Cited by 388Mitochondrial Function and PathologyParkinson's Disease Mechanisms and TreatmentsAlzheimer's disease research and treatments

The DOI matches its Crossref record; 309 of the 309 references it cites were found in a registry or an index.

The Role of Mitochondria in Neurodegenerative Diseases: the Lesson from Alzheimer’s Disease and Parkinson’s Disease

Open access

Monzio Compagnoni, Giacomo, Di Fonzo, Alessio, Corti, Stefania, Comi, Giacomo P., Bresolin, Nereo, Masliah, Eliezer·2020·Molecular Neurobiology

DOI 10.1007/s12035-020-01926-1PMC PMC9047992

Open this paper in CoChat — free account

Abstract

Although the pathogenesis of neurodegenerative diseases is still widely unclear, various mechanisms have been proposed and several pieces of evidence are supportive for an important role of mitochondrial dysfunction. The present review provides a comprehensive and up-to-date overview about the role of mitochondria in the two most common neurodegenerative disorders: Alzheimer's disease (AD) and Parkinson's disease (PD). Mitochondrial involvement in AD is supported by clinical features like reduced glucose and oxygen brain metabolism and by numerous microscopic and molecular findings, including altered mitochondrial morphology, impaired respiratory chain function, and altered mitochondrial DNA. Furthermore, amyloid pathology and mitochondrial dysfunction seem to be bi-directionally correlated. Mitochondria have an even more remarkable role in PD. Several hints show that respiratory chain activity, in particular complex I, is impaired in the disease. Mitochondrial DNA alterations, involving deletions, point mutations, depletion, and altered maintenance, have been described. Mutations in genes directly implicated in mitochondrial functioning (like Parkin and PINK1) are responsible for rare genetic forms of the disease. A close connection between alpha-synuclein accumulation and mitochondrial dysfunction has been observed. Finally, mitochondria are involved also in atypical parkinsonisms, in particular multiple system atrophy. The available knowledge is still not sufficient to clearly state whether mitochondrial dysfunction plays a primary role in the very initial stages of these diseases or is secondary to other phenomena. However, the presented data strongly support the hypothesis that whatever the initial cause of neurodegeneration is, mitochondrial impairment has a critical role in maintaining and fostering the neurodegenerative process.

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

Crossref · 10.1007/s12035-020-01926-1

Cites

309 of 309 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson’s Disease
Bender, A., Desplats, P., Spencer, B. J., Rockenstein, E. M., Adame, A., Elstner, M., Laub, C., Mueller, S. K., Koob, A. O., Mante, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062277 · Cited by 151
Self-citation
Retracted
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Aging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567
α-Synuclein in Lewy bodies
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Parkinson's Disease
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
Parkinson disease
Poewe, W., Seppi, K., Tanner, C. M., Halliday, G. M., Brundin, P., Volkmann, J., Schrag, A.-E., & Lang, A. E. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.13 · Cited by 5,415
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227

