The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Open accessAbstract
Mitochondrial dysfunction is a prominent feature of Alzheimer's disease (AD) neurons. In this study, we explored the involvement of an abnormal mitochondrial dynamics by investigating the changes in the expression of mitochondrial fission and fusion proteins in AD brain and the potential cause and consequence of these changes in neuronal cells. We found that mitochondria were redistributed away from axons in the pyramidal neurons of AD brain. Immunoblot analysis revealed that levels of DLP1 (also referred to as Drp1), OPA1, Mfn1, and Mfn2 were significantly reduced whereas levels of Fis1 were significantly increased in AD. Despite their differential effects on mitochondrial morphology, manipulations of these mitochondrial fission and fusion proteins in neuronal cells to mimic their expressional changes in AD caused a similar abnormal mitochondrial distribution pattern, such that mitochondrial density was reduced in the cell periphery of M17 cells or neuronal process of primary neurons and correlated with reduced spine density in the neurite. Interestingly, oligomeric amyloid-beta-derived diffusible ligands (ADDLs) caused mitochondrial fragmentation and reduced mitochondrial density in neuronal processes. More importantly, ADDL-induced synaptic change (i.e., loss of dendritic spine and postsynaptic density protein 95 puncta) correlated with abnormal mitochondrial distribution. DLP1 overexpression, likely through repopulation of neuronal processes with mitochondria, prevented ADDL-induced synaptic loss, suggesting that abnormal mitochondrial dynamics plays an important role in ADDL-induced synaptic abnormalities. Based on these findings, we suggest that an altered balance in mitochondrial fission and fusion is likely an important mechanism leading to mitochondrial and neuronal dysfunction in AD brain.
Overview
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
Cites
Statistics
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Increased accumulation of APP and its processed peptides in the mitochondria of AD neurons and their effects on mitochondrial dynamics and mitophagy have been documented (21–24).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [24]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Mitochondrial fission-fusion dynamics through alterations of Drp1, Parkin, and Pink1 functions (23,24), which play essential roles in mitophagy induction and mitochondrial quality control during healthy brain aging, are disrupted in various neurodegenerative diseases, including Parkinson’s disease (PD) and AD (25).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [24]
In the citing paper
“Aβ accumulates in mitochondria in AD brain, which is accompanied by altered mitochondrial structure, decreased mitochondrial respiratory function and ATP production, impaired mitochondrial dynamics, and elevated mitochondria-associated oxidative stress.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
In the citing paper
“Mitochondrial Aβ levels correlate with abnormalities in mitochondrial structure and function.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
In the citing paper
“Aβ peptides can induce ROS production from mitochondria, leading to release of cytochrome c and apoptosis-inducing factor, thereby driving mitochondrial dysfunction, cell apoptosis and neuronal loss [97, 100].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
In the citing paper
“Soluble Aβ oligomers disrupted the balance between mitochondrial fission and fusion, leading to significant mitochondrial dysfunction.197,198”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [197]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
DeKosky, S. T., & Scheff, S. W. (1990) · Annals of Neurology · doi:10.1002/ana.410270502 · Cited by 2,376
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
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
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644
The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
Li, Z., Okamoto, K.-I., Hayashi, Y., & Sheng, M. (2004) · Cell · doi:10.1016/j.cell.2004.11.003 · Cited by 1,498
Cited by
Sorted by citations
Items 801–900 of 1,001
High-Throughput Small Molecule Screen Identifies Modulators of Mitochondrial Function in Neurons
Várkuti, B. H., Liu, Z., Képiró, M., Pacifico, R., Gai, Y., Kamenecka, T., & Davis, R. L. (2020) · iScience · doi:10.1016/j.isci.2020.100931 · Cited by 18
Mitofusin-2 is a novel anti-angiogenic factor in pancreatic cancer
Lin, Z., Lin, X., Chen, J., Huang, G., Chen, T., & Zheng, L. (2021) · Journal of Gastrointestinal Oncology · doi:10.21037/jgo-21-176 · Cited by 17
Mitochondria: how eminent in ageing and neurodegenerative disorders?
