Synaptic, Mitochondrial, and Lysosomal Dysfunction in Parkinson’s Disease

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

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

The Role of Oxidative Stress in Parkinson's Disease

Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845

A meta-analysis of genome-wide association studies identifies 17 new Parkinson's disease risk loci

Chang, D., Nalls, M. A., Hallgrímsdóttir, I. B., Hunkapiller, J., van der Brug, M., Cai, F., International Parkinson's Disease Genomics Consortium, 23andMe Research Team, Kerchner, G. A., Ayalon, G., et al. (2017) · Nature Genetics · doi:10.1038/ng.3955 · Cited by 1,112

Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases

Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. (2016) · eLife · doi:10.7554/elife.12813 · Cited by 1,042

Mitochondria–lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis

Wong, Y. C., Ysselstein, D., & Krainc, D. (2018) · Nature · doi:10.1038/nature25486 · Cited by 911

Dopamine oxidation mediates mitochondrial and lysosomal dysfunction in Parkinson’s disease

Burbulla, L. F., Song, P., Mazzulli, J. R., Zampese, E., Wong, Y. C., Jeon, S., Santos, D. P., Blanz, J., Obermaier, C. D., Strojny, C., et al. (2017) · Science · doi:10.1126/science.aam9080 · Cited by 874

Activity-driven local ATP synthesis is required for synaptic function

Rangaraju, V., Calloway, N., & Ryan, T. A. (2014) · Cell · doi:10.1016/j.cell.2013.12.042 · Cited by 836

Complexity of dopamine metabolism

Meiser, J., Weindl, D., & Hiller, K. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-34 · Cited by 726

Elevated Mitochondrial Bioenergetics and Axonal Arborization Size Are Key Contributors to the Vulnerability of Dopamine Neurons

Pacelli, C., Giguère, N., Bourque, M.-J., Lévesque, M., Slack, R. S., & Trudeau, L. (2015) · Current Biology · doi:10.1016/j.cub.2015.07.050 · Cited by 530

Decoding Organelle Interactions: Unveiling Molecular Mechanisms and Disease Therapies

Liu, R., Hong, W., Hou, D., Huang, H., & Duan, C. (2024) · Advanced Biology · doi:10.1002/adbi.202300288 · Cited by 8

α-Synuclein and Mitochondria: Probing the Dynamics of Disordered Membrane-protein Regions Using Solid-State Nuclear Magnetic Resonance

Gallo, A., Mansueto, S., Emendato, A., Fusco, G., & Simone, A. D. (2024) · JACS Au · doi:10.1021/jacsau.4c00323 · Cited by 8

A Single-Cell Atlas of the Substantia Nigra Reveals Therapeutic Effects of Icaritin in a Rat Model of Parkinson’s Disease

Wu, H., Zhang, Z., Zhou, P., Sui, X., Liu, X., Sun, Y. X., Zhao, X., & Pu, X. (2024) · Antioxidants · doi:10.3390/antiox13101183 · Cited by 8

Exercise regulates mitophagy to alleviate parkinsonian neurodegeneration

Liu, C., He, W., & Zhang, J. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1678460 · Cited by 8

Neurexin 2 p.G849D variant, implicated in Parkinson’s disease, increases reactive oxygen species, and reduces cell viability and mitochondrial membrane potential in SH-SY5Y cells

Cuttler, K., de Swardt, D., Engelbrecht, L., Kriel, J., Cloete, R. E. A., & Bardien, S. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-022-02548-8 · Cited by 8

Emerging evidence of context-dependent synapse elimination by phagocytes in the CNS

Shen, F.-S., Liu, C., Sun, H.-Z., Chen, X., Xue, Y., & Chen, L. (2024) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiae098 · Cited by 8

Parkinson’s Disease Master Regulators on Substantia Nigra and Frontal Cortex and Their Use for Drug Repositioning

de Vargas, D. M., Bastiani, M. A. D., Parsons, R. B., & Klamt, F. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02203-x · Cited by 9