Show all 309 references

Sorted by citations

Items 201–300 of 388

Minocycline protects against neuronal mitochondrial dysfunction and cognition impairment
Motaghinejad, M., Motevalian, M., Ulloa, L., Kaviani, N., & Hamurtekin, E. (2023) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2023-008 · Cited by 8
Near-Infrared BODIPY Photosensitizer for Modulating Mitochondrial Fusion Proteins and Inhibiting Choroidal Neovascularization
Li, Y., Liu, S.-B., Ni, W., Gurzadyan, G. G., Wu, Y., Wang, J., Kuang, G., & Jiang, W. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c11053 · Cited by 8
TMT-based quantitative proteomics analysis of neuroprotective effects of Forsythoside A on the MPTP-induced Parkinson's disease mouse model
Niu, B., Zhao, M., Gao, X., Xu, J., & Yu, L. (2023) · Experimental Neurology · doi:10.1016/j.expneurol.2023.114642 · Cited by 8
Aluminum, a colorful gamechanger: Uptake of an aluminum-containing food color in human cells and its implications for human health
Ganhör, C., Rezk, M., Doppler, C., Ruthmeier, T., Wechselberger, C., Müller, M., Kotnik, M., Puh, Š., Meßner, B., & Bernhard, D. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.138404 · Cited by 8
Therapeutic potential of Coumarin-polyphenolic acid hybrids in PD: Inhibition of α-Syn aggregation and disaggregation of preformed fibrils, leading to reduced neuronal inclusion formation
Wang, Z., Zhang, W., Xing, L.-Z., Zhao, Y., Xu, J. P., & Zhang, Y. (2024) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2024.129618 · Cited by 8
Synapses drive local mitochondrial ATP synthesis to fuel plasticityPreprint
Ghosh, I., Fan, R., Shah, M., Bapat, O., & Rangaraju, V. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.09.648032 · Cited by 8
Mitochondrial complex I inhibition enhances astrocyte responsiveness to pro-inflammatory stimuli
Wischhof, L., Mathew, A. J., Bonaguro, L., Beyer, M., Ehninger, D., Nicotera, P., & Bano, D. (2024) · Scientific Reports · doi:10.1038/s41598-024-78434-y · Cited by 7
Emerging perspectives in proteostasis: bridging mechanisms and therapeutics for human diseases
Borlepawar, A., Neu, M., Ma, Z., Deshpande, A., Bühringer, H., Hajieva, P., Frey, N., & Rangrez, A. Y. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02714-4 · Cited by 7
Mitostasis in age-associated neurodegeneration
Panda, M., Markaki, M., & Tavernarakis, N. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167547 · Cited by 7
Therapeutic potential of melatonin-induced mitophagy in the pathogenesis of Alzheimer’s disease
Goleij, P., Tabari, M. A. K., Poudineh, M., Sanaye, P. M., Khan, H. Z., Kumar, A. P., Larsen, D. S., & Daglia, M. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01859-y · Cited by 7
Neuroglobin effectively halts vision loss in Harlequin mice at an advanced stage of optic nerve degeneration
Cwerman‐Thibault, H., Lechauve, C., Malko-Baverel, V., Augustin, S., Guilloux, G. L., Reboussin, É., Dégardin, J., Simonutti, M., Debeir, T., & Corral‐Debrinski, M. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105483 · Cited by 7
Hydrogen Ion Dynamics as the Fundamental Link between Neurodegenerative Diseases and Cancer: Its Application to the Therapeutics of Neurodegenerative Diseases with Special Emphasis on Multiple Sclerosis
Harguindey, S., Alfarouk, K. O., Orozco, J. D. P., Reshkin, S. J., & Devesa, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052454 · Cited by 7
GUCY2C signaling limits dopaminergic neuron vulnerability to toxic insults
Cheslow, L., Byrne, M. D., Kopenhaver, J. S., Iacovitti, L., Smeyne, R. J., Snook, A. E., & Waldman, S. A. (2024) · npj Parkinson s Disease · doi:10.1038/s41531-024-00697-z · Cited by 7
Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins
Venati, S. R., & Uversky, V. N. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158399 · Cited by 6
UQCRC1 is a Key Pathogenic Determinant and Potential Therapeutic Target for Cognitive Impairment in Alzheimer’s Disease
Zhang, J., Wu, Z., Long, Z., Feng, C., Bai, F., & Li, H. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05171-2 · Cited by 6
Remimazolam alleviates hippocampal neuronal injury in an in vitro Alzheimer’s disease model by promoting PINK1/Parkin-mediated mitophagy
Zhang, W., Shi, B., Xie, Y., Li, Y., Yang, J., & Zhao, K. (2025) · European journal of medical research · doi:10.1186/s40001-025-03179-x · Cited by 6
Introduction to Neurodegenerative Diseases
Seyedebrahimi, R., Yang, P., Azimzadeh, M., Farsani, M. E., Ababzadeh, S., Kalhor, N., & Sheykhhasan, M. (2024) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/979-8-3693-1281-0.ch002 · Cited by 6
