Evidence map›Paper›PMID 27729585›Full record

ReviewThe Biochemical journal2016

Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3.

Arno F Alpi, Viduth Chaugule, Helen Walden

Open access · hybridAbstract readReview
In one paragraph

Review in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

49 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Transcriptome sequencing (RNA-Seq) reveals non-coding pseudogene CDC27P9 role in cervical cancer.Apoptosis : an international journal on programmed cell death · 2026
    Article
  4. Article
  5. Review
  6. Ubiquitin-conjugating Enzymes in Cancer.International journal of biological sciences · 2026
    Review
  7. Article
  8. UBE2T-Mediated HP1α Ubiquitination Enhances Nucleolar Function and Promotes the Progression of IDH1/TP53-Mutant Glioma.Clinical cancer research : an official journal of the American Association for Cancer Research · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Review
  16. Article
  17. 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

3 authors at 1 institution in 1 country.

Arno F AlpiMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Viduth ChauguleMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Helen WaldenMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
MRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Cancer Research UK 17739Medical Research Council MC_UU_12016/12Medical Research Council MC_UU_1206/12
6 · The paper itself

Abstract

Ubiquitin signalling is a fundamental eukaryotic regulatory system, controlling diverse cellular functions. A cascade of E1, E2, and E3 enzymes is required for assembly of distinct signals, whereas an array of deubiquitinases and ubiquitin-binding modules edit, remove, and translate the signals. In the centre of this cascade sits the E2-conjugating enzyme, relaying activated ubiquitin from the E1 activating enzyme to the substrate, usually via an E3 ubiquitin ligase. Many disease states are associated with dysfunction of ubiquitin signalling, with the E3s being a particular focus. However, recent evidence demonstrates that mutations or impairment of the E2s can lead to severe disease states, including chromosome instability syndromes, cancer predisposition, and immunological disorders. Given their relevance to diseases, E2s may represent an important class of therapeutic targets. In the present study, we review the current understanding of the mechanism of this important family of enzymes, and the role of selected E2s in disease.

Indexed as

AnimalsAutoimmune DiseasesHumansModels, BiologicalNeoplasmsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesUBE2L3 protein, humanUBE2T protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasesautoimmune diseaseE2-conjugating enzymeFanconi anaemiaUBE2L3UBE2Tubiquitin signalling

Identifiers

PMID27729585
PMCPMC5095918
OpenAlexW2529916409

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.