Mutant VPS35-D620N induces motor dysfunction and impairs DAT-mediated dopamine recycling pathway

Huang, Y. C., Huang, H., Zhou, L., Li, J., Chen, X., Thomas, J., He, X., Guo, W., Zeng, Y., Low, B. C., et al. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac142 · Cited by 8

Integrated insight into the molecular mechanisms of selenium-modulated, MPP+-induced cytotoxicity in a Parkinson’s disease model

Liu, W., Zhang, F., Wu, L., Huang, K., Jia, C., Zhang, J., Li, X., Wei, W., Gong, R., & Chen, J. (2023) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2023.127208 · Cited by 8

(Dys)functional insights into nucleic acids and RNA-binding proteins modulation of the prion protein and α-synuclein phase separation

Cordeiro, Y., Freire, M. H. O., Wiecikowski, A. F., & do Amaral, M. J. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01067-4 · Cited by 7

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

Proteomics based discovery of Salvia miltiorrhiza Bunge treating Parkinson's disease through the PINK1/Parkin pathway

Xu, D.-C., Chen-Yu, S., Zong, C., Fu, W., Ling, J., Shao, P., Liu, X., Chen, Y., & Xu, T. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120079 · Cited by 7

[18F]SynVest-1 PET imaging in people with Parkinson’s disease

Martin, S. L., Uribe, C., Desmond, K. L., Narciso, L., Dolman, B., Torres‐Carmona, E., Boileau, I., Graff‐Guerrero, A., Vasdev, N., & Strafella, A. P. (2025) · Brain Communications · doi:10.1093/braincomms/fcaf258 · Cited by 9

Lysosomal homeostasis at the crossroads of neurodegeneration

Tito, S. D., & Tooze, S. A. (2026) · Journal of Clinical Investigation · doi:10.1172/jci199845 · Cited by 10

Molecular Mechanisms of Dopaminergic Neuron Degeneration in Parkinson’s Disease: A Comprehensive Review

Abubakar, M., Alom, S., Ali, F., Ali, S. R., Adhikary, K., Sarika, S., Gupta, P. K., Puppala, E. R., Murti, K., Nand, S., et al. (2026) · Current Neuropharmacology · doi:10.2174/011570159x446831260303200516 · Cited by 7

Bioinformatic analysis of the SPs and NFTs proteomes unravel putative biomarker candidates for Alzheimer's disease

Ferreira, M., Martins, T. S., Alves, S. R., Rosa, I. M., Vogelgsang, J. S., Hansen, N., Wiltfang, J., Silva, O. A. B. D. C. E., Vitorino, R. M. P., & Henriques, A. G. (2023) · PROTEOMICS · doi:10.1002/pmic.202200515 · Cited by 6

The subventricular zone structure, function and implications for neurological disease

Li, K., Zheng, Y., Cai, S., Fan, Z., Yang, J., Liu, Y., Liang, S., Song, M., Du, S., & Qi, L. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101398 · Cited by 9

Neurological Consequences of Sphingosine Phosphate Lyase Insufficiency

Atreya, K. B., & Saba, J. D. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.938693 · Cited by 7

Ambient atmospheric PM worsens mouse lung injury induced by influenza A virus through lysosomal dysfunction

Li, S., Ju, X., Liu, Q., Yan, Y., Zhang, C., Qin, Y., Deng, X., Li, C., Tian, M., Zhang, Y., et al. (2023) · Respiratory Research · doi:10.1186/s12931-023-02618-9 · Cited by 7

Structuring and validating a prognostic model for low-grade gliomas based on the genes for plasma membrane tension

Li, J., Lv, F., & Jin, T. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.1024869 · Cited by 7

Targeting selective autophagy in CNS disorders by small-molecule compounds

Zheng, Y., Zhou, Z., Liu, M., & Chen, Z. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108729 · Cited by 6

Synaptic Vesicle Disruption in Parkinson’s Disease: Dual Roles of α-Synuclein and Emerging Therapeutic Targets