Bambusa vulgaris attenuates Haloperidol-induced motor deficit and non-Motor co-morbidity in rats through up-regulation of Dopamine transmission and mitigation of pro-inflammatory cytokines activities
Murtala, A. A., Oyinloye, O. E., Oladoja, F. A., Adetutu, K. O., Olashore, A. H. S., Ogunjimi, L., Aderionla, A. A., Olooto, W. E., Soyinka, O. O., Fageyinbo, M. S., et al. (2024) · Pharmacological Research - Modern Chinese Medicine · doi:10.1016/j.prmcm.2024.100375 · Cited by 6
Pathological correlates of cognitive decline in Parkinson’s disease: from molecules to neural networks
Новиков, Н. Ю., Brazhnik, E. S., & Кичигина, В. Ф. (2023) · Biochemistry (Moscow) · doi:10.31857/s0320972523110180 · Cited by 6
Association between Physical Activity and Parkinson’s Disease: A Prospective Cohort Study
Zhang, Q., Shi, M., Zhang, J., Yin, X., Chen, Y., Wang, X., & Zhang, Y. (2024) · Neuroepidemiology · doi:10.1159/000540397 · Cited by 6
Preventing excessive autophagy protects from the pathology of mtDNA mutations in Drosophila melanogaster
Fissi, N. E., Rosenberger, F. A., Chang, K., Wilhalm, A., Barton-Owen, T., Hansen, F. M., Golder, Z. J., Alsina, D., Wedell, A., Mann, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-55559-2 · Cited by 6
Bioinformatics insights into mitochondrial and immune gene regulation in Alzheimer's disease
Tian, M., Zhang, Y., Yuan, Y., Li, H., & He, Y. (2025) · European journal of medical research · doi:10.1186/s40001-025-02297-w · Cited by 7
Could the inhibition of systemic NLRP3 inflammasome mediate central redox effects of yerba mate? An in silico and pre-clinical translational approach
dos Santos, J. M., Touguinha, L. B. A., Bridi, R., Andreazza, A. C., Bick, D. L. U., Davidson, C. B., dos Santos, A. F., Machado, K. A., Scariot, F. J., Delamare, L. A. P., et al. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.119518 · Cited by 6
Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal Dynamics
Verzini, S., Shah, M., Theillet, F., Belsom, A., Bieschke, J., Wanker, E. E., Rappsilber, J., Binolfi, A., & Selenko, P. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.10.023 · Cited by 6
Metabolism-Based Gene Differences in Neurons Expressing Hyperphosphorylated AT8− Positive (AT8+) Tau in Alzheimer’s Disease
York, A., Everhart, A. L., Vitek, M. P., Gottschalk, W. K., & Colton, C. A. (2021) · ASN NEURO · doi:10.1177/17590914211019443 · Cited by 6
Tracking mitochondrial Cu(I) fluctuations through a ratiometric fluorescent probe in AD model cells: Towards understanding how AβOs induce mitochondrial Cu(I) dyshomeostasis
Zhao, Q., Ma, L., Chen, S., Huang, L., She, G., Sun, Y., Shi, W., & Mu, L. (2024) · Talanta · doi:10.1016/j.talanta.2024.125716 · Cited by 6
Mitochondrial DNA copy number associated dementia risk by somatic mutations and frailty
Tian, Q., Zweibaum, D. A., Qian, Y., Oppong, R., Pilling, L. C., Casanova, F., Atkins, J. L., Melzer, D. R., Ding, J., & Ferrucci, L. (2024) · GeroScience · doi:10.1007/s11357-024-01355-1 · Cited by 6
Predicting Which Mitophagy Proteins Are Dysregulated in Spinocerebellar Ataxia Type 3 (SCA3) Using the Auto-p2docking Pipeline
Vieira, J., Barros, M., López-Fernández, H., Glez‐Peña, D., Nogueira-Rodríguez, A., & Vieira, C. P. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031325 · Cited by 5
Plant-Derived Exosome-Like Nanoparticles in Neurodegenerative Diseases: From Dual Bioactive-Delivery Roles to Translational Challenges
Sun, Y., Xu, Z., Cui, L., Guo, J., Zhang, X., & Xiao, Y. (2026) · International Journal of Nanomedicine · doi:10.2147/ijn.s608292 · Cited by 5
A chiral electrochemiluminescence sensor based on isoquinoline complex for the detection of cysteine enantiomers
Duan, Q., Liu, B., Sui, M., Wei, M., & Liu, P. (2025) · Materials Letters · doi:10.1016/j.matlet.2025.138491 · Cited by 5
Fucoxanthinol Mitigates the Cytotoxic Effect of Chlorpyrifos and MPTP on the Dopaminergic Differentiation of SH-SY5Y Human Neuroblastoma Cells
Elmorsy, E. M., Al-Ghafari, A. B., Doghaither, H. A. A., Elghareeb, M. M., & Alsaqati, M. (2025) · Journal of Molecular Neuroscience · doi:10.1007/s12031-025-02342-7 · Cited by 5
Mitochondrial thermogenesis in cancer cells
Zhang, X., & Hu, Y. (2023) · ONCOLOGIE · doi:10.1515/oncologie-2023-0298 · Cited by 5
An Integrated Computational Approaches for Designing of Potential Piperidine based Inhibitors of Alzheimer Disease by Targeting Cholinesterase and Monoamine Oxidases Isoenzymes
