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

Induction of Pluripotent Stem Cells from Adult Human Fibroblasts by Defined Factors

Takahashi, K., Tanabe, K., Ohnuki, M., Narita, M., Ichisaka, T., Tomoda, K., & Yamanaka, S. (2007) · Cell · doi:10.1016/j.cell.2007.11.019 · Cited by 20,221

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

Eng, J. K., McCormack, A. L., & Yates, J. R. (1994) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(94)80016-2 · Cited by 6,484

Parkinson's disease

Kalia, L. V., & Lang, A. E. (2015) · The Lancet · doi:10.1016/s0140-6736(14)61393-3 · Cited by 6,184

Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry

Elias, J. E., & Gygi, S. P. (2007) · Nature Methods · doi:10.1038/nmeth1019 · Cited by 3,925

Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism

Bonifati, V., Rizzu, P., van Baren, M. J., Schaap, O., Breedveld, G. J., Krieger, E., Dekker, M. C. J., Squitieri, F., Ibáñez, P., Joosse, M., et al. (2003) · Science · doi:10.1126/science.1077209 · Cited by 2,854

The mechanism of action of cyclosporin A and FK506

Schreiber, S. L., & Crabtree, G. R. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90111-j · Cited by 2,127

Dopamine neurons derived from human ES cells efficiently engraft in animal models of Parkinson’s disease

Kriks, S., Shim, J., Piao, J., Ganat, Y. M., Wakeman, D. R., Xie, Z., Carrillo‐Reid, L., Auyeung, G., Antonacci, C. L., Buch, A., et al. (2011) · Nature · doi:10.1038/nature10648 · Cited by 1,951

Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies

Mazzulli, J. R., Xu, Y.-H., Sun, Y., Knight, A. L., McLean, P. J., Caldwell, G. A., Sidransky, E., Grabowski, G. A., & Krainc, D. (2011) · Cell · doi:10.1016/j.cell.2011.06.001 · Cited by 1,341

Efficient generation of midbrain and hindbrain neurons from mouse embryonic stem cells

Lee, S., Lumelsky, N. L., Studer, L., Auerbach, J. M., & McKay, R. D. G. (2000) · Nature Biotechnology · doi:10.1038/76536 · Cited by 1,261

Selective neuronal vulnerability in Parkinson disease

Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,116

Dysregulated Interorganellar Crosstalk of Mitochondria in the Pathogenesis of Parkinson’s Disease

Sironi, L., Restelli, L. M., Tolnay, M., Neutzner, A., & Frank, S. (2020) · Cells · doi:10.3390/cells9010233 · Cited by 56

Enhanced tyrosine hydroxylase activity induces oxidative stress, causes accumulation of autotoxic catecholamine metabolites, and augments amphetamine effects in vivo

Vecchio, L. M., Sullivan, P., Dunn, A. R., Bermejo, M. K., Fu, R., Masoud, S. T., Gregersen, E., Urs, N. M., Nazari, R., Jensen, P. H., et al. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15432 · Cited by 56

Lysosomal Ion Channels: What Are They Good For and Are They Druggable Targets?

Riederer, E. A., Cang, C., & Ren, D. (2022) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-051921-013755 · Cited by 58

The role of tyrosine hydroxylase as a key player in neuromelanin synthesis and the association of neuromelanin with Parkinson’s disease

Nagatsu, T., Nakashima, A., Watanabe, H., Ito, S., Wakamatsu, K., Zucca, F. A., Zecca, L., Youdim, M. B. H., Wulf, M., Riederer, P. F., et al. (2023) · Journal of Neural Transmission · doi:10.1007/s00702-023-02617-6 · Cited by 57

Parkinson’s disease neurons exhibit alterations in mitochondrial quality control proteins

Chen, C., McDonald, D., Blain, A. P., Mossman, E., Atkin, K., Marusich, M. F., Capaldi, R., Bone, L., Smith, A., Filby, A. J., et al. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00564-3 · Cited by 61