Bamshad, C., Najafi-Ghalehlou, N., Pourmohammadi-Bejarpasi, Z., Tomita, K., Kuwahara, Y., Sato, T., Feizkhah, A., Roushnadeh, A. M., & Roudkenar, M. H. (2022) · Human Cell · doi:10.1007/s13577-022-00833-y · Cited by 20
Selective Vulnerability of Synaptic Signaling and Metabolism to Nitrosative Stress
Mongin, A. A., Dohare, P., & Jourd’heuil, D. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4559 · Cited by 19
Fu, Q., Gao, N., Yu, J., Ma, G., Du, Y., Wang, F., Su, Q., & Che, F. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1313-3 · Cited by 18
Yan, H., Zhao, H., Kang, Y., Ji, X., Zhang, T., Wang, Y., Cui, R., Zhang, G., & Shi, G. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108627 · Cited by 17
Qin, J., Guo, S., Yang, J., Qazi, I. H., Pan, B., Lv, T., Zang, S., Fang, Y., & Zhou, G. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.752001 · Cited by 19
Ciccone, L., Nencetti, S., Rossello, A., & Orlandini, E. (2023) · Pharmaceuticals · doi:10.3390/ph16071036 · Cited by 18
Music compensates for altered gene expression in age-related cognitive disorders
Gómez‐Carballa, A., Navarro, L., Pardo‐Seco, J., Bello, X., Pischedda, S., Viz-Lasheras, S., Camino‐Mera, A., Currás-Tuala, M. J., Ferreirós-Vidal, I., Mallah, N., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-48094-5 · Cited by 17
Maruthiyodan, S., Mumbrekar, K. D., & Guruprasad, K. P. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101868 · Cited by 18
Rockenstein, E. M., Ubhi, K. K., Trejo, M., Mante, M., Patrick, C., Adame, A., Novak, P. H., Jech, M., Doppler, E., Moessler, H., et al. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-90 · Cited by 18
RetractedHawkins, K., & Duchen, M. R. (2019) · World Journal of Stem Cells · doi:10.4252/wjsc.v11.i5.236 · Cited by 18
Nanomedicines for Subcellular Targeting: The Mitochondrial Perspective
Oladimeji, O., Akinyelu, J., & Singh, M. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666191125092111 · Cited by 17
Mfn2 Overexpression Attenuates MPTP Neurotoxicity In Vivo
Zhao, F., Austria, Q. M., Wang, W., & Zhu, X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020601 · Cited by 19
Self-citationCRMP2 Is Involved in Regulation of Mitochondrial Morphology and Motility in Neurons
Brustovetsky, T., Khanna, R., & Brustovetsky, N. (2021) · Cells · doi:10.3390/cells10102781 · Cited by 17
Bolognin, S., Zatta, P. F., Lorenzetto, E., Valenti, M. T., & Buffelli, M. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.02.008 · Cited by 17
Chua, L. M., Lim, M., & Wong, B. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.07.022 · Cited by 17
Adlimoghaddam, A., Fayazbakhsh, F., Mohammadi, M., Babaei, Z., Behrooz, A. B., Tabasi, F., Guan, T., Beheshti, I., Aghaei, M., Klionsky, D. J., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02490-0 · Cited by 17
Effects of Redox Homeostasis and Mitochondrial Damage on Alzheimer’s Disease
Wu, Y., & Hsieh, H. (2023) · Antioxidants · doi:10.3390/antiox12101816 · Cited by 16
Seong, J. B., Bae, Y. C., Lee, H., Huh, J., Lee, S., Lee, H. J., & Lee, D. (2019) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2019.114797 · Cited by 16
Self-citationGardner, M. R., Baruah, V., Vargas, G., Motamedi, M., Milner, T. E., & Rylander, H. G. (2020) · Translational Vision Science & Technology · doi:10.1167/tvst.9.5.18 · Cited by 17
A Review of ApoE4 Interference Targeting Mitophagy Molecular Pathways for Alzheimer's Disease
Chen, H., Chen, F., Jiang, Y., Zhang, L., Hu, G., Sun, F., Zhang, M., Ji, Y., Chen, Y., Che, G., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.881239 · Cited by 19
Yu, H., Yang, C., Wang, G., & Wang, X. (2025) · Medicine · doi:10.1097/md.0000000000042748 · Cited by 16
Self-citationCRMP2 Participates in Regulating Mitochondrial Morphology and Motility in Alzheimer’s Disease
Brustovetsky, T., Khanna, R., & Brustovetsky, N. (2023) · Cells · doi:10.3390/cells12091287 · Cited by 15