Sarfraz, M., Ibrahim, M. K., Ejaz, S. A., Attaullah, H. M., Aziz, M., Arafat, M., Shamim, T., Elhadi, M., Ruby, T., & Mahmood, H. K. (2024) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-023-04815-0 · Cited by 5
Unbiased complexome profiling and global proteomics analysis reveals mitochondrial impairment and potential changes at the intercalated disk in presymptomatic R14Δ/+ mice hearts
Foo, B., Amedei, H., Kaur, S., Jaawan, S., Boshnakovska, A., Gall, T., de Boer, R. A., Silljé, H. H. W., Urlaub, H., Rehling, P., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0311203 · Cited by 8
The critical role of mitochondrial dysfunction in ADT-induced neurotoxicity
Lin, Y., Lin, K.-J., & Shao, I. (2025) · Prostate Cancer and Prostatic Diseases · doi:10.1038/s41391-025-00958-9 · Cited by 5
The active metabolite of Epimedii Folium promotes hippocampal neurogenesis in APP/PS1 mice by alleviating mitochondrial dysfunction
Bai, J.-M., Li, T., Di, X., Yang, J.-X., Cui, Z.-Q., Min, D.-Y., Shen, Y.-F., Shan, S.-Y., Zhang, Y.-X., Shi, Y.-J., et al. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1546256 · Cited by 5
Design and Synthesis of a Mitochondrial‐Targeted JNK Inhibitor and Its Protective Effect on Parkinson's Disease Phenotypes
Zhou, Z., Zhang, D., Du, F., An, W., Ge, J., Yu, C., Yang, N., Zhang, C., Lim, K., & Li, L. (2023) · ChemBioChem · doi:10.1002/cbic.202200748 · Cited by 5
Mitochondrial DNA and Alzheimer’s disease: a first case–control study of the Tunisian population
Salem, N. B., Boussetta, S., de Rojas, I., Moreno–Grau, S., Montrreal, L., Mokni, N., Mahmoud, I., Younes, S., Daouassi, N., Frih-Ayed, M., et al. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06978-7 · Cited by 5
The Role of Autophagy in the Development of Pathological Conditions of the Body
Kench, U. S., Sologova, S. S., Prasolov, V. S., & Spirin, P. (2023) · Acta Naturae · doi:10.32607/actanaturae.23838 · Cited by 4
Astragaloside IV reduces mutant Ataxin-3 levels and supports mitochondrial function in Spinocerebellar Ataxia Type 3
Lin, Y.-S., Cheng, W., Chang, J., Wu, Y., Hsieh, M., & Liu, C. (2024) · Scientific Reports · doi:10.1038/s41598-024-77763-2 · Cited by 4
Rlip76 in ageing and Alzheimer’s disease: Focus on oxidative stress and mitochondrial mechanisms
Bandaru, M., Sultana, O. F., Islam, M. A., Alvir, R. V., & Reddy, P. H. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102600 · Cited by 4
Inhibition of SIRT1/PGC-1α Axis Exacerbates Fluorine and Aluminium Induced Neurotoxicity via Drp1-dependent Aggravated Mitochondrial Fission
Liu, Y., Qian, X., Jiang, H., & Xie, C. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05400-8 · Cited by 4
Low Intensity Ultrasound-facilitated exosome delivery promotes hippocampal neurogenesis in Alzheimer's disease
Yan, Y., Su, J., Xie, M., Kong, Y., Wang, C., Yuan, G., Fang, Y., Hwang, K., Kim, C., Han, H. S., et al. (2025) · Brain stimulation · doi:10.1016/j.brs.2025.103015 · Cited by 6
Network pharmacology-based identification of potential drug targets and bioactive compounds in Lycii Fructus (Gouqizi) for the therapeutics of Parkinson’s disease
Hashmi, S. A., Tahir, R. A., & Sehgal, S. A. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1714071 · Cited by 4
Transcriptomic Evidence of Mitochondrial Double‐Stranded RNA Accumulation in Brain Aging and Alzheimer's Disease
Doser, R. L., & LaRocca, T. J. (2026) · Aging Cell · doi:10.1111/acel.70616 · Cited by 5
Epigenetic Orchestration of Neurodegenerative Disorders: A Possible Target for Curcumin as a Therapeutic
Tripathi, S., & Bhawana, B. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04167-z · Cited by 4
Emerging perspectives on precision therapy for Parkinson’s disease: multidimensional evidence leading to a new breakthrough in personalized medicine
Wang, Q.-L., Gu, X., Yang, L., Jiang, Y., Zhang, J., & He, J. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1417515 · Cited by 4
Exploring dose and downregulation dynamics in lipid nanoparticles based siRNA therapy: Systematic review and meta-analysis
Kumar, A., Ahmed, B., Kaur, I. P., & Saha, L. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133984 · Cited by 5
Genet identity and season drive gene expression in outplanted Acropora palmata at different reef sites
Young, B. D., Williams, D. E., Bright, A. J., Peterson, A., Traylor‐Knowles, N., & Rosales, S. (2024) · Scientific Reports · doi:10.1038/s41598-024-80479-y · Cited by 4
The protective effects of Araucaria angustifolia (Bertol.) on neurodegeneration induced by LPS and kynurenine exposure in BV-2 microglial cells
