The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Are ubiquitination pathways central to Parkinson’s disease?
Open accessAbstract
Parkinson's disease (PD) is the most common neurodegenerative movement disorder. The major motor disabilities of PD are associated with the extensive loss of dopaminergic neurons in the substantia nigra pars compacta. The physiological changes and biochemical pathways involved in the selective demise of these neurons are still unclear. Recent studies have demonstrated that alterations or reductions in ubiquitin-mediated proteasome function can be causal of at least some forms of parkinsonism, and multiple lines of evidence suggest that this mechanism of protein degradation may play an important role in the etiology of PD.
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“α-Synuclein is degraded by proteasomes [106,107], and phosphorylated α-synuclein is ubiquitinated in α-synucleinopathy lesions [108], indicating that the ubiquitin-proteasome system degrades phosphorylated synuclein.”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [107]
Citations
Cites
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Items 201–234 of 234
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Vps28 Implicated in a-Synuclein Pathobiology: Building Support for Lysosome-Mediated Degradation
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Ayala, A. (2010) · Eukaryon · Cited by 1
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Molecular Chaperones and the Ubiquitin–Proteasome System
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The effect of selected medicinal plants on rotenone-induced toxicity in SH-SY5Y neuroblastoma cells
Seoposengwe, K. (2013) · UpSpace Institutional Repository (University of Pretoria)
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a-Synuclein Causes Non-Specific Toxicity in vps34 Yeast
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Self-citationThe Elucidation of Hydrogen Sulfide Signalling Through Persulfidation
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Metadata
- Authors
- Giasson, B. I., & Lee, V. M.-Y.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Lee, Virginia M.-Y
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 114
- Issue
- 1
- Pages
- 1-8
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2171114341
- Cited by
- 234
- References
- 38
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 5 · 2020: 2 · 2019: 5 · 2018: 5 · 2017: 5 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 8 · 2012: 14
- FWCI
- 4.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3669 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Parkinson's disease, ubiquitination, ubiquitin-proteasome system, proteasome dysfunction, dopaminergic neuron loss, substantia nigra pars compacta, neurodegeneration, parkinsonism, protein degradation
- MeSH terms
- Animals, Cysteine Endopeptidases, Humans, Ligases, Multienzyme Complexes, Nerve Tissue Proteins, Neurons, Parkinson Disease, Substantia Nigra, Thiolester Hydrolases, Receptors, Endothelin, Ubiquitin, Drosophila Proteins, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Synucleins
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