Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835

Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563

ER Tubules Mark Sites of Mitochondrial Division

Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072

PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969

Large-scale meta-analysis of genome-wide association data identifies six new risk loci for Parkinson’s disease

International Parkinson's Disease Genomics Consortium (IPDGC), Nalls, M. A., Parkinson's Study Group (PSG) Parkinson's Research: The Organized GENetics Initiative (PROGENI), 23andMe, GenePD, NeuroGenetics Research Consortium (NGRC), Hussman Institute of Human Genomics (HIHG), Investigator, T. A. J. D., (CHARGE), C. F. H. A. A. R. I. G. E., North American Brain Expression Consortium (NABEC), et al. (2014) · Nature Genetics · doi:10.1038/ng.3043 · Cited by 1,895

MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE

Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757

Autophagosomes form at ER–mitochondria contact sites

Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,683

Ubiquitin is phosphorylated by PINK1 to activate parkin

Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477

PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria

Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323

Age-Related Hearing Loss in C57BL/6J Mice Is Associated with Mitophagy Impairment in the Central Auditory System

Youn, C. K., Jun, Y., Jo, E.-R., & Cho, S. I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197202 · Cited by 43

Endolysosomal dysfunction in Parkinson's disease: Recent developments and future challenges

Kett, L. R., & Dauer, W. T. (2016) · Movement Disorders · doi:10.1002/mds.26797 · Cited by 43

Alpha-synuclein alters differently gene expression of Sirts, PARPs and other stress response proteins: implications for neurodegenerative disorders

Motyl, J. A., Wencel, P. L., Cieślik, M., Strosznajder, R. P., & Strosznajder, J. B. (2017) · Molecular Neurobiology · doi:10.1007/s12035-016-0317-1 · Cited by 42

Fibroblast mitochondria in idiopathic Parkinson’s disease display morphological changes and enhanced resistance to depolarization

Antony, P. M. A., Kondratyeva, O. E., Mommaerts, K., Ostaszewski, M., Sokolowska, K., Baumuratov, A., Longhino, L., Poulain, J. F., Großmann, D., Balling, R., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-58505-6 · Cited by 42

The BSSG rat model of Parkinson’s disease: progressing towards a valid, predictive model of disease

Kampen, J. M. V., & Robertson, H. A. (2017) · The EPMA Journal · doi:10.1007/s13167-017-0114-6 · Cited by 43

Current concepts and controversies in the pathogenesis of Parkinson’s disease dementia and Dementia with Lewy Bodies

Weil, R. S., Lashley, T., Brás, J., Schrag, A. E., & Schott, J. M. (2017) · F1000Research · doi:10.12688/f1000research.11725.1 · Cited by 41

Targeting α‐synuclein: Therapeutic options

Dehay, B., Decressac, M., Bourdenx, M., Guadagnino, I., Fernagut, P., Tamburrino, A., Bassil, F., Meissner, W. G., & Bézard, E. (2016) · Movement Disorders · doi:10.1002/mds.26568 · Cited by 44

The Role of Ubiquitin–Proteasome System and Mitophagy in the Pathogenesis of Parkinson's Disease

Yú, L., Zhong, G., Ren, M., Sun, T., Li, Y., Ye, M., Ma, C., Guo, Y., & Liu, C. (2023) · NeuroMolecular Medicine · doi:10.1007/s12017-023-08755-0 · Cited by 42

PARK7/DJ-1 dysregulation by oxidative stress leads to magnesium deficiency: implications in degenerative and chronic diseases

Kolísek, M., Montezano, A. C. I., Sponder, G., Anagnostopoulou, A., Vormann, J., Touyz, R. M., & Aschenbach, J. R. (2015) · Clinical Science · doi:10.1042/cs20150355 · Cited by 42

Iron-induced generation of mitochondrial ROS depends on AMPK activity

Huang, H., Chen, J., Lu, H., Zhou, M., Chai, Z., & Hu, Y. (2017) · BioMetals · doi:10.1007/s10534-017-0023-0 · Cited by 40