Visentin, A. P. V., dos Santos, J. M., Pereira, A., Scariot, F. J., Ramos, A. P., Touguinha, L. B. A., Machado, A. K., Salvador, M. M., & Branco, C. S. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10637-6 · Cited by 4
Editorial: Mitochondrial and lysosomal dysfunction in neurodegenerative diseases: Molecular mechanisms and therapeutic strategies
Chen, X., Xiao, Y., Xiaolei, Z., Wenjie, Y., Pu, J., & Zhong, P. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1029440 · Cited by 4
A mitochondria targeted nitroreductase-sensitive self-immolative spacer as an efficient shuttle for uncharged amine-based molecules
Michel, L., Steinmetz, V., Godel-Pastre, S., Durand, P., & Chevalier, A. (2025) · Chemical Science · doi:10.1039/d5sc03665h · Cited by 3
The Citric Acid Cycle Modulates Neurologic Health and Is a Therapeutic Target of Dietary and Genetic Modification in Metabolic Disease
Fogle, K. J., Lindley, S., Satterfield, S. L., Amsalu, B. A., Figura, J. R., Eicher, S. L., Scherz, L. A., & Palladino, M. J. (2026) · Genes · doi:10.3390/genes17020192 · Cited by 3
Sercocephalous latifolius fruit attenuates aluminum chloride-induced oxidative stress and neurotoxicity in Drosophila melanogaster via Drn1 regulation of the IMD signaling pathway
Saliu, J. A., Olajuyin, A. M., & Monday, O. O. (2024) · Pharmacological Research - Modern Chinese Medicine · doi:10.1016/j.prmcm.2024.100437 · Cited by 3
An Overview of the Natural Neuroprotective Agents for the Management of Cognitive Impairment Induced by Scopolamine in Zebrafish (Danio rerio)
Abidar, S., Hriţcu, L., & Nhiri, M. (2024) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273309256240702053609 · Cited by 3
The Mitochondrial Transplantation: A New Frontier in Plastic Surgery
Li, H., & Mu, D. (2024) · Journal of Craniofacial Surgery · doi:10.1097/scs.0000000000010706 · Cited by 3
The Alteration of Proteomic Profiles in Hippocampus of Type 2 Diabetic Mice Associated With Cognitive Impairment
Janthakhin, Y., Juntapremjit, S., Hummel, K., Razzazi‐Fazeli, E., & Kingtong, S. (2024) · Bioinformatics and Biology Insights · doi:10.1177/11779322241306290 · Cited by 3
The neuroprotective effects of cholecystokinin in the brain: antioxidant, anti-inflammatory, cognition, and synaptic plasticity
Cui, H., Li, Z., Sun, H., Zhao, W., Ma, H., Li, H., Zhang, Z., Hölscher, C., Ma, D., & Zhang, Z. (2025) · Reviews in the Neurosciences · doi:10.1515/revneuro-2024-0142 · Cited by 3
Study of Intracellular Peptides of the Central Nervous System of Zebrafish (Danio rerio) in a Parkinson’s Disease Model
Fiametti, L. O., Franco, C. A., Nunes, L. O. C., Castro, L. M., & Santos‐Filho, N. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26052017 · Cited by 3
The role of autophagy in the pathogenesis and treatment of multiple sclerosis
Righes, G., Semenzato, L., Koutsikos, K., Zanato, V., Pinton, P., Giorgi, C., & Patergnani, S. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2529196 · Cited by 4
Mitochondrial Dysfunction in Neurodegenerative Diseases
Chen, C., Zhao, Y., Wang, J., Pan, D., Wang, X., Xu, Y., Yan, J., Wang, L., Yang, X., Lu, M., et al. (2025) · MedComm · doi:10.1002/mco2.70326 · Cited by 3
Perspective on Cav-1 for its Potential as Newer Therapeutics for Parkinson’s Disease
Singh, G., Pushpa, T., Gupta, S., Srivastava, S., Khatri, D. K., & Singh, S. B. (2022) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527321666220909150406 · Cited by 3
Mitochondria and Human Immunodeficiency Virus: A Troubled Relationship Enters Its Fourth Decade
Hulgan, T., & Samuels, D. C. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa983 · Cited by 3
Mitochondrial Dysregulation and the Influence in Neurodegenerative Diseases
Zuccoli, G. S., & Carregari, V. C. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-05460-0_8 · Cited by 3
MitoStructSeg: mitochondrial structural complexity resolution via adaptive learning for cross-sample morphometric profilingPreprint
Wang, X., Wan, X., Cai, B., Jia, Z., Chen, Y., Guo, S., Liu, Z., Li, F., Zhang, F., & Hu, B. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.28.601295 · Cited by 3
RNA triggers chronic stress during neuronal agingPreprint
Rhine, K., Epstein, E., Carlson, N. M., Ge, X., Mizrahi, O., Kamat, A., Hermann, A., Brothers, W. R., Ravits, J., Bennett, E. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.04.668575 · Cited by 3
Ayurveda: Ayurvedic herbs against neurological disorders: are they golden nuggets?
