The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation
Open accessAbstract
Parkinson's disease (PD) pathology is characterized by the degeneration of midbrain dopamine neurons (DNs) ultimately leading to a progressive movement disorder in patients. The etiology of DN loss in sporadic PD is unknown, although it is hypothesized that aberrant protein aggregation and cellular oxidative stress may promote DN degeneration. Homozygous mutations in DJ-1 were recently described in two families with autosomal recessive inherited PD (Bonifati et al. 2003). In a companion article (Martinat et al. 2004), we show that mutations in DJ-1 alter the cellular response to oxidative stress and proteasomal inhibition. Here we show that DJ-1 functions as a redox-sensitive molecular chaperone that is activated in an oxidative cytoplasmic environment. We further demonstrate that DJ-1 chaperone activity in vivo extends to alpha-synuclein, a protein implicated in PD pathogenesis.
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Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System
Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-Lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Verdugo, J. M. G., Armanini, M., Ryan, A., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)80886-7 · Cited by 1,722
Self-citationBeal, M. F. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00780-3 · Cited by 763
Cited by
Mitochondria in the aetiology and pathogenesis of Parkinson's disease
Schapira, A. H. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70327-7 · Cited by 883
Expanding insights of mitochondrial dysfunction in Parkinson's disease
Abou-Sleiman, P. M., Muqit, M. M. K., & Wood, N. W. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1868 · Cited by 869
Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
Henchcliffe, C., & Beal, M. F. (2008) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0924 · Cited by 783
Genetics in Parkinson disease: Mendelian versus non‐Mendelian inheritance
Hernandez, D. G., Reed, X., & Singleton, A. B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13593 · Cited by 448
“…of DJ-1 in dopamine neurotransmission and signaling, it has been reported to have multiple functions associated with PD pathogenesis, such as chaperone activity and the ability to inhibit a-synuclein aggregation, which is thought to be a key event in Lewy body formation (Shendelman et al. 2004).”
BackgroundMhyre, T. R., Boyd, J. T., Hamill, R. W., & Maguire-Zeiss, K. A. (2012) · Subcellular Biochemistry · doi:10.1007/978-94-007-5416-4_16 · Cited by 423
Metadata
- Authors
- Shendelman, S., Jonason, A., Martinat, C., Leete, T., & Abeliovich, A.
- Venue
- PLoS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2004-10-05
- Volume
- 2
- Issue
- 11
- Pages
- e362
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- OpenAlex
- W1967603366
- Cited by
- 590
- References
- 4
- FWCI
- 17.72
- Type
- journal article
- Language
- en
- Open access
- gold
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- Shendelman, S., Jonason, A., Martinat, C., Leete, T., & Abeliovich, A. (2004). DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation. PLoS Biology. https://doi.org/10.1371/journal.pbio.0020362
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