Treviño, M., Guerra‐Crespo, M., Padilla-Godínez, F. J., Ortega‐Robles, E., & Arias-Carrión, Ó. (2025) · Brain Sciences · doi:10.3390/brainsci16010007 · Cited by 7

Evaluation of the relationship between SORL1 gene polymorphism and Parkinson's disease in the Chinese population

Wang, Y., Luan, M., Li, X., Jin, J., & Xie, A. (2022) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136602 · 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

A modified density gradient proteomic-based method to analyze endolysosomal proteins in cardiac tissue

Ayagama, T., Bose, S. J., Capel, R. A., Priestman, D. A., Berridge, G., Fischer, R., Galione, A., Platt, F. M., Kramer, H., & Burton, R. A. B. (2021) · iScience · doi:10.1016/j.isci.2021.102949 · Cited by 8

Disruption of Dopamine Homeostasis Associated with Alteration of Proteins in Synaptic Vesicles: A Putative Central Mechanism of Parkinson’s Disease Pathogenesis

Jin, X., Si, X., Lei, X., Liu, H., Shao, A., & Li, L. (2023) · Aging and Disease · doi:10.14336/ad.2023.0821-2 · Cited by 7

Does altering proteasomal activity and trafficking reduce the arborization mediated specific vulnerability of SNpc dopaminergic neurons of Parkinson’s disease?

Bhaskar, S., Gowda, J., Prasanna, J., & Kumar, A. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.110062 · Cited by 6

Alpinetin Targets Mitophagy Pathways to Mitigate Parkinson's Disease Progression

Shen, Z., Shan, X., Zhang, S., Huang, D. A., Hu, H., Liang, Y., Zhu, H. B., Zhang, L., & Chen, Y. (2025) · CNS Neuroscience & Therapeutics · doi:10.1002/cns.70676 · Cited by 5

What Is the Role of Organelle Membrane Contact Sites in Neurodegenerative Diseases?

Benarroch, E. E. (2022) · Neurology · doi:10.1212/wnl.0000000000201354 · Cited by 5

Deciphering the role of heat shock protein HSPA1L: biomarker discovery and prognostic insights in Parkinson's disease and glioma

Cheng, H., Wang, J., Zhao, Y., Hou, X. S., Ling, F., Wang, Y., & Cao, Y. (2024) · SLAS TECHNOLOGY · doi:10.1016/j.slast.2024.100212 · Cited by 5

Disease Progression and Sphingolipids and Neurofilament Light Chain in Early Idiopathic Parkinson’s Disease

Couto, B., Sousa, M., González-Latapí, P., McArthur, E., Lang, A. E., Chen‐Plotkin, A. S., & Marras, C. (2023) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/cjn.2023.281 · Cited by 5

Parkinson’s disease: spatiotemporal regulation and therapeutic prospects of TREM2-mediated microglial responses

Hou, K., An, Z., Xu, Y., Wang, J., Zhou, M., Liu, Y., Zhu, X., & Wei, J. (2026) · npj Parkinson s Disease · doi:10.1038/s41531-025-01247-x · Cited by 5

Oxyphylla A exerts antiparkinsonian effects by ameliorating 6-OHDA-induced mitochondrial dysfunction and dyskinesia in vitro and in vivo

Shao, M., Zhao, C., Pan, Z., Yang, X., Cheng, G., Kam, G. H.-C., Zhou, H., & Lee, S. M. (2024) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2024.111224 · Cited by 5

CoPPIs algorithm: a tool to unravel protein cooperative strategies in pathophysiological conditions

Lomagno, A., Yusuf, I., Tosadori, G., Bonanomi, D., Mauri, P. L., & Silvestre, D. D. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf146 · Cited by 4

A Potential Role of Natural Bioactive Compounds Found in Food in the Prevention of Idiopathic Parkinson’s Disease

Huenchuguala, S., & Segura‐Aguilar, J. (2025) · Nutrients · doi:10.3390/nu17213376 · Cited by 5

Whole-exome sequencing and burden analysis identify six novel candidate risk genes and expand the genetic landscape of Parkinson’s disease

