The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
SIRT1 Protects against α-Synuclein Aggregation by Activating Molecular Chaperones
Open accessAbstract
α-Synuclein is a key molecule in the pathogenesis of synucleinopathy including dementia with Lewy bodies, Parkinson's disease, and multiple system atrophy. Sirtuins are NAD + -dependent protein deacetylases that are highly conserved and counter aging in lower organisms. We show that the life span of a mouse model with A53T α-synuclein mutation is increased by overexpressing SIRT1 and decreased by knocking out SIRT1 in brain. Furthermore, α-synuclein aggregates are reduced in the brains of mice with SIRT1 overexpression and increased by SIRT1 deletion. We show that SIRT1 deacetylates HSF1 (heat shock factor 1) and increases HSP70 RNA and protein levels, but only in the brains of mice with A53T and SIRT1 expression. Thus, SIRT1 responds to α-synuclein aggregation-induced stress by activating molecular chaperones to protect against disease.
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Cites
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
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Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration
Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060
Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy
Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949
Arima, K., Uéda, K., Sunohara, N., Arakawa, K., Hirai, S., Nakamura, M., Tonozuka-Uehara, H., & Kawai, M. (1998) · Acta Neuropathologica · doi:10.1007/s004010050917 · Cited by 239
Cited by
NAD+ and sirtuins in aging and disease
Imai, S.-I., & Guarente, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.002 · Cited by 1,481
Self-citationMitochondrial Dysfunction in Neurodegenerative Diseases
Johri, A., & Beal, M. F. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.192138 · Cited by 806
Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740
SIRT1 Mediates Central Circadian Control in the SCN by a Mechanism that Decays with Aging
Chang, H.-C., & Guarente, L. (2013) · Cell · doi:10.1016/j.cell.2013.05.027 · Cited by 615
Self-citationAthauda, D., & Foltynie, T. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.01.013 · Cited by 383
“122 Donmez, G. and Outeiro, T.F. (2013) SIRT1 and SIRT2: emerging targets in”
Metadata
- Authors
- Donmez, G., Arun, A., Chung, C.-Y., McLean, P. J., Lindquist, S., & Guarente, L.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2012-01-04
- Volume
- 32
- Issue
- 1
- Pages
- 124-132
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W2070982075
- Cited by
- 208
- References
- 5
- FWCI
- 17.20
- Type
- journal article
- Language
- en
- Status
- Retracted
- Open access
- hybrid
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- Donmez, G., Arun, A., Chung, C.-Y., McLean, P. J., Lindquist, S., & Guarente, L. (2012). SIRT1 Protects against α-Synuclein Aggregation by Activating Molecular Chaperones. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.3442-11.2012
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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.