Embelin averts MPTP-induced dysfunction in mitochondrial bioenergetics and biogenesis via activation of SIRT1

Rao, S. P., Sharma, N., & Kalivendi, S. V. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148157 · Cited by 42

P2X7 Receptor and Purinergic Signaling: Orchestrating Mitochondrial Dysfunction in Neurodegenerative Diseases

Zelentsova, A. S., Deykin, A. V., Soldatov, V. O., Ulezko, A. A., Borisova, A. Y., Belyaeva, V. S., Skorkina, M. Y., & Angelova, P. R. (2022) · eNeuro · doi:10.1523/eneuro.0092-22.2022 · Cited by 41

Mic60/mitofilin overexpression alters mitochondrial dynamics and attenuates vulnerability of dopaminergic cells to dopamine and rotenone

Laar, V. S. V., Berman, S. B., & Hastings, T. G. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.03.015 · Cited by 38

microRNAs: Emerging Targets Regulating Oxidative Stress in the Models of Parkinson's Disease

Xie, Y., & Chen, Y. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00298 · Cited by 39

Precise control of mitophagy through ubiquitin proteasome system and deubiquitin proteases and their dysfunction in Parkinson's disease

Park, G. H., Park, J. H., & Chung, K. C. (2021) · BMB Reports · doi:10.5483/bmbrep.2021.54.12.107 · Cited by 40

Role of mitophagy in the neurodegenerative diseases and its pharmacological advances: A review

Wang, Q., Xue, H., Yue, Y., Hao, S., Huang, S., & Zhang, Z. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1014251 · Cited by 38

Mitochondrial Bioenergy in Neurodegenerative Disease: Huntington and Parkinson

Tassone, A., Meringolo, M., Ponterio, G., Bonsi, P., Schirinzi, T., & Martella, G. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087221 · Cited by 42

Deleterious mitochondrial DNA point mutations are overrepresented in Drosophila expressing a proofreading-defective DNA polymerase γ

Samstag, C. L., Hoekstra, J. G., Huang, C.-H., Chaisson, M., Youle, R. J., Kennedy, S. R., & Pallanck, L. J. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007805 · Cited by 42

Accumulation of mitochondrial 7S DNA in idiopathic and LRRK2 associated Parkinson's disease

Podlesniy, P., Puigròs, M., Serra, N., Fernández‐Santiago, R., Ezquerra, M., TOLOSA, E. S., & Trullás, R. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.09.015 · Cited by 38

Alpha-Synuclein Aggregates Associated with Mitochondria in Tunnelling Nanotubes

Valdinocci, D., Kovářová, J., Neužil, J., & Pountney, D. L. (2020) · Neurotoxicity Research · doi:10.1007/s12640-020-00285-y · Cited by 39

Induction of Autophagy by Vasicinone Protects Neural Cells from Mitochondrial Dysfunction and Attenuates Paraquat-Mediated Parkinson’s Disease Associated α-Synuclein Levels

Huang, C., Sivalingam, K., Shibu, M. A., Liao, P., Ho, T., Kuo, W., Chen, R., Day, C. H., Viswanadha, V. P., & Ju, D. (2020) · Nutrients · doi:10.3390/nu12061707 · Cited by 37

Loss of USF2 promotes proliferation, migration and mitophagy in a redox-dependent manner

Chi, T. F., Khoder‐Agha, F., Mennerich, D., Kellokumpu, S., Miinalainen, I., Kietzmann, T., & Dimova, E. Y. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101750 · Cited by 37

Hallmarks and Molecular Tools for the Study of Mitophagy in Parkinson’s Disease

Goiran, T., Eldeeb, M. A., Zorca, C. E., & Fon, E. A. (2022) · Cells · doi:10.3390/cells11132097 · Cited by 38

Drug Development for Alzheimer’s and Parkinson’s Disease: Where Do We Go Now?

