 to Regulate the Ephrin-A2/EphA7 Pathway

Fan, L., He, M., Mo, W., Yao, Q., He, M., & Jiang, J. (2022) · Journal of Biomedical Nanotechnology · doi:10.1166/jbn.2022.3470 · Cited by 1 · see citing works

APP β-CTF triggers cell-autonomous synaptic toxicity independent of AβPreprint

Luo, M., Zhou, J., Sun, C., Chen, W., Fu, C., Si, C., Zhang, Y., Geng, Y., & Chen, Y. (2025) · eLife · doi:10.7554/elife.100968.2 · Cited by 1 · see citing works

Targeting Lysosomal Dysfunction to Alleviate Plaque Deposition in an Alzheimer Disease Model

Fremuth, L. E., van de Vlekkert, D., Hu, H., Weesner, J. A., Annunziata, I., Yogalingam, G., & d’Azzo, A. (2025) · doi:10.1101/2025.04.28.651121 · Cited by 1 · see citing works

Mitochondria alterations in fibroblasts from sporadic Alzheimer’s disease (AD) patients correlate with AD-related clinical hallmarksPreprint

Eysert, F., Kinoshita, P. F., Lagarde, J., Lacas‐Gervais, S., Xicota, L., Dorothée, G., Bottlaender, M., Checler, F., Potier, M., Sarazin, M., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.21.570579

Pathways in the brain, heart and lung influenced by SARS-CoV-2 NSP6 and SARS-CoV-2 regulated miRNAs: an in silico study hinting cancer incidencePreprint

Chatterjee, S., Mahata, J., Kateriya, S., & Anirudhan, G. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.11.578752

Cell growth and mitochondrial anomalies in induced pluripotent stem cells with Presenilin 1 mutationPreprint

Hamam, R., Hanna, R., Barabino, A., Serhani, D., Tavares, E. S., Héon, E., & Bernier, G. (2024) · Research Square · doi:10.21203/rs.3.rs-4415469/v1

Sphingolipid metabolism in the regulation of mitophagy: implications in cancer therapy, immune cell function, and neurodegeneration

Kassir, M. F., & Öğretmen, B. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00005-3

Large extracellular vesicles containing mitochondria (EVMs) derived from Alzheimer’s disease cells harbor pathologic functional and molecular profiles and spread mitochondrial dysfunctionsPreprint

Eysert, F., Legros, V., Gay, A.-S., Debayle, D., Lacas‐Gervais, S., Chevreux, G., Bottlaender, M., Dorothée, G., Checler, F., Potier, M.-C., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.08.631851

Additional file 1 of Mitochondrial alterations in fibroblasts from sporadic Alzheimer's disease (AD) patients correlate with AD-related clinical hallmarks

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Investigating the molecular mechanisms of glutamine metabolism and mitochondria-related biomarkers in Alzheimer’s disease through transcriptomics and experimental validation

Si, X., Tian, S., Chen, Y., Li, X., Wu, G., Yao, Y., & Wang, M. (2026) · European journal of medical research · doi:10.1186/s40001-025-03747-1

Autophagy and neuroinflammation modulation by nano-graphene oxide in PSEN1 Alzheimer’s brain organoidsPreprint

Kim, N. G., Chun, J., Park, H., Kim, H., Choi, S. W., Ryu, J., & Kang, K. (2026) · Research Square · doi:10.21203/rs.3.rs-8383146/v1

Ketone-Dependent Restoration of Autophagy and Mitochondrial Quality Control Through VPS35 in a Drosophila Model of C99-Induced Neurodegeneration

Huang, H., Xu, K., & Lardelli, M. T. (2026) · Cells · doi:10.3390/cells15121082

Exercise as a Systemic Prevention and Management for Alzheimer’s Disease: Restoring Brain–Body Homeostasis Through Metabolic, Neurovascular, Anti-Inflammatory, and Regenerative Mechanisms

Xiao, L., Green, J. M., Mochizuki, M., & Nakahara, T. (2026) · Cells · doi:10.3390/cells15151368

PrPC limits APP delivery to the plasma membrane and alters its processing to facilitate Aβ release

Mehta, N. A., Jo, S., Smirnou, S., Thinakaran, G., & Mastrianni, J. A. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107576

Accumulation of amyloid precursor protein C-terminal fragments triggers mitochondrial structure, function, and mitophagy defects in Alzheimer’s disease models and human brains

Vaillant-Beuchot, L., Mary, A., Pardossi-Piquard, R., Bourgeois, A., Lauritzen, I., Eysert, F., Kinoshita, P. F., Cazareth, J., Badot, C., Fragaki, K., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02234-7 · Cited by 263 · see citing works

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

Devi, L., & Ohno, M. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.09.001 · Cited by 133 · see citing works

Mechanisms underlying mitochondrial dysfunctions, mitophagy failureand mitochondrial transport defects in Alzheimer's disease

Vaillant-Beuchot, L. (2022) · theses.fr (ABES)

Mitochondrial Localized Amyloid Precursor Protein Alters Mitochondrial Function and Mitophagy

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The amyloid precursor protein and its derived fragments concomitantly contribute to the alterations of mitochondrial transport machinery in Alzheimer’s disease

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