Muralidhara, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-19084-1.00022-3 · Cited by 2
Mitochondria‐Targeted Molecular Tools in Precise Tumor Therapy
Wang, X., Tang, Y., & Li, Q. (2025) · Angewandte Chemie · doi:10.1002/ange.202511230 · Cited by 2
A Perspective on the Role of Mitochondrial Biomolecular Condensates (mtBCs) in Neurodegenerative Diseases and Evolutionary Links to Bacterial BCs
Calcagnile, M., Alifano, P., Damiano, F., Pontieri, P., & Giudice, L. D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178216 · Cited by 2
The ubiquitin-binding protein ANKRD13A mediates VCP-dependent mitochondrial outer membrane rupture during PINK1/Parkin-mediated mitophagy
Chu, W.-H., Lin, Y.-S., Guo, J., Jane, W., Wang, W., Lin, Y.-Y., Liu, P.-H., Huang, P.-Y., & Chiang, W. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110739 · Cited by 2
Semaglutide and the pathogenesis of progressive neurodegenerative disease: the central role of mitochondria
Stefano, G. B., Büttiker, P., Weissenberger, S., Raboch, J., & Anders, M. (2025) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2025.101217 · Cited by 2
Deep Profiling of the Aging Proteome Depicts Neuroinflammation, Synaptic Function, and Phosphorylation in an Accelerated Alzheimer's Disease Cell Model
Gentry, E., Islam, M. T., Xue, H., Cao, K., & Nemes, P. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101490 · Cited by 2
Deciphering the Neuroprotective Potential of the Ayurvedic Ashokarishta GC–MS Derived Bioactives Through Network Pharmacology and in silico Multi-Target Analysis Against Alzheimer’s and Parkinson’s Diseases
Wang, Q., Vinothkanna, A., Prathiviraj, R., Li, X., Prabhu, S., & Dass, K. (2026) · Journal of Computational Biophysics and Chemistry · doi:10.1142/s2737416526500535 · Cited by 2
Nicotinamide mononucleotide supplementation modulates gut microbiota and metabolites to mitigate Alzheimer's disease pathology in APP/PS1 mice
Zhou, H., Zhao, X., Li, Y., Wang, Y., Zhang, S., Xu, H., Sui, S., Wang, Q., He, Y., & Gu, J. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261422502 · Cited by 2
Cryptoxanthin as a multitarget neuroprotective agent: mechanistic and in silico perspectives
Sadhukhan, A., Chauhan, A., Kumar, M., Singh, T., Mujwar, S., & Awasthi, A. (2026) · Journal of Pharmacy and Pharmacology · doi:10.1093/jpp/rgag029 · Cited by 2
Pink1 at the crossroads of aging, exercise, and diet in Parkinson’s disease: a mechanistic review
Lin, Y., & Wen, D. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1738559 · Cited by 2
The Molecular Basis of Partial Reversal or Significant Slowing of ALS, Parkinson’s Disease, and Lewy Body Dementia by Mesenchymal Exosomes/Secretome
Prodromos, C. C., Villar, R. D., Striegel, A., Pena, G. R., & Dixit, R. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27104483 · Cited by 2
Targeting Mitochondria in Aging‐Related Diseases: Therapeutic Potential and Obstacles
Xiang, Z., Chen, Y., Liu, X., Lu, H., Yang, Y., Xing, L., Zhang, Y., Lang, C., Zhang, S., Zhao, S., et al. (2026) · MedComm · doi:10.1002/mco2.70790 · Cited by 2
Iron-Induced Dopaminergic Cell Death In Vivo as a Model of Parkinson’s Disease
Gerlach, M., Double, K. L., & Riederer, P. F. (2021) · Springer eBooks · doi:10.1007/978-3-030-71519-9_100-1 · Cited by 2
Insights on the Correlation between Mitochondrial Dysfunction and the Progression of Parkinson's Disease
Chauhan, P., Pandey, P., Khan, F., & Maqsood, R. (2023) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/0118715303249690231006114308 · Cited by 2
Short-term regulation of TSFM level does not alter amyloidogenesis and mitochondrial function in type-specific cells
Li, X., Zhou, G., Xie, X.-Y., Pu, Y., Chen, X., Li, C., Yang, J., Wang, L., & Chen, G. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09426-4 · Cited by 2
Identifying shared diagnostic genes and mechanisms in vascular dementia and Alzheimer's disease via bioinformatics and machine learning
Zheng, W., Lin, D., Shi, S., Ren, J., Wu, J., Wang, M., & Wan, S. (2024) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823241289804 · Cited by 2
Fucoxanthin and its metabolite fucoxanthinol alleviate paraquat-induced oxidative damage and neurotoxicity in differentiated human neuroblastoma cells
Elmorsy, E. M., Al-Ghafari, A. B., Doghaither, H. A. A., Salama, M., Elzahed, H., & AlRuwaili, R. (2025) · Journal of Taibah University for Science · doi:10.1080/16583655.2025.2512661 · Cited by 2
Etiology and treatment challenges for neurodegenerative disorders