Regulating Lars2 in mitochondria: A potential Alzheimer's therapy by inhibiting tau phosphorylation
Qian, W., Yuan, L., Zhuge, W., Gu, L., Chen, Y., Zhuge, Q., Ni, H., & Lv, X. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00353 · Cited by 17
Liao, Z., Zhang, Q., Ren, N., Zhao, H., & Zheng, X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1418939 · Cited by 15
Road to Alzheimer’s Disease: The Pathomechanism Underlying
Anand, R., Kaushal, A., Wani, W. Y., & Gill, K. D. (2011) · Pathobiology · doi:10.1159/000332218 · Cited by 16
The Amyloid Precursor Protein—A Novel Player within the Molecular Array of Presynaptic Nanomachines
Laßek, M., Weingarten, J., Wegner, M., & Volknandt, W. (2016) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2015.00021 · Cited by 15
Dynamic Changes of Mitochondrial Fusion and Fission in Brain Injury after Cardiac Arrest in Rats
Li, Y., Tang, Q., Wang, P., Qin, J., Wu, H., Lin, J., & Huang, Z. (2017) · BioMed Research International · doi:10.1155/2017/1948070 · 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
Gauba, E., Sui, S., Tian, J., Driskill, C. M., Jia, K., Yu, C., Rughwani, T., Wang, Q., Kroener, S., Guo, L., et al. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.09.018 · Cited by 15
Oxygen Sensing and Signaling in Alzheimer’s Disease: A Breathtaking Story!
Correia, S. C., & Moreira, P. I. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01148-6 · Cited by 14
Du, H., & Yan, S. S. (2010) · Pharmaceuticals · doi:10.3390/ph3061936 · Cited by 15
Alterations in Prefrontal Cortical Circuitry and Cognitive Dysfunction in Schizophrenia
Lewis, D. A., & Glausier, J. R. (2016) · Nebraska Symposium on Motivation/The Nebraska symposium on motivation · doi:10.1007/978-3-319-30596-7_3 · Cited by 15
Zhao, Y.-J., Tian, J., Sui, S.-M., Yuan, X.-D., Chen, H., Qu, C.-Q., Du, Y.-F., Guo, L., & Du, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-05168-5 · Cited by 13
Ivancic, V. A., Krasinski, C. A., Zheng, Q., Meservier, R. J., Spratt, D. E., & Lazo, N. D. (2018) · Bioscience Reports · doi:10.1042/bsr20181416 · Cited by 15
Bertan, F., Wischhof, L., Sosulina, L., Mittag, M., Dalügge, D., Fornarelli, A., Gardoni, F., Marcello, E. E., Luca, M. D., Fuhrmann, M., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00605-x · Cited by 15
Ju, T., Zhang, Y., Liu, L., Zhao, X., Li, X., Liu, C., Sun, S., & Wu, L. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01419 · Cited by 16
Self-citationMitochondrial Dysfunction in Aging: Future Therapies and Precision Medicine Approaches
Jia, L., Wei, Z., Luoqian, J., Wang, X., & Huang, C. (2025) · MedComm – Future Medicine · doi:10.1002/mef2.70026 · Cited by 14
Self-citationZhang, Y. C., Li, Z., Guan, H., Qiu, Z., & Zou, C. (2025) · Clinical and Translational Medicine · doi:10.1002/ctm2.70548 · Cited by 17
Rosenberg, N., Reva, M., Binda, F., Restivo, L., Depierre, P., Puyal, J., Briquet, M., Bernardinelli, Y., Rocher, A., Markram, H., et al. (2022) · Glia · doi:10.1002/glia.24317 · Cited by 14
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
Volloch, V., Olsen, B. R., & Rits‐Volloch, S. (2019) · Annals of Integrative Molecular Medicine · doi:10.33597/aimm.01-1005 · Cited by 15
Functional Network Profiles in ARSACS Disclosed by Aptamer-Based Proteomic Technology
Morani, F., Doccini, S., Chiorino, G., Fattori, F., Galatolo, D., Sciarrillo, E., Gemignani, F., Zuchner, S. L., Bertini, E., & Santorelli, F. M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.603774 · Cited by 14
Mitochondrial Fusion Suppresses Tau Pathology-Induced Neurodegeneration and Cognitive Decline
Wang, L., Liu, M., Gao, J., Smith, A. M., Fujioka, H., Liang, J., Perry, G. L., & Wang, X. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215175 · Cited by 15
Self-citationAyabe, T., Takahashi, C., Ohya, R., & Ano, Y. (2022) · The FASEB Journal · doi:10.1096/fj.202101366rr · Cited by 15