Fan, Y., Hu, Z. J., Yan, Q., Wan, J.-J., & Liu, J. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-01195-6 · Cited by 4

Alleviating Neurodegenerative Diseases Associated with Mitochondrial Defects by Therapeutic Biomolecules

Roy, T., Padhi, S., Mazumder, R., Majee, C., Das, S., Monika, Mishra, R., & Kapoor, B. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266299148240329062647 · Cited by 5

Emergence of pathological beta oscillation and its uncertainty quantification in a time-delayed feedback Parkinsonian model

Chen, Y., Nakao, H., & Kang, Y. (2024) · Chaos Solitons & Fractals · doi:10.1016/j.chaos.2024.115113 · 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

Rebalance of mitophagy by inhibiting LRRK2 improves colon alterations in an MPTP in vivo model

Filippone, A., Mannino, D., Cucinotta, L., Calapai, F., Crupi, L., Paterniti, I., & Esposito, E. (2024) · iScience · doi:10.1016/j.isci.2024.110980 · Cited by 4

Analysis of the Neuroproteome Associated With Cell Therapy After Intranigral Grafting in a Mouse Model of Parkinson Disease

Dakik, H., Mantash, S., Nehme, A., Kobeissy, F. H., Zabet‐Moghaddam, M., Mirzaei, P., Mechref, Y. S., Gaillard, A., Prestoz, L., & Zibara, K. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.621121 · Cited by 4

Decreased soluble Nogo-B in serum as a promising biomarker for Parkinson's disease

Liang, H., Guo, W., He, H., Zhang, H., Ye, Q., Zhang, Q., Liao, J., Shen, Y., Wang, J., Xiao, Y., et al. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.894454 · Cited by 4

Macrophages in the dCLN are required for α-synuclein proteostasis in A53T PD model mice

Xu, L., Deng, J., Xiong, W., Li, L., & Liu, Z. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149692 · Cited by 3

Detection assays of mitochondrial permeability transition pore: Current status and future prospects

Hong, D., Huang, J., Hu, S., Zheng, Y., Wu, Y., Cao, Z., Yan, Z., Zhang, H., Feng, H., Wang, J., et al. (2025) · Acta Histochemica · doi:10.1016/j.acthis.2025.152278 · Cited by 3

LRRK2 and the fragile synapse: a molecular prelude to Parkinson’s disease?

Masotti, B., Tombesi, G., Parisiadou, L., & Greggio, E. (2025) · Biochemical Journal · doi:10.1042/bcj20253351 · Cited by 8

Systematic discovery of disease-modifying targets by prediction from knowledge graph-based AI model and experimental validation: Parkinson’s disease case

So, M. L., Park, S. J., Kim, D., Han, S., Koo, H. J., Kim, T., Shin, M.-G., & Lee, E. J. (2026) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.12.035 · Cited by 3

Behavioral screening defines the molecular Parkinsonism-related subgroups in Drosophila

Kaempf, N., Valadas, J. S., Robberechts, P., Schoovaerts, N., Praschberger, R., Ortega, A., Nachman, E., Ghezzi, L., Kilic, A., Chabot, D., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70303-8 · Cited by 20

Gut microbiota-derived succinate links proteostasis collapse to α-synuclein pathology and aging

Akbar, M., Yadav, S., Naseer, A., Hameed, R., Sarkar, A., & Nazir, A. (2026) · iScience · doi:10.1016/j.isci.2026.115941 · Cited by 3

Neurogenesis in neurodegenerative diseases in the adult human brain

Stępień, T. (2021) · Postepy psychiatrii neurologii · doi:10.5114/ppn.2021.111950 · Cited by 5

Aberrant Dopamine Homeostasis as a Focal Point in the Mechanism of Environmental Contaminant-Induced Dopaminergic Dysfunction

Cagle, B. S., Crawford, R. A., & Doorn, J. A. (2022) · Molecular and integrative toxicology · doi:10.1007/978-3-030-87451-3_3 · Cited by 3

