ReviewBiomolecules2015
Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity.
Review in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Curcumin attenuates α-synuclein pathology in Parkinson's disease model mice through modulation of UBC9-associated SUMOylation signaling.Frontiers in neuroscience · 2026Article
- Posttranslational Modifications ofPharmacological reviews · 2024Review
- RNA and Protein Delivery by Cell-Secreted and Bioengineered Extracellular Vesicles.Advanced healthcare materials · 2022Review
- Ferritinophagy and α-Synuclein: Pharmacological Targeting of Autophagy to Restore Iron Regulation in Parkinson's Disease.International journal of molecular sciences · 2022Review
- Alterations in Striatal microRNA-mRNA Networks Contribute to Neuroinflammation in Multiple System Atrophy.Molecular neurobiology · 2019Article
- Intracellular and Intercellular Mitochondrial Dynamics in Parkinson's Disease.Frontiers in neuroscience · 2019Review
- The Small GTPase RAC1/CED-10 Is Essential in Maintaining Dopaminergic Neuron Function and Survival Against α-Synuclein-Induced Toxicity.Molecular neurobiology · 2018Article
- SUMOylation of Alpha-Synuclein Influences on Alpha-Synuclein Aggregation Induced by Methamphetamine.Frontiers in cellular neuroscience · 2018Article
- Post-translational add-ons mark the path in exosomal protein sorting.Cellular and molecular life sciences : CMLS · 2018Review
- Sumoylation in Synaptic Function and Dysfunction.Frontiers in synaptic neuroscience · 2016Review
- Neuroinflammation in Multiple System Atrophy: Response to and Cause of α-Synuclein Aggregation.Frontiers in cellular neuroscience · 2015Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Synuclein inclusion bodies are a pathological hallmark of several neurodegenerative diseases, including Parkinson's disease, and contain aggregated α-synuclein and a variety of recruited factors, including protein chaperones, proteasome components, ubiquitin and the small ubiquitin-like modifier, SUMO-1. Cell culture and animal model studies suggest that misfolded, aggregated α-synuclein is actively translocated via the cytoskeletal system to a region of the cell where other factors that help to lessen the toxic effects can also be recruited. SUMO-1 covalently conjugates to various intracellular target proteins in a way analogous to ubiquitination to alter cellular distribution, function and metabolism and also plays an important role in a growing list of cellular pathways, including exosome secretion and apoptosis. Furthermore, SUMO-1 modified proteins have recently been linked to cell stress responses, such as oxidative stress response and heat shock response, with increased SUMOylation being neuroprotective in some cases. Several recent studies have linked SUMOylation to the ubiquitin-proteasome system, while other evidence implicates the lysosomal pathway. Other reports depict a direct mechanism whereby sumoylation reduced the aggregation tendency of α-synuclein, and reduced the toxicity. However, the precise role of SUMO-1 in neurodegeneration remains unclear. In this review, we explore the potential direct or indirect role(s) of SUMO-1 in the cellular response to misfolded α-synuclein in neurodegenerative disorders.
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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.