Evidence map›Paper›PMID 18282128›Full record

ReviewExpert review of proteomics2008

Ubiquitin proteolytic system: focus on SUMO.

Van G Wilson, Phillip R Heaton

Open access · greenAbstract readReview
In one paragraph

Review in Expert review of proteomics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Regulation of germ cell function by SUMOylation.Cell and tissue research · 2016
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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 at 1 institution in 1 country.

Van G WilsonDepartment of Microbial & Molecular Pathogenesis, College of Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114, USA. wilson@medicine.tamhsc.edu
Phillip R Heaton
Texas A&M Health Science Center · US

Funding

Cellular Regulation of Papillomavirus E1 FunctionR01CA089298 · NCI · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI WILSON, VAN G. · 2003 to 2007
$1.4M
NCI NIH HHS CA089298NCI NIH HHS R01 CA089298
6 · The paper itself

Abstract

The small ubiquitin-like modifier proteins (Smt3 in yeast and SUMOs 1-4 in vertebrates) are members of the ubiquitin super family. Like ubiquitin, the SUMOs are protein modifiers that are covalently attached to the epsilon-amino group of lysine residues in the substrates. The application of proteomics to the SUMO field has greatly expanded both the number of known targets and the number of identified target lysines. As new refinements of proteomic techniques are developed and applied to sumoylation, an explosion of novel data is likely in the next 5 years. This ability to examine sumoylated proteins globally, rather than individually, will lead to new insights into both the functions of the individual SUMO types, and how dynamic changes in overall sumoylation occur in response to alterations in cellular environment. In addition, there is a growing appreciation for the existence of cross-talk mechanisms between the sumoylation and ubiquitinylation processes. Rather than being strictly parallel, these two systems have many points of intersection, and it is likely that the coordination of these two systems is a critical contributor to the regulation of many fundamental cellular events.

Indexed as

UbiquitinationAnimalsCaenorhabditis elegans ProteinsConserved SequenceEndopeptidasesHumansLigasesLysineMass SpectrometryMiceModels, MolecularNeoplasm ProteinsNuclear ProteinsProteasome Endopeptidase ComplexProtein Array AnalysisProtein Processing, Post-TranslationalCaenorhabditis elegans ProteinsEndopeptidasesLigasesLysineNeoplasm ProteinsNuclear ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsTOPORS protein, humanUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID18282128
PMCPMC3467698
OpenAlexW1987601566

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.