Mitochondrial ubiquitin ligase alleviates Alzheimer’s disease pathology via blocking the toxic amyloid-β oligomer generation
Open accessAbstract
Mitochondrial pathophysiology is implicated in the development of Alzheimer's disease (AD). An integrative database of gene dysregulation suggests that the mitochondrial ubiquitin ligase MITOL/MARCH5, a fine-tuner of mitochondrial dynamics and functions, is downregulated in patients with AD. Here, we report that the perturbation of mitochondrial dynamics by MITOL deletion triggers mitochondrial impairments and exacerbates cognitive decline in a mouse model with AD-related Aβ pathology. Notably, MITOL deletion in the brain enhanced the seeding effect of Aβ fibrils, but not the spontaneous formation of Aβ fibrils and plaques, leading to excessive secondary generation of toxic and dispersible Aβ oligomers. Consistent with this, MITOL-deficient mice with Aβ etiology exhibited worsening cognitive decline depending on Aβ oligomers rather than Aβ plaques themselves. Our findings suggest that alteration in mitochondrial morphology might be a key factor in AD due to directing the production of Aβ form, oligomers or plaques, responsible for disease development.
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
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?
MITOL-deleted APP/PS1 mice show severe cognitive impairment, synapse alteration, and neuroinflammation mediated by excessive generation of toxic and dispersible Aβ oligomers.
“MITOL-deleted APP/PS1 mice show severe cognitive impairment, synapse alteration, and neuroinflammation mediated by excessive generation of toxic and dispersible Aβ oligomers.”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [131]
MITOL deletion triggers mitochondrial impairments and exacerbates cognitive decline in the APP/PS1 mouse model of AD.
“It is possible to affirm that MITOL deletion triggers mitochondrial impairments and exacerbates cognitive decline in APP/PS1 mouse model with AD [131].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [131]
MITOL is supposed to be downregulated in patients with AD.
“It is supposed to be downregulated in patients with AD [131,132].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [131]
MITOL is an integral mitochondrial outer membrane protein that regulates mitochondrial functions and morphology.
“MITOL is an integral mitochondrial outer membrane protein which regulates mitochondrial functions and morphology [131].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [131]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397 · see citing works
Self-citationObject recognition test in mice
Leger, M., Quiedeville, A., Bouet, V., Haelewyn, B., Boulouard, M., Schumann-Bard, P., & Freret, T. (2013) · Nature Protocols · doi:10.1038/nprot.2013.155 · Cited by 1,357 · see citing works
Garriques, L. N., Khurana, R., Coats, A. C., Frøkjær, S., Brange, J., Vyas, S. B., Uversky, V. N., & Fink, A. L. (2001) · Biochemistry · doi:10.1021/bi002555c · Cited by 1,178 · see citing works
Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066 · see citing works
Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease
Venegas, C., Kumar, S., Franklin, B. S., Dierkes, T., Brinkschulte, R., Tejera, D., Vieira-Saecker, A., Schwartz, S., Santarelli, F., Kummer, M. P., et al. (2017) · Nature · doi:10.1038/nature25158 · Cited by 983 · see citing works
Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells
Wieckowski, M. R., Giorgi, C., Lebiedzinska, M., Duszynski, J., & Pinton, P. (2009) · Nature Protocols · doi:10.1038/nprot.2009.151 · Cited by 979 · see citing works
Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 935 · 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