Sequeira, L., Benfeito, S., Fernandes, C., Gaspar, A., Lima, I., Peixoto, J., Alves, C., Machado, C. S., Borges, F., & Chavarria, D. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16060708 · Cited by 37

Mitophagy and the therapeutic clearance of damaged mitochondria for neuroprotection

East, D. A., & Campanella, M. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.08.019 · Cited by 37

Can GBA1-Associated Parkinson Disease Be Modeled in the Mouse?

Farfel‐Becker, T., Do, J., Tayebi, N., & Sidransky, E. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2019.05.010 · Cited by 35

Cracking the Monoubiquitin Code of Genetic Diseases

Sewduth, R. N., Baietti, M. F., & Sablina, A. A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093036 · Cited by 36

A Critical LRRK at the Synapse? The Neurobiological Function and Pathophysiological Dysfunction of LRRK2

Kuhlmann, N., & Milnerwood, A. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00153 · Cited by 37

The Zebrafish, an Outstanding Model for Biomedical Research in the Field of Melatonin and Human Diseases

Aranda‐Martínez, P., Fernández‐Martínez, J., Ramírez‐Casas, Y., Guerra‐Librero, A., Rodríguez-Santana, C., Escames, G., & Acuña-Castroviejo, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137438 · Cited by 36

Role of c-Abl-GSK3β Signaling in MPP+-Induced Autophagy-Lysosomal Dysfunction

Ren, Y., Chen, J., Wu, X. G., Gui, C., Mao, K., Zou, F., & Li, W. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy155 · Cited by 35

Fenpropathrin induces degeneration of dopaminergic neurons via disruption of the mitochondrial quality control system

Jiao, Z., Wu, Y., & Qu, S. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00313-y · Cited by 35

REST Protects Dopaminergic Neurons from Mitochondrial and α-Synuclein Oligomer Pathology in an Alpha Synuclein Overexpressing BAC-Transgenic Mouse Model

Ryan, B. J., Bengoa‐Vergniory, N., Williamson, M. G., Kirkiz, E., Roberts, R. F., Corda, G., Sloan, M., Saqlain, S., Cherubini, M., Poppinga, J., et al. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.1478-20.2021 · Cited by 38

Parkinson Disease: Translating Insights from Molecular Mechanisms to Neuroprotection

Pirooznia, S. K., Rosenthal, L. S., Dawson, V. L., & Dawson, T. M. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000189 · Cited by 36

Vitamin K2 Modulates Mitochondrial Dysfunction Induced by 6-Hydroxydopamine in SH-SY5Y Cells via Mitochondrial Quality-Control Loop

Tang, H., Zheng, Z., Wang, H., Wang, L., Zhao, G., & Wang, P. (2022) · Nutrients · doi:10.3390/nu14071504 · Cited by 36

The interplay between parkin and alpha-synuclein; possible implications for the pathogenesis of Parkinson’s disease

Jęśko, H. M., Lenkiewicz, A. M., Wilkaniec, A., & Adamczyk, A. (2019) · Acta Neurobiologiae Experimentalis · doi:10.21307/ane-2019-026 · Cited by 34

LIN28A loss of function is associated with Parkinson's disease pathogenesis

Chang, M., Oh, B., Choi, J., Sulistio, Y. A., Woo, H., Jo, A.-Y., Kim, J.-I., Kim, E., Kim, S. W., Hwang, J., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018101196 · Cited by 33

Significance of mitochondrial activity in neurogenesis and neurodegenerative diseases

Sun, N., Ozgen, S., Krigman, J., & Zhang, R. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.322429 · Cited by 38

Potential benefits of medium chain fatty acids in aging and neurodegenerative disease

Dunn, E., Zhang, B., Sahota, V. K., & Augustin, H. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1230467 · Cited by 38

