Evidence map›Paper›PMID 23747565›Full record

ReviewBiochimica et biophysica acta2014

RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination.

Meredith B Metzger, Jonathan N Pruneda, Rachel E Klevit, Allan M Weissman

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 372 papers.

0numbers the graph read from it
0cells of the map it votes in
372citing 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

372 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Siah2 regulates lipid uptake in adipose tissue macrophages.The Journal of biological chemistry · 2026
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. MARCH E3 Ligases: Understudied Regulators of Pulmonary Immune Function.Journal of respiratory biology and translational medicine · 2026
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  20. Article

312 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.

Meredith B MetzgerLaboratory of Protein Dynamics and Signaling, Center for Cancer Research, National Cancer Institute, 1050 Boyles Street, Frederick, MD 21702, USA.
Jonathan N Pruneda
Rachel E Klevit
Allan M Weissman

Funding

Determining the Fate of Transmembrane ProteinsZIABC009392 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WEISSMAN, ALLAN M · 2009 to 2024
$15.5M
Enzymes and Substrates of the Ubiquitin Conjugating SystemZIABC010292 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WEISSMAN, ALLAN M · 2009 to 2024
$12.2M
Structural and Functional Characterization of BRCA1/BARD1R01GM088055 · NIGMS · UNIVERSITY OF WASHINGTON · PI KLEVIT, RACHEL E · 2009 to 2020
$6.5M
Unconventional Interactions of Human Ubiquitin Conjugating EnzymesR01GM098503 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRZOVIC, PETER S · 2012 to 2016
$1.5M
Intramural NIH HHS ZIA BC010292NIGMS NIH HHS R01 GM088055NIGMS NIH HHS R01 GM098503
6 · The paper itself

Abstract

RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin-conjugating enzymes (E2s) to mediate ubiquitination and are implicated in numerous cellular processes. In part because of their importance in human physiology and disease, these proteins and their cellular functions represent an intense area of study. Here we review recent advances in RING-type E3 recognition of substrates, their cellular regulation, and their varied architecture. Additionally, recent structural insights into RING-type E3 function, with a focus on important interactions with E2s and ubiquitin, are reviewed. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.

Indexed as

AnimalsEnzyme ActivationHumansModels, MolecularProtein MultimerizationProtein Structure, TertiaryProtein SubunitsUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesProtein SubunitsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesCatalysisProtein degradationRING fingerUbiquitin-conjugating enzyme (E2)Ubiquitin ligase (E3)U-box

Identifiers

PMID23747565
PMCPMC4109693

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.