Yuan, P., Condello, C., Keene, C. D., Wang, Y., Bird, T. D., Paul, S. M., Luo, W., Colonna, M., Baddeley, D., & Grutzendler, J. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.003 · Cited by 817 · see citing works
Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., et al. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-18 · Cited by 773 · see citing works
Webster, S. J., Bachstetter, A. D., Nelson, P. T., Schmitt, F. A., & Van Eldik, L. J. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00088 · Cited by 755 · see citing works
Kondo, T., Asai, M., Tsukita, K., Kutoku, Y., Ohsawa, Y., Sunada, Y., Imamura, K., Egawa, N., Yahata, N., Okita, K., et al. (2013) · Cell Stem Cell · doi:10.1016/j.stem.2013.01.009 · Cited by 741 · see citing works
The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy
Sengupta, U., Nilson, A. N., & Kayed, R. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.03.035 · Cited by 740 · see citing works
Enhancing mitochondrial proteostasis reduces amyloid-β proteotoxicity
Sorrentino, V., Romani, M., Mouchiroud, L., Beck, J. S., Zhang, H., D’Amico, D., Moullan, N., Potenza, F., Schmid, A. W., Rietsch, S., et al. (2017) · Nature · doi:10.1038/nature25143 · Cited by 630 · see citing works
PlotsOfData—A web app for visualizing data together with their summaries
Postma, M., & Goedhart, J. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000202 · Cited by 554 · see citing works
Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.211 · Cited by 532 · see citing works
A new amyloid β variant favoring oligomerization in Alzheimer's‐type dementia
Tomiyama, T., Nagata, T., Shimada, H., Teraoka, R., Fukushima, A., Kanemitsu, H., Takuma, H., Kuwano, R., Imagawa, M., Ataka, S., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21321 · Cited by 414 · see citing works
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
Cohen, S. I. A., Arosio, P., Presto, J., Kurudenkandy, F. R., Biverstål, H., Dolfe, L., Dunning, C. J. R., Yang, X., Frohm, B., Vendruscolo, M., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2971 · Cited by 408 · see citing works
Presenilins Are Enriched in Endoplasmic Reticulum Membranes Associated with Mitochondria
Área-Gómez, E., de Groof, A. J. C., Boldogh, I. R., Bird, T. D., Gibson, G. E., Koehler, C. M., Yu, W. H., Duff, K., Yaffe, M. P., Pon, L. A., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090219 · Cited by 397 · see citing works
A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics
Yonashiro, R., Ishido, S., Kyo, S., Fukuda, T., Gotō, E., Matsuki, Y., Ohmura‐Hoshino, M., Sada, K., Hotta, H., Yamamura, H., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601249 · Cited by 378 · see citing works
Self-citationFerreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373 · see citing works
MITOL Regulates Endoplasmic Reticulum-Mitochondria Contacts via Mitofusin2
Sugiura, A., Nagashima, S., Tokuyama, T., Amo, T., Matsuki, Y., Ishido, S., Kudo, Y., McBride, H. M., Fukuda, T., Matsushita, N., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.023 · Cited by 303 · see citing works
Self-citationDickson, T. C., & Vickers, J. C. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00169-5 · Cited by 294 · see citing works
Potent amyloidogenicity and pathogenicity of Aβ43
Saito, T., Suemoto, T., Brouwers, N., Sleegers, K., Funamoto, S., Mihira, N., Matsuba, Y., Yamada, K., Nilsson, P., Takano, J., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2858 · Cited by 280 · see citing works
Akagi, T., Sasai, K., & Hanafusa, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834876100 · Cited by 259 · see citing works
APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease
Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 259 · see citing works