Mitochondrial Dysfunction Combined with High Calcium Load Leads to Impaired Antioxidant Defense Underlying the Selective Loss of Nigral Dopaminergic Neurons

Ricke, K. M., Paß, T., Kimoloi, S., Fährmann, K., Jüngst, C., Schauss, A. C., Baris, O. R., Croon, M., Trifunović, A., Faelker, T. M. E., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1345-19.2019 · Cited by 57

PARK7/DJ-1 promotes pyruvate dehydrogenase activity and maintains Treg homeostasis during ageing

Danileviciute, E., Zeng, N., Capelle, C., Paczia, N., Gillespie, M. A. K., Kurniawan, H., Benzarti, M., Merz, M. P., Coowar, D., Fritah, S., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00576-y · Cited by 56

Nanoscale monitoring of mitochondria and lysosome interactions for drug screening and discovery

Chen, Q., Shao, X., Tian, Z., Chen, Y., Mondal, P., Liu, F., Wang, F., Ling, P., He, W., Zhang, K., et al. (2019) · Nano Research · doi:10.1007/s12274-019-2331-x · Cited by 54

The Role of Lysosomes in a Broad Disease-Modifying Approach Evaluated across Transgenic Mouse Models of Alzheimer’s Disease and Parkinson’s Disease and Models of Mild Cognitive Impairment

Hwang, J., Estick, C., Ikonne, U. S., Butler, D., Pait, M. C., Elliott, L. H., Ruiz, S., Smith, K., Rentschler, K. M., Mundell, C. T., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184432 · Cited by 55

Roflupram exerts neuroprotection via activation of CREB/PGC‐1α signalling in experimental models of Parkinson's disease

Zhong, J., Dong, W., Qin, Y., Xie, J., Xiao, J., Xu, J., & Wang, H. (2020) · British Journal of Pharmacology · doi:10.1111/bph.14983 · Cited by 55

PM2.5 exposure triggers cell death through lysosomal membrane permeabilization and leads to ferroptosis insensitivity via the autophagy dysfunction/p62-KEAP1-NRF2 activation in neuronal cells

Wei, M., Bao, G., Li, S., Yang, Z., Cheng, C., & Le, W. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.114333 · Cited by 55

Discovery of coumarin Mannich base derivatives as multifunctional agents against monoamine oxidase B and neuroinflammation for the treatment of Parkinson's disease

Tao, D., Wang, Y., Bao, X.-Q., Yang, B., Gao, F., Wang, L., Zhang, D., & Li, L. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.04.016 · Cited by 54

Biodegradable PLGA Nanoparticles Restore Lysosomal Acidity and Protect Neural PC-12 Cells against Mitochondrial Toxicity

Zeng, J., Martin, A., Han, X., Shirihai, O. S., & Grinstaff, M. W. (2019) · Industrial & Engineering Chemistry Research · doi:10.1021/acs.iecr.9b02003 · Cited by 56

Catalytic‐Enhanced Lactoferrin‐Functionalized Au‐Bi2Se3 Nanodots for Parkinson's Disease Therapy via Reactive Oxygen Attenuation and Mitochondrial Protection

Li, L., Lu, Y., Xu, X., Yang, X., Chen, L., Jiang, C., Wang, Y., Hu, W., Wei, X., & Yang, Z. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202100316 · Cited by 54

Involvement of Mitochondria in Parkinson’s Disease

Choong, C., & Mochizuki, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242317027 · Cited by 58

HSP90-incorporating chaperome networks as biosensor for disease-related pathways in patient-specific midbrain dopamine neurons

Kishinevsky, S., Wang, T., Rodina, A., Chung, S. Y., Xu, C., Philip, J., Taldone, T., Joshi, S., Alpaugh, M. L., Bolaender, A., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06486-6 · Cited by 53

Vascular Dysfunction Induced by Mercury Exposure

Takahashi, T., & Shimohata, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102435 · Cited by 54

Acquired dysregulation of dopamine homeostasis reproduces features of Parkinson’s disease