Volloch, V., & Rits‐Volloch, S. (2022) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-220031 · Cited by 15
Transcriptional profiles of genes related to mitochondrial aging in placental pathologies
Bartho, L. A., McKeating, D. R., Hannan, N. J., Kaitu’u‐Lino, T. J., & Perkins, A. V. (2022) · Molecular Human Reproduction · doi:10.1093/molehr/gaac026 · Cited by 14
Li, W., Wu, M., Li, Y., & Shen, J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.07.032 · Cited by 16
Yim, N., Ryu, S.-W., Han, E. C., Yoon, J. W., Choi, K. S., & Choi, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099937 · Cited by 14
The role of modulation of antioxidant enzyme systems in the treatment of neurodegenerative diseases
Obuobi, S. A. O., Karatayev, S., Chai, C. L. L., Ee, P. L. R., & Mátyus, P. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2016.1205047 · Cited by 15
Blockage of Drp1 phosphorylation at Ser579 protects neurons against Aβ1‑42‑induced degeneration
Xu, D., Yang, P. C., Yang, Z., Li, Q.-G., Ouyang, Y., Yu, T., Shangguan, J.-H., Wan, Y., Jiang, L., Qu, X.-H., et al. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12296 · Cited by 16
Cheng, D., Su, L., Wang, X., Li, X., Li, L., Hu, M., & Lu, Y. (2021) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-021-03375-2 · Cited by 14
Self-citationMonsalvo-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
Therapeutic Potential of P110 Peptide: New Insights into Treatment of Alzheimer’s Disease
Srivastava, A., Johnson, M., Renna, H. A., Sheehan, K. M., Ahmed, S., Palaia, T. A., Pinkhasov, A., Gomolin, I. H., Leon, J. D., & Reiss, A. B. (2023) · Life · doi:10.3390/life13112156 · Cited by 13
Rahman, M. A., Rahman, M. H., Rhim, H., & Kim, B. (2024) · Current Neuropharmacology · doi:10.2174/1570159x22666240426091311 · Cited by 14
Jia, W., Lin, H., Yang, M., Dai, Y.-L., Ding, Y., Xu, W.-S., Wang, S.-N., Cao, Y., Liang, S., Wang, Z., et al. (2024) · Journal of Chinese Integrative Medicine · doi:10.1016/j.joim.2024.08.002 · Cited by 14
Wei, W., Jiang, Y. Y., Hu, G., He, Y., & Chen, H. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240092 · Cited by 13
Enteropathogenic Escherichia coli regulates host-cell mitochondrial morphology
Roxas, J. L., Ramamurthy, S., Cocchi, K., Rutins, I., Harishankar, A., Agellon, A. B., Wilbur, J. S., Sylejmani, G., Vedantam, G., & Viswanathan, V. K. (2022) · Gut Microbes · doi:10.1080/19490976.2022.2143224 · Cited by 13
Gao, C., Shang, J., Sun, Z., Xia, M., Gao, D., Sun, R., Li, W., Wang, F., & Zhang, J. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03858-y · Cited by 13
Mitochondrial dynamics in neurodegeneration: from cell death to energetic states
Khacho, M., & Slack, R. S. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.2.161 · Cited by 13
Synaptic localization of the SUMOylation‐regulating protease SENP5 in the adult mouse brain
Akiyama, H., Nakadate, K., & Sakakibara, S. (2017) · The Journal of Comparative Neurology · doi:10.1002/cne.24384 · Cited by 13
Dentoni, G., Naia, L., Portal, B., Leal, N. S., Nilsson, P., Lindskog, M., & Ankarcrona, M. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220383 · Cited by 13
Volloch, V., & Rits‐Volloch, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417586 · Cited by 13
DDQ anti-aging properties expressed with improved mitophagy in mutant tau HT22 neuronal cells
Pradeepkiran, J. A., Rawat, P., Reddy, A. P., Orlov, E., & Reddy, P. H. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101843 · Cited by 12
Kadian, M., Saini, N., Khera, A., & Kumar, A. (2024) · Inflammopharmacology · doi:10.1007/s10787-023-01413-8 · Cited by 12
ER-organelle contacts: A signaling hub for neurological diseases
Wang, Y., & Yang, J. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107149 · Cited by 15