Wankhede, N. L., Kale, M. B., Shende, P. V., Ratne, N., Taksande, B. G., Upaganlawar, A. B., Umekar, M. J., & Magrulkar, S. V. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-23841-3.00001-7 · Cited by 3
The PINK1 p.Asn521Thr Variant Is Associated with Earlier Disease Onset in GRN/C9orf72 Frontotemporal Lobar Degeneration
Rossi, G., Salvi, E., Benussi, L., Mehmeti, E., Geviti, A., Bellini, S., Longobardi, A., Facconi, A., Carrara, M., Bonvicini, C., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112847 · Cited by 2
Self-renewal of neuronal mitochondria through asymmetric divisionPreprint
Waingankar, T. P., Zurita, C., Lang, A. E., Vuong, C., Shami, A., Bautista, D. M., Drerup, C. M., & Lewis, S. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.17.694973 · Cited by 2
Plate-Based Assays for the Characterization of Mitochondrial and Cellular Phenotypes
Arnold, B. H., Sanislav, O., Fisher, P. R., & Annesley, S. J. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3585-8_1 · Cited by 1
Mitochondria: A source of potential biomarkers for non-communicable diseases
Ichegiri, A., Kodolikar, K., Bagade, V., Selukar, M., & Dey, T. (2024) · Advances in clinical chemistry · doi:10.1016/bs.acc.2024.04.007 · Cited by 1
High-Resolution Respirometry Methodology for Bioenergetic and Metabolic Studies in Intact Brain Slices
Dias, C., Lourenço, C. F., Laranjinha, J. A. N., & Ledo, A. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4264-1_2 · Cited by 1
Effect of C-Phycocyanin on Isolated Mitochondria
Kuvirchenkova, A. P., Goleva, T. N., Sukhinov, D. V., Sergeeva, Y. E., & Vasilov, R. G. (2024) · Nanobiotechnology Reports · doi:10.1134/s2635167624602420 · Cited by 1
Screening strategy using a filamentous fungus model to repurpose drugs for mitochondrial complex I deficiencies
Sellem, C. H., Bounaix, N., Logerais, M., Renaud, A., d'Elia, M. A., Richard, J., Almyre, C., Becker, G., Rivron, J., Hoarau, A., et al. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124251 · Cited by 1
A synthetic resilience framework for stabilizing dynamical neural networks in neurodegeneration
Nirmal, A. K., Dayalan, H., Ayyar, G., Nithiananthan, G., & Thiruvengadam, H. (2026) · Discover Neuroscience · doi:10.1186/s13064-026-00301-5 · Cited by 1
MERCNN-EP: A deep transformer-based protein language model using multi-headed ensemble residual convolutional neural network for epigenetic protein prediction with applications in host–pathogen interactions and infectious disease dynamics
Ullah, K., Ali, F., Masmoudi, A., Rajkhan, N. W., Babour, A., & Alghamdi, W. (2026) · Journal of Computational Science · doi:10.1016/j.jocs.2026.102991 · Cited by 1
Bioactive polypeptide improves neuroinflammation by regulating microglia polarization
Zhai, L., Shen, H., Sheng, Y., Guo, W., Guan, Q., & Zhu, Y. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17059 · Cited by 1
Changes in the Number of CD38 and CX43 Immunopositive Cells in the Neurovascular Unit of the Brain in Experimental Alzheimer’s Disease
Хилажева, Е. Д., Mosiagina, A. I., Morgun, A. V., Malinovskaya, N. A., Gorina, Y. V., Kharitonova, E. V., Lopatina, O. L., & Salmina, A. B. (2022) · Cell and Tissue Biology · doi:10.1134/s1990519x22020067 · Cited by 1
Dopamine controls the sensitivity to manganese induced dopaminergic neurotoxicity in Caenorhabditis elegans
Raj, V., & Thekkuveettil, A. (2026) · Toxicology and Environmental Health Sciences · doi:10.1007/s13530-026-00310-1 · Cited by 1
Comparative Analysis of the Bioactivity and Anti-Inflammatory Effects Against Endotoxin in Mitochondria for Transplantation: Impact of Muscle Origin in Rats
Huang, D.-W., Hsu, H.-J., Chen, P.-W., Wu, M.-T., Wong, C., Huang, C.-C., Lee, P., Chen, H.-F., & Lee, J. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl37367 · Cited by 1
Dificultades vocales percibidas por pacientes con enfermedad de Parkinson y sus familiares. Un estudio comparativo
Cabrera, G. J., & Osses, M. H. (2025) · Revista de Investigación en Logopedia · doi:10.5209/rlog.99602 · Cited by 1
Galectin-3 directs mitophagy in response to Parkin-/proteasome-dependent rupture of mitochondrial outer membrane
Liu, P.-H., Lin, Y.-S., Chu, W.-H., Sun, W.-T., Huang, P.-Y., Huang, J., & Chiang, W. (2025) · Biology Direct · doi:10.1186/s13062-025-00692-1 · Cited by 2
Heterotrimetallic Au@Cu2Se nanozymes target inflamed neurons via suppression of oxidative stress and apoptosis to alleviate Alzheimer's disease
Jing, C., Li, J., Yu, D., Chao, M., Yan, H., Ge, K., Ma, G., Wang, J., Gao, F., & Zhang, G. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102646 · Cited by 1