Mitophagy regulation in aging and neurodegenerative disease

Banarase, T. A., Sammeta, S. S., Wankhede, N. L., Mangrulkar, S. V., Rahangdale, S. R., Aglawe, M. M., Taksande, B. G., Upaganlawar, A. B., Umekar, M. J., & Kale, M. B. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01057-6 · Cited by 35

Protein-protein interaction networks identify targets which rescue the MPP+ cellular model of Parkinson’s disease

Keane, H. A., Ryan, B. J., Jackson, B., Whitmore, A. V., & Wade‐Martins, R. (2015) · Scientific Reports · doi:10.1038/srep17004 · Cited by 33

Pathophysiological Consequences of Neuronal α-Synuclein Overexpression: Impacts on Ion Homeostasis, Stress Signaling, Mitochondrial Integrity, and Electrical Activity

Tolö, J., Taschenberger, G., Leite, K., Stahlberg, M. A., Spehlbrink, G., Kues, J., Munari, F., Capaldi, S., Becker, S., Zweckstetter, M., et al. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00049 · Cited by 33

NADPH ameliorates MPTP-induced dopaminergic neurodegeneration through inhibiting p38MAPK activation

Zhou, J.-S., Zhu, Z., Wu, F., Zhou, Y. Y., Sheng, R., Wu, J., & Qin, Z. (2018) · Acta Pharmacologica Sinica · doi:10.1038/s41401-018-0003-0 · Cited by 33

Inhibition of the deubiquitinase USP8 corrects a Drosophila PINK1 model of mitochondria dysfunction

von Stockum, S., Sanchez-Martinez, A., Corrà, S., Chakraborty, J., Marchesan, E., Locatello, L., Da Rè, C., Cusumano, P., Caicci, F., Ferrari, V., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900392 · Cited by 30

The therapeutic role of cannabinoid receptors and its agonists or antagonists in Parkinson's disease

Han, Q.-W., Yuan, Y., & Chen, N. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.109745 · Cited by 37

CHCHD2 harboring Parkinson’s disease-linked T61I mutation precipitates inside mitochondria and induces precipitation of wild-type CHCHD2

Cornelissen, T., Spinazzi, M., Martin, S., Imberechts, D., Vangheluwe, P., Bird, M., Strooper, B. D., & Vandenberghe, W. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa028 · Cited by 33

Novel PET Biomarkers to Disentangle Molecular Pathways across Age-Related Neurodegenerative Diseases

Wilson, H., Politis, M., Rabiner, E. A., & Middleton, L. T. (2020) · Cells · doi:10.3390/cells9122581 · Cited by 34

From cradle to grave: neurogenesis, neuroregeneration and neurodegeneration in Alzheimer’s and Parkinson’s diseases

Wakhloo, D., Mahajani, S. U., Oberhauser, J., & Madira, A. E. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.336138 · Cited by 38

Neuroprotective effect of cellular prion protein (PrPC) is related with activation of alpha7 nicotinic acetylcholine receptor (α7nAchR)-mediated autophagy flux

Jeong, J., & Park, S. (2015) · Oncotarget · doi:10.18632/oncotarget.4953 · Cited by 33

miR-155 inhibits mitophagy through suppression of BAG5, a partner protein of PINK1

Tsujimoto, T., Mori, T., Houri, K., Onodera, Y., Takehara, T., Shigi, K., Nakao, S., Teramura, T., & Fukuda, K. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.022 · Cited by 32

Heterotypic interactions in amyloid function and disease

Konstantoulea, K., Louros, N. N., Rousseau, F., & Schymkowitz, J. W. H. (2021) · FEBS Journal · doi:10.1111/febs.15719 · Cited by 34

Leucine‐rich repeat kinase 2 and Parkinson's disease

Kang, U., & Marto, J. A. (2016) · PROTEOMICS · doi:10.1002/pmic.201600092 · Cited by 34

Regulation of mitophagy by the ubiquitin pathway in neurodegenerative diseases

Desai, S. D., Juncker, M. A., & Kim, C. (2018) · Experimental Biology and Medicine · doi:10.1177/1535370217752351 · Cited by 31