Bucher, M. L., Barrett, C. W., Moon, C., Mortimer, A. D., Burton, E. A., Greenamyre, J. T., & Hastings, T. G. (2020) · npj Parkinson s Disease · doi:10.1038/s41531-020-00134-x · Cited by 55

Recent Advances in In Vivo Neurochemical Monitoring

Tan, C., Robbins, E. M., Wu, B., & Cui, X. T. (2021) · Micromachines · doi:10.3390/mi12020208 · Cited by 57

Icaritin Provides Neuroprotection in Parkinson’s Disease by Attenuating Neuroinflammation, Oxidative Stress, and Energy Deficiency

Wu, H., Liu, X., Gao, Z., Lin, M. S., Zhao, X. S., Sun, Y. X., & Pu, X. (2021) · Antioxidants · doi:10.3390/antiox10040529 · Cited by 53

The Membrane Interactions of Synuclein: Physiology and Pathology

Runwal, G., & Edwards, R. H. (2021) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-031920-092547 · Cited by 57

The Catecholaldehyde Hypothesis for the Pathogenesis of Catecholaminergic Neurodegeneration: What We Know and What We Do Not Know

Goldstein, D. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115999 · Cited by 53

Altered neural cell junctions and ion-channels leading to disrupted neuron communication in Parkinson’s disease

Choudhury, S. P., Bano, S., Sen, S., Suchal, K., Kumar, S., Nikolajeff, F., Dey, S. K., & Sharma, V. (2022) · npj Parkinson's Disease · doi:10.1038/s41531-022-00324-9 · Cited by 52

Efficient Polysulfide‐Based Nanotheranostics for Triple‐Negative Breast Cancer: Ratiometric Photoacoustics Monitored Tumor Microenvironment‐Initiated H2S Therapy

Li, J., Li, X., Yuan, Y. H., Wang, Q., Xie, L., Dai, Y., Wang, W., Li, L., Lü, X., Fan, Q., et al. (2020) · Small · doi:10.1002/smll.202002939 · Cited by 52

Detecting Oxidative Stress Biomarkers in Neurodegenerative Disease Models and Patients

Sidorova, Y. A., & Domanskyi, A. (2020) · Methods and Protocols · doi:10.3390/mps3040066 · Cited by 50

Therapeutic targeting of mitophagy in Parkinson's disease

Masaldan, S., Callegari, S., & Dewson, G. (2022) · Biochemical Society Transactions · doi:10.1042/bst20211107 · Cited by 56

Systems level analysis of sex-dependent gene expression changes in Parkinson’s disease

Tranchevent, L.-C., Halder, R., & Glaab, E. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00446-8 · Cited by 50

Neuronal Senescence in the Aged Brain

Chou, S.-M., Yen, Y., Yuan, F., Zhang, S., & Chong, C. (2023) · Aging and Disease · doi:10.14336/ad.2023.0214 · Cited by 56

Implantable Electrochemical Microsensors for In Vivo Monitoring of Animal Physiological Information

Zhou, J., Zhou, S., Fan, P., Li, X., Ying, Y. B., Ping, J. F., & Pan, Y. (2023) · Nano-Micro Letters · doi:10.1007/s40820-023-01274-4 · Cited by 60

Similarity and Differences in Inflammation-Related Characteristics of the Peripheral Immune System of Patients with Parkinson’s and Alzheimer’s Diseases

Boyko, A., Troyanova, N. I., Kovalenko, E. I., & Sapozhnikov, A. M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122633 · Cited by 54

Toxic Feedback Loop Involving Iron, Reactive Oxygen Species, α-Synuclein and Neuromelanin in Parkinson’s Disease and Intervention with Turmeric

van Rensburg, Z. J., Abrahams, S., Bardien, S., & Kenyon, C. P. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02516-5 · Cited by 52

A Proposed Mechanism for Neurodegeneration in Movement Disorders Characterized by Metal Dyshomeostasis and Oxidative Stress

Trist, B. G., Hare, D. J., & Double, K. L. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.05.004 · Cited by 51