Authors: Monzio Compagnoni, G., Di Fonzo, A., Corti, S., Comi, G. P., Bresolin, N., & Masliah, E.
Affiliations: University of Milan (IT)
National Institutes of Health (US)
ORCID: Monzio Compagnoni, Giacomo
Corti, Stefania
Comi, Giacomo P.
Bresolin, Nereo
Masliah, Eliezer
Venue: Molecular Neurobiology
Publisher: Springer Science and Business Media LLC
Published: 2020-05-22
Volume: 57
Issue: 7
Pages: 2959-2980
ISSN: 0893-7648 (ISSN-L)
1559-1182
DOI: 10.1007/s12035-020-01926-1
PMC: PMC9047992
OpenAlex: W3027900078
Cited by: 378
References: 309
Citations by year: 2026: 44 · 2025: 71 · 2024: 96 · 2023: 61 · 2022: 57 · 2021: 38 · 2020: 11
FWCI: 4.00
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Molecular Neurobiology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
Funders: Fresco Institute for Parkinson's and Movement Disorders (not available)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Keywords: mitochondria, mitochondrial dysfunction, neurodegenerative diseases, Alzheimer's disease, Parkinson's disease, mitochondrial DNA, electron transport chain, complex I, Parkin, PINK1, alpha-synuclein, amyloid pathology, multiple system atrophy, atypical parkinsonism, brain metabolism
MeSH terms: Alzheimer Disease, Animals, Brain, DNA, Mitochondrial, Humans, Mitochondria, Parkinson Disease, Electron Transport Complex I

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The Role of Mitochondria in Neurodegenerative Diseases: the Lesson from Alzheimer’s Disease and Parkinson’s Disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks