Evidence map›Paper›PMID 23979994›Full record

ReviewNeuromolecular medicine2013

SUMO and Parkinson's disease.

Katrin Eckermann

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neuromolecular medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. SUMOylation in development and neurodegeneration.Development (Cambridge, England) · 2020
    Review
  11. Article
  12. Article
  13. Epigenetic regulation of astrocyte function in neuroinflammation and neurodegeneration.Biochimica et biophysica acta. Molecular basis of disease · 2018
    Review
  14. Sumoylation Protects Against β-Synuclein Toxicity in Yeast.Frontiers in molecular neuroscience · 2018
    Article
  15. Review
  16. The Roles of SUMO in Metabolic Regulation.Advances in experimental medicine and biology · 2017
    Review
  17. Ubiquitin-dependent and independent roles of SUMO in proteostasis.American journal of physiology. Cell physiology · 2016
    Review
  18. Review
  19. Sumoylation in Synaptic Function and Dysfunction.Frontiers in synaptic neuroscience · 2016
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Katrin EckermannDepartment of Neurology, University Medical Center Goettingen, Waldweg 33, 37073, Goettingen, Germany, keckerm@gwdg.de.
University of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parkinson's disease (PD) is one of the most common degenerative disorders of the central nervous system that produces motor and non-motor symptoms. The majority of cases are idiopathic and characterized by the presence of Lewy bodies containing fibrillar α-synuclein. Small ubiquitin-related modifier (SUMO) immunoreactivity was observed among others in cases with PD. Key disease-associated proteins are SUMO-modified, linking this posttranslational modification to neurodegeneration. SUMOylation and SUMO-mediated mechanisms have been intensively studied in recent years, revealing nuclear and extranuclear functions for SUMO in a variety of cellular processes, including the regulation of transcriptional activity, modulation of signal transduction pathways, and response to cellular stress. This points to a role for SUMO more than just an antagonist to ubiquitin and proteasomal degradation. The identification of risk and age-at-onset gene loci was a breakthrough in PD and promoted the understanding of molecular mechanisms in the pathology. PD has been increasingly linked with mitochondrial dysfunction and impaired mitochondrial quality control. Interestingly, SUMO is involved in many of these processes and up-regulated in response to cellular stress, further emphasizing the importance of SUMOylation in physiology and disease.

Indexed as

alpha-SynucleinDopaminergic NeuronsGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsMitochondriaNerve Tissue ProteinsNeurotoxinsOncogene ProteinsOxidative StressParkinson DiseaseParkinsonian DisordersProteasome Endopeptidase ComplexProtein BindingProtein Deglycase DJ-1Signal Transductionalpha-SynucleinIntracellular Signaling Peptides and ProteinsNerve Tissue ProteinsNeurotoxinsOncogene ProteinsPARK7 protein, humanparkin proteinProteasome Endopeptidase ComplexProtein Deglycase DJ-1Small Ubiquitin-Related Modifier ProteinsUbiquitinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID23979994
OpenAlexW2063747935

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.