ArticlePloS one2010
The HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathy.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 41 citations in OpenAlex.
- Fluc-EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease.The EMBO journal · 2021Article
- Heat shock protein signaling in brain ischemia and injury.Neuroscience letters · 2020Review
- Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Human Disease.Advances in experimental medicine and biology · 2020Review
- The role of chaperone-mediated autophagy in neurotoxicity induced by alpha-synuclein after methamphetamine exposure.Brain and behavior · 2019Article
- Hsp90 Co-chaperone p23 contributes to dopaminergic mitochondrial stress via stabilization of PHD2: Implications for Parkinson's disease.Neurotoxicology · 2018Article
- FLZ Attenuates α-Synuclein-Induced Neurotoxicity by Activating Heat Shock Protein 70.Molecular neurobiology · 2017Article
- A Novel Hsp90 Inhibitor Activates Compensatory Heat Shock Protein Responses and Autophagy and Alleviates Mutant A53T α-Synuclein Toxicity.Molecular pharmacology · 2015Article
- Targeting protein aggregation for the treatment of degenerative diseases.Nature reviews. Drug discovery · 2015Review
- Molecular chaperones and neuronal proteostasis.Seminars in cell & developmental biology · 2015Review
- Barcoding heat shock proteins to human diseases: looking beyond the heat shock response.Disease models & mechanisms · 2014Review
- Article
- Heat shock protein 70 reduces α-synuclein-induced predegenerative neuronal dystrophy in the α-synuclein viral gene transfer rat model of Parkinson's disease.CNS neuroscience & therapeutics · 2014Article
- Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies.Acta neuropathologica communications · 2013Review
- Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2013Review
- Yet another role for SIRT1: reduction of α-synuclein aggregation in stressed neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- α-Synuclein in Parkinson's disease.Cold Spring Harbor perspectives in medicine · 2012Review
- SIRT1 protects against α-synuclein aggregation by activating molecular chaperones.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- High LRRK2 levels fail to induce or exacerbate neuronal alpha-synucleinopathy in mouse brain.PloS one · 2012Article
- Excess α-synuclein worsens disease in mice lacking ubiquitin carboxy-terminal hydrolase L1.Scientific reports · 2012Article
- Hsc70 protein interaction with soluble and fibrillar alpha-synuclein.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAggregation and misfolded alpha-synuclein is thought to be central in the pathogenesis of Parkinson's disease (PD). Heat-shock proteins (HSPs) that are involved in refolding and degradation processes could lower the aggregate load of alpha-synuclein and thus be beneficial in alpha-synucleinopathies. METHODOLOGY/PRINCIPAL
findingsWe co-overexpressed human A53T point-mutated alpha-synuclein and human HSP70 in mice, both under the control of Thy1 regulatory sequences. Behavior read-outs showed no beneficial effect of HSP70 expression in mice. In contrast, motor coordination, grip strength and weight were even worse in the alpha-synucleinopathy model in the presence of HSP70 overexpression. Biochemical analyses revealed no differences in alpha-synuclein oligomers/aggregates, truncations and phosphorylation levels and alpha-synuclein localization was unchanged in immunostainings. CONCLUSION/SIGNIFICANCE: Overexpressing HSP70 in a mouse model of alpha-synucleinopathy did not lower the toxic load of alpha-synuclein species and had no beneficial effect on alpha-synuclein-related motor deficits.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.