Evidence map›Paper›PMID 17987030›Full record

ReviewNature reviews. Neuroscience2007

Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction.

Stéphane Martin, Kevin A Wilkinson, Atsushi Nishimune, Jeremy M Henley

Abstract readReview
In one paragraph

Review in Nature reviews. Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing 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

113 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

53 more citing papers are in PubMed but not listed here.

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

4 authors.

Stéphane MartinMRC Centre for Synaptic Plasticity, Department of Anatomy, School of Medical Sciences, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Kevin A Wilkinson
Atsushi Nishimune
Jeremy M Henley

Funding

Medical Research Council G0601810Medical Research Council G9629038Medical Research Council G9629038(61600)Wellcome Trust 059917Wellcome Trust 083721
6 · The paper itself

Abstract

Post-translational protein modifications are integral components of signalling cascades that enable cells to efficiently, rapidly and reversibly respond to extracellular stimuli. These modifications have crucial roles in the CNS, where the communication between neurons is particularly complex. SUMOylation is a post-translational modification in which a member of the small ubiquitin-like modifier (SUMO) family of proteins is conjugated to lysine residues in target proteins. It is well established that SUMOylation controls many aspects of nuclear function, but it is now clear that it is also a key determinant in many extranuclear neuronal processes, and it has also been implicated in a wide range of neuropathological conditions.

Indexed as

Amino Acid SequenceAnimalsCell NucleusHumansMolecular Sequence DataNeuronsProtein Processing, Post-TranslationalSmall Ubiquitin-Related Modifier ProteinsSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID17987030
PMCPMC3314512

What OpenQuestion holds

Textmetadata
LicenceTDM
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.