Exhaustion of mitochondrial and autophagic reserve may contribute to the development of LRRK2 G2019S -Parkinson’s disease

Juárez‐Flores, D. L., González‐Casacuberta, I., Ezquerra, M., Bañó, M., Carmona, F., Catalán‐García, M., Guitart‐Mampel, M., Rivero, J. J., Tobías, E., Milisenda, J. C., et al. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1526-3 · Cited by 32

Compartmentalized Signaling in Aging and Neurodegeneration

Benedetto, G. D., Iannucci, L. F., Surdo, N. C., Zanin, S., Conca, F., Grisan, F., Gerbino, A., & Lefkimmiatis, K. (2021) · Cells · doi:10.3390/cells10020464 · Cited by 30

The Therapeutic Potential of Mitochondria Transplantation Therapy in Neurodegenerative and Neurovascular Disorders

Khan, M. M., Paez, H. G., Pitzer, C. R., & Alway, S. E. (2022) · Current Neuropharmacology · doi:10.2174/1570159x05666220908100545 · Cited by 30

Alpha synuclein modulates mitochondrial Ca2+ uptake from ER during cell stimulation and under stress conditions

Ramezani, M., Wagenknecht-Wiesner, A., Wang, T., Holowka, D. A., Eliezer, D., & Baird, B. A. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00578-x · Cited by 33

Mitochondrial Targeting in Neurodegeneration: A Heme Perspective

Fiorito, V., Chiabrando, D., & Tolosano, E. (2018) · Pharmaceuticals · doi:10.3390/ph11030087 · Cited by 31

Induced pluripotent stem cell‐based modeling of mutant LRRK 2‐associated Parkinson's disease

Weykopf, B., Haupt, S., Jungverdorben, J., Flitsch, L. J., Hebisch, M., Liu, G., Suzuki, K., Belmonte, J. C. I., Peitz, M., Blaess, S., et al. (2019) · European Journal of Neuroscience · doi:10.1111/ejn.14345 · Cited by 30

Culprit or Bystander: Defective Mitophagy in Alzheimer’s Disease

Xie, C., Aman, Y., Adriaanse, B. A., Cader, M. Z., Plun‐Favreau, H., Xiao, J., & Fang, E. F. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00391 · Cited by 29

Mitochondrial-based therapies for neurodegenerative diseases: a review of the current literature

Wadan, A. S., Shaaban, A., El-Sadek, M. Z., Mostafa, S. A., Moshref, A. S., El‐Hussein, A., Ellakwa, D. E., & Mehanny, S. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04014-0 · Cited by 38

Neurodegenerative diseases have genetic hallmarks of autoinflammatory disease

Richards, R. I., Robertson, S. A., & Kastner, D. L. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy139 · Cited by 27

PINK1/Parkin-Mediated Mitophagy Promotes Resistance to Sonodynamic Therapy

Song, L., Huang, Y., Hou, X., Yang, Y., Kala, S., Qiu, Z., Zhang, R., & Sun, L. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000493629 · Cited by 29

Brain Cytochrome P450: Navigating Neurological Health and Metabolic Regulation

Durairaj, P., & Liu, Z. L. (2025) · Journal of Xenobiotics · doi:10.3390/jox15020044 · Cited by 30

Knockdown of the mitochondria‐localized protein p13 protects against experimental parkinsonism

Inoue, N., Ogura, S., Kasai, A., Nakazawa, T., Ikeda, K., Higashi, S., Isotani, A., Baba, K., Mochizuki, H., Fujimura, H., et al. (2018) · EMBO Reports · doi:10.15252/embr.201744860 · Cited by 29

Modulation of mitochondrial phenotypes by endurance exercise contributes to neuroprotection against a MPTP-induced animal model of PD

Jang, Y., Kwon, I., Song, W., Cosío-Lima, L., Taylor, S. M., & Lee, Y. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.08.045 · Cited by 29