New insights of poly(ADP-ribosylation) in neurodegenerative diseases: A focus on protein phase separation and pathologic aggregation

Liu, C., & Fang, Y. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.04.028 · Cited by 50

Gelator Length Precisely Tunes Supramolecular Hydrogel Stiffness and Neuronal Phenotype in 3D Culture

Godbe, J. M., Freeman, R., Burbulla, L. F., Lewis, J. A., Krainc, D., & Stupp, S. I. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.9b01585 · Cited by 51

Mitochondrial Homeostasis and Signaling in Parkinson’s Disease

Scorziello, A., Borzacchiello, D., Sisalli, M. J., Martino, R. D., Morelli, M., & Feliciello, A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00100 · Cited by 50

Understanding LRRK2 kinase activity in preclinical models and human subjects through quantitative analysis of LRRK2 and pT73 Rab10

Wang, X., Negrou, E., Maloney, M. T., Bondar, V. V., Andrews, S. V., Montalban, M., Llapashtica, C., Maciuca, R. D., Nguyen, H. N., Solanoy, H. O., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-91943-4 · Cited by 50

Fucoidan from Fucus vesiculosus prevents the loss of dopaminergic neurons by alleviating mitochondrial dysfunction through targeting ATP5F1a

Xing, M., Li, G., Liu, Y., Yang, L., Zhang, Y., Zhang, Y., Ding, J., Lu, M., Yu, G., & Hu, G. (2022) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2022.120470 · Cited by 51

Parkinson's disease: Is it a consequence of human brain evolution?

Diederich, N. J., Surmeier, D. J., Uchihara, T., Grillner, S. E., & Goetz, C. G. (2019) · Movement Disorders · doi:10.1002/mds.27628 · Cited by 48

Neuroprotective and Neurotherapeutic Effects of Tetrahedral Framework Nucleic Acids on Parkinson’s Disease in Vitro

Cui, W., Zhan, Y., Shao, X., Fu, W., Xiao, D., Zhu, J., Qin, X., Zhang, T., Zhang, M., Zhou, Y., et al. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b10308 · Cited by 49

The interplay between Glucocerebrosidase, α-synuclein and lipids in human models of Parkinson’s disease

Muñoz, S. S., Petersen, D., Marlet, F. R., Kücükköse, E., & Galvagnion, C. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106534 · Cited by 49

The Role of Oxygen Homeostasis and the HIF-1 Factor in the Development of Neurodegeneration

Mitroshina, E. V., & Vedunova, M. V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094581 · Cited by 48

Ferroptosis as a New Mechanism in Parkinson’s Disease Therapy Using Traditional Chinese Medicine

Wu, L., Liu, M., Liang, J., Li, N., Yang, D., Cai, J., Zhang, Y., He, Y. Z., Chen, Z., & Ma, T. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.659584 · Cited by 50

CNTNAP4 deficiency in dopaminergic neurons initiates parkinsonian phenotypes

Zhang, W., Zhou, M., Lu, W., Gong, J., Gao, F., Li, Y., Xu, X., Lin, Y., Zhang, X., Ding, L., et al. (2020) · Theranostics · doi:10.7150/thno.40798 · Cited by 49

Standpoints in mitochondrial dysfunction: Underlying mechanisms in search of therapeutic strategies

Videla, L. A., Mariman, A. P., Ramos, B., Silva, M. J., & del Campo, A. (2022) · Mitochondrion · doi:10.1016/j.mito.2021.12.006 · Cited by 54

Advancing preclinical models of psychiatric disorders with human brain organoid cultures

Dixon, T. A., & Muotri, A. R. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01708-2 · Cited by 49

Cell biology of Parkinson's disease: Mechanisms of synaptic, lysosomal, and mitochondrial dysfunction

Brooker, S. M., Naylor, G. E., & Krainc, D. (2024) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2024.102841 · Cited by 47

Cell-Penetrating Peptides: Promising Therapeutics and Drug-Delivery Systems for Neurodegenerative Diseases