Aberrant somatic calcium channel function in cNurr1 and LRRK2-G2019S mice

Skiteva, O., Yao, N., Mantas, I., Zhang, X., Perlmann, T., Svenningsson, P., & Chergui, K. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00500-5 · Cited by 3

SYNJ1 rescues motor functions in hereditary and sporadic Parkinson's disease mice by upregulating TSP-1 expression

Tian, Y., Yi, S., Guo, W., Feng, C., Zhang, X., Dong, H., Wang, K., Li, R., Tian, Y., Gan, M., et al. (2023) · Behavioural Brain Research · doi:10.1016/j.bbr.2023.114569 · Cited by 3

Glycation modulates glutamatergic signalling and exacerbates Parkinson’s disease-like phenotypesPreprint

Chegão, A., Guarda, M., Alexandre, B. M., Shvachiy, L., Temido‐Ferreira, M., Marques-Morgado, I., Gomes, B. F., Matthiesen, R., Lopes, L. V., Florindo, P. R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.24.457507 · Cited by 3

A Computational Approach Reveals the Ability of Amyloids to Sequester RNA: the Alpha Synuclein CasePreprint

Rupert, J., Monti, M. M., Zacco, E., & Tartaglia, G. G. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.20.508776 · Cited by 3

N-acetyl-l-leucine lowers pS129-synuclein and improves synaptic function in models of Parkinson’s diseasePreprint

Song, P., Franchini, R., Chen, C., Duong, B., Wang, Y., Savas, J. N., Parisiadou, L., & Krainc, D. (2025) · Research Square · doi:10.21203/rs.3.rs-6298077/v1 · Cited by 3

GRP94 mediates blood-brain barrier permeation and substantia nigra-specific drug distribution in Parkinson’s disease

Lv, Z., Zeng, Y., Lv, T., Liu, Q., & Han, L. (2025) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2025.114585 · Cited by 3

Gene Polymorphisms of Parkinson’s Disease Risk Locus and Idiopathic REM Sleep Behavior Disorder

Zhong, M., Jiao, Y., Zhao, A., Niu, M., Ran, J., Liu, J., & Li, Y. (2025) · Biomedicines · doi:10.3390/biomedicines13040788 · Cited by 2

High-frequency repetitive transcranial magnetic stimulation upregulates BDNF expression and promotes synaptogenesis in mouse models of Parkinson’s disease

Chen, D., Jiang, Y., Feng, G., Liu, X., Huang, Q., & Gong, Y. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.05.307 · Cited by 3

Dopamine neurotransmission in Parkinson's disease

Cramb, K. M. L., Noor, H., Wade-Martins, R., & Cragg, S. J. (2025) · Handbook of behavioral neuroscience · doi:10.1016/b978-0-443-21992-4.00012-9 · Cited by 2

Oxidative stress in neurodegeneration: from a simple insult to a dynamic regulator

Zhang, L., Zhai, X., Yan, Y., Xiang, L., Zhang, Y., Zhou, X., Cai, L., Tang, Z., & Xia, Y. (2026) · Redox Report · doi:10.1080/13510002.2026.2654906 · Cited by 3

DYRK1A and Parkinson’s disease, facts and hypotheses

Meijer, L., Lindberg, M. F., Hogrel, G., & Khor, B. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107379 · Cited by 2

A Proteome-Wide Effect of PHF8 Knockdown on Cortical Neurons Shows Downregulation of Parkinson’s Disease-Associated Protein Alpha-Synuclein and Its Interactors

Oey, N. E., Zhou, L., Chan, C. H. S., VanDongen, A. M. J., & Tan, E. K. (2023) · Biomedicines · doi:10.3390/biomedicines11020486 · 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

The Impact of 90 Parkinson’s Disease-Risk Single Nucleotide Polymorphisms on Urinary Bis(monoacylglycerol)phosphate Levels in the Prodromal and PD Cohorts

Fang, S., Lee, P. A. H., Wang, Z., & Zhao, B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042286 · Cited by 2

Probing molecular pathways: Illuminating the connection between COVID‐19 and Alzheimer's disease through the endocannabinoid system dynamics