Research on developing drugs for Parkinson's disease

Zhang, C., Han, Q.-W., Chen, N., & Yuan, Y. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.12.017 · Cited by 28

Mice with disrupted mitochondria used to model Parkinson’s disease

Doric, Z., & Nakamura, K. (2021) · Nature · doi:10.1038/d41586-021-02955-z · Cited by 28

Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers

Louros, N., Ramakers, M., Michiels, E., Konstantoulea, K., Morelli, C., Garcia, T., Moonen, N., D’Haeyer, S., Goossens, V., Thal, D. R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28955-9 · Cited by 28

HIF‐1α Ameliorates Diabetic Neuropathic Pain via Parkin‐Mediated Mitophagy in a Mouse Model

He, J., Qin, Z., Chen, X., He, W., Li, D., Zhang, L., Le, Y., Xiong, Q., Zhang, B., & Wang, H. (2022) · BioMed Research International · doi:10.1155/2022/5274375 · Cited by 29

N -acetylcysteine protects against motor, optomotor and morphological deficits induced by 6-OHDA in zebrafish larvae

Benvenutti, R., Marcon, M., Reis, C. G., Nery, L. R., Miguel, C., Herrmann, A. P., Vianna, M. R. M. R., & Piato, Â. (2018) · PeerJ · doi:10.7717/peerj.4957 · Cited by 28

Impact of Physical Activity on Cellular Metabolism Across Both Neurodegenerative and General Neurological Conditions: A Narrative Review

Clemente‐Suárez, V. J., Rubio-Zarapuz, A., Belinchón-deMiguel, P., Beltrán-Velasco, A. I., Martín-Rodríguez, A., & Tornero-Aguilera, J. F. (2024) · Cells · doi:10.3390/cells13231940 · Cited by 30

Activating autophagy to eliminate toxic protein aggregates with small molecules in neurodegenerative diseases

Fu, Y., Zhang, J., Qin, R., Ren, Y., Zhou, T., Han, B., & Liu, B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100053 · Cited by 29

Characterization of oromotor and limb motor dysfunction in the DJ1 -/- model of Parkinson disease

Yang, K. M., Blue, K. V., Mulholland, H. N., Kurup, M., Kelm‐Nelson, C. A., & Ciucci, M. R. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.10.036 · Cited by 27

A mitochondrial uncoupler prodrug protects dopaminergic neurons and improves functional outcome in a mouse model of Parkinson’s disease

Kishimoto, Y., Johnson, J. E., Fang, W., Halpern, J., Marosi, K., Liu, D., Geisler, J. G., & Mattson, M. P. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.09.011 · Cited by 27

Novel Insights into Parkin–Mediated Mitochondrial Dysfunction and “Mito-Inflammation” in α-Synuclein Toxicity. The Role of the cGAS–STING Signalling Pathway

Gąssowska-Dobrowolska, M., Olech-Kochańczyk, G., Culmsee, C., & Adamczyk, A. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s468609 · Cited by 29

Selective autophagy: The new player in the fight against neurodegenerative diseases?

Wu, M.-Y., Song, J., Wang, S.-F., Cai, C.-Z., Li, M., & Lu, J. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.11.009 · Cited by 27

Nonmercaptalbumin as an oxidative stress marker in Parkinson’s and PARK2 disease

Ueno, S., Hatano, T., Okuzumi, A., Saiki, S., Oji, Y., Mori, A., Koinuma, T., Fujimaki, M., Takeshige‐Amano, H., Kondo, A., et al. (2020) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.50990 · Cited by 25

Autophagy and Redox Homeostasis in Parkinson’s: A Crucial Balancing Act

Jiménez-Moreno, N., & Lane, J. D. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8865611 · Cited by 26