Baek, S. H., Park, S. J., Jeong, J. I., Kim, S. H., Han, J., Kyung, J. W., Baik, S.-H., Choi, Y., Choi, B. Y., Park, J. S., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2385-16.2017 · Cited by 258 · see citing works
Massaad, C. A., Washington, T. M., Pautler, R. G., & Klann, E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902714106 · Cited by 223 · see citing works
Kumar, S., Rezaei‐Ghaleh, N., Terwel, D., Thal, D. R., Richard, M., Hoch, M., Donald, J. M. M., Wüllner, U., Glebov, K., Heneka, M. T., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.138 · Cited by 220 · see citing works
Moreno‐González, I., Edwards, G. A., Salvadores, N., Shahnawaz, M., Díaz‐Espinoza, R., & Soto, C. A. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.230 · Cited by 210 · see citing works
Fukui, H., Diaz, F., Garcia, S., & Moraes, C. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705738104 · Cited by 185 · see citing works
Bussière, T., Bard, F., Barbour, R., Grajeda, H., Guido, T., Khan, K., Schenk, D., Games, D., Seubert, P. A., & Buttini, M. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63360-3 · Cited by 169 · see citing works
Amyloid-β-Induced Mitochondrial Dysfunction
Chen, J. X., & Yan, S. D. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12208 · Cited by 167 · see citing works
Upadhaya, A. R., Kosterin, I., Kumar, S., Arnim, C. A. F. V., Yamaguchi, H., Fändrich, M., Walter, J., & Thal, D. R. (2014) · Brain · doi:10.1093/brain/awt362 · Cited by 165 · see citing works
The mitochondrial ubiquitin ligase MARCH5 resolves MAVS aggregates during antiviral signalling
Yoo, Y., Park, Y., Kim, J., Cho, H., Kim, S., Lee, H., Kim, T.-H., Kim, Y. S., Lee, Y., Chul-Joong, K., et al. (2015) · Nature Communications · doi:10.1038/ncomms8910 · Cited by 161 · see citing works
Drew, B., & Leeuwenburgh, C. (2003) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00264.2003 · Cited by 161 · see citing works
Jeong, J. S., Ansaloni, A., Mezzenga, R., Lashuel, H. A., & Dietler, G. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.02.005 · Cited by 152 · see citing works
Xu, S., Cherok, E., Das, S., Li, S., Roelofs, B. A., Ge, S. X., Polster, B. M., Boyman, L., Lederer, W. J., Wang, C., et al. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-09-0678 · Cited by 146 · see citing works
Joshi, A. U., Saw, N. L., Shamloo, M., & Mochly‐Rosen, D. (2017) · Oncotarget · doi:10.18632/oncotarget.23640 · Cited by 146 · see citing works
Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration
Liu, P., Reed, M. N., Kotilinek, L., Grant, M. K. O., Forster, C. L., Qiang, W., Shapiro, S. L., Reichl, J. H., Chiang, A. C. A., Jankowsky, J. L., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.05.021 · Cited by 143 · see citing works
Rifampicin is a candidate preventive medicine against amyloid-β and tau oligomers
Umeda, T., Ono, K., Sakai, A., Yamashita, M., Mizuguchi, M., Klein, W. L., Yamada, M., Mori, H., & Tomiyama, T. (2016) · Brain · doi:10.1093/brain/aww042 · Cited by 124 · see citing works
MITOL prevents ER stress‐induced apoptosis by IRE1α ubiquitylation at ER–mitochondria contact sites
Takeda, K., Nagashima, S., Shiiba, I., Uda, A., Tokuyama, T., Ito, N., Fukuda, T., Matsushita, N., Ishido, S., Iwawaki, T., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018100999 · Cited by 123 · see citing works
Self-citationDorsal telencephalon‐specific expression of Cre recombinase in PAC transgenic mice
Iwasato, T., Nomura, R., Ando, R., Ikeda, T., Tanaka, M., & Itohara, S. (2004) · genesis · doi:10.1002/gene.20009 · Cited by 116 · see citing works
ADDLs and the signaling web that leads to Alzheimer’s disease
Krafft, G. A., & Klein, W. L. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.07.012 · Cited by 111 · see citing works