Pirhaghi, M., Mamashli, F., Moosavi-Movahedi, F., Arghavani, P., Amiri, A., Davaeil, B., Mohammad-Zaheri, M., Mousavi-Jarrahi, Z., Sharma, D., Langel, Ü., et al. (2024) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c01167 · Cited by 47

Combining Automated Organoid Workflows with Artificial Intelligence‐Based Analyses: Opportunities to Build a New Generation of Interdisciplinary High‐Throughput Screens for Parkinson's Disease and Beyond

Renner, H., Schöler, H. R., & Bruder, J. M. (2021) · Movement Disorders · doi:10.1002/mds.28775 · Cited by 47

From mitochondrial dysfunction to neuroinflammation in Parkinson’s disease: Pathogenesis and mitochondrial therapeutic approaches

Ebadpour, N., Mahmoudi, M., Kheder, R. K., Abavisani, M., Baridjavadi, Z., Abdollahi, N., & Esmaeili, S. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113015 · Cited by 48

Inflammasomes: An Emerging Mechanism Translating Environmental Toxicant Exposure Into Neuroinflammation in Parkinson’s Disease

Anderson, F. L., Coffey, M., Berwin, B. L., & Havrda, M. C. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy219 · Cited by 48

Iron Dysregulation in Parkinson’s Disease: Focused on the Autophagy–Lysosome Pathway

Chen, L., Huang, Y., Cui, J., Song, N., & Xie, J. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00390 · Cited by 47

The potential roles of dopamine in traumatic brain injury: a preclinical and clinical update.

Lan, Y., Li, S., Lou, J., Ma, X., & Zhang, B. (2019) · PubMed Central · Cited by 47

In situ formation of (001)TiO2/Ti3C2 heterojunctions for enhanced photoelectrochemical detection of dopamine

Chen, Y., Li, X., Cai, G., Li, M., & Tang, D. (2021) · Electrochemistry Communications · doi:10.1016/j.elecom.2021.106987 · Cited by 46

β-Synuclein: An Enigmatic Protein with Diverse Functionality

Hayashi, J., & Carver, J. A. (2022) · Biomolecules · doi:10.3390/biom12010142 · Cited by 50

Medicinal Chemistry and Chemical Biology of Nurr1 Modulators: An Emerging Strategy in Neurodegeneration

Willems, S., & Merk, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00585 · Cited by 46

Photoactive Nanomaterials for Wireless Neural Biomimetics, Stimulation, and Regeneration

Zhao, D. S., Huang, R., Gan, J.-M., & Shen, Q. (2022) · ACS Nano · doi:10.1021/acsnano.2c08543 · Cited by 45

Research progress in the molecular mechanism of ferroptosis in Parkinson's disease and regulation by natural plant products

Yang, K., Zeng, L., Zeng, J., Deng, Y., Wang, S., Xu, H., He, Q., Yuan, M., Luo, Y., Ge, A., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102063 · Cited by 46

Kinetic Modeling of pH-Dependent Oxidation of Dopamine by Iron and Its Relevance to Parkinson's Disease

Sun, Y., Pham, A. N., Hare, D. J., & Waite, T. D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00859 · Cited by 47

Evaluation of Strategies for Measuring Lysosomal Glucocerebrosidase Activity

Ysselstein, D., Young, T. J., Nguyen, M. N., Padmanabhan, S., Hirst, W. D., Dzamko, N. L., & Krainc, D. (2021) · Movement Disorders · doi:10.1002/mds.28815 · Cited by 42

Molecular heterogeneity in the substantia nigra: A roadmap for understanding PD motor pathophysiology

Gaertner, Z. A., Azcorra, M., Dombeck, D. A., & Awatramani, R. B. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105925 · Cited by 45

The effects of bioactive components from the rhizome of gastrodia elata blume (Tianma) on the characteristics of Parkinson’s disease