Rat Models of Vocal Deficits in Parkinson’s Disease

Krasko, M. N., Hoffmeister, J. D., Schaen‐Heacock, N. E., Welsch, J. M., Kelm‐Nelson, C. A., & Ciucci, M. R. (2021) · Brain Sciences · doi:10.3390/brainsci11070925 · Cited by 26

Defects of Nutrient Signaling and Autophagy in Neurodegeneration

Ondaro, J., Hernández-Eguiazu, H., Garciandia-Arcelus, M., Loera‐Valencia, R., Rodríguez-Gómez, L., Jiménez-Zúñiga, A., Goikolea, J., Rodriguez‐Rodriguez, P., Ruiz‐Martínez, J., Moreno, F., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.836196 · Cited by 28

Monocyte biomarkers define sargramostim treatment outcomes for Parkinson's disease

Abdelmoaty, M. M., Machhi, J., Yeapuri, P., Shahjin, F., Kumar, V. S., Olson, K. E., Mosley, R. L., & Gendelman, H. E. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.958 · Cited by 25

Deubiquitylating enzymes in neuronal health and disease

Amer‐Sarsour, F., Kordonsky, A., Berdichevsky, Y., Prag, G., & Ashkenazi, A. (2021) · Cell Death and Disease · doi:10.1038/s41419-020-03361-5 · Cited by 27

Extremely low-frequency pulses of faint magnetic field induce mitophagy to rejuvenate mitochondria

Toda, T., Ito, M., Takeda, J., Masuda, A., Mino, H., Hattori, N., Mohri, K., & Ohno, K. (2022) · Communications Biology · doi:10.1038/s42003-022-03389-7 · Cited by 25

Melatonin Mitigates Rotenone-Induced Oxidative Stress and Mitochondrial Dysfunction in the Drosophila melanogaster Model of Parkinson’s Disease-like Symptoms

Rasheed, M. Z., Khatoon, R., Talat, F., Alam, M. M., Tabassum, H., & Parvez, S. (2023) · ACS Omega · doi:10.1021/acsomega.2c03992 · Cited by 25

Tetramethylpyrazine Analogue T-006 Exerts Neuroprotective Effects against 6-Hydroxydopamine-Induced Parkinson’s Disease In Vitro and In Vivo

Zhou, H., Shao, M., Yang, X., Li, C., Cui, G., Cheng, G., Di, L., Zhong, H., Wang, Y., Zhang, Z., et al. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8169125 · Cited by 25

Dietary Antioxidants and the Mitochondrial Quality Control: Their Potential Roles in Parkinson’s Disease Treatment

Lee, D., Jo, M. G., Kim, S. Y., Chung, C. G., & Lee, S. B. (2020) · Antioxidants · doi:10.3390/antiox9111056 · Cited by 24

Neurodegenerative disorders associated with genes of mitochondria

Marde, V. S., Tiwari, P. L., Wankhede, N. L., Taksande, B. G., Upaganlawar, A., Umekar, M. J., & Kale, M. B. (2021) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-021-00215-5 · Cited by 24

Circulating cell-free mitochondrial DNA in brain health and disease: A systematic review and meta-analysis

Park, S. S., Jeong, H., & Andreazza, A. C. (2021) · The World Journal of Biological Psychiatry · doi:10.1080/15622975.2021.1938214 · Cited by 27

The PINK1—Parkin mitophagy signalling pathway is not functional in peripheral blood mononuclear cells

Bradshaw, A., Campbell, P., Schapira, A. H. V., Morris, H. R., & Taanman, J. (2021) · PLoS ONE · doi:10.1371/journal.pone.0259903 · Cited by 23

SARS-CoV-2 Spike Protein S1 Domain Accelerates α-Synuclein Phosphorylation and Aggregation in Cellular Models of Synucleinopathy

Wang, J., Dai, L., Deng, M., Xiao, T., Zhang, Z., & Zhang, Z. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03726-9 · Cited by 24

Targeting brain‐derived neurotrophic factor in the treatment of neurodegenerative diseases: A review