Diéguez, H. H., Romeo, H. E., Alaimo, A., Aguirre, N. A. B., Calanni, J. S., Areán, J. S. A., Álvarez, S., Sciurano, R. B., Rosenstein, R. E., & Dorfman, D. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.03.024 · Cited by 13
Cai, J., Xie, D., Kong, F., Zhai, Z., Zhu, Z., Zhao, Y., Xu, Y., & Sun, T. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231249 · Cited by 13
Park, J., Won, J., Yang, E., Seo, J., Cho, J., Seong, J. B., Yeo, H.-G., Kim, K., Kim, Y. G., Kim, M., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-66256-x · Cited by 12
Dendrimers—Novel Therapeutic Approaches for Alzheimer’s Disease
Mroziak, M., Kozłowski, G., Kołodziejczyk, W., Pszczołowska, M., Walczak, K., Beszłej, J. A., & Leszek, J. (2024) · Biomedicines · doi:10.3390/biomedicines12081899 · Cited by 12
Mitochondrial Dynamics and mRNA Translation: A Local Synaptic Tale
Zaninello, M., Baptista, P., & Duarte, F. V. (2024) · Biology · doi:10.3390/biology13090746 · Cited by 12
Das, H., Sarkar, S., Paidi, R. K., & Biswas, S. C. (2021) · The FASEB Journal · doi:10.1096/fj.202001676rr · Cited by 12
Tau phosphorylation and OPA1 proteolysis are unrelated events: Implications for Alzheimer's Disease
Alavi, M. V. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119116 · Cited by 12
Viel, C., Brandtner, A. T., Weißhaar, A., Lehto, A., Fuchs, M., & Klein, J. (2021) · Pharmaceuticals · doi:10.3390/ph14121218 · Cited by 13
Reed, A. L., Mitchell, W., Alexandrescu, A. T., & Alder, N. N. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1263420 · Cited by 13
Sadowska‐Bartosz, I., Ott, C., Grune, T., & Bartosz, G. (2014) · Free Radical Research · doi:10.3109/10715762.2014.953494 · Cited by 13
Our Tau Tales from Normal to Pathological Behavior
Alonso, A. D. C., & Cohen, L. S. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179906 · Cited by 12
Effects of Al Exposure on Mitochondrial Dynamics in Rat Hippocampus
Nie, J., Lv, S., Fu, X., & Niu, Q. L. (2019) · Neurotoxicity Research · doi:10.1007/s12640-019-00045-7 · Cited by 13
Kallianpur, K. J., Walker, M., Gerschenson, M., Shikuma, C. M., Gangcuangco, L. M. A., Kohorn, L. B., Libutti, D. E., Nir, T. M., Jahanshad, N., Thompson, P. M., et al. (2019) · AIDS Research and Human Retroviruses · doi:10.1089/aid.2019.0240 · Cited by 12
Ishikawa, K., Yamamoto, S., Hattori, S., Nishimura, N., Matsumoto, H., Miyakawa, T., & Nakada, K. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105246 · Cited by 11
Wang, Y., Pan, Y. H., Price, A. C., & Martin, L. J. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-75 · Cited by 13
MFN2 ameliorates cell apoptosis in a cellular model of Parkinson's disease induced by rotenone
Yang, Y., Xue, L., Xue, X., Ou, Z., Jiang, T., & Zhang, Y. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.6595 · Cited by 12
Acetylated tau exacerbates apoptosis by disturbing mitochondrial dynamics in HEK293 cells
Zhang, J., Fang, Z., Zhao, J., Liu, G., Shen, X., Jiang, G., & Liu, Q. R. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16053 · Cited by 11
Testosterone deficiency worsens mitochondrial dysfunction in APP/PS1 mice
Zhang, T., Chu, Y., Wang, Y., Wang, Y., Wang, J., Ji, X., Zhang, G., Shi, G., Cui, R., & Kang, Y. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1390915 · Cited by 13
Unraveling the mystery of citrate transporters in Alzheimer’s disease: An updated review
Mukherjee, A. G., Mishra, S., Gopalakrishnan, A. V., Kannampuzha, S., Murali, R., Wanjari, U. R., Stany, B. K., Vellingiri, B., Madhyastha, H., Deepankumar, K., et al. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102726 · Cited by 11
Wang, N., Pan, Y., Starling, S. C., Haskell, D. H., Quintero, A. C., Kawatani, K., Inoue, Y., Shue, F., Ma, X., Aikawa, T., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70112 · Cited by 11
Imbalanced mitochondrial dynamics in human PD and α-synuclein mouse brains