Lu, C., Qu, S., Zhong, Z., Luo, H., Lei, S. S., Zhong, H., Su, H., Wang, Y., & Chong, C. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.963327 · Cited by 43

The interplay between α-Synuclein and NLRP3 inflammasome in Parkinson's disease

Huang, Q., Yang, P., Liu, Y., Ding, J., Lu, M., & Hu, G. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115735 · Cited by 45

Astroglial DJ-1 over-expression up-regulates proteins involved in redox regulation and is neuroprotective in vivo

Frøyset, A. K., Edson, A. J., Gharbi, N., Khan, E. A., Dondorp, D. C., Bai, Q., Tiraboschi, E., Suster, M. L., Connolly, J. B., Burton, E. A., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.02.010 · Cited by 43

Impaired cellular bioenergetics caused by GBA1 depletion sensitizes neurons to calcium overload

Plotegher, N., Perocheau, D. P. B., Ferrazza, R., Massaro, G., Bhosale, G., Zambon, F., Rahim, A. A., Guella, G., Waddington, S. N., Szabadkai, G., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0442-2 · Cited by 41

Neurobehavioral changes arising from early life dopamine signaling perturbations

Areal, L. B., & Blakely, R. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104747 · Cited by 45

DOPAL initiates αSynuclein-dependent impaired proteostasis and degeneration of neuronal projections in Parkinson’s disease

Masato, A., Plotegher, N., Terrin, F., Sandre, M., Faustini, G., Thor, A., Adams, S., Berti, G., Cogo, S., Lazzari, F. D., et al. (2023) · npj Parkinson s Disease · doi:10.1038/s41531-023-00485-1 · Cited by 49

Multi-omic insights into Parkinson's Disease: From genetic associations to functional mechanisms

Schilder, B. M., Navarro, E., & Raj, T. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105580 · Cited by 44

Age-related endolysosome dysfunction in the rat urothelium

Truschel, S. T., Clayton, D. R., Beckel, J. M., Yabes, J. G., Yao, Y., Wolf‐Johnston, A., Birder, L. A., & Apodaca, G. L. (2018) · PLoS ONE · doi:10.1371/journal.pone.0198817 · Cited by 46

Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity

Daniels, M. J., Nourse, J. B., Kim, H., Sainati, V., Schiavina, M., Murrali, M. G., Pan, B., Ferrie, J. J., Haney, C. M., Moons, R., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-39480-z · Cited by 42

Glial α‐synuclein promotes neurodegeneration characterized by a distinct transcriptional program in vivo

Olsen, A. L., & Feany, M. Β. (2019) · Glia · doi:10.1002/glia.23671 · Cited by 45

Patient-Derived Midbrain Organoids to Explore the Molecular Basis of Parkinson's Disease

Galet, B., Cheval, H., & Ravassard, P. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.01005 · Cited by 47

Inhibition of the dopamine transporter promotes lysosome biogenesis and ameliorates Alzheimer's disease–like symptoms in mice

Yin, L., Zhou, J., Li, T., Wang, X., Xue, W., Zhang, J., Lin, L., Wang, N., Kang, X., Zhou, Y., et al. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12776 · Cited by 43

Modeling Parkinson’s Disease Using Patient-specific Induced Pluripotent Stem Cells

Li, H., Jiang, H., Zhang, B., & Feng, J. (2018) · Journal of Parkinson s Disease · doi:10.3233/jpd-181353 · Cited by 44

Foods with Potential Prooxidant and Antioxidant Effects Involved in Parkinson’s Disease

Miranda‐Díaz, A. G., García-Sánchez, A., & Cardona-Muñóz, E. G. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6281454 · Cited by 46

Mitochondrial dysfunction in neurodegenerative diseases: A focus on iPSC-derived neuronal models

Trombetta-Lima, M., Sabogal-Guáqueta, A. M., & Dolga, A. M. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102362 · Cited by 42

N-Acetyl-Cysteine: Modulating the Cysteine Redox Proteome in Neurodegenerative Diseases