Sun, Q., Gao, J., An, R., Wang, M., & Wang, Y. (2024) · Journal of Medical Virology · doi:10.1002/jmv.29590 · Cited by 2

Analysis of significance of mitochondrial dysfunction in the pathogenesis of diseases of the central nervous system

Соколик, Е. П., & Prozorova, G. O. (2022) · Neuroscience Research Notes · doi:10.31117/neuroscirn.v5i3.151 · Cited by 2

Endophilin A2 regulates B cell protein trafficking and humoral responsesPreprint

Malinova, D., Wasim, L., Engels, N., & Tolar, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.20.050419 · Cited by 2

Canagliflozin attenuates haloperidol-induced motor and spatial working memory deficits in mice: Evidence of its role in the treatment of Parkinson’s disease

Irokosu, E. S., Oladoja, F. A., Olayemi, S. O., & Ishola, I. O. (2024) · Pharmacological Research - Reports · doi:10.1016/j.prerep.2024.100025 · Cited by 1

Dynamic Molecular Changes in Brain, Lung, and Heart of Hamsters Infected With SARS‐CoV‐2: Insights From a Severe and Recovery Phase Model

Peng, W., Wei, X., Wu, Y., Shi, C., Liu, X., Wu, J., Yang, H., Rong, N., Zhao, B., Zhang, G., et al. (2025) · Journal of Medical Virology · doi:10.1002/jmv.70410 · Cited by 1

Roles of Glia in Synapse Nano-organization

Choi, Y., & Chung, W. (2026) · Advances in neurobiology · doi:10.1007/978-3-032-12594-1_11 · Cited by 1

APP E590D mutation increases generation of Aβ and Aη peptides and exacerbates tauopathy

Liu, T., Wetzel, L., Roy, D., Zhang, K., Zhu, Z., Kumaraguru, P., Gorthi, V., Jeon, H., Woo, J. A., & Kang, D. E. (2026) · npj Dementia · doi:10.1038/s44400-026-00069-9 · Cited by 1

Modeling Synaptic Maturation From Growth Cone to Synapse in Human Organoids

Øhlenschlæger, M. S., Criscuolo, L., Jensen, P., Sanchez, D. J. L.-D., Sutcliffe, M. A., Bhosale, S., Bogetofte, H., Tahir, M., Jakobsen, L. A., Pihl, M., et al. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70458 · Cited by 3

Organelle-Targeted Nanotherapeutics for Parkinson’s Disease: From Pathogenesis to Preclinical Strategies and Translational Challenges

Liu, M., Peng, Q., Zhai, H., Wu, Y., Ma, Z., Tang, Z., Ouyang, H., Chang, A., Cao, X., Xu, Y., et al. (2026) · International Journal of Nanomedicine · doi:10.2147/ijn.s607870 · Cited by 1

Herbal Neurotherapeutics for Cognitive Disorders: Integrative Mechanisms Linking Neurotransmitter Systems, Neurodegeneration, and the Gut-Brain Axis

Rahman, M., Akter, K., Rani, A., Park, M. N., & Kim, B. (2026) · Nutrients · doi:10.3390/nu18111796 · Cited by 2

The role of Th17 cells in the pathogenesis of Parkinson's disease: From immune dysregulation to neurodegeneration

Zhao, J., Liang, H., & Bi, Y. (2026) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2026.111990 · Cited by 1

Parkinson's disease gene prioritising using an efficient and biologically appropriate network-based consensus strategy

Kumari, B., & Dholaniya, P. S. (2022) · Journal of Computational Science · doi:10.1016/j.jocs.2022.101879 · Cited by 1

Protein–Protein Interactions in Neurodegenerative Diseases

Poluri, K. M., Gulati, K., Tripathi, D. K., & Nagar, N. (2023) · Springer eBooks · doi:10.1007/978-981-99-2423-3_3 · Cited by 2

STW-MD: a novel spatio-temporal weighting and multi-step decision tree method for considering spatial heterogeneity in brain gene expression data

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