Cited by 874Parkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and TherapyNuclear Receptors and Signaling

The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.

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

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Abstract

Human-derived neurons provide the answers: Pathways involved in energy metabolism and removal of cellular debris by lysosomes play an important role in protecting our brain from degeneration in Parkinson's disease. Burbulla et al. identified a toxic cascade of mitochondrial and lysosomal dysfunction in human neurons derived from patients with Parkinson's. The dysfunction was mediated by accumulation of oxidized dopamine and α-synuclein, but it was not found in Parkinson's mouse models, owing to species-specific differences in dopamine metabolism. Inherent species-specific differences between human and mouse neurons emphasize the value of studying human neurons to identify relevant targets for treatment of Parkinson's disease and related synucleinopathies. Science , this issue p. 1255

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Metadata

Authors
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., Savas, J. N., Kiskinis, E., Zhuang, X., Krüger, R., Surmeier, D. J., & Krainc, D.
Affiliations
  • Northwestern University (US)
  • University of Luxembourg (LU)
  • University of Chicago (US)
  • Centre Hospitalier de Luxembourg (LU)
Corresponding author
Krainc, Dimitri
Venue
Science
Published
2017-09-22
Volume
357
Issue
6357
Pages
1255-1261
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2752710053
Cited by
874
References
37
Citations by year
2026: 83 · 2025: 99 · 2024: 110 · 2023: 93 · 2022: 100 · 2021: 98 · 2020: 108 · 2019: 91 · 2018: 76 · 2017: 16
FWCI
54.93
Type
journal article
Language
en
Open access
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • Open Repository and Bibliography (University of Luxembourg) (submittedVersion)
  • DZNE Pub (submittedVersion)
Funders
  • NIH Office of the Director (award301003, R01NS076054, award301024, R00DC013805-02, award346646, T32NS041234, award346647, F32NS101778, award346648, R01NS092823)
  • IDP Foundation (award346545)
  • Michael J. Fox Foundation for Parkinson’s Research (award346546)
  • JPB Foundation (award346543)
  • NIH (award346544, NS047085)
  • German Academic Exchange Service (award301004)
  • Spinal Muscular Atrophy Foundation (award301007)
  • Les Turner ALS Foundation (award301005)
  • Target ALS (award301006)
Topics
  • Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Keywords
Parkinson's disease, dopamine oxidation, mitochondrial dysfunction, lysosomal dysfunction, dopaminergic neurons, substantia nigra, glucocerebrosidase, alpha-synuclein, oxidative stress, familial Parkinson's disease, neurodegeneration
MeSH terms
Protein Deglycase DJ-1, Animals, Antioxidants, Cell Line, Disease Models, Animal, Dopamine, Glucosylceramidase, Humans, Lysosomes, Melanins, Mesencephalon, Mitochondria, Oxidation-Reduction, Parkinson Disease, Substantia Nigra, Tacrolimus, Mice, Knockout, Oxidative Stress, Mice, alpha-Synuclein, Dopaminergic Neurons, Calcineurin Inhibitors

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