Evidence map›Paper›PMID 24052421›Full record

ReviewNeuromolecular medicine2013

SUMO: a (oxidative) stressed protein.

Marco Feligioni, Robert Nisticò

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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Protective Effect of Curcuma Extract in anOxidative medicine and cellular longevity · 2022
    Article
  10. Article
  11. Article
  12. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. [Human RhoA is modified by SUMO2/3].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018
    Article
  19. Article
  20. Review
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

2 authors.

Marco FeligioniLaboratory of Pharmacology of Synaptic Plasticity, EBRI "Rita Levi-Montalcini" Foundation, Via del Fosso di Fiorano 64/65, 00143, Rome, Italy, m.feligioni@ebri.it.
Robert Nisticò

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Redox species are produced during the physiological cellular metabolism of a normal tissue. In turn, their presence is also attributed to pathological conditions including neurodegenerative diseases. Many are the molecular changes that occur during the unbalance of the redox homeostasis. Interestingly, posttranslational protein modifications (PTMs) play a remarkable role. In fact, several target proteins are modified in their activation, localization, aggregation, and expression after the cellular stress. Among PTMs, protein SUMOylation represents a very important molecular modification pathway during "oxidative stress". It has been reported that this ubiquitin-like modification is a fine sensor for redox species. Indeed, SUMOylation pathway efficiency is affected by the exposure to oxidative species in a different manner depending on the concentration and time of application. Thus, we here report updated evidence that states the role of SUMOylation in several pathological conditions, and we also outline the key involvement of c-Jun N-terminal kinase and small ubiquitin modifier pathway cross talk.

Indexed as

AnimalsDiabetes MellitusHumansJNK Mitogen-Activated Protein KinasesMAP Kinase Signaling SystemNeoplasm ProteinsNeoplasmsNerve Tissue ProteinsNeurodegenerative DiseasesOxidation-ReductionOxidative StressReactive Oxygen SpeciesSignal TransductionSmall Ubiquitin-Related Modifier ProteinsSumoylationUbiquitinJNK Mitogen-Activated Protein KinasesNeoplasm ProteinsNerve Tissue ProteinsReactive Oxygen SpeciesSmall Ubiquitin-Related Modifier ProteinsUbiquitinUbiquitin-Protein Ligase Complexes

Identifiers

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.