Brown, H. J., Fan, R. Z., Bell, R., Salehe, S. S., Gil, C. M., Lai, Y., & Tieu, K. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106976 · Cited by 16
Neurobiology of mitochondrial dynamics in sleep
Sarnataro, R. (2025) · The Journal of Physiology · doi:10.1113/jp288054 · Cited by 11
Fatigue and body mass index in the Fragile X premutation carrier
Summers, S. M., Cogswell, J. B., Goodrich, J. E., Mu, Y., Nguyen, D. V., Brass, S. D., & Hagerman, R. J. (2014) · Fatigue Biomedicine Health & Behavior · doi:10.1080/21641846.2014.881155 · Cited by 11
Pope, C. A., Wilkins, H., Swerdlow, R. H., & Wolfe, M. S. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210366 · Cited by 8
Zhang, M. Y., Lear, B. C., & Allada, R. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab303 · Cited by 11
Recent advances in, and challenges of, designing OMA1 drug screens
Alavi, M. V. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106063 · Cited by 12
Wang, Q., Lu, M., Zhu, X., Gu, X., Zhang, T., Xia, C., Li, Y., Xu, Y., & Zhou, M. (2022) · Aging and Disease · doi:10.14336/ad.2022.0221 · Cited by 11
Self-citationMulti-Targeting Intranasal Nanoformulation as a Therapeutic for Alzheimer’s Disease
Fihurka, O., Wang, Y., Hong, Y., Lin, X., Shen, N., Yang, H., Brown, B., Mommer, M., Zieneldien, T., Li, Y., et al. (2023) · Biomolecules · doi:10.3390/biom13020232 · Cited by 12
Zhang, L., Gan, X., Zhu, Z., Yang, Y., He, Y., & Yu, H. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.01.120 · Cited by 11
Fengshou, L., Yang, X., Cui, C., & Su, C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176183 · Cited by 11
Mitochondrial dysfunction in iPSC-derived neurons of subjects with chronic mountain sickness
Zhao, H. W., Perkins, G. A., Yao, H., Callacondo, D., Appenzeller, O., Ellisman, M. H., Spada, A. R. L., & Haddad, G. G. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00689.2017 · Cited by 11
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
Self-citationTargeted to neuronal organelles for CNS drug development
Ying, Z., Ye, N., Ma, Q., Chen, F., Li, N., & Zhen, X. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.115025 · Cited by 11
Metadata
- Authors
- Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X.
- Affiliations
- Case Western Reserve University (US)
- The University of Texas at San Antonio (US)
- Venue
- Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-07-15
- Volume
- 29
- Issue
- 28
- Pages
- 9090-9103
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2735241
- OpenAlex
- W2089141103
- Cited by
- 1,224
- References
- 50
- Citations by year
- 2026: 49 · 2025: 82 · 2024: 71 · 2023: 92 · 2022: 77 · 2021: 102 · 2020: 83 · 2019: 71 · 2018: 60 · 2017: 75 · 2016: 67 · 2015: 59 · 2014: 57 · 2013: 58 · 2012: 84
- FWCI
- 29.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association (AG031852, IIRG-07-60196)
- National Institutes of Health (IIRG-07-60196)
- National Institute on Aging (AG 031852, R01AG031852)
- 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 › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Alzheimer's disease, mitochondrial dynamics, mitochondrial fission, mitochondrial fusion, Drp1, OPA1, Mfn1, mitofusin 2, Fis1, mitochondrial distribution, axons, pyramidal neurons, synaptic loss, dendritic spines, PSD-95, mitochondrial dysfunction
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Antibodies, Monoclonal, Biotin, Cells, Cultured, Embryo, Mammalian, Gene Expression Regulation, Hippocampus, Humans, Membrane Proteins, Microtubule-Associated Proteins, Middle Aged, Mitochondria, Mutation, Neuroblastoma, Neurons, Postmortem Changes, Time Factors, Transfection, Amyloid beta-Peptides, Microscopy, Immunoelectron, Reactive Oxygen Species, GTP Phosphohydrolases, Mitochondrial Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Dynamins, Green Fluorescent Proteins, Rats, Cyclooxygenase 1
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