Mitochondrial Dynamics in Alzheimerʼs Disease
Bonda, D., Wang, X., Perry, G. L., Smith, M. A., & Zhu, X. (2010) · Drugs & Aging · doi:10.2165/11532140-000000000-00000 · Cited by 106 · see citing works
Kukreja, L., Kujoth, G. C., Prolla, T. A., LEUVEN, F. V., & Vassar, R. J. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-16 · Cited by 86 · see citing works
Prangkio, P., Yusko, E. C., Sept, D., Yang, J., & Mayer, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047261 · Cited by 86 · see citing works
Oka, S., Leon, J., Sakumi, K., Ide, T., Kang, D., LaFerla, F. M., & Nakabeppu, Y. (2016) · Scientific Reports · doi:10.1038/srep37889 · Cited by 78 · see citing works
Presenilin-1 is located in rat mitochondria
Ankarcrona, M., & Hultenby, K. R. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00735-0 · Cited by 63 · see citing works
Murakami, K. (2014) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.940275 · Cited by 52 · see citing works
Isolation and Biochemical Characterization of Amyloid Plaques and Paired Helical Filaments
Rostagno, A. A., & Ghiso, J. A. (2009) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0333s44 · Cited by 44 · see citing works
AlzBase: An Integrative Database for Gene Dysregulation in Alzheimer’s Disease
Bai, Z., Han, G., Xie, B., Wang, J., Song, F., Peng, X., & Lei, H. (2016) · Molecular Neurobiology · doi:10.1007/s12035-014-9011-3 · Cited by 44 · see citing works
Intranasal rifampicin for Alzheimer's disease prevention
Umeda, T., Tanaka, A., Sakai, A., Yamamoto, A., Sakane, T., & Tomiyama, T. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.012 · Cited by 40 · see citing works
Xu, F., Fu, Z., Dass, S., Kotarba, A. E., Davis, J., Smith, S. O., & Nostrand, W. E. V. (2016) · Nature Communications · doi:10.1038/ncomms13527 · Cited by 35 · see citing works
Izuo, N., Kume, T., Sato, M., Murakami, K., Irie, K., Izumi, Y., & Akaike, A. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300033k · Cited by 34 · see citing works
Nagashima, S., Takeda, K., Ohno, N., Ishido, S., Aoki, M., Saitoh, Y., Takada, T., Tokuyama, T., Sugiura, A., Fukuda, T., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900308 · Cited by 34 · see citing works
Self-citationDesign of Metastable β-Sheet Oligomers from Natively Unstructured Peptide
Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Sengupta, U., White, M. A., & Kayed, R. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn4001395 · Cited by 18 · see citing works
Acquired expression of mutant Mitofusin 2 causes progressive neurodegeneration and abnormal behavior
Ishikawa, K., Yamamoto, S., Hattori, S., Nishimura, N., Mito, T., Matsumoto, H., Miyakawa, T., & Nakada, K. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.2139-18.2018 · Cited by 14 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Buccellato, F. R., D’Anca, M., Fenoglio, C., Scarpini, E., & Galimberti, D. (2021) · Antioxidants · doi:10.3390/antiox10091353 · Cited by 179 · see citing works
Disentangling Mitochondria in Alzheimer’s Disease
Johri, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111520 · Cited by 96 · see citing works
Oxidative stress–mediated neuroinflammation in Alzheimer’s disease
Firdous, S. M., Khan, S. A., & Maity, A. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03188-3 · Cited by 85 · see citing works
Amyloid Cascade Hypothesis for the Treatment of Alzheimer’s Disease: Progress and Challenges
Wu, T., Ding, L., Cheng, Y., Jiang, S., Riaz, M. W., Fu, N., Mou, C., Ye, M., & Zheng, Y. (2022) · Aging and Disease · doi:10.14336/ad.2022.0412 · Cited by 75 · see citing works
New Insights into Mitochondria in Health and Diseases
Li, Y., Zhang, H., Yu, C., Dong, X., Yang, F., Wang, M., Wen, Z., Su, M., Li, B., & Yang, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189975 · Cited by 46 · see citing works