Wang, D., Lang, Z., Wei, S., Wang, W., & Zhang, H. (2024) · Neuroprotection/Neuroprotection (Chichester, England. Print) · doi:10.1002/nep3.43 · Cited by 31

DNA damage preceding dopamine neuron degeneration in A53T human α-synuclein transgenic mice

Wang, D., Yu, T., Liu, Y., Yan, J., Guo, Y., Jing, Y., Yang, X., Song, Y., & Tian, Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.11.008 · Cited by 23

PET Imaging Unveils Neuroinflammatory Mechanisms in Psychiatric Disorders: From Microglial Activation to Therapeutic Innovation

Liu, Y.-D., Chang, Y., Xie, X., Wang, X., Ma, H.-Y., Liu, M., & Zhang, H. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05177-w · Cited by 31

Exercise and mitochondrial remodeling to prevent age-related neurodegeneration

O’Reilly, C. L., Miller, B. F., & Lewis, T. L. (2022) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00611.2022 · Cited by 25

Morinda citrifoliamitigates rotenone-induced striatal neuronal loss in male Sprague-Dawley rats by preventing mitochondrial pathway of intrinsic apoptosis

Narasimhan, K. K. S., Jayakumar, D., Saraswathi, U., Mohan, T., Sathyamoorthy, Y. K., Ezhil, P., & Kalaiselvi, P. (2016) · Redox Report · doi:10.1080/13510002.2016.1253449 · Cited by 23

Identification of distinct blood-based biomarkers in early stage of Parkinson’s disease

Wu, Y., Yao, Q., Jiang, G., Wang, G., & Cheng, Q. (2019) · Neurological Sciences · doi:10.1007/s10072-019-04165-y · Cited by 23

PARKIN overexpression in human mesenchymal stromal cells from Wharton's jelly suppresses 6-hydroxydopamine–induced apoptosis: Potential therapeutic strategy in Parkinson's disease

Bonilla-Porras, A. R., Arévalo-Arbeláez, Á. J., Álzate, J. F., Velez‐Pardo, C., & Jiménez-Del-Río, M. (2017) · Cytotherapy · doi:10.1016/j.jcyt.2017.09.011 · Cited by 22

Mitochondrial health maintenance in axons

Harbauer, A. B. (2017) · Biochemical Society Transactions · doi:10.1042/bst20170023 · Cited by 22

Mitochondria dynamics in the aged mice eye and the role in the RPE phagocytosis

Yako, T., Nakamura, M., Otsu, W., Nakamura, S., Shimazawa, M., & Hara, H. (2021) · Experimental Eye Research · doi:10.1016/j.exer.2021.108800 · Cited by 21

Cell-free mitochondrial DNA deletions in idiopathic, but not LRRK2, Parkinson's disease

Puigròs, M., Calderon, A., Pérez‐Soriano, A., de Dios, C., Fernández, M., Colell, A., Martı́, M. J., TOLOSA, E. S., & Trullás, R. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105885 · Cited by 22

Mitochondrial dysfunction and mitophagy in parkinson’s disease: from mechanism to therapy

Malpartida, A. B., Williamson, M., Narendra, D. P., Wade-Martins, R., & Ryan, B. J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.11.007 · Cited by 482

Current perspective of mitochondrial biology in Parkinson's disease

Kaidery, N. A., & Thomas, B. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.03.001 · Cited by 95

Mitochondrial dysfunction in Parkinson’s disease

Hu, Q., & Wang, G. (2016) · Translational Neurodegeneration · doi:10.1186/s40035-016-0060-6 · Cited by 213

Mitochondrial Dysfunction in Parkinson’s Disease: New Mechanistic Insights and Therapeutic Perspectives

Park, J.-S., Davis, R. L., & Sue, C. M. (2018) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-018-0829-3 · Cited by 516

Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis

Banerjee, R., Starkov, A. A., Beal, M. F., & Thomas, B. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.11.007 · Cited by 262