The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Proteomic identification of novel proteins associated with Lewy bodies
Open accessAbstract
The manifestation of Lewy bodies (LB) in the brain is a hallmark of Parkinson's disease. Here, we present a comprehensive analysis of protein elements in Lewy bodies by comparative mass spectrometry. Cortical LB inclusions were enriched by sucrose gradient centrifugation from postmortem brains, and a negative control sample was prepared from specimen without LB pathology. Whereas approximately 550 proteins were identified in the LB-enriched sample by mass spectrometry, quantitative comparison with the control sample revealed that approximately 40 proteins were co-enriched with alpha-synuclein, the major component in Lewy bodies. As expected, the list of proteins included previously reported constituents, such as those involved in protein folding, membrane trafficking and oxidative stress. More interestingly, we discovered in the LB-enriched sample several kinases (MAPKK1/MEK1, protein kinase C, and doublecortin-like kinase), a novel deubiquitinating enzyme (otubain 1), and numerous ubiquitin ligases (KPC and SCF). The proteomic studies provide enzyme candidates to investigate the regulation of alpha-synuclein and/or other LB proteins, which may contribute to the formation of Lewy bodies and the toxicity of alpha-synuclein in the related neurodegenerative disorders.
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Mass spectrometry-based proteomics
Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955
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Phosphorylated α-Synuclein Is Ubiquitinated in α-Synucleinopathy Lesions
Hasegawa, M., Fujiwara, H., Nonaka, T., Wakabayashi, K., Takahashi, H., Lee, V. M.-Y., Trojanowski, J. Q., Mann, D., & Iwatsubo, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208046200 · Cited by 428
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The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Mahul-Mellier, A.-L., Burtscher, J., Maharjan, N., Weerens, L., Croisier, M., Kuttler, F., Leleu, M., Knott, G. W., & Lashuel, H. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913904117 · Cited by 710
Widespread protein aggregation as an inherent part of aging in C. elegans
David, D. C., Ollikainen, N., Trinidad, J. C., Cary, M. P., Burlingame, A. L., & Kenyon, C. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000450 · Cited by 627
Lee, W.-H., Loo, C.-Y., Bebawy, M., Luk, F., Mason, R., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 537
Parkinson’s Disease: Etiology, Neuropathology, and Pathogenesis
John van Geest Centre for Brain Repair, D. O. C. N., Kouli, A., Torsney, K. M., Department of Medicine for the Elderly, C. U. H. N. F. T., Clinical Gerontology Unit, D. O. P. H. A. P. C., Kuan, W.-L., & John van Geest Centre for Brain Repair, D. O. C. N. (2018) · Parkinson’s Disease: Pathogenesis and Clinical Aspects · doi:10.15586/codonpublications.parkinsonsdisease.2018.ch1 · Cited by 507
Metadata
- Authors
- Xia, Q.
- Venue
- Frontiers in Bioscience
- Publisher
- IMR Press
- Published
- 2008
- Volume
- Volume
- Issue
- 13
- Pages
- 3850
- ISSN
- 1093-4715 (ISSN-L)
- 1093-9946
- DOI
- 10.2741/2973
- OpenAlex
- W2069537999
- Cited by
- 176
- References
- 5
- FWCI
- 4.52
- Type
- journal article
- Language
- en
- Open access
- bronze
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