Park, Y., Dodantenna, N., Kim, Y., Kim, T., Lee, H., Yoo, Y., Heo, J., Lee, J. H., Kwon, M., Kang, H. C., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2023113481 · Cited by 44 · see citing works
Hinge, N. S., Kathuria, H., & Pandey, M. M. (2021) · Applied Materials Today · doi:10.1016/j.apmt.2021.101303 · Cited by 25 · see citing works
Mitochondrial defects: An emerging theranostic avenue towards Alzheimer's associated dysregulations
Mani, S., Swargiary, G., Singh, M., Agarwal, S., Dey, A., Ojha, S. K., & Jha, N. K. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119985 · Cited by 23 · see citing works
Jia, K., Tian, J., Wang, T., Guo, L., Xuan, Z., Swerdlow, R. H., & Du, H. (2023) · JCI Insight · doi:10.1172/jci.insight.174290 · Cited by 19 · see citing works
Development of a Mitochondrial Targeting Lipid Nanoparticle Encapsulating Berberine
Hori, I., Harashima, H., & Yamada, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020903 · Cited by 17 · see citing works
Ali, S. A., Chung, K. H. K., Forgham, H., Olsen, W. P., Käkinen, A., Balaji, A., Otzen, D. E., Davis, T. P., & Javed, I. (2023) · Advanced Science · doi:10.1002/advs.202301423 · Cited by 16 · see citing works
Tsumagari, K., Sato, Y., Shimozawa, A., Aoyagi, H., Okano, H., & Kuromitsu, J. (2022) · iScience · doi:10.1016/j.isci.2022.104832 · Cited by 15 · see citing works
Review of FUNDC1-mediated mitochondrial autophagy in Alzheimer’s disease
Shi, D., Guo, X., Ning, Z., Zhang, Y., Liu, F., Liu, M., & Wei, Y. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1544241 · Cited by 15 · see citing works
Targeting the molecular web of Alzheimer’s disease: unveiling pathways for effective pharmacotherapy
Jadhav, D., Saraswat, N., Vyawahare, N. S., & Shirode, D. S. (2024) · The Egyptian Journal of Neurology Psychiatry and Neurosurgery · doi:10.1186/s41983-023-00775-8 · Cited by 14 · see citing works
Dai, D., Xie, J., Zheng, Y., Chen, F., Zhao, B., & Li, M. (2023) · Cytotechnology · doi:10.1007/s10616-023-00589-9 · Cited by 11 · see citing works
Gamal, N., Bakly, W. M. S. E., Saad, S. S. T., El-Waseef, D. A. E.-D. A., El‐Shal, A. S., Morsy, W. E., & Magdy, Y. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04136-5 · Cited by 10 · see citing works
Ubiquitin-mediated mitochondrial regulation by MITOL/MARCHF5 at a glance
Nagashima, S., Ito, N., Shiiba, I., Shimura, H., & Yanagi, S. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvac092 · Cited by 10 · see citing works
Self-citationHeo, J., Park, Y., Kim, Y., Lee, H., Kim, J., Kwon, S., Kang, M., Rhee, H., Sun, W., Lee, J., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06315-9 · Cited by 7 · see citing works
March5-mediated Trim28 degradation preserves islet β-cell function in mice
Chen, Y.-S., Pang, W., Ma, G., Yan, Y.-C., Xiao, Z., Chen, Y., Ding, Z., Chen, L.-T., Hou, X., & Cao, H.-L. (2025) · Nature Communications · doi:10.1038/s41467-025-62587-z · Cited by 4 · see citing works
Identification of highest neurotoxic amyloid-β plaque type showing reduced contact with astrocytes
Mitsubori, M., Takeda, K., Nagashima, S., Ishido, S., Matsuoka, M., Inatome, R., & Yanagi, S. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.02.081 · Cited by 6 · see citing works
Self-citationFirdous, S. M., Chakrabortty, S., Undale, V., Mallik, S., & Gouda, M. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02169-7 · Cited by 6 · see citing works
Wang, S., Zhang, J., Zhang, H., Yang, Y., & Wen, Y. (2024) · Cellular and Molecular Biology · doi:10.14715/cmb/2024.70.6.18 · Cited by 4 · see citing works
Ohara, T., Taki, Y., & Yamamoto, S. (2026) · Brain Sciences · doi:10.3390/brainsci16020242 · Cited by 3 · see citing works
Natural products regulate mitochondrial function in cognitive dysfunction—A scoping review