Martínez, M. (2022) · Antioxidants · doi:10.3390/antiox11020416 · Cited by 46

Emerging links between pediatric lysosomal storage diseases and adult parkinsonism

Ysselstein, D., Shulman, J. M., & Krainc, D. (2019) · Movement Disorders · doi:10.1002/mds.27631 · Cited by 41

Organoid and pluripotent stem cells in Parkinson’s disease modeling: an expert view on their value to drug discovery

Marotta, N., Kim, S., & Krainc, D. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1703671 · Cited by 40

The Evolution-Driven Signature of Parkinson’s Disease

Diederich, N. J., Uchihara, T., Grillner, S. E., & Goetz, C. G. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.05.001 · Cited by 39

Nanomedicine in the Face of Parkinson’s Disease: From Drug Delivery Systems to Nanozymes

Padilla-Godínez, F. J., Ruiz-Ortega, L. I., & Guerra‐Crespo, M. (2022) · Cells · doi:10.3390/cells11213445 · Cited by 40

Loss of DJ-1 function contributes to Parkinson’s disease pathogenesis in mice via RACK1-mediated PKC activation and MAO-B upregulation

Liu, L.-L., Han, Y., Zhang, Z., Wang, Y., Hu, Y., Kaznacheyeva, E. V., Ding, J., Guo, D., Wang, G., Li, B., et al. (2023) · Acta Pharmacologica Sinica · doi:10.1038/s41401-023-01104-8 · Cited by 39

Implications and progression of peroxiredoxin 2 (PRDX2) in various human diseases

Balasubramanian, P., Vijayarangam, V., Deviparasakthi, M. K. G., Palaniyandi, T., Ravi, M., Natarajan, S., Viswanathan, S., Baskar, G., Wahab, M. R. A., & Surendran, H. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.155080 · Cited by 40

Neurochemicals, Behaviours and Psychiatric Perspectives of Neurological Diseases

Choudhury, A., Sahu, T., Ramanujam, P. L., Banerjee, A. K., Chakraborty, I., Arun Kumar, R., & Arora, N. (2018) · Neuropsychiatry · doi:10.4172/neuropsychiatry.1000361 · Cited by 41

3,4-Dihydroxyphenylacetaldehyde Is More Efficient than Dopamine in Oligomerizing and Quinonizing α-Synuclein

Jinsmaa, Y., Isonaka, R., Sharabi, Y., & Goldstein, D. S. (2019) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.119.262246 · Cited by 39

Demonstration of brain region-specific neuronal vulnerability in human iPSC-based model of familial Parkinson’s disease

Brazdis, R.-M., Alecu, J. E., Marsch, D., Dahms, A., Simmnacher, K., Lörentz, S., Brendler, A., Schneider, Y., Marxreiter, F., Roybon, L., et al. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa039 · Cited by 37

Dopaminergic Axons: Key Recitalists in Parkinson’s Disease

Mishra, A. K., & Dixit, A. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03464-1 · Cited by 37

Effects of Peroxiredoxin 2 in Neurological Disorders: A Review of its Molecular Mechanisms

Liu, J., Su, G., Gao, J., Tian, Y., Liu, X., & Zhang, Z. (2020) · Neurochemical Research · doi:10.1007/s11064-020-02971-x · Cited by 38

Long-term running exercise alleviates cognitive dysfunction in APP/PSEN1 transgenic mice via enhancing brain lysosomal function

Wang, X., Zhu, Y., Zhu, Y., Sun, Y.-L., Huang, J., Li, Z., Wang, Y., Wu, J., Qin, Z., & Lin, F. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00720-6 · Cited by 40

In vivo reduction of age-dependent neuromelanin accumulation mitigates features of Parkinson’s disease

González-Sepúlveda, M., Compte, J., Cuadros, T., Nicolau, A., Guillard-Sirieix, C., Peñuelas, N., Picón, M. L., Parent, A., Romero‐Giménez, J., Cladera-Sastre, J. M., et al. (2022) · Brain · doi:10.1093/brain/awac445 · Cited by 38