Tuo, J., Peng, Y., Linghu, Y., Ming, T., Huang, S., & Xu, Z. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1091879 · Cited by 2 · see citing works
MARCH5-dependent NLRP3 ubiquitination is an essential step for NEK7 docking on the mitochondriaPreprint
Park, Y., Dodantenna, N., Kim, T., Lee, H., Yoo, Y., Lee, E., Lee, J. H., Kwon, M., Kang, H. C., Lee, J.-S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.12.523764 · Cited by 2 · see citing works
Sato, M., Tanabu, D., Torigoe, D., Kadomatsu, T., Taniwaka, K., Ogata, Y., Shiiba, I., Suzuki, Y., Ito, N., Inatome, R., et al. (2026) · npj Aging · doi:10.1038/s41514-026-00366-w · Cited by 1 · see citing works
Self-citationE3 ubiquitin ligases in neurodegenerative diseases
Hou, D. L., Ho, J., Guan, T., Dong, X.-X., Zeng, L., Sanders, L. H., Wu, Y., Tan, E., & Zhou, Z. D. (2026) · Military Medical Research · doi:10.1016/j.mmr.2026.100032 · Cited by 1 · see citing works
Novel Strategy for Alzheimer’s Disease Treatment through Oral Vaccine Therapy with Amyloid Beta
Matsuzaka, Y., & Yashiro, R. (2023) · Biologics · doi:10.3390/biologics3010003 · Cited by 1 · see citing works
Determining the Stoichiometry of Amyloid Oligomers by Single-Molecule Photobleaching
Dey, A., & Maiti, S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2529-3_5
Ma, M., Yang, J., Yang, Y., & Li, L. (2026) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2026.1762088
Çakır, Z., Bilkan, Ç., Ertekin, B., & Bilkan, M. T. (2026) · Online Türk Sağlık Bilimleri Dergisi · doi:10.26453/otjhs.1753751
Mechanisms and Therapeutic Potential of Targeting Mitophagy in Neurodegenerative Diseases
Wang, Y.-N., Wang, X., Huang, Q., Yang, Y., Wang, T., Qu, X.-H., & Han, X. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06104-3
- Authors
- Takeda, K., Uda, A., Mitsubori, M., Nagashima, S., Iwasaki, H., Ito, N., Shiiba, I., Ishido, S., Matsuoka, M., Inatome, R., & Yanagi, S.
- Affiliations
- University of Padua (IT)
- Tokyo University of Pharmacy and Life Sciences (JP)
- Hyogo Medical University (JP)
- Tokyo Medical University (JP)
- Corresponding author
- Yanagi, Shigeru
- ORCID
- Venue
- Communications Biology
- Published
- 2021-02-12
- Volume
- 4
- Issue
- 1
- Pages
- 192-192
- ISSN
- 2399-3642 (ISSN-L)
- PMC
- PMC7881000
- OpenAlex
- W3127288553
- Cited by
- 32
- References
- 61
- Citations by year
- 2026: 7 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 4 · 2021: 5
- FWCI
- 3.46
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Communications Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- MEXT | Japan Society for the Promotion of Science (18H04869, 20H04911)
- Ministry of Education, Culture, Sports, Science and Technology (S1411014)
- Japan Agency for Medical Research and Development (17gm5010002, 18gm5010002, 19gm5010002 and 20gm5010002)
- Uehara Memorial Foundation (N/A)
- Naito Foundation (N/A)
- Takeda Medical Research Foundation (N/A)
- Sumitomo Foundation (N/A)
- Cosmetology Research Foundation (N/A)
- Ono Medical Research Foundation (N/A)
- Tokyo Biochemical Research Foundation (N/A)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, MARCH5, mitochondrial dynamics, amyloid-beta oligomers, amyloid-beta fibrils, amyloid plaques, cognitive decline, mitochondrial morphology, gene expression dysregulation
- MeSH terms
- Alzheimer Disease, Animals, Behavior, Animal, Blood Proteins, Brain, Cognition, Disease Models, Animal, Humans, Membrane Proteins, Mitochondria, Amyloid beta-Peptides, Mice, Knockout, Mitochondrial Proteins, Poly(A)-Binding Proteins, Ubiquitin-Protein Ligases, Cell Line, Tumor, Mice, Presenilin-1, Plaque, Amyloid, Protein Aggregation, Pathological, Protein Aggregates
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