Plant Secondary Metabolites as Modulators of Mitochondrial Health: An Overview of Their Anti-Oxidant, Anti-Apoptotic, and Mitophagic Mechanisms

Anchimowicz, J., Zielonka, P., & Jakieła, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26010380 · Cited by 39

Aminochrome Induces Irreversible Mitochondrial Dysfunction by Inducing Autophagy Dysfunction in Parkinson's Disease

Segura‐Aguilar, J., & Huenchuguala, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00106 · Cited by 38

N-glycome of the Lysosomal Glycocalyx is Altered in Niemann-Pick Type C Disease (NPC) Model Cells

Košiček, M., Gudelj, I., Horvatić, A., Jovic, T., Vučković, F., Lauc, G., & Hecimovic, S. K. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000129 · Cited by 38

Chaperone-mediated autophagy as a therapeutic target for Parkinson disease

Campbell, P., Morris, H. R., & Schapira, A. H. V. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1517156 · Cited by 39

l ‐3,4‐dihydroxyphenylalanine ( l ‐DOPA) modulates brain iron, dopaminergic neurodegeneration and motor dysfunction in iron overload and mutant alpha‐synuclein mouse models of Parkinson's disease

Billings, J. L., Gordon, S. L., Rawling, T., Doble, P., Bush, A. I., Adlard, P. A., Finkelstein, D. I., & Hare, D. J. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14676 · Cited by 38

α-Synuclein aggregation and transmission in Parkinson’s disease: a link to mitochondria and lysosome

Wang, R., Sun, H., Ren, H., & Wang, G. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1756-9 · Cited by 38

Simplified Brain Organoids for Rapid and Robust Modeling of Brain Disease

Ha, J., Kang, J. S., Lee, M., Baek, A., Kim, S., Chung, S., Lee, M., & Kim, J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.594090 · Cited by 40

Interaction of Neuromelanin with Xenobiotics and Consequences for Neurodegeneration; Promising Experimental Models

Capucciati, A., Zucca, F. A., Monzani, E., Zecca, L., Casella, L., & Hofer, T. (2021) · Antioxidants · doi:10.3390/antiox10060824 · Cited by 36

Cellular alterations identified in pluripotent stem cell-derived midbrain spheroids generated from a female patient with progressive external ophthalmoplegia and parkinsonism who carries a novel variation (p.Q811R) in the POLG1 gene

Chumarina, M., Russ, K., Azevedo, C., Heuer, A., Pihl, M., Collin, A., Frostner, E. Å., Elmér, E., Hyttel, P., Cappelletti, G., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0863-7 · Cited by 38

The contribution of Parkin, PINK1 and DJ‐1 genes to selective neuronal degeneration in Parkinson's disease

van der Vlag, M., Havekes, R., & Heckman, P. R. A. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14689 · Cited by 37

Modelling Parkinson’s Disease: iPSCs towards Better Understanding of Human Pathology

Avazzadeh, S., Baena-Montes, J. M., Keighron, C. N., Sánchez, Y. F., & Quinlan, L. R. (2021) · Brain Sciences · doi:10.3390/brainsci11030373 · Cited by 38

Dopamine oxidation mediates a human-specific cascade of 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 · Cited by 3

The role of dopamine oxidation in mitochondrial dysfunction: implications for Parkinson’s disease

Hastings, T. G. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9257-z · Cited by 199

The Convergence of Alpha-Synuclein, Mitochondrial, and Lysosomal Pathways in Vulnerability of Midbrain Dopaminergic Neurons in Parkinson’s Disease

Minakaki, G., Krainc, D., & Burbulla, L. F. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.580634 · Cited by 87

Dopamine Oxidation and Parkinson’s Disease

Barrett, C. W., Bucher, M. L., & Hastings, T. G. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622888-00116 · Cited by 1

Toxic effects of the oxidized products of the neurotransmitter dopamine on mitochondria and their implications in Parkinson's disease

Arduini, I. (2008) · Padua Research Archive (University of Padova)